Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O88397
|
SO1A5_RAT
|
MGETEKRVATHEVRCFSKIKMFLLALTWAYVSKSLSGIYMNTMLTQIERQFDIPTSIVGFINGSFEIGNLLLIIFVSYFGTKLHRPIMIGVGCVIMGLGCFLMSLPHFLMGRYEYETTISPTSNLSSNSFLCMENRSQTLKPTQDPAECIKEMKSLMWIYVLVGNIIRGIGETPIMPLGISYIEDFAKSENSPLYIGILETGKVFGPIVGLLLGSFCASIYVDTGSVNTDDLTITPTDTRWVGAWWIGFLICAGVNILSSIPFFFFPKTLPKEGLQDDVDGTNNDKEEKHREKAKEENRGITKDFLPFMKSLSCNPIYMLLILTSVLQINAFINMFTFLPKYLEQQYGKSTAEVVLLIGVYNLPPICIGYLLIGFIMKKFKITVKKAAYMAFCLSLFEYLLYFLHFMITCDNFPVAGLTASYEGVHHPLYVENKVLADCNRGCSCSTNSWDPVCGDNGLAYMSACLAGCKKSVGTGTNMVFQNCSCIRSSGNSSAVLGLCKKGPECANKLQYFLIMSVIGSFIYSITAIPGYMVLLRCIKPEEKSLGIGLHAFCTRVFAGIPAPIYFGALIDRTCLHWGTLKCGEPGACRMYNINNFRRIYLVLPAALRGSSYLPALFILILMRKFQFPGEIDSSETELAEMKITVKKSECTDVHGSPQVENDGELKTRL
| null | null |
animal organ regeneration [GO:0031100]; bile acid and bile salt transport [GO:0015721]; intestinal absorption [GO:0050892]; monoatomic ion transport [GO:0006811]; monocarboxylic acid transport [GO:0015718]; organic anion transport [GO:0015711]; sodium-independent organic anion transport [GO:0043252]
|
basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]
|
bile acid transmembrane transporter activity [GO:0015125]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; organic anion transmembrane transporter activity [GO:0008514]; sodium-independent organic anion transmembrane transporter activity [GO:0015347]; thyroid hormone transmembrane transporter activity [GO:0015349]
|
PF07648;PF03137;
|
1.20.1250.20;
|
Organo anion transporter (TC 2.A.60) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P46721}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:P46721}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703, ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:11093941, ECO:0000269|PubMed:9712861, ECO:0000305|PubMed:19129463}; CATALYTIC ACTIVITY: Reaction=glycocholate(out) = glycocholate(in); Xref=Rhea:RHEA:71851, ChEBI:CHEBI:29746; Evidence={ECO:0000269|PubMed:11093941}; CATALYTIC ACTIVITY: Reaction=taurochenodeoxycholate(out) = taurochenodeoxycholate(in); Xref=Rhea:RHEA:71855, ChEBI:CHEBI:9407; Evidence={ECO:0000269|PubMed:11093941}; CATALYTIC ACTIVITY: Reaction=tauroursodeoxycholate(out) = tauroursodeoxycholate(in); Xref=Rhea:RHEA:71843, ChEBI:CHEBI:132028; Evidence={ECO:0000269|PubMed:11093941}; CATALYTIC ACTIVITY: Reaction=3,3',5'-triiodo-L-thyronine(out) = 3,3',5'-triiodo-L-thyronine(in); Xref=Rhea:RHEA:71815, ChEBI:CHEBI:57261; Evidence={ECO:0000269|PubMed:9712861}; CATALYTIC ACTIVITY: Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819, ChEBI:CHEBI:58448; Evidence={ECO:0000269|PubMed:9712861, ECO:0000305|PubMed:19129463}; CATALYTIC ACTIVITY: Reaction=taurodeoxycholate(out) = taurodeoxycholate(in); Xref=Rhea:RHEA:71863, ChEBI:CHEBI:36261; Evidence={ECO:0000269|PubMed:11093941}; CATALYTIC ACTIVITY: Reaction=glycodeoxycholate(out) = glycodeoxycholate(in); Xref=Rhea:RHEA:71867, ChEBI:CHEBI:82982; Evidence={ECO:0000269|PubMed:11093941}; CATALYTIC ACTIVITY: Reaction=glycochenodeoxycholate(out) = glycochenodeoxycholate(in); Xref=Rhea:RHEA:71859, ChEBI:CHEBI:36252; Evidence={ECO:0000269|PubMed:11093941}; CATALYTIC ACTIVITY: Reaction=glycoursodeoxycholate(out) = glycoursodeoxycholate(in); Xref=Rhea:RHEA:71847, ChEBI:CHEBI:132030; Evidence={ECO:0000269|PubMed:11093941}; CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in); Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050; Evidence={ECO:0000305|PubMed:19129463}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000305|PubMed:19129463}; CATALYTIC ACTIVITY: Reaction=substance P(out) = substance P(in); Xref=Rhea:RHEA:74367, ChEBI:CHEBI:190692; Evidence={ECO:0000250|UniProtKB:P46721};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17.99 uM for taurocholate {ECO:0000269|PubMed:9712861}; KM=20.9 uM for taurocholate {ECO:0000269|PubMed:11093941}; KM=4.93 uM for L-thyroxine {ECO:0000269|PubMed:9712861}; KM=7.33 uM for 3,3',5'-triiodo-L-thyronine {ECO:0000269|PubMed:9712861}; KM=8.8 uM for cholate {ECO:0000269|PubMed:11093941}; KM=15.4 uM for glycocholate {ECO:0000269|PubMed:11093941}; KM=5.8 uM for taurodeoxycholate {ECO:0000269|PubMed:11093941}; KM=4.3 uM for glycodeoxycholate {ECO:0000269|PubMed:11093941}; KM=7 uM for taurochenodeoxycholate {ECO:0000269|PubMed:11093941}; KM=6.6 uM for tauroursodeoxycholate {ECO:0000269|PubMed:11093941}; KM=5.6 uM for glycochenodeoxycholate {ECO:0000269|PubMed:11093941}; KM=5.3 uM for glycoursodeoxycholate {ECO:0000269|PubMed:11093941}; KM=83.5 uM for estrone 3-sulfate (at pH 6.5) {ECO:0000269|PubMed:19129463}; KM=177 uM for estrone 3-sulfate (at pH 8.0) {ECO:0000269|PubMed:19129463}; KM=8.5 uM for taurocholate (at pH 6.5) {ECO:0000269|PubMed:19129463}; KM=18.2 uM for taurocholate (at pH 8.0) {ECO:0000269|PubMed:19129463}; KM=56.8 uM for prostaglandin E2 (at pH 6.5) {ECO:0000269|PubMed:19129463}; KM=108 uM for prostaglandin E2 (at pH 8.0) {ECO:0000269|PubMed:19129463}; Vmax=38.7 pmol/min/mg protein for cholate {ECO:0000269|PubMed:11093941}; Vmax=110.6 pmol/min/mg protein for taurocholate {ECO:0000269|PubMed:11093941}; Vmax=56.7 pmol/min/mg protein for taurodeoxycholate {ECO:0000269|PubMed:11093941}; Vmax=65.5 pmol/min/mg protein for glycodeoxycholate {ECO:0000269|PubMed:11093941}; Vmax=106.7 pmol/min/mg protein for taurochenodeoxycholate {ECO:0000269|PubMed:11093941}; Vmax=120.2 pmol/min/mg protein for glycochenodeoxycholate {ECO:0000269|PubMed:11093941}; Vmax=43.6 pmol/min/mg protein for tauroursodeoxycholate {ECO:0000269|PubMed:11093941}; Vmax=44.2 pmol/min/mg protein for glycoursodeoxycholate {ECO:0000269|PubMed:11093941}; Vmax=383 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 6.5) {ECO:0000269|PubMed:19129463}; Vmax=453 pmol/min/mg enzyme with estrone 3-sulfate as substrate (at pH 8.0) {ECO:0000269|PubMed:19129463}; Vmax=55.1 pmol/min/mg enzyme with taurocholate as substrate (at pH 6.5) {ECO:0000269|PubMed:19129463}; Vmax=46.6 pmol/min/mg enzyme with taurocholate as substrate (at pH 8.0) {ECO:0000269|PubMed:19129463}; Vmax=85.1 pmol/min/mg enzyme with prostaglandin E2 as substrate (at pH 6.5) {ECO:0000269|PubMed:19129463}; Vmax=98.2 pmol/min/mg enzyme with prostaglandin E2 as substrate (at pH 8.0) {ECO:0000269|PubMed:19129463};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 with estrone 3-sulfate, taurocholate, prostaglandin E2 and L-thyroxine (T4) as substrates. {ECO:0000269|PubMed:19129463};
| null |
FUNCTION: Na(+)-independent transporter that mediates the cellular uptake of a broad range of organic anions such as the endogenous bile salts cholate and deoxycholate, either in their unconjugated or conjugated forms (taurocholate and glycocholate), estrone 3-sulfate and prostaglandin E2, at the plasma membrane (PubMed:11093941, PubMed:19129463, PubMed:9712861). Responsible for intestinal absorption of bile acids (PubMed:11093941). Capable of thyroid hormone transport (both T3 or 3,3',5'-triiodo-L-thyronine, and T4 or L-tyroxine) (PubMed:19129463, PubMed:9712861). Plays roles in blood-brain and -cerebrospinal fluid barrier transport of organic anions and signal mediators, and in hormone uptake by neural cells (By similarity). May also play a role in the reuptake of neuropeptides such as substance P/TAC1 and vasoactive intestinal peptide/VIP released from retinal neurons (By similarity). Shows a pH-sensitive substrate specificity which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment (PubMed:19129463). Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions (PubMed:19129463). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity). {ECO:0000250|UniProtKB:P46721, ECO:0000250|UniProtKB:Q91YY5, ECO:0000269|PubMed:11093941, ECO:0000269|PubMed:19129463, ECO:0000269|PubMed:9712861}.
|
Rattus norvegicus (Rat)
|
O88398
|
AVIL_MOUSE
|
MSLSSAFRAVSNDPRIITWRIEKMELALVPLSAHGNFYEGDCYIVLSTRRVGSLLSQNIHFWIGKDSSQDEQSCAAIYTTQLDDYLGGSPVQHREVQYHESDTFRGYFKQGIIYKKGGVASGMKHVETNTYDVKRLLHVKGKRNIQATEVEMSWDSFNRGDVFLLDLGMVIIQWNGPESNSGERLKAMLLAKDIRDRERGGRAEIGVIEGDKEAASPGLMTVLQDTLGRRSMIKPAVSDEIMDQQQKSSIMLYHVSDTAGQLSVTEVATRPLVQDLLNHDDCYILDQSGTKIYVWKGKGATKVEKQAAMSKALDFIKMKGYPSSTNVETVNDGAESAMFKQLFQKWSVKDQTTGLGKIFSTGKIAKIFQDKFDVSLLHTKPEVAAQERMVDDGKGQVEVWRIENLELVPVEYQWHGFFYGGDCYLVLYTYDVNGKPHYILYIWQGRHASRDELAASAYRAVEVDQQFDGAPVQVRVSMGKEPRHFMAIFKGKLVIYEGGTSRKGNEEPDPPVRLFQIHGNDKSNTKAVEVSASASSLNSNDVFLLRTQAEHYLWYGKGSSGDERAMAKELVDLLCDGNADTVAEGQEPPEFWDLLGGKTAYANDKRLQQETLDVQVRLFECSNKTGRFLVTEVTDFTQEDLSPGDVMLLDTWDQVFLWIGAEANATEKKGALSTAQEYLVTHPSGRDPDTPILIIKQGFEPPTFTGWFLAWDPHIWSEGKSYEQLKNELGDATAIVRITADMKNATLYLNPSDGEPKYYPVEVLLKGQNQELPEDVDPAKKENYLSEQDFVSVFGITRGQFTALPGWKQLQLKKERGLF
| null | null |
actin filament organization [GO:0007015]; actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]; cilium assembly [GO:0060271]; nervous system development [GO:0007399]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of neuron projection development [GO:0010976]; regulation of diacylglycerol biosynthetic process [GO:1900480]
|
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; axon [GO:0030424]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]
|
actin binding [GO:0003779]; actin filament binding [GO:0051015]; Arp2/3 complex binding [GO:0071933]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF00626;PF02209;
|
3.40.20.10;1.10.950.10;
|
Villin/gelsolin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O75366}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O75366}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O75366}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9WU06}. Cell projection, axon {ECO:0000250|UniProtKB:Q9WU06}. Note=In podocytes, present in the F-actin-enriched cell periphery that generates lamellipodia and focal adhesions. {ECO:0000250|UniProtKB:O75366}.
| null | null | null | null | null |
FUNCTION: Ca(2+)-regulated actin-binding protein which plays an important role in actin bundling. May have a unique function in the morphogenesis of neuronal cells which form ganglia. Required for SREC1-mediated regulation of neurite-like outgrowth. Plays a role in regenerative sensory axon outgrowth and remodeling processes after peripheral injury in neonates. Involved in the formation of long fine actin-containing filopodia-like structures in fibroblast. Plays a role in ciliogenesis (PubMed:15247299, PubMed:18160648). In podocytes, controls lamellipodia formation through the regulation of EGF-induced diacylglycerol generation by PLCE1 and ARP2/3 complex assembly (By similarity). {ECO:0000250|UniProtKB:O75366, ECO:0000269|PubMed:15247299, ECO:0000269|PubMed:18160648}.
|
Mus musculus (Mouse)
|
O88406
|
SMAD7_RAT
|
MFRTKRSALVRRLWRSRAPGGEDEEEGVGGGGGGGGLRGEGATDGRAYGAGGGGAGRAGCCLGKAVRGAKGHHHPHPPSSGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPASAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTADCPDAVPSSDETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCGIQLTREVDGVWVYNRSSYPIFIKSATLDNPDSRTLLVHKVFPGFSIKAFDYEKAYSLQRPNDHEFMQQPWTGFTVQISFVKGWGQCYTRQFISSCPCWLEVIFNSR
| null | null |
adherens junction assembly [GO:0034333]; anatomical structure morphogenesis [GO:0009653]; artery morphogenesis [GO:0048844]; cell differentiation [GO:0030154]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to transforming growth factor beta stimulus [GO:0071560]; intracellular signal transduction [GO:0035556]; negative regulation of activin receptor signaling pathway [GO:0032926]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of chondrocyte proliferation [GO:1902731]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of ossification [GO:0030279]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of SMAD protein signal transduction [GO:0060392]; negative regulation of T cell cytokine production [GO:0002725]; negative regulation of T-helper 17 cell differentiation [GO:2000320]; negative regulation of T-helper 17 type immune response [GO:2000317]; negative regulation of transcription by competitive promoter binding [GO:0010944]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of chondrocyte hypertrophy [GO:1903043]; protein stabilization [GO:0050821]; protein-containing complex localization [GO:0031503]; regulation of cardiac muscle contraction [GO:0055117]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; response to laminar fluid shear stress [GO:0034616]; SMAD protein signal transduction [GO:0060395]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ureteric bud development [GO:0001657]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]; ventricular septum morphogenesis [GO:0060412]
|
cytoplasm [GO:0005737]; heteromeric SMAD protein complex [GO:0071144]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
activin receptor binding [GO:0070697]; beta-catenin binding [GO:0008013]; collagen binding [GO:0005518]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]; transcription regulator inhibitor activity [GO:0140416]; type I transforming growth factor beta receptor binding [GO:0034713]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625]
|
PF03165;PF03166;
|
2.60.200.10;3.90.520.10;
|
Dwarfin/SMAD family
|
PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription (By similarity). Phosphorylated by PDPK1 (By similarity). {ECO:0000250|UniProtKB:O15105, ECO:0000250|UniProtKB:O35253}.; PTM: Ubiquitinated by WWP1 (By similarity). Polyubiquitinated by RNF111, which is enhanced by AXIN1 and promotes proteasomal degradation. In response to TGF-beta, ubiquitinated by SMURF1; which promotes its degradation (By similarity). {ECO:0000250|UniProtKB:O15105, ECO:0000250|UniProtKB:O35253}.; PTM: Acetylation prevents ubiquitination and degradation mediated by SMURF1. {ECO:0000250|UniProtKB:O15105}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O15105}. Cytoplasm {ECO:0000250|UniProtKB:O15105}. Note=Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm. TGF-beta stimulates its translocation from the nucleus to the cytoplasm. PDPK1 inhibits its translocation from the nucleus to the cytoplasm in response to TGF-beta. {ECO:0000250|UniProtKB:O15105}.
| null | null | null | null | null |
FUNCTION: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. {ECO:0000250|UniProtKB:O15105}.
|
Rattus norvegicus (Rat)
|
O88407
|
LFG2_RAT
|
MTQGKLSVANKAPGTEGQQQANGEKKDAPAVPSAPPSYEEATSGEGLKAGAFPQGPTAVPLHPSWAYVDPSSSSGYEGGFPAGHHELFSTFSWDDQKVRQLFIRKVYTILLVQLLVTLAVVALFTFCDVVKDYVQANPGWYWASYAVFFATYLTLACCSGPRRHFPWNLILLTIFTLSMAYLTGMLSSYYNTTSVLLCLGITALVCLSVTIFSFQTKFDFTSCHGVLFVLLMTLFFSGLLLAILLPFQYVPWLHAVYAVLGAGVFTLFLAFDTQLLMGNRRHSLSPEEYIFGALNIYLDIIYIFTFFLQLFGTNRE
| null | null |
apoptotic signaling pathway [GO:0097190]; cerebellar granular layer development [GO:0021681]; cerebellar Purkinje cell differentiation [GO:0021702]; cerebellar Purkinje cell layer development [GO:0021680]; cerebellum development [GO:0021549]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; negative regulation of neuron apoptotic process [GO:0043524]; neuron apoptotic process [GO:0051402]; regulation of neuron apoptotic process [GO:0043523]; response to ischemia [GO:0002931]
|
endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; membrane raft [GO:0045121]; postsynaptic membrane [GO:0045211]
| null |
PF01027;
| null |
BI1 family, LFG subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12414123}; Multi-pass membrane protein {ECO:0000269|PubMed:12414123}. Membrane raft {ECO:0000250}. Postsynaptic cell membrane {ECO:0000269|PubMed:12414123}.
| null | null | null | null | null |
FUNCTION: Antiapoptotic protein which protects cells uniquely from Fas-induced apoptosis. Regulates Fas-mediated apoptosis in neurons by interfering with caspase-8 activation. Plays a role in cerebellar development by affecting cerebellar size, internal granular layer (IGL) thickness, and Purkinje cell (PC) development (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88410
|
CXCR3_MOUSE
|
MYLEVSERQVLDASDFAFLLENSTSPYDYGENESDFSDSPPCPQDFSLNFDRTFLPALYSLLFLLGLLGNGAVAAVLLSQRTALSSTDTFLLHLAVADVLLVLTLPLWAVDAAVQWVFGPGLCKVAGALFNINFYAGAFLLACISFDRYLSIVHATQIYRRDPRVRVALTCIVVWGLCLLFALPDFIYLSANYDQRLNATHCQYNFPQVGRTALRVLQLVAGFLLPLLVMAYCYAHILAVLLVSRGQRRFRAMRLVVVVVAAFAVCWTPYHLVVLVDILMDVGVLARNCGRESHVDVAKSVTSGMGYMHCCLNPLLYAFVGVKFREQMWMLFTRLGRSDQRGPQRQPSSSRRESSWSETTEASYLGL
| null | null |
angiogenesis [GO:0001525]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; negative regulation of execution phase of apoptosis [GO:1900118]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chemotaxis [GO:0050921]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; regulation of cell adhesion [GO:0030155]; regulation of leukocyte migration [GO:0002685]; T cell chemotaxis [GO:0010818]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
|
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; C-X-C chemokine binding [GO:0019958]; C-X-C chemokine receptor activity [GO:0016494]; signaling receptor activity [GO:0038023]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: Sulfation on Tyr-27 and Tyr-29 is essential for CXCL10 binding. {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of mesangial cells through a heterotrimeric G-protein signaling pathway. Probably promotes cell chemotaxis response (By similarity). Binds to CCL21. Upon activation by PF4, induces activated T-lymphocytes migration mediated via downstream Ras/extracellular signal-regulated kinase (ERK) signaling. {ECO:0000250|UniProtKB:P49682, ECO:0000269|PubMed:9653165, ECO:0000269|PubMed:9790904}.
|
Mus musculus (Mouse)
|
O88413
|
TULP3_MOUSE
|
MEAARCAPGPRGDSAFDDETLRLRQLKLDNQRALLEKKQRKKRLEPLMVQPNPEARLRRLKPRGSEEHTPLVDPQMPRSDVILHGIDGPAAFLKPEAQDLESKPQVLSVGSPAPEEGTEGSADGESPEETAPKPDLQEILQKHGILSSVNYDEEPDKEEDEGGNLSSPSARSEESAAASQKAASETGASGVTAQQGDAQLGEVENLEDFAYSPAPRGVTVKCKVTRDKKGMDRGLFPTYYMHLEREENRKIFLLAGRKRKKSKTSNYLVSTDPTDLSREGESYIGKLRSNLMGTKFTVYDHGVNPVKAQGLVEKAHTRQELAAICYETNVLGFKGPRKMSVIIPGMNMNHERIPFRPRNEHESLLSKWQNKSMENLIELHNKAPVWNDDTQSYVLNFHGRVTQASVKNFQIVHGNDPDYIVMQFGRVADDVFTLDYNYPLCALQAFAIGLSSFDSKLACE
| null | null |
anterior/posterior pattern specification [GO:0009952]; bone development [GO:0060348]; brain development [GO:0007420]; bronchus morphogenesis [GO:0060434]; central nervous system neuron differentiation [GO:0021953]; dorsal/ventral neural tube patterning [GO:0021904]; embryonic camera-type eye development [GO:0031076]; embryonic digit morphogenesis [GO:0042733]; embryonic neurocranium morphogenesis [GO:0048702]; ganglion development [GO:0061548]; limb development [GO:0060173]; negative regulation of smoothened signaling pathway [GO:0045879]; neural tube closure [GO:0001843]; neural tube development [GO:0021915]; neural tube formation [GO:0001841]; protein localization to cilium [GO:0061512]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; regulation of smoothened signaling pathway [GO:0008589]; smoothened signaling pathway [GO:0007224]; smoothened signaling pathway involved in dorsal/ventral neural tube patterning [GO:0060831]
|
9+0 non-motile cilium [GO:0097731]; axoneme [GO:0005930]; ciliary base [GO:0097546]; cilium [GO:0005929]; extracellular region [GO:0005576]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
enzyme binding [GO:0019899]; G protein-coupled receptor binding [GO:0001664]; intraciliary transport particle A binding [GO:0120160]; phosphatidylinositol binding [GO:0035091]; protein-containing complex binding [GO:0044877]
|
PF01167;PF16322;
| null |
TUB family
| null |
SUBCELLULAR LOCATION: Nucleus. Cell membrane. Cell projection, cilium. Cytoplasm. Secreted. Note=Translocates from the plasma membrane to the nucleus upon activation of guanine nucleotide-binding protein G(q) subunit alpha (By similarity). Does not have a cleavable signal peptide and is secreted by a non-conventional pathway. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Negative regulator of the Shh signaling transduction pathway: recruited to primary cilia via association with the IFT complex A (IFT-A) and is required for recruitment of G protein-coupled receptor GPR161 to cilia, a promoter of PKA-dependent basal repression machinery in Shh signaling. Binds to phosphorylated inositide (phosphoinositide) lipids. Both IFT-A- and phosphoinositide-binding properties are required to regulate ciliary G protein-coupled receptor trafficking. During adipogenesis, regulates ciliary trafficking of FFAR4 in preadipocytes. {ECO:0000269|PubMed:19286674, ECO:0000269|PubMed:19334287, ECO:0000269|PubMed:31761534}.
|
Mus musculus (Mouse)
|
O88419
|
B4GT6_RAT
|
MSALKRMMRVSNRSLIAFIFFFSLSTSCLYFIYVAPGIANTYLFMVQARGIMLRENVKTIGHMIRLYTNKNTTLNGTDYPEGNNTSDYLVQTTTYLPQNFTYSPHLPCPEKLPYMRGFLSVNVSEISFDEVHQLFSKDSEIEPGGHWRPQDCKPRWKVAVLIPFRNRHEHLPIFFLHLIPMLQKQRLEFAFYVIEQTGTQPFNRAMLFNVGFKEAMKDRAWDCVIFHDVDHLPENDRNYYGCGEMPRHFAAKLDKYMYILPYKEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVHYSGYNVTRPEGDLGKYTSIPHHHRGEVQFLGRYKLLRYSKERQFIDGLNNLLYTPKILVDRLYTNISVNLMPELAPVEDY
|
2.4.1.-; 2.4.1.274
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9593693}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9593693}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:9593693};
|
carbohydrate metabolic process [GO:0005975]; central nervous system myelination [GO:0022010]; central nervous system neuron axonogenesis [GO:0021955]; ganglioside biosynthetic process via lactosylceramide [GO:0010706]; glycosphingolipid biosynthetic process [GO:0006688]; glycosylation [GO:0070085]; lactosylceramide biosynthetic process [GO:0001572]; neuron maturation [GO:0042551]; protein glycosylation [GO:0006486]
|
Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]
|
galactosyltransferase activity [GO:0008378]; metal ion binding [GO:0046872]; UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity [GO:0008489]
|
PF02709;PF13733;
| null |
Glycosyltransferase 7 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31495, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:22801, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.274; Evidence={ECO:0000269|PubMed:9593693}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31496; Evidence={ECO:0000269|PubMed:9593693};
| null |
PATHWAY: Protein modification; protein glycosylation.; PATHWAY: Sphingolipid metabolism.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2. {ECO:0000269|PubMed:9593693};
| null |
FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (PubMed:9593693). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity). {ECO:0000250|UniProtKB:Q9WVK5, ECO:0000269|PubMed:9593693}.
|
Rattus norvegicus (Rat)
|
O88420
|
SCN8A_RAT
|
MAARLLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLEAGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNLIRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPEWSKNVEYTFTGIYTFESLVKIIARGFCIDGFTFLRDPWNWLDFSVIMMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTRGFDWEEYINNKTNFYMVPGMLEPLLCGNSSDAGQCPEGFQCMKAGRNPNYGYTSFDTFSWAFLALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQATLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEDGVGSPRSSSELSKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKFSIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDSLFIPIRARERRSSYSGYSGYSQCSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGPGSHIGRLLPEATTEVEIKKKGPGSLLVSMDQLASYGRKDRINSIMSVVTNTLVEELEESQRKCPPCWYKFANTFLIWECHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQFEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELSLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINQECKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMVMVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWTKVKVHAFMQAHFKQREADEVKPLDELYEKKANCIANHTGVDIHRNGDFQKNGNGTTSGIGSSVEKYIIDEDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIKPEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNWFETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFFTNAWCWLDFLIVAVSLVSLIANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIDIVNNKTDCEKLMEGNSTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPDYEGNIYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLVFVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEAGIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPSVGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDATQFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSGELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICRKMASNKLENGGTHRDKKESTPSTASLPSYDSVTKPDKEKQQRAEEGRRERAKRQKEVRESKC
| null | null |
adult walking behavior [GO:0007628]; locomotory behavior [GO:0007626]; membrane depolarization during action potential [GO:0086010]; muscle organ development [GO:0007517]; myelination [GO:0042552]; nerve development [GO:0021675]; neuronal action potential [GO:0019228]; optic nerve development [GO:0021554]; peripheral nervous system development [GO:0007422]; response to toxic substance [GO:0009636]; sensory perception of sound [GO:0007605]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]
|
axon [GO:0030424]; axon initial segment [GO:0043194]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; node of Ranvier [GO:0033268]; parallel fiber to Purkinje cell synapse [GO:0098688]; postsynaptic density membrane [GO:0098839]; presynaptic active zone membrane [GO:0048787]; sodium channel complex [GO:0034706]; voltage-gated sodium channel complex [GO:0001518]; Z disc [GO:0030018]
|
ATP binding [GO:0005524]; sodium ion binding [GO:0031402]; voltage-gated sodium channel activity [GO:0005248]
|
PF00520;PF00612;PF06512;PF11933;
|
1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350;
|
Sodium channel (TC 1.A.1.10) family, Nav1.6/SCN8A subfamily
|
PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis. {ECO:0000250}.; PTM: Phosphorylation at Ser-1495 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9603190}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cell projection, axon {ECO:0000250|UniProtKB:Q9WTU3}. Note=Mainly localizes to the axon initial segment. {ECO:0000250|UniProtKB:Q9WTU3}.
| null | null | null | null | null |
FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. {ECO:0000269|PubMed:9603190}.
|
Rattus norvegicus (Rat)
|
O88422
|
GALT5_RAT
|
MNKIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTGILKEDIMRREQTGFRVEADQMTILSPSSRGMRPPRNGAGGKESFRKAENRVLKVEENVDQVQRKGKMQFLLGRGKAVSLWHRTHVQTLPVTLPMQKTQGRDSKPEVSSLHMMSKQTTVLGSEKDSFTVSRGVPLNKTAEHTETLDKKQEAPENYNLSSDTSKQASQRALNVTISVRTDRSKQQSQTVTKSSIQFASLPILKPEEVTVTKKTEAQGKDLKYEAHKARPLLKFTADVGHLKKQSTNETGLGVLPEADGAKVAPGKKLNFSESQIVIITKEEGQKTDTKEVPNSKIQTVFPKLLGESQGKHIPRSQSQTLSSPLAPKRAVSQSKPTLAEELHTARSNLTAKATTVGHQQSHANISENPGKHHVLRIDVTLSPRDLNAPGQFGRPVVVPPGKKKEAEQRWKEGNFNVYLSDLIPVDRAIEDTRPAGCAEQLVHNDLPTTSIIMCFVDEVWSALLRSVHSVLNRSPPHLIKEILLVDDFSTKDYLKANLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVECNVGWLEPLLERVYLNRKKVACPVIEVINDKDMSYMTVDNFQRGVFTWPMNFGWRTIPPDVIAKNGIKETDIIRCPVMAGGLFSIDKSYFYELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRNDNPYSFPKDRMKTVERNLVRVAEVWLDEYKELFYGHGDHLIDQGLDVGNLTQQRELRKKLKCQSFKWYLDNVFPDLKAPVVRASGVFINLALGKCVSIKNITVVLEDCDGSSELQQFNYTWVRLIKHGEWCVAPIPDKGSLTLYPCDNRNNRLKWLHRSASAFHPELVDHIVFESYQQLLCMEGNFSQKTLKLAACNPTEPQQKWKFEKYYDV
|
2.4.1.41
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
protein O-linked glycosylation [GO:0006493]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]
|
PF00535;PF00652;
|
2.80.10.50;
|
Glycosyltransferase 2 family, GalNAc-T subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41; Evidence={ECO:0000269|PubMed:9765313}; CATALYTIC ACTIVITY: Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41; Evidence={ECO:0000269|PubMed:9765313};
| null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2, Muc1b, rMuc-2 or mG-Muc substrates.
|
Rattus norvegicus (Rat)
|
O88427
|
CAC1H_MOUSE
|
MTEGTLAADEVRVPLGASPSAPAAPVRASPASPGVPGREEQRGSGSSVLAPESPGTECGADLGADEEQPVPYPALAATVFFCLGQTTRPRSWCLRLVSRRWFEHISMLVIMLNCVTLGMFRPCEDVECRSERCSILEAFDDFIFAFFAVEMVIKMVALGLFGQKCYLGDTWNRLDFFIVMAGMMEYSLDGHNVSLSAIRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLDSAFVRNNNLTFLRPYYQTEEGEENPFICSSRRDNGMQKCSHIPSRRELRVQCTLGWEAYGQPQAEDGGAGRNACINWNQYYNVCRSGEFNPHNGAINFDNIGYAWIAIFQVITLEGWVDIMYYVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRENQLMREQRARYLSNDSTLASFSEPGSCYEELLKYVGHIFRKVKRRSLRLYARWQSRWRKKVDPSSTLHGQGPRRRPRRAGRRTASVHHLVYHHHHHHHHHYHFSHGGPRRPSPEPGAGDTRLVRACVPPSPPSPGHGPPDSESVHSIYHADCHVEGPQERARVAHTIATAASLKLASGLGTMNYPTILPSGAVNSKGSTSSRPKGLRSAGTPGATAHSPLSLGSPSPYEKIQHVVGEQGLGRASSHLSGLSVPCPLPSPQAGTLTCELKSCPYCASALEDPEFEFSGSESGDSDAHGVYEFTQDVRHGDCRDPVQQPHEGGTPGHGNERWRPPLRTASQPGGLGRLWASFSSKLRRIVDSKYFNRGIMAAILVNTLSMGVEYHEQPDELTNALEISNIVFTSMFALEMLLKLLACGPLGYIRNPYNIFDGIVVIISVWEIVGQADGGLSVLRTFRLLRVLKLVRFLPALRRQLVVLMRTMDNVATFCMLLMLFIFIFSILGMHLFGCKFSLKTDSGDTVPDRKNFDSLLWAIVTVFQILTQEDWNVVLYNGMASTSSWAALYFVALMTFGNYVLFNLLVAILVEGFQAEGDATRSDTDEDKTSTHLEEDFDKLRDVQATEMKMYSLAVTPNGHLEGRGSLPPPLITHTAATPMPTPKSSPHLDMAHTLLDSRRSSSGSVDPQLGDQKSLASLRSSPCAPWGPNSAGSSRRSSWNSLGRAPSLKRRSQCGERESLLSGEGKGSTDDEAEDSRPNSGTHPGASPGPRATPLRRAESLGHRSTMDLCPPRPATLLPTKFRDCNGQMVALPSEFFLRIDSHKEDAAEFDDDIEDSCCFRLHKVLEPYAPQWCSSRESWALYLFPPQNRLRVSCQKVIAHKMFDHVVLVFIFLNCITIALERPDIDPGSTERAFLSVSNYIFTAIFVVEMMVKVVALGLLWGEHAYLQSSWNVLDGLLVLVSLVDIIVAVASAGGAKILGVLRVLRLLRTLRPLRVISRAPGLKLVVETLISSLRPIGNIVLICCAFFIIFGILGVQLFKGKFYYCEGTDTRNITTKAECHAAHYRWVRRKYNFDNLGQALMSLFVLSSKDGWVNIMYDGLDAVGIDQQPVQNHNPWMLLYFISFLLIVSFFVLNMFVGVVVENFHKCRQHQEAEEARRREEKRLRRLERRRRSTFPNPEAQRRPYYADYSHTRRSIHSLCTSHYLDLFITFIICLNVITMSMEHYNQPKSLDEALKYCNYVFTIVFVFEAALKLVAFGFRRFFKDRWNQLDLAIVLLSIMGIALEEIEMNAALPINPTIIRIMRVLRIARVLKLLKMATGMRALLDTVVQALPQVGNLGLLFMLLFFIYAALGVELFGRLECSEDNPCEGLSRHATFTNFGMAFLTLFRVSTGDNWNGIMKDTLRECTREDKHCLSYLPALSPVYFVTFVLVAQFVLVNVVVAVLMKHLEESNKEAREDAEMDAEIELEIAQGSTAQPPSTAQESQGTEPDTPNLLVVRKVSVSRMLSLPNDSYMFRPVAPAAAPHSHPLQEVEMETYTGPVTSAHSPSLEPRTSFQVPSAASSPARVSDPLCALSPRDTPRSLSLSRILCRQEAMHAESLEGQIDDAGEDSIPDYTEPAENISMSQAPLGTLRSPPCSPRPASVRTRKHTFGQHCISSRPPTLGGDDAEAADPADEEVSHITSSAHPWPATEPHSPEASPTASPAKGTVGSGRDPHRFCSVDAQSFLDKPGRPDAQRWSSVELDNGDGHLESGEVRARASELEPALGARRKKKMSPPCISIDPPTEDEGSSRPPAAEGGNTTLRRRTPSCEAALHRDCPESTEGPGTGGDPVAKGERWGQASCRAEHLTVPNFAFEPLDMGGPGGDCFLDSDQSVTPEPRVSSLGAIVPLILETELSMPSGDPPEKEQGLYLTVPQTPLKKPGSPPATPAPDDSGDEPV
| null | null |
aldosterone biosynthetic process [GO:0032342]; calcium ion import [GO:0070509]; calcium ion transport [GO:0006816]; cortisol biosynthetic process [GO:0034651]; inorganic cation transmembrane transport [GO:0098662]; membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; positive regulation of cardiac muscle cell contraction [GO:0106134]; sodium ion transmembrane transport [GO:0035725]
|
caveola [GO:0005901]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic active zone membrane [GO:0048787]; sarcolemma [GO:0042383]; voltage-gated calcium channel complex [GO:0005891]; voltage-gated sodium channel complex [GO:0001518]
|
low voltage-gated calcium channel activity [GO:0008332]; metal ion binding [GO:0046872]; voltage-gated monoatomic ion channel activity [GO:0005244]; voltage-gated sodium channel activity [GO:0005248]
|
PF00520;
|
1.10.287.70;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1H subfamily
|
PTM: In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95180}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95180}. Note=Interaction with STAC increases expression at the cell membrane. {ECO:0000250|UniProtKB:O95180}.
| null | null | null | null | null |
FUNCTION: Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation. T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle. They may also be involved in the modulation of firing patterns of neurons. In the adrenal zona glomerulosa, participates in the signaling pathway leading to aldosterone production in response to either AGT/angiotensin II, or hyperkalemia. {ECO:0000250|UniProtKB:O95180}.
|
Mus musculus (Mouse)
|
O88428
|
PAPS2_MOUSE
|
MSANFKMNHKRDQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNKNLGFSAGDREENIRRIAEVARLFADAGLVCITSFISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPECVLKTNLSSVSDCVQQVVELLQEQNIVPHTTIKGIHELFVPENKVDQIRAEAETLPSLPITKLDLQWVQILSEGWATPLKGFMREKEYLQTLHFDTLLDGVVPRDGVINMSIPIVLPVSADDKARLEGCSKFALMYEGRRVALLQDPEFYEHRKEERCSRVWGTATAKHPHIKMVMESGDWLVGGDLQVLERIRWDDGLDQYRLTPLELKQKCKDMNADAVFAFQLRNPVHNGHALLMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLEWRMKQHAAVLEERVLDPKSTIVAIFPSPMLYAGPTEVQWHCRCRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVAAYNKIKKAMDFYDPARHEEFDFISGTRMRKLAREGEDPPDGFMAPKAWKVLTDYYRSLEKTN
|
2.7.1.25; 2.7.7.4
| null |
3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; blood coagulation [GO:0007596]; bone development [GO:0060348]; hormone metabolic process [GO:0042445]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103]
|
cytosol [GO:0005829]
|
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; nucleotidyltransferase activity [GO:0016779]; sulfate adenylyltransferase (ATP) activity [GO:0004781]
|
PF01583;PF01747;PF14306;
|
3.40.50.620;3.40.50.300;3.10.400.10;
|
APS kinase family; Sulfate adenylyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:10559207}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18134; Evidence={ECO:0000305|PubMed:10559207}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25; Evidence={ECO:0000269|PubMed:10559207}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24153; Evidence={ECO:0000305|PubMed:10559207};
| null |
PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000305|PubMed:10559207}.
| null | null |
FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate/PAPS, the activated sulfate donor used by sulfotransferases (PubMed:10559207). In mammals, PAPS is the sole source of sulfate while APS appears to only be an intermediate in the sulfate-activation pathway. May have an important role in skeletogenesis during postnatal growth. {ECO:0000269|PubMed:10559207}.
|
Mus musculus (Mouse)
|
O88436
|
PAX4_RAT
|
MQQDGLSSVNQLGGLFVNGRPLPLDTRQQIVQLAIRGMRPCDISRSLKVSNGCVSKILGRYYRTGVLEPKGIGGSKPRLATPAVVARIAQLKDEYPALFAWEIQRQLCAEGLCTQDKAPSVSSINRVLRALQEDQRLHWTQLRSPAVLAPALPSPHSNCEAPRGPHPGTSHRNRTIFSPGQAEALEKEFQRGQYPDSVVRGKLAAATSLPEDTVRVWFSNRRAKWRRQEKLKWETQMPGASQDLMVPKDSPGIISAQQSPGSVPSAALPVLEQLNPSFCQLCWGAVPDRCSSDTTSQACLQPYWECHSLLPVASSSYMEFAWPCLTTHPVHHLIGGPGQAPSTYYLHWP
| null | null |
circadian rhythm [GO:0007623]; negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of epithelial cell differentiation [GO:0030858]; regulation of cell differentiation [GO:0045595]; regulation of transcription by RNA polymerase II [GO:0006357]; response to cAMP [GO:0051591]; response to xenobiotic stimulus [GO:0009410]; retina development in camera-type eye [GO:0060041]; type B pancreatic cell differentiation [GO:0003309]
|
nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; double-stranded DNA binding [GO:0003690]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;PF00292;
|
1.10.10.60;1.10.10.10;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Plays an important role in the differentiation and development of pancreatic islet beta cells. Transcriptional repressor that competes with PAX6 in binding to a common element in the glucagon, insulin and somatostatin promoters (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88444
|
ADCY1_MOUSE
|
MAGAPRGQGGGGGAGEPGGAERAAGPGGRRGFRACGEEFACPELEALFRGYTLRLEQAATLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCILFLALFVVTNVRSLQVSQLQQVGQLALFFSLTFALLCCPFALGGPARSSAGGAMGSTVAEQGVWQLLLVTFVSYALLPVRSLLAIGFGLVVAASHLLVTAALVPAKRPRLWRTLGANALLFFGVNMYGVFVRILTERSQRKAFLQARNCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGHGHERNTFLRTHNIETFFIVPSHRRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALRTASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQKYHQLQDEYFTSAVVLALILAALFGLIYLLVIPQSVAVLLLLVFSICFLVACTLYLHITRVQCFPGCLTIQIRTALCVFIVVLIYSVAQGCVVGCLPWAWSSQSNSSLVVLAAGGRRTVLPALPCESAHHALLCCLVGTLPLAIFLRVSSLPKMILLSGLTTSYILVLELSGYTKVGGGALSGRSYEPIMAILLFSCTLALHARQVDVRLRLDYLWAAQAEEERDDMERVKLDNKRILFNLLPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEIIADFDELMDKDFYKDLEKIKTIGSTYMAAVGLAPTAGTRAKKSISSHLCTLADFAIDMFDVLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQVTEEVHRLLKRCSYQFVCRGKVSVKGKGEMLTYFLEGRTDGNSSHGRTFRLERRMCPYGRGGGQARRPPLCPAAGPPVRPGLPPAPTSQYLSSTAAGKEA
|
4.6.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P19754}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P19754}; Note=Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro). {ECO:0000250|UniProtKB:P30803};
|
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; axonogenesis [GO:0007409]; cAMP biosynthetic process [GO:0006171]; cAMP-mediated signaling [GO:0019933]; cellular response to calcium ion [GO:0071277]; cellular response to forskolin [GO:1904322]; circadian rhythm [GO:0007623]; long-term memory [GO:0007616]; modulation of chemical synaptic transmission [GO:0050804]; neuroinflammatory response [GO:0150076]; positive regulation of CREB transcription factor activity [GO:0032793]; positive regulation of long-term synaptic potentiation [GO:1900273]; presynaptic modulation of chemical synaptic transmission [GO:0099171]; regulation of circadian rhythm [GO:0042752]; response to xenobiotic stimulus [GO:0009410]
|
cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; Schaffer collateral - CA1 synapse [GO:0098685]
|
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; calcium- and calmodulin-responsive adenylate cyclase activity [GO:0008294]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]
|
PF16214;PF00211;
|
3.30.70.1230;
|
Adenylyl cyclase class-4/guanylyl cyclase family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19754}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9662407}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P19754}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19754}. Cytoplasm {ECO:0000269|PubMed:24482543}. Membrane raft {ECO:0000250|UniProtKB:P19754}. Note=Expressed in the cytoplasm of supporting cells and hair cells of the cochlea vestibule, as well as to the cochlear hair cell nuclei and stereocilia|. {ECO:0000269|PubMed:24482543}.
|
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:9662407};
| null | null | null | null |
FUNCTION: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Mediates responses to increased cellular Ca(2+)/calmodulin levels (PubMed:7816821, PubMed:9662407). May be involved in regulatory processes in the central nervous system (PubMed:9662407). May play a role in memory and learning (PubMed:7816821). Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (PubMed:24048828). {ECO:0000269|PubMed:24048828, ECO:0000269|PubMed:7816821, ECO:0000269|PubMed:9662407}.
|
Mus musculus (Mouse)
|
O88445
|
AURKC_MOUSE
|
MEPSTSTRKHFTINDFEIGRPLGRGKFGRVYLARLKENHFIVALKVLFKSEIEKEGLEHQLRREVEIQAHLQHRNILRLYNYFYDDTRIYLILEYAPGGELYKELQRHQKLDQQRTATIIQELSDALTYCHEKKVIHRDIKPENLLLGLNGEVKISDFGWSVHTPSLRRKTMCGTLDYLPPEMIAQKPYNEMVDLWCIGVLCYELLVGKPPFESSTSSETYRRIRQVDFKFPSSVPAGAQDLISKLLRYHPSERLSLAQVLKHPWVREHSRRVLPC
|
2.7.11.1
| null |
cell division [GO:0051301]; meiotic cell cycle [GO:0051321]; mitotic spindle organization [GO:0007052]; protein phosphorylation [GO:0006468]; regulation of cytokinesis [GO:0032465]
|
chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; meiotic spindle midzone [GO:1990385]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [GO:0031616]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9UQB9}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UQB9}. Note=Distributes in the condensed chromosomes during prophase to metaphase. After entering anaphase, there is a dissociation from separated chromosomes and a redistribution to midzone microtubules, and finally remains in the midbody during cytokinesis (By similarity). {ECO:0000250|UniProtKB:Q9UQB9}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Also plays a role in meiosis and more particularly in spermatogenesis. Has redundant cellular functions with AURKB and can rescue an AURKB knockdown. Like AURKB, AURKC phosphorylates histone H3 at 'Ser-10' and 'Ser-28'. AURKC phosphorylates the CPC complex subunits BIRC5/survivin and INCENP leading to increased AURKC activity. Phosphorylates TACC1, another protein involved in cell division, at 'Ser-228'. {ECO:0000269|PubMed:11879579, ECO:0000269|PubMed:21613325}.
|
Mus musculus (Mouse)
|
O88446
|
S22A3_RAT
|
MPTFDQALRKAGEFGRFQRRVFLLLCLTGVTFAFLFVGVVFLGSQPDYYWCRGPRATALAERCAWSPEEEWNLTTPELHVPAERRGQGHCHRYLLEDTNTSSELSCDPLAAFPNRSAPLVPCSGDWRYVETHSTIVSQFDLVCGNAWMLDLTQAILNLGFLAGAFTLGYAADRYGRLIVYLISCFGVGITGVVVAFAPNFSVFVIFRFLQGVFGKGAWMTCFVIVTEIVGSKQRRIVGIVIQMFFTLGIIILPGIAYFTPSWQGIQLAISLPSFLFLLYYWVVPESPRWLITRKQGEKALQILRRVAKCNGKHLSSNYSEITVTDEEVSNPSCLDLVRTPQMRKCTLILMFAWFTSAVVYQGLVMRLGLIGGNLYMDFFISGLVELPGALLILLTIERLGRRLPFAASNIVAGVSCLVTAFLPEGIPWLRTTVATLGRLGITMAFEIVYLVNSELYPTTLRNFGVSLCSGLCDFGGIIAPFLLFRLAAIWLELPLIIFGILASVCGGLVMLLPETKGIALPETVEDVEKLGSSQLHQCGRKKKTQVSTSNV
| null | null |
dopamine transport [GO:0015872]; dopamine uptake [GO:0090494]; epinephrine transport [GO:0048241]; epinephrine uptake [GO:0051625]; establishment of localization in cell [GO:0051649]; histamine transport [GO:0051608]; histamine uptake [GO:0051615]; monoamine transport [GO:0015844]; monocarboxylic acid transport [GO:0015718]; neurotransmitter transport [GO:0006836]; norepinephrine transport [GO:0015874]; norepinephrine uptake [GO:0051620]; organic anion transport [GO:0015711]; organic cation transport [GO:0015695]; organic hydroxy compound transport [GO:0015850]; quaternary ammonium group transport [GO:0015697]; regulation of appetite [GO:0032098]; serotonin transport [GO:0006837]; serotonin uptake [GO:0051610]; spermidine transport [GO:0015848]; toxin transport [GO:1901998]; xenobiotic transport [GO:0042908]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; endomembrane system [GO:0012505]; mitochondrial membrane [GO:0031966]; neuronal cell body [GO:0043025]; nuclear outer membrane [GO:0005640]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
|
dopamine:sodium symporter activity [GO:0005330]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; spermidine transmembrane transporter activity [GO:0015606]; toxin transmembrane transporter activity [GO:0019534]; transmembrane transporter activity [GO:0022857]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27659446}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:15817714}; Multi-pass membrane protein {ECO:0000305}. Basolateral cell membrane {ECO:0000250|UniProtKB:O75751}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000269|PubMed:27659446}. Endomembrane system {ECO:0000269|PubMed:27659446}. Nucleus membrane {ECO:0000305|PubMed:27659446}. Nucleus outer membrane {ECO:0000305|PubMed:27659446}. Note=Localized to neuronal and glial plasma membranes (PubMed:27659446). Localized to the luminal/apical membrane of ciliated and brush epithelial cells in the airway (PubMed:15817714). Located to neuronal and glial endomembranes, including mitochondrial and nuclear membranes (PubMed:27659446). {ECO:0000269|PubMed:15817714, ECO:0000269|PubMed:27659446}.
|
CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000269|PubMed:16581093}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000269|PubMed:16581093}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000269|PubMed:16581093}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:9830022}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000269|PubMed:16581093}; CATALYTIC ACTIVITY: Reaction=tyramine(in) = tyramine(out); Xref=Rhea:RHEA:74783, ChEBI:CHEBI:327995; Evidence={ECO:0000250|UniProtKB:O75751}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000250|UniProtKB:O75751}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000269|PubMed:12538837}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000305|PubMed:23458604}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000250|UniProtKB:O75751}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000250|UniProtKB:O75751};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=500 uM for serotonin {ECO:0000269|PubMed:16581093}; KM=900 uM for agmatine {ECO:0000269|PubMed:12538837}; KM=1900 uM for noradrenaline {ECO:0000269|PubMed:16581093}; KM=1500 uM for adrenaline {ECO:0000269|PubMed:16581093}; KM=1500 uM for dopamine {ECO:0000269|PubMed:16581093}; KM=5400 uM for histamine {ECO:0000269|PubMed:16581093}; Vmax=8.3 nmol/min/mg enzyme for agmatine uptake {ECO:0000269|PubMed:12538837};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for MPP(+) uptake (PubMed:9830022). Optimum pH is 8.5 for TEA uptake (PubMed:9632645). {ECO:0000269|PubMed:9632645, ECO:0000269|PubMed:9830022};
| null |
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:12538837, PubMed:16581093, PubMed:23458604, PubMed:9830022). Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient (PubMed:9632645, PubMed:9830022). Functions as a Na(+)- and Cl(-)-independent, bidirectional uniporter (PubMed:9830022). Implicated in neuronal monoamine neurotransmitters cellular uptake such as dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, histamine, serotonin and tyramine, thereby supporting a role in homeostatic regulation of aminergic neurotransmission in the brain (PubMed:16581093, PubMed:19416912, PubMed:9830022). Transports dopaminergic neuromodulators cyclo(his-pro) and salsolinol with low efficiency (By similarity). May be involved in the uptake and disposition of cationic compounds by renal clearance from the blood flow (By similarity). May contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (PubMed:17616214). Mediates the transport of polyamine spermidine and putrescine (PubMed:12538837, PubMed:23458604). Mediates the bidirectional transport of polyamine agmatine (PubMed:12538837). Also transports guanidine (PubMed:9632645). May also mediate intracellular transport of organic cations, thereby playing a role in amine metabolism and intracellular signaling (PubMed:27659446). {ECO:0000250|UniProtKB:O75751, ECO:0000269|PubMed:12538837, ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:17616214, ECO:0000269|PubMed:19416912, ECO:0000269|PubMed:23458604, ECO:0000269|PubMed:27659446, ECO:0000269|PubMed:9632645, ECO:0000269|PubMed:9830022}.
|
Rattus norvegicus (Rat)
|
O88447
|
KLC1_MOUSE
|
MYDNMSTMVYIKEEKLENVTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSSMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQNVRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDSDSSKEPLDDLFPNDEDEPGQGIQHSDSSAAAARQGYEIPARLRTLHNLVIQYASQGRYEVAVPSCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGRDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALGIYQTKLGPDRTPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEAEFGSVDDENKPIWMHAEEREECKGKQKDGSAFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPESMEKRRSRESLNMDVVKYESGPDGGEEA
| null | null |
axo-dendritic transport [GO:0008088]; cell adhesion [GO:0007155]; intracellular protein transport [GO:0006886]; microtubule-based movement [GO:0007018]; protein localization to synapse [GO:0035418]; stress granule disassembly [GO:0035617]
|
axon [GO:0030424]; ciliary rootlet [GO:0035253]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; growth cone [GO:0030426]; kinesin complex [GO:0005871]; membrane [GO:0016020]; membrane-bounded organelle [GO:0043227]; microtubule [GO:0005874]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; vesicle [GO:0031982]
|
kinesin binding [GO:0019894]; tubulin binding [GO:0015631]
|
PF13374;PF13424;
|
1.25.40.10;
|
Kinesin light chain family
|
PTM: Phosphorylation at Ser-459 by ERK inhibits interaction with CLSTN1 and localization to cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q07866}.
|
SUBCELLULAR LOCATION: Cell projection, growth cone {ECO:0000250|UniProtKB:P37285}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P37285}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P37285}.
| null | null | null | null | null |
FUNCTION: Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. {ECO:0000250|UniProtKB:P37285}.
|
Mus musculus (Mouse)
|
O88448
|
KLC2_MOUSE
|
MATMVLPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLASHEAGEAEPGSQERCLLLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEMLPQEEKGDVPKDSLDDLFPNEDEQSPAPSPGGGDVAAQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGENKPIWMHAEEREESKDKRRDRRPMEYGSWYKACKVDSPTVNTTLRTLGALYRPEGKLEAAHTLEDCASRSRKQGLDPASQTKVVELLKDGSGRGHRRGSRDVAGPQSESDLEESGPAAEWSGDGSGSLRRSGSFGKLRDALRRSSEMLVRKLQGGGPQEPNSRMKRASSLNFLNKSVEEPVQPGGRVFLTAAL
| null | null |
axo-dendritic transport [GO:0008088]; lysosome localization [GO:0032418]; microtubule-based movement [GO:0007018]
|
ciliary rootlet [GO:0035253]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; kinesin complex [GO:0005871]; lysosomal membrane [GO:0005765]; microtubule [GO:0005874]; neuron projection [GO:0043005]
|
kinesin binding [GO:0019894]
|
PF13374;PF13424;
|
1.25.40.10;
|
Kinesin light chain family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9H0B6}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H0B6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H0B6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H0B6}.
| null | null | null | null | null |
FUNCTION: Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends. {ECO:0000250|UniProtKB:Q9H0B6}.
|
Mus musculus (Mouse)
|
O88450
|
DEAF1_RAT
|
MEDSDSAAKQLGLAEAAAVAAAAAVAAAAAAAAESEAEEPVLSRDEDSEEDADSEAERETRRVTAVAVMAAESGHMDMGTEALPSPDEAAAAAAFAEVTTVTVANVGSSADNVFTTSVANAASISGHVLSGRTALQIGDSLNTEKATLIVVHTDGSIVETTGLKGPAAPLTPGPQSPPTPLAPGQEKGGTKYNWDPSVYDSELPVRCRNISGTLYKSRLGSGGRGRCIKQGENWYSPTEFEAMAGRASSKDWKRSIRYAGRPLQCLIQDGILNPHAASCTCAACCDDMTLSGPVRLFVPYKRRKKENELPTTPVKKDSPKNITLLPATAATTFTVTPSGQITTSGALTFDRASTVEATAVISESPAQGDVFAGATVQEAGVQPPCRVGHPEPHYPGYQDSCQIAPFPEAALPTSHPKIVLTSLPALAVPPSTPTKAVSPTVVSGLEMSEHRSWLYLEEMVNSLLNTAQQLKTLFEQAKQASSCREAAVTQARMQVDAERKEQSCVNCGREAMSECTGCHKVNYCSTFCQRKDWKDHQHVCGQSASVTVQADDVHVEESVIEKVAV
| null | null |
behavioral fear response [GO:0001662]; embryonic skeletal system development [GO:0048706]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural tube closure [GO:0001843]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of mammary gland epithelial cell proliferation [GO:0033599]; regulation of transcription by RNA polymerase II [GO:0006357]; visual learning [GO:0008542]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF01342;PF01753;
|
6.10.140.2220;3.10.390.10;
| null |
PTM: May be phosphorylated by DNA-PK complex in a DNA independent manner (in vitro). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Secreted. Note=Secreted in some cell types.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction. When secreted, behaves as an inhibitor of cell proliferation, by arresting cells in the G0 or G1 phase. Regulates epithelial cell proliferation and side-branching in the mammary gland. Required for neural tube closure and skeletal patterning. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Transcriptional activator of EIF4G3. May also involved in behavior (By similarity). {ECO:0000250|UniProtKB:O75398, ECO:0000250|UniProtKB:Q9Z1T5}.
|
Rattus norvegicus (Rat)
|
O88452
|
STC2_MOUSE
|
MCAERLGQFVTLALVFATLDPAQGTDSTNPPEGPQDRSSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIQGLHGICMTFLHNAGKFDAQGKSFIKDALRCKAHALRHKFGCISRKCPAIREMVFQLQRECYLKHDLCSAAQENVGVIVEMIHFKDLLLHEPYVDLVNLLLTCGEDVKEAVTRSVQAQCEQSWGGLCSILSFCTSNIQRPPTAAPEHQPLADRAQLSRPHHRDTDHHLTANRGAKGERGSKSHPNAHARGRTGGQSAQGPSGSSEWEDEQSEYSDIRR
| null | null |
calcium ion homeostasis [GO:0055074]; cellular response to hypoxia [GO:0071456]; decidualization [GO:0046697]; embryo implantation [GO:0007566]; endoplasmic reticulum unfolded protein response [GO:0030968]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of gene expression [GO:0010629]; negative regulation of multicellular organism growth [GO:0040015]; regulation of hormone biosynthetic process [GO:0046885]; regulation of sodium-dependent phosphate transport [GO:2000118]; regulation of store-operated calcium entry [GO:2001256]; response to endoplasmic reticulum stress [GO:0034976]; response to oxidative stress [GO:0006979]; response to peptide hormone [GO:0043434]; response to vitamin D [GO:0033280]
|
endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]
|
enzyme binding [GO:0019899]; heme binding [GO:0020037]; hormone activity [GO:0005179]; protein homodimerization activity [GO:0042803]
|
PF03298;
| null |
Stanniocalcin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Has an anti-hypocalcemic action on calcium and phosphate homeostasis.
|
Mus musculus (Mouse)
|
O88453
|
SAFB1_RAT
|
MAETLSGLGDSGAASAAAVSSAASETGTRRLSDLRVIDLRAELRKRNLTSSGNKSVLMERLKKAIEEEGGNPDEIEVISEGNKKMPKRPSKGKKPEDEGVEDNGLEENSGDGQEDVETSLENLQDMDMMDISVLDEADIDNGSVADCVEEEEEATLPEGLGLLRIGRLQSKGLPEQLQELAIDDKEAINNVDTSSSDFTILQEMEEASLEPENEKILDILGETCKSEPVKEEGSELEQPFAQATSSVGPDRKLAEEEDLFESCGHPEEEEEEEEEEEQEEEQEEEGDLALASSSKSESSSTRCQWSEADALLAVVKREPAEAPGGGTGMDREPVGLEEPVEQSSTAAQLPETTSQELVRAPTAAPSPEPRDSKDDVKKFAFDACNDVPAAPKESSASEGADQKMSSVEDDSDTKRLSREEKGRSSCGRNFWVSGLSSTTRATDLKNLFSRYGKVVGAKVVTNARSPGARCYGFVTMSTAEEATKCINHLHKTELHGKMISVEKAKSEPAGKRVPDRRDGDSKKEKTSTSDRSANLKREEKGDRKDDAKKTDDGSTEKSKDADDQKPGPSERSRTTKSGSRGTERTVVMDKSKGVPVISVKTSGSKERASKSQDRKSVSREKRSVVSFDKVKESRKSRDSESRRERERERSEREQRLQAQWEREERERLEIARERLAFHRHRLERERMERERLERERMHVEQERRREQERIHREREELRRQQELRYEQERRPAVRRPYEVDGRRDDAYWPEAKRAALDDRYHSDFSRQDRFHDFDHRDRGRYPNHSVDRREGSRSMMGDREGQHYPERHGGPERHGRDSRDGWGYGSNKRLSEGRGLPLLPRRDWGEHARRLEDDRAWQGTADGGMMERDQQRWQGGERSMSGHSGPGHMMNRGGMSGRGSFAPGGASRRHVIPRGGMQAGFGGTEPGQQTQ
| null | null |
hormone metabolic process [GO:0042445]; intracellular estrogen receptor signaling pathway [GO:0030520]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of growth [GO:0040008]; regulation of mRNA processing [GO:0050684]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00076;PF02037;
|
3.30.70.330;1.10.720.30;
| null |
PTM: Phosphorylated by CDC-like kinase 2 (CLK2). {ECO:0000269|PubMed:11118435}.; PTM: Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1. Sumoylation is required for transcriptional repressor activity. {ECO:0000250|UniProtKB:Q15424}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9671816}.
| null | null | null | null | null |
FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing (By similarity). Functions as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription (By similarity). Thereby acts as a negative regulator of cell proliferation (By similarity). When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter (By similarity). {ECO:0000250|UniProtKB:D3YXK2, ECO:0000250|UniProtKB:Q15424}.
|
Rattus norvegicus (Rat)
|
O88454
|
KCNK4_MOUSE
|
MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQAQKKMDHGRDQFLRDHPCVSQKSLEDFIKLLVEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIVLHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAIFLKWHVPPGLVRSLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVVEPAGRPGSPAPAEKVETPSPPTASALDYPSENLAFIDESSDTQSERGCALPRAPRGRRRPNPSKKPSRPRGPGRLRDKAVPV
| null | null |
cellular response to alkaline pH [GO:0071469]; cellular response to fatty acid [GO:0071398]; cellular response to temperature stimulus [GO:0071502]; detection of mechanical stimulus involved in sensory perception of touch [GO:0050976]; potassium ion transmembrane transport [GO:0071805]; sensory perception of pain [GO:0019233]; sensory perception of temperature stimulus [GO:0050951]; stabilization of membrane potential [GO:0030322]
|
plasma membrane [GO:0005886]; potassium channel complex [GO:0034705]
|
mechanosensitived potassium channel activity [GO:0098782]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]; temperature-gated cation channel activity [GO:0097604]
|
PF07885;
|
1.10.287.70;
|
Two pore domain potassium channel (TC 1.A.1.8) family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NYG8}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9628867}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Voltage-insensitive potassium channel (PubMed:9628867). Channel opening is triggered by mechanical forces that deform the membrane. Channel opening is triggered by raising the intracellular pH to basic levels (By similarity). The channel is inactive at 24 degrees Celsius (in vitro); raising the temperature to 37 degrees Celsius increases the frequency of channel opening, with a further increase in channel activity when the temperature is raised to 42 degrees Celsius (By similarity). Plays a role in the sensory perception of pain caused by pressure (PubMed:19279663). Plays a role in the perception of pain caused by heat (PubMed:19279663). {ECO:0000250|UniProtKB:G3V8V5, ECO:0000269|PubMed:19279663, ECO:0000269|PubMed:9628867}.
|
Mus musculus (Mouse)
|
O88455
|
DHCR7_MOUSE
|
MASKSQHNAPKVKSPNGKAGSQGQWGRAWEVDWFSLASIIFLLLFAPFIVYYFIMACDQYSCSLTAPALDIATGHASLADIWAKTPPVTAKAAQLYALWVSFQVLLYSWLPDFCHRFLPGYVGGVQEGAITPAGVVNKYEVNGLQAWLITHILWFVNAYLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMIKGYLFPTSAEDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQQELYGHVTNSMILVNVLQAIYVLDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPNALGILLLGLVGYYIFRMTNHQKDLFRRTDGRCLIWGKKPKAIECSYTSADGLKHHSKLLVSGFWGVARHFNYTGDLMGSLAYCLACGGGHLLPYFYIIYMTILLTHRCLRDEHRCANKYGRDWERYTAAVPYRLLPGIF
|
1.3.1.21
| null |
blood vessel development [GO:0001568]; brassinosteroid biosynthetic process [GO:0016132]; cholesterol biosynthetic process [GO:0006695]; lung development [GO:0030324]; lung epithelial cell differentiation [GO:0060487]; multicellular organism growth [GO:0035264]; post-embryonic development [GO:0009791]; regulation of cell population proliferation [GO:0042127]; regulation of cholesterol biosynthetic process [GO:0045540]; sterol biosynthetic process [GO:0016126]
|
endoplasmic reticulum membrane [GO:0005789]
|
7-dehydrocholesterol reductase activity [GO:0047598]; NADP binding [GO:0050661]
|
PF01222;
|
1.20.120.1630;
|
ERG4/ERG24 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9UBM7}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH; Xref=Rhea:RHEA:23984, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:17759, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.21; Evidence={ECO:0000305|PubMed:11230174}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23986; Evidence={ECO:0000305|PubMed:11230174}; CATALYTIC ACTIVITY: Reaction=7-dehydrodesmosterol + H(+) + NADPH = desmosterol + NADP(+); Xref=Rhea:RHEA:46740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17737, ChEBI:CHEBI:27910, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:11230174}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46741; Evidence={ECO:0000305|PubMed:11230174};
| null |
PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000269|PubMed:11230174}.
| null | null |
FUNCTION: 7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway. {ECO:0000269|PubMed:11230174}.
|
Mus musculus (Mouse)
|
O88457
|
SCNBA_RAT
|
MEERYYPVIFPDERNFRPFTSDSLAAIEKRIAIQKERKKSKDKAAAEPQPRPQLDLKASRKLPKLYGDIPPELVAKPLEDLDPFYKDHKTFMVLNKKRTIYRFSAKRALFILGPFNPLRSLMIRISVHSVFSMFIICTVIINCMFMANSMERSFDNDIPEYVFIGIYILEAVIKILARGFIVDEFSFLRDPWNWLDFIVIGTAIATCFPGSQVNLSALRTFRVFRALKAISVISGLKVIVGALLRSVKKLVDVMVLTLFCLSIFALVGQQLFMGILNQKCIKHNCGPNPASNKDCFEKEKDSEDFIMCGTWLGSRPCPNGSTCDKTTLNPDNNYTKFDNFGWSFLAMFRVMTQDSWERLYRQILRTSGIYFVFFFVVVIFLGSFYLLNLTLAVVTMAYEEQNRNVAAETEAKEKMFQEAQQLLREEKEALVAMGIDRSSLNSLQASSFSPKKRKFFGSKTRKSFFMRGSKTAQASASDSEDDASKNPQLLEQTKRLSQNLPVDLFDEHVDPLHRQRALSAVSILTITMQEQEKFQEPCFPCGKNLASKYLVWDCSPQWLCIKKVLRTIMTDPFTELAITICIIINTVFLAVEHHNMDDNLKTILKIGNWVFTGIFIAEMCLKIIALDPYHYFRHGWNVFDSIVALLSLADVLYNTLSDNNRSFLASLRVLRVFKLAKSWPTLNTLIKIIGHSVGALGNLTVVLTIVVFIFSVVGMRLFGTKFNKTAYATQERPRRRWHMDNFYHSFLVVFRILCGEWIENMWGCMQDMDGSPLCIIVFVLIMVIGKLVVLNLFIALLLNSFSNEEKDGSLEGETRKTKVQLALDRFRRAFSFMLHALQSFCCKKCRRKNSPKPKETTESFAGENKDSILPDARPWKEYDTDMALYTGQAGAPLAPLAEVEDDVEYCGEGGALPTSQHSAGVQAGDLPPETKQLTSPDDQGVEMEVFSEEDLHLSIQSPRKKSDAVSMLSECSTIDLNDIFRNLQKTVSPKKQPDRCFPKGLSCHFLCHKTDKRKSPWVLWWNIRKTCYQIVKHSWFESFIIFVILLSSGALIFEDVNLPSRPQVEKLLRCTDNIFTFIFLLEMILKWVAFGFRRYFTSAWCWLDFLIVVVSVLSLMNLPSLKSFRTLRALRPLRALSQFEGMKVVVYALISAIPAILNVLLVCLIFWLVFCILGVNLFSGKFGRCINGTDINMYLDFTEVPNRSQCNISNYSWKVPQVNFDNVGNAYLALLQVATYKGWLEIMNAAVDSREKDEQPDFEANLYAYLYFVVFIIFGSFFTLNLFIGVIIDNFNQQQKKLGGQDIFMTEEQKKYYNAMKKLGTKKPQKPIPRPLNKCQAFVFDLVTSQVFDVIILGLIVLNMIIMMAESADQPKDVKKTFDILNIAFVVIFTIECLIKVFALRQHYFTNGWNLFDCVVVVLSIISTLVSRLEDSDISFPPTLFRVVRLARIGRILRLVRAARGIRTLLFALMMSLPSLFNIGLLLFLVMFIYAIFGMSWFSKVKKGSGIDDIFNFETFTGSMLCLFQITTSAGWDTLLNPMLEAKEHCNSSSQDSCQQPQIAVVYFVSYIIISFLIVVNMYIAVILENFNTATEESEDPLGEDDFEIFYEVWEKFDPEASQFIQYSALSDFADALPEPLRVAKPNKFQFLVMDLPMVMGDRLHCMDVLFAFTTRVLGDSSGLDTMKTMMEEKFMEANPFKKLYEPIVTTTKRKEEEQGAAVIQRAYRKHMEKMVKLRLKDRSSSSHQVFCNGDLSSLDVAKVKVHND
| null | null |
action potential [GO:0001508]; action potential initiation [GO:0099610]; acute inflammatory response [GO:0002526]; artery development [GO:0060840]; axonogenesis [GO:0007409]; behavioral response to acetic acid induced pain [GO:0061367]; behavioral response to formalin induced pain [GO:0061368]; behavioral response to pain [GO:0048266]; calcitonin gene-related peptide receptor signaling pathway [GO:1990408]; calcium ion transmembrane transport [GO:0070588]; cell motility [GO:0048870]; cellular response to cold [GO:0070417]; chemosensory behavior [GO:0007635]; chronic inflammatory response [GO:0002544]; circadian rhythm [GO:0007623]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; establishment of localization in cell [GO:0051649]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; mast cell degranulation [GO:0043303]; membrane depolarization during action potential [GO:0086010]; micturition [GO:0060073]; neuronal action potential [GO:0019228]; optic nerve development [GO:0021554]; protein kinase A signaling [GO:0010737]; reflex [GO:0060004]; regulation of membrane potential [GO:0042391]; response to auditory stimulus [GO:0010996]; response to cold [GO:0009409]; response to heat [GO:0009408]; response to high light intensity [GO:0009644]; response to nitric oxide [GO:0071731]; response to pain [GO:0048265]; response to prostaglandin E [GO:0034695]; response to toxic substance [GO:0009636]; response to xenobiotic stimulus [GO:0009410]; sensory perception of itch [GO:0160025]; sensory perception of pain [GO:0019233]; skeletal muscle organ development [GO:0060538]; small intestine smooth muscle contraction [GO:1990770]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]; thermosensory behavior [GO:0040040]; thigmotaxis [GO:0001966]; transmission of nerve impulse [GO:0019226]
|
axon [GO:0030424]; axonal growth cone [GO:0044295]; C-fiber [GO:0044299]; cell body [GO:0044297]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; voltage-gated sodium channel complex [GO:0001518]
|
voltage-gated sodium channel activity [GO:0005248]
|
PF00520;PF06512;
|
1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350;
|
Sodium channel (TC 1.A.1.10) family, Nav1.9/SCN11A subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10196578}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10196578};
| null | null | null | null |
FUNCTION: Sodium channel mediating the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient (PubMed:10196578). Involved in membrane depolarization during action potential in nociceptors which function as key relay stations for the electrical transmission of pain signals from the periphery to the central nervous system. Also involved in rapid BDNF-evoked neuronal depolarization (By similarity). {ECO:0000250|UniProtKB:Q9UI33, ECO:0000269|PubMed:10196578}.
|
Rattus norvegicus (Rat)
|
O88466
|
ZN106_MOUSE
|
MVRERKCILCHIVYGSKKEMDEHMRSMLHHRELENLKGRDISHECRVCRVTEVGLSAYAKHISGQLHKDNVDAQEREDDGKEEEEEEYFDKELVQLIQERKEQSRQDEPPSNSQEVNSDDRQPQWRREDRIPYQDRESYSQPPRHHRGPPQRDWKWEKDGFNSTRKNSFPHSLRNSGGPRGSSVWHKGATRGSSTWFLNHSNSGGGWHSNNGMVDWNYNGTGRNSSWHSEGTGGFPSWHMNNSNGNWKSSVRGTNSWNYNGLGDKFQQGRNRNPNYQMEDMTKMWNKKSNKPSKYSQERCKWQRQDRDKAAKYRSPPEGYASDTFPSEGLLEFNFEQRESQTTKQTDTAASKINGKNGTKARDKFRRWTPYPSQKTLDLQSALKEVIGSKSDTLEKPLFNFSLITAGLRKPVDKTSNPPVIKTQKAGPPGSPSHKAISDGTAFCEVARACSITEQSEPHQKSNKIPLLKSPLLPLPTPKSGPHKQNLKNRSKNKETKSFPSGDHSHLLNTSTLEGSHGSSYTSKSLGLCPRVLKENKTVSGTQKEPDEKLNNTSQKAQDTVLQCPKTLQNPLPTTPKRMENDAKESSVEESAKDSLSIESQPHSAGNSAMTSDAENHGIKSEGVASLTTEVVSCSTHTVDKEQGSQIPGTPENLSTSPRNSTVLQKEAEVQVSAATSPHSGLLLDLKTSLEDAQDNNLVKSDGPFETESFEDTSLDTELQKPDLNNQPPGTLLPELSKLGFPASLQRDLSRHISLKSKTGTHLPEPNLNSARRIRNVSGHRKNETEKESGLKPTLRQILNASRRNVNWEQVIQQVTKKKQELGKGLPRFGIEMVPLVQNEQEVLDLDEEPDLSSLEGFQWEGVSIPSSSGLARKRSLSESSVVMDRAPVYSFFTGEGTGKENEAQQSPSPNTALSAAQSQKTAMYLEQEVAPLTPSVGTGERVGNIPTQRRHSAQLPSGHIMPVMHSARDLHSQERSTPLSERHAQESTGEGNSLSSNASSGHAVSSLADAATDSSCTSGAEQTDGHSIRKKRRATGDGSSPELPSLERKNKRRKIKGKKERSQVDQLLTISLREEELSKSLQCMDNKLLQARAALQTAYVEVQRLLVLKQQITVEMSALRTHRIQILQGLQETYEPPEHPDQAPCSLISREQRNSRSQTSFETALLPAPFFPGFLDPPPSHASLPSPGNPLQITMSTFQAHGTAPDSSVQIKQEPMSPEQEGNMNALPQGCASNVSKELLQTNRVVDDGSSVYPAIPAVIASESTENCQEVSKDLNFSVEQGNSRSKGNSPSCQSPDLPGINRGEETAKGSSGSEACSSSFLRLSFTPETPAEKETQSPADQPEQQAESTLASAETRGSKKKKKLRKKKTLRATHVPENSDTEQDVFTAKPARKVKTAKAAKGAKVTTSQTGQEQGTARDEPDSDSSLEVLEVTNPQLEVVAIDTSESGDEKPDSPSKKDAWIAAEQNPIETSRSGCDEVSSTSELGTRYKDGVPVSVAETQTVISIKASKHSSEISSEPGDDEEPTEGSFEGHQAAVNAIQIFGNFLYTCSADTTVRVYNLVSRKCVGVFEGHTSKVNCLLVTHTSGKSSVLYTGSSDHTIRCYNIKTRECMEQLQLEDRVLCLHNRWRTLYAGLANGTVVTFDIKNNKRQEIFECHGPRAVSCLATAQEGARKLLVVGSYDCTISVRDARNGLLLRTLEGHSKTVLCMKVVNDLVFSGSSDQSVHAHNIHTGELVRIYKGHNHAVTVVNILGKVMVTACLDKFVRVYELQSHDRLQVYGGHKDMIMCMTIHKSVIYTGCYDGSIQAVRLNLMQNYRCWWYGCTLIFGVVDHLKQHLLTDHTNPNFQTLKCRWRNCDAFFTARKGSKQDVAGHIERHAEDDSKIDS
| null | null |
insulin receptor signaling pathway [GO:0008286]
|
cytosol [GO:0005829]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]
|
metal ion binding [GO:0046872]; opioid peptide activity [GO:0001515]; RNA binding [GO:0003723]; SH3 domain binding [GO:0017124]
|
PF00400;
|
2.130.10.10;
| null |
PTM: Phosphorylated by FYN in vitro. {ECO:0000269|PubMed:9507006}.
|
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15833274, ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389, ECO:0000269|PubMed:9507006}. Nucleus speckle {ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389}. Note=Colocalizes with RBM39 in nuclear speckles. Inhibition of RNA synthesis, or overexpression of KNOP1, induces translocation from nuclear speckles to the nucleolus. {ECO:0000269|PubMed:27418600}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein (PubMed:27418600, PubMed:28072389). Specifically binds to 5'-GGGGCC-3' sequence repeats in RNA (PubMed:28072389). Essential for maintenance of peripheral motor neuron and skeletal muscle function (PubMed:26604141, PubMed:27418600, PubMed:28072389). Required for normal expression and/or alternative splicing of a number of genes in spinal cord and skeletal muscle, including the neurite outgrowth inhibitor RTN4 (PubMed:26604141, PubMed:27418600). Also contributes to normal mitochondrial respiratory function in motor neurons, via an unknown mechanism (PubMed:26604141). {ECO:0000269|PubMed:26604141, ECO:0000269|PubMed:27418600, ECO:0000269|PubMed:28072389}.
|
Mus musculus (Mouse)
|
O88470
|
FOXL2_MOUSE
|
MMASYPEPEDTAGTLLAPESGRAVKEAEASPPSPGKGGGTTPEKPDPAQKPPYSYVALIAMAIRESAEKRLTLSGIYQYIIAKFPFYEKNKKGWQNSIRHNLSLNECFIKVPREGGGERKGNYWTLDPACEDMFEKGNYRRRRRMKRPFRPPPAHFQPGKGLFGSGGAAGGCGVPGAGADGYGYLAPPKYLQSGFLNNSWPLPQPPSPMPYASCQMAAAAAAAAAAAAAAGPGSPGAAAVVKGLAGPAASYGPYSRVQSMALPPGVVNSYNGLGGPPAAPPPPPPPPHPHPHPHAHHLHAAAAPPPAPPHHGAAAPPPGQLSPASPATAAPPAPAPTSAPGLQFACARQPELAMMHCSYWDHDSKTGALHSRLDL
| null | null |
anatomical structure morphogenesis [GO:0009653]; apoptotic DNA fragmentation [GO:0006309]; cell differentiation [GO:0030154]; embryonic eye morphogenesis [GO:0048048]; extraocular skeletal muscle development [GO:0002074]; female gonad development [GO:0008585]; female somatic sex determination [GO:0019101]; granulosa cell differentiation [GO:0060014]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of transcription by RNA polymerase II [GO:0000122]; ovarian follicle development [GO:0001541]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of follicle-stimulating hormone secretion [GO:0046881]; positive regulation of luteinizing hormone secretion [GO:0033686]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to human chorionic gonadotropin [GO:0044752]; response to organic cyclic compound [GO:0014070]; single fertilization [GO:0007338]; uterus development [GO:0060065]
|
Flemming body [GO:0090543]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
cysteine-type endopeptidase regulator activity involved in apoptotic process [GO:0043028]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear estrogen receptor binding [GO:0030331]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; ubiquitin conjugating enzyme binding [GO:0031624]
|
PF00250;
|
1.10.10.10;
| null |
PTM: Sumoylated with SUMO1; sumoylation is required for transcriptional repression activity. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089, ECO:0000269|PubMed:19797124}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator. Critical factor essential for ovary differentiation and maintenance, and repression of the genetic program for somatic testis determination. Prevents trans-differentiation of ovary to testis through transcriptional repression of the Sertoli cell-promoting gene SOX9. Has apoptotic activity in ovarian cells. Suppresses ESR1-mediated transcription of PTGS2/COX2 stimulated by tamoxifen. Activates SIRT1 transcription under cellular stress conditions. Activates transcription of OSR2. Is a regulator of CYP19 expression. Is a transcriptional repressor of STAR. Participates in SMAD3-dependent transcription of FST via the intronic SMAD-binding element. {ECO:0000269|PubMed:15059956, ECO:0000269|PubMed:15944199, ECO:0000269|PubMed:19106105, ECO:0000269|PubMed:19797124, ECO:0000269|PubMed:20005806}.
|
Mus musculus (Mouse)
|
O88477
|
IF2B1_MOUSE
|
MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQITQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQPVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNLAQARRK
| null | null |
CRD-mediated mRNA stabilization [GO:0070934]; dendrite arborization [GO:0140059]; mRNA transport [GO:0051028]; negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900152]; negative regulation of translation [GO:0017148]; nervous system development [GO:0007399]; neuronal stem cell population maintenance [GO:0097150]; pallium cell proliferation in forebrain [GO:0022013]; positive regulation of cytoplasmic translation [GO:2000767]; regulation of gene expression [GO:0010468]; regulation of mRNA stability involved in response to stress [GO:0010610]; RNA localization [GO:0006403]
|
axon [GO:0030424]; CRD-mediated mRNA stability complex [GO:0070937]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932]; perinuclear region of cytoplasm [GO:0048471]; ribonucleoprotein complex [GO:1990904]
|
mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; translation regulator activity [GO:0045182]
|
PF00013;PF00076;
|
3.30.310.210;3.30.70.330;3.30.1370.10;
|
RRM IMP/VICKZ family
|
PTM: Phosphorylated. Phosphorylation may impair association with ACTB mRNA and hence abolishes translational repression (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9NZI8}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9NZI8}. Cell projection, lamellipodium {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, growth cone {ECO:0000250}. Cell projection, filopodium {ECO:0000250}. Cell projection, axon {ECO:0000250}. Note=In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription (By similarity). In the cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with microtubules in growth cone filopodia and along neurites in neuronal cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript (By similarity). In hippocampal neurons, predominantly located within dendrites, particularly at dendritic branching points in young cells, compared to axons (By similarity). In axons, predominantly found in axonal branches and their growth cones (By similarity). In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited (By similarity). Dendritic levels are regulated by neuronal activity and glutaminergic signals: they are increased by KCl-induced depolarization, which induces rapid efflux from the cell body into dendrites, and decreased by NMDA receptor agonists (By similarity). In motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails (By similarity). In motile cells, transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments (By similarity). In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules, but not to processing bodies (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells (By similarity). Binds to the oncofetal H19 transcript and regulates its localization (By similarity). Binds to and stabilizes BTRC/FBW1A mRNA (By similarity). Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2 (By similarity). During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts (By similarity). Interacts with GAP43 transcript and transports it to axons. Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binding to MYC mRNA is enhanced by m6A-modification of the CRD (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA. Binds to the neuron-specific TAU mRNA and regulates its localization. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons. During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing. {ECO:0000250, ECO:0000250|UniProtKB:Q9NZI8, ECO:0000269|PubMed:15355996, ECO:0000269|PubMed:17264115, ECO:0000269|PubMed:21964071, ECO:0000269|PubMed:22465430}.
|
Mus musculus (Mouse)
|
O88480
|
CABIN_RAT
|
MIRIAALNASSTIEDDHEGSFKSHKIQTKEAQEAEAFALYHKALDLQKHDRFEESAKAYHELLEARLLREAVSSGDEKEGLKHPGLILKYSTYKNLAQLAAQREDLETAMEFYLEAVMLDSTDVNLWYKIGHVALRLIRLPLARHAFEEGLRCNPDHWPCLDNLITVLYTLSDYTTCLYFICKALEKDCRYSKGLVLKEKIFEEQPCLRKDSLRMFLKCDMSVHEVSVNAAETQAIVDEALGLRKKRQALIVREKEPDLKLVQPIPFFTWKCLGESLLAMYNHLTTCEPPRPSLGKRIDLSDYQDPSQLLAPSIVVTPVSVVQPSPVCTNPTVAVAEPVLSYTSVTTTSFPLHSPGLLDTGTPMGDVSGGDKSKKGVKRKKTLEESGETAKRRSARVRNTKCKKEEKVDFQGLLVKFLPSRLRKLDPEEEDDPFNNYEVQSEAKLESFSNVGPHRLSFDSATFMESEKQDVHAFLMENLTNGGVLELMMRYLKSMGHKFLLKWPPGLAEVVLSVYHSWRRHSTSLPNPLLRDCSNKHIKDMMLMSLSCMELQLDQWLLTKGRSSTVSPRNCPAGVVTGRFGPDFPGTHCLGDLLQLSFASSQRDLFEDGWLEFVVRVYWLKARFLALQGDMEQALENYDICTEILQSSTALQAQAGAEQRDIVIRLPNLHNDSIVSLEEIDKNLKSLERCQSLEEIQRLFEAGDYKAVVQLLRPTLCTSGFDRAKHLEFMTSIPERPAQLLLLQDSLLRLEEHRQCFECSDVALNEAVQQMLNSSDSAAKEEWAATVTQLLLGMEQALSSDSRGSILKESSSPTGLVRLTNNLIQVIDCSMAVQEEPKEPYVSSVLPWIILHRIIWQEEDTFRSLCHQQQLQNPTEEGISEMPMLPSSLMLLNTAHEYLGRRSWCCNSDGALLRFYVHVLQKELAASASEDTHPYKEELETALEQCFYCLYSFPSKKSKARYLEEHSAQQVDLTWEDALFMFEYFKPKTLPEFDSYKTSTVSADLANLLKRIATIVPRTEKPALSMDKVSAYIEGTSAEVPCLPDGADPAPPVLNELYYLLADYHFKNKEQSKAIKFYMHDICICPNRFDSWAGMALARASRIQDKLNSNELKSDGPIWRHATPVLNCFRRALEIDSSNLSLWIEYGTMSYALHSFASRQLKQWRAELPPEVVQQMEDRRDSMLETARHCFTSAAHCEGDGDEEEWLIHYMLGKVAEKQQQPPTVYLLHYRQAGHYLHEEAARYPKKIHYHNPPELAMEALEVYFRLHASILKLLGKPDSGVSAEVLVSFMKEAAEGPFARGEEKNTPKASEKEKACLVDEDSHSSAGTLPGPGASLPSSSGPGLTSPPYTATPIDHDYVKCKKPRQQATPDDRSQDSTAVALSDSSSTQDFFNEPTSLLDGSRKLLPEKRISGLSAQAGPSGKDLPGPTEERGKTEESLESTEAFRVVEPSVQKPVADSSASAYIPSKPAVSTPPPWDGKKRSDPLGEPVAFPQGLPAGAEEQRQFLTEQCIASFCLCLSRFPQHYKSLYRLAFLYTYSKTHRNLQWARDVLLGSSIPWQQLQHMPAQGLFCERNKTNFFNGIWRIPVDEIDRPGSFAWHMNRSIVLLLKVLAQLRDHSTLLKVSSMLQRTPDQGKKYLRDADRQVLAQRAFILTVKVLEDTLSELAEGLEHPGSKACGLSGARMTTDVSHKASPEDGQESLPHPKKLPLADGSGPGPEPGGKVGPLHQLPVATDTRDNTEQGGEPKDKERPPVGPTEPMDTGETAARHPDLEPTPRLLPGRPPRDRGPESRSAELSLEELSISTRQQPAPLVPSPVTPTTAAPTTMGARAAGHPEEAPPRPNRKRKLLQDTESGKTLLLDAYRVWQQGQKAMAYDLSRIEKIMSETYMLIKQVDEETALEQAVKFCQVHLGAAAQRQASGDAPTTPKHPKDSRENFFPATVAPSAPDTTAPDALQRPSDSHLKPGLAAAITCPPSASASTPDPGIPQPHRPEAVPSRAPLSPDGEEVSGVTEGPSFLSQEPRHSHQMKMAATGPLAEQHCWPVEAACQTGAEPTFSQATSTKVPSSGSTQTPESHQGKTESSRAKSRLLPNMPKLVIPSATTKFPPEITVTPPTPTLLSPKGSISEETKQKLKSAILSAQSAANVRKESLCQPALEVLETSSQESSLESETDEDDDFMDV
| null | null |
negative regulation of apoptotic process [GO:0043066]; nucleosome assembly [GO:0006334]; response to activity [GO:0014823]
|
cytoplasm [GO:0005737]; HIR complex [GO:0000417]; nucleus [GO:0005634]
|
nucleosome binding [GO:0031491]; protein domain specific binding [GO:0019904]; protein phosphatase 2B binding [GO:0030346]; protein phosphatase inhibitor activity [GO:0004864]
|
PF09047;
|
1.25.40.10;
| null |
PTM: Activated through PKC-mediated hyperphosphorylation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:9660798}.
| null | null | null | null | null |
FUNCTION: May be required for replication-independent chromatin assembly (By similarity). May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. {ECO:0000250, ECO:0000269|PubMed:9660798}.
|
Rattus norvegicus (Rat)
|
O88483
|
PDP1_RAT
|
MPAPTQLFFPLVRNCELSRIYGTACYCHHKHLCCSPPYIPQNRLRYTPHPAYATFCRPRENWWQYTQGRRYASTPQKFYLTPPQVNSILKANEYSFKVPEFDGKNVSSILGFDSNQLPANAPIEDRRSAATCLQTRGMLLGVFDGHAGCACSQAVSERLFYYIAVSLLPHETLLEIENAVESGRALLPILQWHKHPNDYFSKEASKLYFNSLRTYWQELIDLNTGESADIDVKEALINAFKRLDNDISLEAQVGDPNSFLNYLVLRVAFSGATACVAHVDGVDLHVANTGDSRAMLGVQEEDGSWSAVTLSNDHNAQNERELERLKLEHPKNEAKSVVKQDRLLGLLMPFRAFGDVKFKWSIDLQKRVIESGPDQLNDNEYTKFIPPNYHTPPYLTAEPEVTYHRLRPQDKFLVLATDGLWETMHRQDVVRIVGEYLTGMHHQQPIAVGGYKVTLGQMHGLLTERRAKMSSVFEDQNAATHLIRHAVGNNEFGAVDHERLSKMLSLPEELARMYRDDITIIVVQFNSHVVGAYQNQEQ
|
3.1.3.43
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P35816}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17532339, ECO:0000269|PubMed:9651365}; Note=Binds 2 Mn(2+) ions per subunit (By similarity). Binds 2 Mg(2+) ions per subunit (PubMed:17532339). Mn(2+) can substitute Mg2(+) for catalytic activity (By similarity). {ECO:0000250|UniProtKB:P35816, ECO:0000269|PubMed:17532339};
| null |
mitochondrion [GO:0005739]
|
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity [GO:0004741]; [pyruvate dehydrogenase (lipoamide)] phosphatase regulator activity [GO:0019909]; calcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; protein serine/threonine phosphatase activity [GO:0004722]; protein-containing complex binding [GO:0044877]
|
PF00481;
|
3.60.40.10;
|
PP2C family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9651365}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] + phosphate; Xref=Rhea:RHEA:12669, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.43; Evidence={ECO:0000269|PubMed:15210124, ECO:0000269|PubMed:9651365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12670; Evidence={ECO:0000305|PubMed:9651365};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for Mg(2+) (in absence of Ca(2+)) {ECO:0000269|PubMed:9651365}; KM=0.7 mM for Mg(2+) (in presence of Ca(2+)) {ECO:0000269|PubMed:9651365};
| null | null | null |
FUNCTION: Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA. {ECO:0000269|PubMed:15210124, ECO:0000269|PubMed:9651365}.
|
Rattus norvegicus (Rat)
|
O88484
|
PDP2_RAT
|
MSSTASYRIFNFARNRIAVLRGGRRLYSRAATSRNQVKWRLFSPASLAVNDSSPHGGFALRKAYRHTSTEEEDFHLQLSPEQVSDLLRAGESSHKVLDFNSGVPNSVLRFESNQLAANSPVEDRQGVASCVQTRGTMFGIFDGHGGHACAQAVSERLFYYMAVSLMSHKTLEQMEEAMENMKPLLPILQWLKHPGDSIYKDITSVHLDHLRVYWQELLDLHMETGLSTEEALMYSFQRLDSDISLEIQAPLEDEVTKNLSLQVAFSGATACMAHVDGVHLHIANAGDCRAILGVQGDNGAWSCLPLTCDHNAWNEAELSRLKREHPESEDRTLIIDDRLLGVLLPCRAFGDVQLKWSKELQRNVLERGFDTEALNIYQFTPPHYHTPPYLTAKPEVTYHRLRPQDKFLVLASDGLWDMLDNEDVVRLVVGHLSKVGHQKPALDQRPANLGHMQSLLLQRKASGLHAADQNAATHLIRHAIGSNEYGEMEPERLAAMLTLPEDVARMYRDDITVMVVFFNSESIDTYFKEG
|
3.1.3.43
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9651365}; Note=Binds 2 magnesium ions per subunit. {ECO:0000250|UniProtKB:P35816};
|
peptidyl-threonine dephosphorylation [GO:0035970]; response to starvation [GO:0042594]; T-helper cell differentiation [GO:0042093]
|
mitochondrion [GO:0005739]
|
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase activity [GO:0004741]; [pyruvate dehydrogenase (lipoamide)] phosphatase regulator activity [GO:0019909]; metal ion binding [GO:0046872]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF00481;
|
3.60.40.10;
|
PP2C family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:9651365}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = L-seryl-[pyruvate dehydrogenase E1 alpha subunit] + phosphate; Xref=Rhea:RHEA:12669, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.43; Evidence={ECO:0000269|PubMed:14644048, ECO:0000269|PubMed:9651365}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12670; Evidence={ECO:0000305|PubMed:9651365};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=17.4 mM for Mg(2+) {ECO:0000269|PubMed:9651365};
| null | null | null |
FUNCTION: Mitochondrial enzyme that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex (PDC), thereby stimulating the conversion of pyruvate into acetyl-CoA (PubMed:14644048, PubMed:9651365). Acts as a crucial regulator of T cell metabolism and function, with a particular focus on T-helper Th17 (By similarity). {ECO:0000250|UniProtKB:Q504M2, ECO:0000269|PubMed:14644048, ECO:0000269|PubMed:9651365}.
|
Rattus norvegicus (Rat)
|
O88485
|
DC1I1_MOUSE
|
MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKEADMQQKKEPVQDDSDLDRKRRETEALLQSIGISPEPPLVPTPMSPSSKSVSTPSDAGSQDSGDLGPLTRTLQWDTDPSVLQLQSDSELGRRLHKLGVSKVTQVDFLPREVVSYSKETQTPLATHQSEEDEEDEEMVEPKIGHDSELENQEKKQETKEAPPRELTEEEKQQILHSEEFLIFFDRTIRVIERALAEDSDIFFDYSGRELEEKDGDVQAGANLSFNRQFYDEHWSKHRVVTCMDWSLQYPELMVASYSNNEDAPHEPDGVALVWNMKFKKTTPEYVFHCQSSVMSVCFARFHPNLVVGGTYSGQIVLWDNRSHRRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLITVSTDGKMCSWSLDMLSTPQESMELVYNKSKPVAVTGMAFPTGDVNNFVVGSEEGTVYTACRHGSKAGIGEVFEGHQGPVTGINCHMAVGPIDFSHLFVTSSFDWTVKLWTTKHNKPLYSFEDNADYVYDVMWSPVHPALFACVDGMGRLDLWNLNSDTEVPTASVAIEGASALNRVRWAQGGKEVAVGDSEGRIWIYDVGELAVPHNDEWTRFARTLVEIRANRADSEEEGAVELAA
| null | null |
transport along microtubule [GO:0010970]; vesicle transport along microtubule [GO:0047496]
|
axon cytoplasm [GO:1904115]; cytoplasmic dynein complex [GO:0005868]; kinetochore [GO:0000776]; microtubule [GO:0005874]; perinuclear region of cytoplasm [GO:0048471]; spindle pole [GO:0000922]; vesicle [GO:0031982]
|
dynein heavy chain binding [GO:0045504]; dynein light chain binding [GO:0045503]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; spectrin binding [GO:0030507]
|
PF11540;PF00400;
|
2.130.10.10;
|
Dynein intermediate chain family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores.
|
Mus musculus (Mouse)
|
O88487
|
DC1I2_MOUSE
|
MSDKSDLKAELERKKQRLAQIREEKKRKEEERKKKETDQKKEAAVSVQEESDLEKKRREAEALLQSMGLTTDSPIVPPPMSPSSKSVSTPSEAGSQDSGDGAVGSRRGPIKLGMAKITQVDFPPREIVTYTKETQTPVTAQPKEDEEEEDDVATPKPPVEPEEEKTLKKDEENDSKAPPHELTEEEKQQILHSEEFLSFFDHSTRIVERALSEQINIFFDYSGRDLEDKEGEIQAGAKLSLNRQFFDERWSKHRVVSCLDWSSQYPELLVASYNNNEEAPHEPDGVALVWNMKYKKTTPEYVFHCQSAVMSATFAKFHPNLVVGGTYSGQIVLWDNRSNKRTPVQRTPLSAAAHTHPVYCVNVVGTQNAHNLISISTDGKICSWSLDMLSHPQDSMELVHKQSKAVAVTSMSFPVGDVNNFVVGSEEGSVYTACRHGSKAGISEMFEGHQGPITGIHCHAAVGAVDFSHLFVTSSFDWTVKLWTTKNNKPLYSFEDNSDYVYDVMWSPTHPALFACVDGMGRLDLWNLNNDTEVPTASISVEGNPALNRVRWTHSGREIAVGDSEGQIVIYDVGEQIAVPRNDEWARFGRTLAEINANRADAEEEAATRIPA
| null | null |
negative regulation of neuron projection development [GO:0010977]; transport along microtubule [GO:0010970]
|
cytoplasmic dynein complex [GO:0005868]; dynein complex [GO:0030286]; microtubule [GO:0005874]; outer dynein arm [GO:0036157]; vesicle [GO:0031982]
|
dynein heavy chain binding [GO:0045504]; dynein light chain binding [GO:0045503]; protein-containing complex binding [GO:0044877]
|
PF11540;PF00400;
|
2.130.10.10;
|
Dynein intermediate chain family
|
PTM: The phosphorylation status of Ser-84 appears to be involved in dynactin-dependent target binding. {ECO:0000250|UniProtKB:Q62871}.; PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-IP7) promotes interaction with DCTN1 (PubMed:27474409). Serine pyrophosphorylation is achieved by Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated serine residue (PubMed:27474409). {ECO:0000269|PubMed:27474409}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:28619825}. Cytoplasm {ECO:0000269|PubMed:28619825}. Note=Detected in the cytoplasm of pachytene spermatocytes. Localizes to the manchette in elongating spermatids. {ECO:0000269|PubMed:28619825}.
| null | null | null | null | null |
FUNCTION: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function (By similarity). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCTN1 (PubMed:27474409). Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes (PubMed:27474409). {ECO:0000250|UniProtKB:Q62871, ECO:0000269|PubMed:27474409}.
|
Mus musculus (Mouse)
|
O88488
|
PTPRQ_RAT
|
MMDFHFSFLFLLIGTSESQVDVSSSFDGTGYDITLSSVSATTYSSPVSRTLATNVTKPGPPVFLAGERVGSAGILLSWNTPPNPNGRIISYVVKYKEVCPWMQTAYTRARAKPDSLEVLLTNLNPGTTYEIKVAAENNAGIGVFSDPFLFQTAESAPGKVVNLTVEALNYSAVNLIWYLPRQPNGKITSFKISVKHARSGIVVKDVSLRVEDILSGKLPECNENSESFLWSTTSPSPTLGRVTPTVRTTQSSSTAARSKISSVWKEPISFVVTHLRPYTTYLFEVSAVTTEAGYIDSTIVRTPESVPEGPPQNCIMGNVTGKAFSISWDPPTIVTGKFSYRVELYGPSGRILDNSTKDLRFAFTHLTPFTMYDVYVAAETSAGVGPKSNLSVFTPPDVPGAVFDLQIAEVEATEIRITWRKPRQPNGIISQYRVKVSVLETGVVLENTLLTGQDESISNPMSPEIMNLVDPMIGFYEGSGEMSSDLHSPASFIYNSHPHNDFPASTRAEEQSSPVVTTRNQYMTDITAEQLSYVVRRLVPFTEHTISVSAFTIMGEGPPTVLTVRTREQVPSSIQIINYKNISSSSILLYWDPPEYPNGKITHYTIYATELDTNRAFQMTTVDNSFLITGLKKYTRYKMRVAASTHVGESSLSEENDIFVRTPEDEPESSPQDVQVTGVSPSELRLKWSPPEKPNGIIIAYEVLYQNADTLFVKNTSTTDIIISDLKPYTLYNISIRSYTRLGHGNQSSSLLSVRTSETVPDSAPENITYKNISSGEIEISFLPPRSPNGIIQKYTIYLKRSNSHEARTINTTSLTQTIGGLKKYTHYVIEVSASTLKGEGIRSRPISILTEEDAPDSPPQNFSVKQLSGVTVMLSWQPPLEPNGIILYYTVYVWDKSSLRAINATEASLVLSDLDYNVDYGACVTASTRFGDGNARSSIINFRTPEGEPSDPPNDVHYVNLSSSSIILFWTPPVKPNGIIQYYSVYYQNTSGTFVQNFTLLQVTKESDNVTVSARIYRLAIFSYYTFWLTASTSVGNGNKSSDIIHVYTDQDIPEGPVGNLTFESISSTAIHVSWEPPSQPNGLVFYYLSLNLQQSPPRHMIPPLVTYENSIDFDDLEKYTDYIFKITPSTEKGFSETYTTQLHIKTEEDVPDTPPIINTFKNLSSTSILLSWDPPLKPNGAILGYHLTLQGPHANHTFVTSGNHIVLEELSPFTLYSFFAAARTMKGLGPSSILFFYTDESAPLAPPQNLTLINYTSDFVWLTWSPSPLPGGIVKVYSFKIHEHETDTVFYKNISGLQTDAKLEGLEPVSTYSVSVSAFTKVGNGNQYSNVVEFTTQESVPEAVRNIECVARDWQSVSVRWDPPRKTNGIIIHYMITVGGNSTKVSPRDPTYTFTKLLPNTSYVFEVRASTSAGEGNESRCDISTLPETVPSAPTNVAFSNVQSTSATLTWTKPDTIFGYFQNYKITTQLRAQKCREWEPEECIEHQKDQYLYEANQTEETVHGLKKFRWYRFQVAASTNVGYSNASEWISTQTLPGPPDGPPENVHVVATSPFGINISWSEPAVITGPTFYLIDVKSVDDDDFNISFLKSNEENKTTEINNLEVFTRYSVVITAFVGNVSRAYTDGKSSAEVIITTLESVPKDPPNNMTFQKIPDEVTKFQLTFLPPSQPNGNIRVYQALVYREDDPTAVQIHNFSIIQKTDTSIIAMLEGLKGGHTYNISVYAINSAGAGPKVQMRITMDIKAPARPKSKPIPIRDATGKLLVTSTTITIRMPICYYNDDHGPIRNVQVLVAETGAQQDGNVTKWYDAYFNKARPYFTNEGFPNPPCIEGKTKFSGNEEIYVIGADNACMIPGNEEKICNGPLKPKKQYLFKFRATNVMGQFTDSEYSDPIKTLGEGLSERTVEIILSVTLCILSIILLGTAIFAFVRIRQKQKEGGTYSPRDAEIIDTKFKLDQLITVADLELKDERLTRLLSYRKSIKPISKKSFLQHVEELCTNSNLKFQEEFSELPKFLQDLSSTDADLPWNRAKNRFPNIKPYNNNRVKLIADVSLPGSDYINASYVSGYLCPNEFIATQGPLPGTVGDFWRMVWETRTKTLVMLTQCFEKGRIRCHQYWPEDNKPVTVFGDIVITKLMEDIQIDWTIRDLKIERHGDCMTVRQCNFTGWPEHGVPENTTPLIHFVKLVRTSRAHDTTPMVVHCSAGVGRTGVFIALDHLTQHINNHDFVDIYGLVAELRSERMCMVQNLAQYIFLHQCILDLLSNKGGHQPVCFVNYSTLQKMDSLDAMEGDVELEWEETTM
|
3.1.3.-; 3.1.3.48
| null |
dephosphorylation [GO:0016311]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; hematopoietic progenitor cell differentiation [GO:0002244]; inner ear morphogenesis [GO:0042472]; neuromuscular process controlling balance [GO:0050885]; regulation of fat cell differentiation [GO:0045598]; vestibular receptor cell morphogenesis [GO:0060116]
|
apical plasma membrane [GO:0016324]; receptor complex [GO:0043235]; stereocilium base [GO:0120044]; stereocilium bundle [GO:0032421]
|
protein tyrosine phosphatase activity [GO:0004725]
|
PF00041;PF00102;
|
2.60.40.10;3.90.190.10;
|
Protein-tyrosine phosphatase family, Receptor class 2A subfamily
| null |
SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000250|UniProtKB:P0C5E4}. Apical cell membrane {ECO:0000250|UniProtKB:P0C5E4}; Single-pass type I membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000250|UniProtKB:Q9UMZ3}; Single-pass type I membrane protein {ECO:0000255}. Note=Detected at the stereocilium base and at the apical cell membrane in mature hair cells (By similarity). Forms ring-like structures in the stereocilium taper region (By similarity). Detected at the basal cell membrane in fetal kidney podocytes (By similarity). A small isoform that lacks the N-terminal part and starts after the transmembrane region localizes in the cytoplasm (PubMed:12837292). {ECO:0000250|UniProtKB:P0C5E4, ECO:0000250|UniProtKB:Q9UMZ3, ECO:0000269|PubMed:12837292}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:12802008};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=125 uM for diC8-PI(3,4,5)P3 {ECO:0000269|PubMed:12802008}; Vmax=18.3 nmol/min/mg enzyme with diC8-PI(3,4,5)P3 as substrate {ECO:0000269|PubMed:12802008};
| null | null | null |
FUNCTION: Phosphatidylinositol phosphatase required for auditory function. May act by regulating the level of phosphatidylinositol 4,5-bisphosphate (PIP2) level in the basal region of hair bundles. Can dephosphorylate a broad range of phosphatidylinositol phosphates, including phosphatidylinositol 3,4,5-trisphosphate and most phosphatidylinositol monophosphates and diphosphates. Phosphate can be hydrolyzed from the D3 and D5 positions in the inositol ring. Has low tyrosine-protein phosphatase activity; however, the relevance of such activity in vivo is unclear. Plays an important role in adipogenesis of mesenchymal stem cells (MSCs). Regulates the phosphorylation state of AKT1 by suppressing the phosphatidylinositol 3,4,5-trisphosphate (PIP3) level in MSCs and preadipocyte cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:12802008}.
|
Rattus norvegicus (Rat)
|
O88491
|
NSD1_MOUSE
|
MDRTCELSRRNCLLSFSNPVNLDASEDKDSPFGNGQSNFSEPLNGCTMQLPTAASGTSQNAYGQDSPSCYIPLRRLQDLASMINVEYLSGSADGSESFQDPAKSDSRAQSPIVCTSLSPGGPTALAMKQEPTCNNSPELQLRVTKTTKNGFLHFENFTGVDDADVDSEMDPEQPVTEDESIEEIFEETQTNATCNYEPKSENGVEVAMGSEQDSMPESRHGAVERPFLPLAPQTEKQKNKQRSEVDGSNEKTALLPAPTSLGDTNVTVEEQFNSINLSFQDDPDSSPSPLGNMLEIPGTSSPSTSQELPFVPQKILSKWEASVGLAEQYDVPKGSKNQKCVSSSVKLDSEEDMPFEDCTNDPDSEHLLLNGCLKSLAFDSEHSADEKEKPCAKSRVRKSSDNIKRTSVKKDLVPFESRKEERRGKIPDNLGLDFISGGVSDKQASNELSRIANSLTGSSTAPGSFLFSSSVQNTAKTDFETPDCDSLSGLSESALISKHSGEKKKLHPGQVCSSKVQLCYVGAGDEEKRSNSVSVSTTSDDGCSDLDPTEHNSGFQNSVLGITDAFDKTENALSVHKNETQYSRYPVTNRIKEKQKSLITNSHADHLMGSTKTMEPETAELSQVNLSDLKISSPIPKPQPEFRNDGLTTKFSAPPGIRNENPLTKGGLANQTLLPLKCRQPKFRSIKCKHKESPAVAETSATSEDLSLKCCSSDTNGSPLANISKSGKGEGLKLLNNMHEKTRDSSDIETAVVKHVLSELKELSYRSLSEDVSDSGTAKASKPLLFSSASSQNHIPIEPDYKFSTLLMMLKDMHDSKTKEQRLMTAQNLASYRTPDRGDCSSGSPVGTSKVLVLGSSTPNSEKPGDSTQDSVHQSPGGGDSALSGELSSSLSSLASDKRELPACGKIRSNCIPRRNCGRAKPSSKLRETISAQMVKPSVNPKALKTERKRKFSRLPAVTLAANRLGNKESGSVNGPSRGGAEDPGKEEPLQQMDLLRNEDTHFSDVHFDSKAKQSDPDKNLEKEPSFENRKGPELGSEMNTENDELHGVNQVVPKKRWQRLNQRRPKPGKRANRFREKENSEGAFGVLLPADAVQKAREDYLEQRAPPTSKPEDSAADPNHGSHSESVAPRLNVCEKSSVGMGDVEKETGIPSLMPQTKLPEPAIRSEKKRLRKPSKWLLEYTEEYDQIFAPKKKQKKVQEQVHKVSSRCEDESLLARCQPSAQNKQVDENSLISTKEEPPVLEREAPFLEGPLAQSDLGVTHAELPQLTLSVPVAPEASPRPALESEELLVKTPGNYESKRQRKPTKKLLESNDLDPGFMPKKGDLGLSRKCFEASRSGNGIVESRATSHLKEFSGGTTKIFDKPRKRKRQRLVTARVHYKKVKKEDLTKDTPSSEGELLIHRTAASPKEILEEGVEHDPGMSASKKLQVERGGGAALKENVCQNCEKLGELLLCEAQCCGAFHLECLGLPEMPRGKFICNECHTGIHTCFVCKQSGEDVKRCLLPLCGKFYHEECVQKYPPTVTQNKGFRCPLHICITCHAANPANVSASKGRLMRCVRCPVAYHANDFCLAAGSKILASNSIICPNHFTPRRGCRNHEHVNVSWCFVCSEGGSLLCCDSCPAAFHRECLNIDIPEGNWYCNDCKAGKKPHYREIVWVKVGRYRWWPAEICHPRAVPSNIDKMRHDVGEFPVLFFGSNDYLWTHQARVFPYMEGDVSSKDKMGKGVDGTYKKALQEAAARFEELKARKELRQLQEDRKNDKKPPPYKHIKVNRPIGRVQIFTADLSEIPRCNCKATDENPCGIDSECINRMLLYECHPTVCPAGVRCQNQCFSKRQYPDVEIFRTLQRGWGLRTKTDIKKGEFVNEYVGELIDEEECRARIRYAQEHDITNFYMLTLDKDRIIDAGPKGNYARFMNHCCQPNCETQKWSVNGDTRVGLFALSDIKAGTELTFNYNLECLGNGKTVCKCGAPNCSGFLGVRPKNQPIVTEEKSRKFKRKPHGKRRSQGEVTKEREDECFSCGDAGQLVSCKKPGCPKVYHADCLNLTKRPAGKWECPWHQCDVCGKEAASFCEMCPSSFCKQHREGMLFISKLDGRLSCTEHDPCGPNPLEPGEIREYVPPTATSPPSPGTQPKEQSSEMATQGPKKSDQPPTDATQLLPLSKKALTGSCQRPLLPERPPERTDSSSHLLDRIRDLAGSGTKSQSLVSSQRPQDRPPAKEGPRPQPPDRASPMTRPSSSPSVSSLPLERPLRMTDSRLDKSIGAASPKSQAVEKTPASTGLRLSSPDRLLTTNSPKPQISDRPPEKSHASLTQRLPPPEKVLSAVVQSLVAKEKALRPVDQNTQSKHRPAVVMDLIDLTPRQKERAASPQEVTPQADEKTAMLESSSWPSSKGLGHIPRATEKISVSESLQPSGKVAAPSEHPWQAVKSLTHARFLSPPSAKAFLYESATQASGRTPVGAEQTPGPPSPAPGLVKQVKQLSRGLTAKSGQSFRSLGKISASLPNEEKKLTTTEQSPWGLGKASPGAGLWPIVAGQTLAQACWSAGGTQTLAQTCWSLGRGQDPKPENAIQALNQAPSSRKCADSEKK
|
2.1.1.357
| null |
gastrulation with mouth forming second [GO:0001702]; methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of peptidyl-serine phosphorylation [GO:0033135]
|
chromatin [GO:0000785]; histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; histone H3K36 dimethyltransferase activity [GO:0140954]; histone H3K36 methyltransferase activity [GO:0046975]; histone H4K20 methyltransferase activity [GO:0042799]; histone methyltransferase activity [GO:0042054]; nuclear androgen receptor binding [GO:0050681]; nuclear estrogen receptor binding [GO:0030331]; nuclear retinoic acid receptor binding [GO:0042974]; nuclear retinoid X receptor binding [GO:0046965]; nuclear thyroid hormone receptor binding [GO:0046966]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]; zinc ion binding [GO:0008270]
|
PF17907;PF17982;PF00628;PF00855;PF00856;
|
2.30.30.140;2.170.270.10;3.30.40.10;
|
Class V-like SAM-binding methyltransferase superfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9628876}. Chromosome {ECO:0000305|PubMed:9628876}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+) + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60308, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.357; Evidence={ECO:0000269|PubMed:12805229};
| null | null | null | null |
FUNCTION: Histone methyltransferase that dimethylates Lys-36 of histone H3 (H3K36me2). Transcriptional intermediary factor capable of negatively influencing transcription. May also positively influence transcription. Essential for early post-implantation development. {ECO:0000269|PubMed:12805229, ECO:0000269|PubMed:9628876}.
|
Mus musculus (Mouse)
|
O88495
|
MTR1L_MOUSE
|
MATVPKSNMGPTKAVPTPFGCIGCKLPKPDYPPALIIFMFCAMVITVVVDLIGNSMVILAVTKNKKLRNSGNIFVASLSVADMLVAIYPYPLMLYAMSVGGWDLSQLQCQMVGLVTGLSVVGSIFNITAIAINRYCYICHSLQYKRIFSLRNTCIYLVVTWVMTVLAVLPNMYIGTIEYDPRTYTCIFNYVNNPAFTVTIVCIHFVLPLIIVGYCYTKIWIKVLAARDPAGQNPDNQFAEVRNFLTMFVIFLLFAVCWCPVNVLTVLVAVIPKEMAGKIPNWLYLAAYCIAYFNSCLNAIIYGILNESFRREYWTIFHAMRHPILFISHLISDIRETWETRALTRARVRARDQVREQERARACVAVEGTPRNVRNVLLPGDASAPHSDRASVRPKPQTRSTSVYRKPASIHHKSISGHPKSASVYPKPASSVHCKPASVHFKPASVHFKGDSVYFKGDTVHYRAASKLVTSHRISAGPSTSHPTSMAGYIKSGTSHPATTTVDYLEPATTSHSVLTAVDLPEVSASHCLEMTSTGHLRADISASVLPSVPFELAATPPDTTAIPIASGDYRKVVLIDDDSDDSDCSDEMAV
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]
|
nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
|
G protein-coupled receptor activity [GO:0004930]; melatonin receptor activity [GO:0008502]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19699797, ECO:0000269|PubMed:29572483}; Multi-pass membrane protein. Postsynaptic density {ECO:0000269|PubMed:19699797}.
| null | null | null | null | null |
FUNCTION: G protein-coupled receptor that plays a role in numerous physiological processes including regulation of energy metabolism, neurite outgrowth or cell migration (PubMed:17957037, PubMed:19699797). Promotes self-renewal and neuronal differentiation of neural progenitor cells through activation of the NOTCH and WNT/beta-catenin signaling pathways (PubMed:25689717). Modulates the KAT5-dependent glucocorticoid receptor signaling by modulating KAT5 subcellular compartmentalisation (PubMed:21858214). Plays also a role in the activation TGFBR1 in the absence of TGFBR2 by interfering with FKBP1A binding to TGFBR1, leading to induction of both canonical and non-canonical SMAD signaling pathways resulting in inhibition of proliferation or promotion of migration (PubMed:29572483). {ECO:0000269|PubMed:17957037, ECO:0000269|PubMed:19699797, ECO:0000269|PubMed:21858214, ECO:0000269|PubMed:25689717, ECO:0000269|PubMed:29572483}.
|
Mus musculus (Mouse)
|
O88496
|
VKGC_RAT
|
MAVHRGSARAAPASDKVQKNKPAQTSGLEQGSRMARIFGFEWADLSSWQSVVTLLNRPTDPANLAVFRFLFAFLMLLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLWYRLSCMLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLSAQKKNAHVPLWNYTVLRGQIFIVYFIAGVKKLDADWVEGYSMEHLSRHWLFSPFKLVLSEELTSLLVVHWCGLLLDLSAGFLLFFDASRPIGLVFVSYFHCMNSQLFSIGMFPYVMLASSPLFCSAEWPRKLVARCPKRLQELLPAKAAPRPSASCVYKRARAKAGQKPGLRHHLGTVFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGLTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSLLLPKYNVTEPQIYFDIWVSINDRFQQRLFDPRVDIVQAVWSPFRRTPWVQPLLMDLSPWRTKLQDIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTVSSSPSCYMYIYVNTTEVALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQRKLQEIERRRNSPLHERFLRFVLRKLYVFRRSFLMTRISLRNLLFGRPSLEQLAQEVTYANLRPFEPVDESSASNTDSSDPHPSEPDSEHVHSEL
|
4.1.1.90
| null |
lung growth [GO:0060437]; response to dexamethasone [GO:0071548]; response to manganese ion [GO:0010042]; response to oxygen levels [GO:0070482]; response to parathyroid hormone [GO:0071107]; response to Thyroglobulin triiodothyronine [GO:1904016]; response to vitamin D [GO:0033280]; response to vitamin K [GO:0032571]; vitamin K metabolic process [GO:0042373]
|
endoplasmic reticulum membrane [GO:0005789]
|
gamma-glutamyl carboxylase activity [GO:0008488]; peptide binding [GO:0042277]; vitamin binding [GO:0019842]
|
PF05090;
| null |
Vitamin K-dependent gamma-carboxylase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P38435}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P38435}.
|
CATALYTIC ACTIVITY: Reaction=2,3-epoxyphylloquinone + 4-carboxy-L-glutamyl-[protein] + H(+) + H2O = CO2 + L-glutamyl-[protein] + O2 + phylloquinol; Xref=Rhea:RHEA:45140, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:11094, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15759, ChEBI:CHEBI:16526, ChEBI:CHEBI:28433, ChEBI:CHEBI:29973, ChEBI:CHEBI:84990; EC=4.1.1.90; Evidence={ECO:0000250|UniProtKB:P38435}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45142; Evidence={ECO:0000250|UniProtKB:P38435};
| null | null | null | null |
FUNCTION: Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide. Catalyzes gamma-carboxylation of various proteins, such as blood coagulation factors (F2, F7, F9 and F10), osteocalcin (BGLAP) or matrix Gla protein (MGP). {ECO:0000250|UniProtKB:P38435}.
|
Rattus norvegicus (Rat)
|
O88498
|
B2L11_RAT
|
MAKQPSDVNSECDREGGQLQPAERPPQLRPGAPTSLQTESQGNPDGEGDRCPHGSPQGPLAPPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRAFANDYREAEDHPQMVILQLLRFIFRLVWRRH
| null | null |
apoptotic process involved in embryonic digit morphogenesis [GO:1902263]; B cell homeostasis [GO:0001782]; cell-matrix adhesion [GO:0007160]; cellular response to amyloid-beta [GO:1904646]; cellular response to estradiol stimulus [GO:0071392]; cellular response to nerve growth factor stimulus [GO:1990090]; developmental pigmentation [GO:0048066]; ear development [GO:0043583]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; in utero embryonic development [GO:0001701]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; kidney development [GO:0001822]; leukocyte homeostasis [GO:0001776]; lymphocyte apoptotic process [GO:0070227]; lymphocyte homeostasis [GO:0002260]; male gonad development [GO:0008584]; mammary gland development [GO:0030879]; meiosis I [GO:0007127]; myeloid cell homeostasis [GO:0002262]; odontogenesis of dentin-containing tooth [GO:0042475]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy in response to ER overload [GO:0034263]; positive regulation of cell cycle [GO:0045787]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of lymphocyte apoptotic process [GO:0070230]; positive regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902110]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of T cell apoptotic process [GO:0070234]; post-embryonic development [GO:0009791]; regulation of apoptotic process [GO:0042981]; regulation of developmental pigmentation [GO:0048070]; regulation of organ growth [GO:0046620]; response to endoplasmic reticulum stress [GO:0034976]; spermatogenesis [GO:0007283]; spleen development [GO:0048536]; T cell apoptotic process [GO:0070231]; T cell homeostasis [GO:0043029]; thymocyte apoptotic process [GO:0070242]; thymus development [GO:0048538]; tube formation [GO:0035148]
|
Bcl-2 family protein complex [GO:0097136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]
|
dynein complex binding [GO:0070840]; microtubule binding [GO:0008017]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]
|
PF08945;PF06773;
| null |
Bcl-2 family
|
PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with TRIM2 and ubiquitination, followed by proteasomal degradation. Deubiquitination catalyzed by USP27X stabilizes the protein. {ECO:0000250|UniProtKB:O54918}.; PTM: Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3 leads to proteasomal degradation (PubMed:21478148). Conversely, deubiquitination catalyzed by USP27X stabilizes the protein (By similarity). {ECO:0000250|UniProtKB:O54918, ECO:0000269|PubMed:21478148}.
|
SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic membranes. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Induces apoptosis and anoikis. {ECO:0000269|PubMed:9731710}.
|
Rattus norvegicus (Rat)
|
O88502
|
PDE8A_MOUSE
|
MGCAPSIHTSENRTFSHSDGEDEDVDVDVPGPAPRSIQRWSTAPGLVEPQPRDNGASKVSVADVQFGPMRFHQDQLQVLLVFTKEDSQCNGFHRACEKAGFKCTVTKEVQTVLTCFQDKLHDIIIIDHRYPRQMDAETLCRSIRSSKFSENTVIVGVVRRVDKEESSLMPFLAAGFTRRFIENPNVMACYNELLQLACGEVRSQLKLRACNSVFTALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKVETTTECVQTDSQTDNQAGKHKDRRKHSMDAKAVSSRTSDVSSQRRHSSLARIHSMMIEAPITKVINIINAAQENSPVPVTEALNRVLDILRTTELYSPQFNAQDDPHATDLVGGLMSDGLRRFSGNEYILATKNLPPLSNNLATPVSLHDVPPRIALAIENEEQWDFDIFELEVATQNRPLIYLGLKTFARFGMCEFLQCSETTLRSWFQMIESNYHSSNPYHNSTHAADVLHATAYFLSRDKIKETLDRIDEVAALIAATVHDVDHPGRTNSFLCNAGNQLAVLYNDTAVLESHHVALAFQLTLENDQCNIFKQMERNDYRTLRQSIIDMVLATEMTKHFEHVNKFINSINKPLTAQESEEPDRSLEDIKAMLKTPESRALIKRMMIKCADVSNPCRPLEHCIEWAARISEEYFSQTDEEKQLDLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFVDLPNLMQHLDDNFRYWKGLDEKKLRSLRPPPE
|
3.1.4.53
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250};
|
cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; cellular response to epidermal growth factor stimulus [GO:0071364]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; regulation of DNA-templated transcription [GO:0006355]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; kinase binding [GO:0019900]; metal ion binding [GO:0046872]; protein kinase activator activity [GO:0030295]
|
PF00989;PF00233;
|
3.40.50.2300;1.10.1300.10;3.30.450.20;
|
Cyclic nucleotide phosphodiesterase family, PDE8 subfamily
|
PTM: Phosphorylated at Ser-355 by PKA under elevated cAMP conditions, this enhances catalytic activity. {ECO:0000250}.
| null |
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000269|PubMed:9671792}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278; Evidence={ECO:0000269|PubMed:9671792};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 uM for cAMP {ECO:0000269|PubMed:9671792};
|
PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
| null | null |
FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development. Binding to RAF1 reduces RAF1 'Ser-259' inhibitory-phosphorylation and stimulates RAF1-dependent EGF-activated ERK-signaling. Protects against cell death induced by hydrogen peroxide and staurosporine. {ECO:0000250|UniProtKB:O60658}.
|
Mus musculus (Mouse)
|
O88506
|
STK39_RAT
|
MAEPSGSPVHVQLPQQAAPVTAAAAAPAAATSAPAPAPAPAAPAAPAPAPAAAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQRAKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAASQEKSRRVKEENPEISVNAGGIPEQIQSLSVHDSQGQPNANEDYREGPCAVNLVLRLRNSRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGAEIPDEVKLIGFAQLSVS
|
2.7.11.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9Z1W9};
|
cell volume homeostasis [GO:0006884]; cellular hyperosmotic response [GO:0071474]; cellular hypotonic response [GO:0071476]; cellular response to chemokine [GO:1990869]; cellular response to potassium ion [GO:0035865]; chemokine (C-X-C motif) ligand 12 signaling pathway [GO:0038146]; inflammatory response [GO:0006954]; intracellular chloride ion homeostasis [GO:0030644]; intracellular signal transduction [GO:0035556]; macrophage activation [GO:0042116]; maintenance of lens transparency [GO:0036438]; monoatomic ion homeostasis [GO:0050801]; negative regulation of pancreatic juice secretion [GO:0090188]; negative regulation of potassium ion transmembrane transport [GO:1901380]; positive regulation of ion transmembrane transporter activity [GO:0032414]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of potassium ion transport [GO:0043268]; positive regulation of T cell chemotaxis [GO:0010820]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of blood pressure [GO:0008217]; regulation of inflammatory response [GO:0050727]; renal sodium ion absorption [GO:0070294]; response to aldosterone [GO:1904044]; response to dietary excess [GO:0002021]; signal transduction [GO:0007165]; sodium ion transmembrane transport [GO:0035725]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell body [GO:0044297]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF12202;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Phosphorylation at Thr-240 by WNK kinases (WNK1, WNK2, WNK3 or WNK4) is required for activation (PubMed:16083423, PubMed:16263722). Autophosphorylation at Thr-240 positively regulates its activity (By similarity). Phosphorylated at Ser-318 by PRKCQ (By similarity). {ECO:0000250|UniProtKB:Q9UEW8, ECO:0000269|PubMed:16083423, ECO:0000269|PubMed:16263722}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Nucleus when caspase-cleaved. {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9UEW8}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q9UEW8};
| null | null | null | null |
FUNCTION: Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure (PubMed:22544747). Specifically recognizes and binds proteins with a RFXV motif (By similarity). Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity (PubMed:22544747). Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases (By similarity). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:22544747). Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4 (By similarity). Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities. Phosphorylates RELT (By similarity). {ECO:0000250|UniProtKB:Q9UEW8, ECO:0000250|UniProtKB:Q9Z1W9, ECO:0000269|PubMed:22544747}.
|
Rattus norvegicus (Rat)
|
O88507
|
CNTFR_MOUSE
|
MAASVPWACCAVLAAAAAAVYTQKHSPQEAPHVQYERLGADVTLPCGTASWDAAVTWRVNGTDLAPDLLNGSQLILRSLELGHSGLYACFHRDSWHLRHQVLLHVGLPPREPVLSCRSNTYPKGFYCSWHLPTPTYIPNTFNVTVLHGSKIMVCEKDPALKNRCHIRYMHLFSTIKYKVSISVSNALGHNTTAITFDEFTIVKPDPPENVVARPVPSNPRRLEVTWQTPSTWPDPESFPLKFFLRYRPLILDQWQHVELSDGTAHTITDAYAGKEYIIQVAAKDNEIGTWSDWSVAAHATPWTEEPRHLTTEAQAPETTTSTTSSLAPPPTTKICDPGELGSGGGPSILFLTSVPVTLVLAAAAATANNLLI
| null | null |
brainstem development [GO:0003360]; ciliary neurotrophic factor-mediated signaling pathway [GO:0070120]; motor neuron apoptotic process [GO:0097049]; negative regulation of motor neuron apoptotic process [GO:2000672]; positive regulation of cell population proliferation [GO:0008284]; sex differentiation [GO:0007548]; skeletal muscle organ development [GO:0060538]; suckling behavior [GO:0001967]
|
apical plasma membrane [GO:0016324]; ciliary neurotrophic factor receptor complex [GO:0070110]; CNTFR-CLCF1 complex [GO:0097059]; external side of plasma membrane [GO:0009897]
|
ciliary neurotrophic factor receptor activity [GO:0004897]; cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; signaling receptor binding [GO:0005102]
|
PF00041;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 3 subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Binds to CNTF. The alpha subunit provides the receptor specificity (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O88508
|
DNM3A_MOUSE
|
MPSSGPGDTSSSSLEREDDRKEGEEQEENRGKEERQEPSATARKVGRPGRKRKHPPVESSDTPKDPAVTTKSQPMAQDSGPSDLLPNGDLEKRSEPQPEEGSPAAGQKGGAPAEGEGTETPPEASRAVENGCCVTKEGRGASAGEGKEQKQTNIESMKMEGSRGRLRGGLGWESSLRQRPMPRLTFQAGDPYYISKRKRDEWLARWKREAEKKAKVIAVMNAVEENQASGESQKVEEASPPAVQQPTDPASPTVATTPEPVGGDAGDKNATKAADDEPEYEDGRGFGIGELVWGKLRGFSWWPGRIVSWWMTGRSRAAEGTRWVMWFGDGKFSVVCVEKLMPLSSFCSAFHQATYNKQPMYRKAIYEVLQVASSRAGKLFPACHDSDESDSGKAVEVQNKQMIEWALGGFQPSGPKGLEPPEEEKNPYKEVYTDMWVEPEAAAYAPPPPAKKPRKSTTEKPKVKEIIDERTRERLVYEVRQKCRNIEDICISCGSLNVTLEHPLFIGGMCQNCKNCFLECAYQYDDDGYQSYCTICCGGREVLMCGNNNCCRCFCVECVDLLVGPGAAQAAIKEDPWNCYMCGHKGTYGLLRRREDWPSRLQMFFANNHDQEFDPPKVYPPVPAEKRKPIRVLSLFDGIATGLLVLKDLGIQVDRYIASEVCEDSITVGMVRHQGKIMYVGDVRSVTQKHIQEWGPFDLVIGGSPCNDLSIVNPARKGLYEGTGRLFFEFYRLLHDARPKEGDDRPFFWLFENVVAMGVSDKRDISRFLESNPVMIDAKEVSAAHRARYFWGNLPGMNRPLASTVNDKLELQECLEHGRIAKFSKVRTITTRSNSIKQGKDQHFPVFMNEKEDILWCTEMERVFGFPVHYTDVSNMSRLARQRLLGRSWSVPVIRHLFAPLKEYFACV
|
2.1.1.-; 2.1.1.37
| null |
autosome genomic imprinting [GO:0141068]; cellular response to amino acid stimulus [GO:0071230]; cellular response to bisphenol A [GO:1903926]; cellular response to ethanol [GO:0071361]; cellular response to hypoxia [GO:0071456]; DNA methylation-dependent heterochromatin formation [GO:0006346]; genomic imprinting [GO:0071514]; hepatocyte apoptotic process [GO:0097284]; heterochromatin formation [GO:0031507]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression via chromosomal CpG dinucleotide methylation [GO:0044027]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron differentiation [GO:0030182]; positive regulation of cellular response to hypoxia [GO:1900039]; post-fertilization epigenetic regulation of gene expression [GO:0043045]; response to cocaine [GO:0042220]; response to estradiol [GO:0032355]; response to ionizing radiation [GO:0010212]; response to lead ion [GO:0010288]; response to toxic substance [GO:0009636]; response to vitamin A [GO:0033189]; response to xenobiotic stimulus [GO:0009410]; S-adenosylmethionine metabolic process [GO:0046500]; spermatogenesis [GO:0007283]
|
catalytic complex [GO:1902494]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; XY body [GO:0001741]
|
chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA (cytosine-5-)-methyltransferase activity, acting on CpN substrates [GO:0051719]; DNA binding [GO:0003677]; identical protein binding [GO:0042802]; lncRNA binding [GO:0106222]; metal ion binding [GO:0046872]; protein-cysteine methyltransferase activity [GO:0106363]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
|
PF17980;PF21255;PF00145;PF00855;
|
2.30.30.140;1.10.720.50;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
|
PTM: Auto-methylated at Cys-706: auto-methylation takes place in absence of DNA substrate and inactivates the DNA methyltransferase activity (PubMed:21481189). Inactivation by auto-methylation may be used to inactivate unused DNA methyltransferases in the cell (PubMed:21481189). {ECO:0000269|PubMed:21481189}.; PTM: Sumoylated; sumoylation disrupts the ability to interact with histone deacetylases (HDAC1 and HDAC2) and repress transcription. {ECO:0000269|PubMed:14752048}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12138111, ECO:0000269|PubMed:15456878, ECO:0000269|PubMed:20547484}. Chromosome {ECO:0000269|PubMed:20547484}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K1}. Note=Accumulates in the major satellite repeats at pericentric heterochromatin. {ECO:0000269|PubMed:20547484}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10018, ECO:0000269|PubMed:11399089, ECO:0000269|PubMed:9662389}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13682; Evidence={ECO:0000269|PubMed:11399089, ECO:0000269|PubMed:9662389}; CATALYTIC ACTIVITY: Reaction=L-cysteinyl-[protein] + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + S-methyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:66544, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:82612; Evidence={ECO:0000269|PubMed:21481189}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66545; Evidence={ECO:0000269|PubMed:21481189};
| null | null | null | null |
FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). DNA methylation is coordinated with methylation of histones (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). It modifies DNA in a non-processive manner and also methylates non-CpG sites (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 (PubMed:18823905). Plays a role in paternal and maternal imprinting (PubMed:15215868). Required for methylation of most imprinted loci in germ cells (PubMed:15215868). Acts as a transcriptional corepressor for ZBTB18 (PubMed:11350943). Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites (PubMed:20547484). Can actively repress transcription through the recruitment of HDAC activity (PubMed:11350943). Also has weak auto-methylation activity on Cys-706 in absence of DNA (PubMed:21481189). {ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:11350943, ECO:0000269|PubMed:11399089, ECO:0000269|PubMed:11919202, ECO:0000269|PubMed:15215868, ECO:0000269|PubMed:16567415, ECO:0000269|PubMed:17713477, ECO:0000269|PubMed:18823905, ECO:0000269|PubMed:20547484, ECO:0000269|PubMed:21481189, ECO:0000269|PubMed:9662389}.
|
Mus musculus (Mouse)
|
O88509
|
DNM3B_MOUSE
|
MKGDSRHLNEEEGASGYEECIIVNGNFSDQSSDTKDAPSPPVLEAICTEPVCTPETRGRRSSSRLSKREVSSLLNYTQDMTGDGDRDDEVDDGNGSDILMPKLTRETKDTRTRSESPAVRTRHSNGTSSLERQRASPRITRGRQGRHHVQEYPVEFPATRSRRRRASSSASTPWSSPASVDFMEEVTPKSVSTPSVDLSQDGDQEGMDTTQVDAESRDGDSTEYQDDKEFGIGDLVWGKIKGFSWWPAMVVSWKATSKRQAMPGMRWVQWFGDGKFSEISADKLVALGLFSQHFNLATFNKLVSYRKAMYHTLEKARVRAGKTFSSSPGESLEDQLKPMLEWAHGGFKPTGIEGLKPNKKQPVVNKSKVRRSDSRNLEPRRRENKSRRRTTNDSAASESPPPKRLKTNSYGGKDRGEDEESRERMASEVTNNKGNLEDRCLSCGKKNPVSFHPLFEGGLCQSCRDRFLELFYMYDEDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGAGTAEDAKLQEPWSCYMCLPQRCHGVLRRRKDWNMRLQDFFTTDPDLEEFEPPKLYPAIPAAKRRPIRVLSLFDGIATGYLVLKELGIKVEKYIASEVCAESIAVGTVKHEGQIKYVNDVRKITKKNIEEWGPFDLVIGGSPCNDLSNVNPARKGLYEGTGRLFFEFYHLLNYTRPKEGDNRPFFWMFENVVAMKVNDKKDISRFLACNPVMIDAIKVSAAHRARYFWGNLPGMNRPVMASKNDKLELQDCLEFSRTAKLKKVQTITTKSNSIRQGKNQLFPVVMNGKDDVLWCTELERIFGFPAHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDYFACE
|
2.1.1.37
| null |
autosome genomic imprinting [GO:0141068]; cellular response to amino acid stimulus [GO:0071230]; DNA methylation-dependent heterochromatin formation [GO:0006346]; heterochromatin formation [GO:0031507]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of neuron differentiation [GO:0045666]; post-fertilization epigenetic regulation of gene expression [GO:0043045]; protein-containing complex localization [GO:0031503]; retrotransposon silencing by DNA methylation-dependent heterochromatin formation [GO:0141095]
|
chromosome, centromeric region [GO:0000775]; heterochromatin [GO:0000792]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA (cytosine-5-)-methyltransferase activity [GO:0003886]; DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates [GO:0051718]; DNA (cytosine-5-)-methyltransferase activity, acting on CpN substrates [GO:0051719]; DNA binding [GO:0003677]; histone deacetylase binding [GO:0042826]; lncRNA binding [GO:0106222]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]
|
PF17980;PF21255;PF00145;PF00855;
|
2.30.30.140;1.10.720.50;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
|
PTM: Sumoylated. {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15456878}. Note=Accumulates in the major satellite repeats at pericentric heterochromatin.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
| null | null | null | null |
FUNCTION: Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing. In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Functions as a transcriptional corepressor by associating with ZHX1 (By similarity). Required for DUX4 silencing in somatic cells (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UBC3, ECO:0000269|PubMed:10555141, ECO:0000269|PubMed:11836534, ECO:0000269|PubMed:11919202, ECO:0000269|PubMed:16567415, ECO:0000269|PubMed:18056424, ECO:0000269|PubMed:18567530}.
|
Mus musculus (Mouse)
|
O88513
|
GEMI_MOUSE
|
MNLSMKQKQEGAQENVKNSPVPRRTLKMIQPSADGSLVGRENELPKGLFKRKLWDDQLASQTSSCGPEANENKDVGDLTQEAFDLISKENPSSQYWKEVAEQRRKALYEALKENEKLHKEIEQKDSEIARLRKENKDLAEVAEHVQYMAEVIERLSNEPLDNFESPDSQEFDSEEEAVEYSELEDSGAGTCAEETVSSSTDARPCT
| null | null |
animal organ morphogenesis [GO:0009887]; DNA replication preinitiation complex assembly [GO:0071163]; negative regulation of cell cycle [GO:0045786]; negative regulation of DNA replication [GO:0008156]; negative regulation of DNA-templated DNA replication [GO:2000104]; negative regulation of DNA-templated transcription [GO:0045892]; protein-containing complex assembly [GO:0065003]; regulation of DNA-templated DNA replication initiation [GO:0030174]; regulation of mitotic cell cycle [GO:0007346]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor binding [GO:0140297]; histone deacetylase binding [GO:0042826]; transcription corepressor activity [GO:0003714]
|
PF07412;
|
1.20.5.1180;
|
Geminin family
|
PTM: Phosphorylated during mitosis. Phosphorylation at Ser-181 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity. {ECO:0000250|UniProtKB:O75496}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75496}. Nucleus {ECO:0000250|UniProtKB:O75496}. Note=Mainly cytoplasmic but can be relocalized to the nucleus. {ECO:0000250|UniProtKB:O75496}.
| null | null | null | null | null |
FUNCTION: Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC) (PubMed:12192004, PubMed:9635433). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle (PubMed:12192004, PubMed:9635433). Inhibits histone acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, inhibiting histone H4 acetylation and DNA replication licensing (By similarity). Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control (By similarity). {ECO:0000250|UniProtKB:O75496, ECO:0000269|PubMed:12192004, ECO:0000269|PubMed:9635433}.
|
Mus musculus (Mouse)
|
O88516
|
DLL3_MOUSE
|
MVSLQVSPLSQTLILAFLLPQALPAGVFELQIHSFGPGPGLGTPRSPCNARGPCRLFFRVCLKPGVSQEATESLCALGAALSTSVPVYTEHPGESAAALPLPDGLVRVPFRDAWPGTFSLVIETWREQLGEHAGGPAWNLLARVVGRRRLAAGGPWARDVQRTGTWELHFSYRARCEPPAVGAACARLCRSRSAPSRCGPGLRPCTPFPDECEAPSVCRPGCSPEHGYCEEPDECRCLEGWTGPLCTVPVSTSSCLNSRVPGPASTGCLLPGPGPCDGNPCANGGSCSETSGSFECACPRGFYGLRCEVSGVTCADGPCFNGGLCVGGEDPDSAYVCHCPPGFQGSNCEKRVDRCSLQPCQNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGSRRCSCALGFGGRDCRERADPCASRPCAHGGRCYAHFSGLVCACAPGYMGVRCEFAVRPDGADAVPAAPRGLRQADPQRFLLPPALGLLVAAGLAGAALLVIHVRRRGPGQDTGTRLLSGTREPSVHTLPDALNNLRLQDGAGDGPSSSADWNHPEDGDSRSIYVIPAPSIYAREDWLIQVLF
| null | null |
cell fate determination [GO:0001709]; compartment pattern specification [GO:0007386]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; in utero embryonic development [GO:0001701]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of neurogenesis [GO:0050768]; negative regulation of Notch signaling pathway [GO:0045746]; nervous system development [GO:0007399]; Notch signaling pathway [GO:0007219]; paraxial mesoderm development [GO:0048339]; positive regulation of neurogenesis [GO:0050769]; skeletal system development [GO:0001501]; somitogenesis [GO:0001756]; tissue development [GO:0009888]
|
endosome membrane [GO:0010008]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
calcium ion binding [GO:0005509]; Notch binding [GO:0005112]
|
PF00008;PF12661;PF07657;
|
2.60.40.3510;2.10.25.10;
| null |
PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm.
|
Mus musculus (Mouse)
|
O88522
|
NEMO_MOUSE
|
MNKHPWKNQLSEMVQPSGGPAEDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRSQREQALKELEQLKKCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKDRQALEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVEKKEYLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVETPQPPLLPAPAHHSFHLALSNQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE
| null | null |
anoikis [GO:0043276]; B cell homeostasis [GO:0001782]; canonical NF-kappaB signal transduction [GO:0007249]; DNA damage response [GO:0006974]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of gene expression [GO:0010628]; positive regulation of macroautophagy [GO:0016239]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of T cell receptor signaling pathway [GO:0050862]; positive regulation of transcription by RNA polymerase II [GO:0045944]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
cytoplasm [GO:0005737]; IkappaB kinase complex [GO:0008385]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; linear polyubiquitin binding [GO:1990450]; metal ion binding [GO:0046872]; peroxisome proliferator activated receptor binding [GO:0042975]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; signaling adaptor activity [GO:0035591]
|
PF16516;PF11577;PF18414;
|
1.20.5.390;1.20.5.990;
| null |
PTM: Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Polyubiquitinated on Lys-278 via 'Lys-63'-linked ubiquitin; the ubiquitination is mediated downstream of NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway (By similarity). Polyubiquitinated on Lys-278 and Lys-302 through 'Lys-63'-linked ubiquitin; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway (By similarity). Monoubiquitinated on Lys-270 and Lys-302; promotes nuclear export (By similarity). Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses (By similarity). Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-270, Lys-278, Lys-285, Lys-295, Lys-302 and Lys-319; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation (By similarity). Deubiquitinated by USP10 in a TANK-dependent and -independent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage (By similarity). Ubiquitinated at Lys-319 by MARCHF2 following bacterial and viral infection which leads to its degradation (By similarity). Polyubiquitinated via 'Lys-29'-linked ubiquitin; leading to lysosomal degradation (By similarity). {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Sumoylated on Lys-270 and Lys-302 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues. {ECO:0000250|UniProtKB:Q9Y6K9}.; PTM: Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity. {ECO:0000250|UniProtKB:Q9Y6K9}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6K9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6K9}. Note=Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. {ECO:0000250|UniProtKB:Q9Y6K9}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor (PubMed:9927690). Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways. Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much highr affinity for linear polyubiquitin. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination (By similarity). {ECO:0000250|UniProtKB:Q9Y6K9, ECO:0000269|PubMed:9927690}.
|
Mus musculus (Mouse)
|
O88529
|
BMAL1_MESAU
|
MADQRMDISSTISDFMSPGPTDLLSSSLGTSGVDCNRKRKGSATDYQESMDTDKDDPHGRLEYAEHQGRIKNAREAHSQIEKRRRDKMNSFIDELASLVPTCNAMSRKLDKLTVLRMAVQHMKTLRGATNPYTEANYKPTFLSDDELKHLILRAADGFLFVVGCDRGKILFVSESVFKILNYSQNDLIGQSLFDYLHPKDIAKVKEQLSSSDTAPRERLIDAKTGLPVKTDITPGPSRLCSGARRSFFCRMKCNRPSVKVEDKDFASTCSKKKADRKSFCTIHSTGYLKSWPPTKMGLDEDNEPDNEGCNLSCLVAIGRLHSHVVPQPVNGEIRVKSMEYVSRHAIDGKFVFVDQRATAILAYLPQELLGTSCYEYFHQDDIGHLAECHRQVLQTREKITTNCYKFKIKDGSFITLRSRWFSFMNPWTKEVEYIVSTNTVVLANVLEGGDPTFPQLTASPHSMDSMLPSGEGGPKRTHPTVPGIPGGTRAGAGKIGRMIAEEIMEIHRIRGSSPSSCGSSPLNITSTPPPDASSPGGKKILNGGTPDIPSTGLLPGQAQETPGYPYSDSSSILGENPHIGIDMIDNDQGSSSPSNDEAAMAVIMSLLEADAGLGGPVDFSDLPWPL
| null | null |
circadian regulation of gene expression [GO:0032922]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of glucocorticoid receptor signaling pathway [GO:2000323]; negative regulation of TOR signaling [GO:0032007]; oxidative stress-induced premature senescence [GO:0090403]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of circadian rhythm [GO:0042753]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of protein acetylation [GO:1901985]; positive regulation of skeletal muscle cell differentiation [GO:2001016]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of cell cycle [GO:0051726]; regulation of cellular senescence [GO:2000772]; regulation of DNA-templated transcription [GO:0006355]; regulation of hair cycle [GO:0042634]; regulation of insulin secretion [GO:0050796]; regulation of neurogenesis [GO:0050767]; regulation of type B pancreatic cell development [GO:2000074]; response to redox state [GO:0051775]; spermatogenesis [GO:0007283]
|
aryl hydrocarbon receptor complex [GO:0034751]; chromatoid body [GO:0033391]; CLOCK-BMAL transcription complex [GO:1990513]; nucleus [GO:0005634]; PML body [GO:0016605]; transcription regulator complex [GO:0005667]
|
aryl hydrocarbon receptor binding [GO:0017162]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; Hsp90 protein binding [GO:0051879]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
|
PF00010;PF00989;PF14598;
|
4.10.280.10;3.30.450.20;
| null |
PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP9X. {ECO:0000250|UniProtKB:Q9WTL8}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-BMAL1 heterodimer thereby increasing CLOCK-BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2/3 and CRY1/2. {ECO:0000250|UniProtKB:Q9WTL8}.; PTM: Acetylated on Lys-538 by CLOCK during the repression phase of the circadian cycle. Acetylation facilitates recruitment of CRY1 protein and initiates the repression phase of the circadian cycle. Acetylated at Lys-538 by KAT5 during the activation phase of the cycle, leading to recruitment of the positive transcription elongation factor b (P-TEFb) and BRD4, followed by productive elongation of circadian transcripts. Deacetylated by SIRT1, which may result in decreased protein stability. {ECO:0000250|UniProtKB:Q9WTL8}.; PTM: Phosphorylated upon dimerization with CLOCK. Phosphorylation enhances the transcriptional activity, alters the subcellular localization and decreases the stability of the CLOCK-BMAL1 heterodimer by promoting its degradation. Phosphorylation shows circadian variations in the liver with a peak between CT10 to CT14. Phosphorylation at Ser-90 by CK2 is essential for its nuclear localization, its interaction with CLOCK and controls CLOCK nuclear entry. Dephosphorylation at Ser-78 is important for dimerization with CLOCK and transcriptional activity. {ECO:0000250|UniProtKB:O00327, ECO:0000250|UniProtKB:Q9WTL8}.; PTM: Sumoylated on Lys-259 upon dimerization with CLOCK. Predominantly conjugated to poly-SUMO2/3 rather than SUMO1 and the level of these conjugates undergo rhythmic variation, peaking at CT9-CT12. Sumoylation localizes it exclusively to the PML body and promotes its ubiquitination in the PML body, ubiquitin-dependent proteasomal degradation and the transcriptional activity of the CLOCK-BMAL1 heterodimer. {ECO:0000250|UniProtKB:Q9WTL8}.; PTM: Undergoes lysosome-mediated degradation in a time-dependent manner in the liver. {ECO:0000250|UniProtKB:Q9WTL8}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. Cytoplasm {ECO:0000250|UniProtKB:Q9WTL8}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9WTL8}. Note=Shuttles between the nucleus and the cytoplasm and this nucleocytoplasmic shuttling is essential for the nuclear accumulation of CLOCK, target gene transcription and the degradation of the CLOCK-BMAL1 heterodimer. The sumoylated form localizes in the PML body. Sequestered to the cytoplasm in the presence of ID2. {ECO:0000250|UniProtKB:Q9WTL8}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. BMAL1 positively regulates myogenesis and negatively regulates adipogenesis via the transcriptional control of the genes of the canonical Wnt signaling pathway. Plays a role in normal pancreatic beta-cell function; regulates glucose-stimulated insulin secretion via the regulation of antioxidant genes NFE2L2/NRF2 and its targets SESN2, PRDX3, CCLC and CCLM. Negatively regulates the mTORC1 signaling pathway; regulates the expression of MTOR and DEPTOR. Controls diurnal oscillations of Ly6C inflammatory monocytes; rhythmic recruitment of the PRC2 complex imparts diurnal variation to chemokine expression that is necessary to sustain Ly6C monocyte rhythms. Regulates the expression of HSD3B2, STAR, PTGS2, CYP11A1, CYP19A1 and LHCGR in the ovary and also the genes involved in hair growth. Plays an important role in adult hippocampal neurogenesis by regulating the timely entry of neural stem/progenitor cells (NSPCs) into the cell cycle and the number of cell divisions that take place prior to cell-cycle exit. Regulates the circadian expression of CIART and KLF11. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The NPAS2-BMAL1 heterodimer positively regulates the expression of MAOA, F7 and LDHA and modulates the circadian rhythm of daytime contrast sensitivity by regulating the rhythmic expression of adenylate cyclase type 1 (ADCY1) in the retina. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence. CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3'. The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3'. Essential for the rhythmic interaction of CLOCK with ASS1 and plays a critical role in positively regulating CLOCK-mediated acetylation of ASS1. Plays a role in protecting against lethal sepsis by limiting the expression of immune checkpoint protein CD274 in macrophages in a PKM2-dependent manner (By similarity). Regulates the diurnal rhythms of skeletal muscle metabolism via transcriptional activation of genes promoting triglyceride synthesis (DGAT2) and metabolic efficiency (COQ10B) (By similarity). {ECO:0000250|UniProtKB:O00327, ECO:0000250|UniProtKB:Q9WTL8}.
|
Mesocricetus auratus (Golden hamster)
|
O88531
|
PPT1_MOUSE
|
MASSCSRRLLAAALLPWCCAAWALGHLDPPSPPPLVIWHGMGDSCCNPMSMGVIKKMVEKEIPGIYVLSLEIGKNMMEDVENSFFLNVNVQVNMVCQILEKDPKLQQGYNAIGFSQGGQFLRAVAQRCPTPPMMTLISVGGQHQGVFGLPRCPGESSHICDFIRKSLNAGAYSKLVQERLVQAQYWHDPIKESVYRNYSIFLADINQERCVNESYKKNLMALKKFVMVKFFNDSIVDPVDSEWFGFYRSGQAKETIPLQESTLYTEDRLGLKKMDKAGKLVFLAKEGDHLQISKEWFTAHIIPFLK
|
3.1.2.22
| null |
adult locomotory behavior [GO:0008344]; associative learning [GO:0008306]; brain development [GO:0007420]; grooming behavior [GO:0007625]; lipid catabolic process [GO:0016042]; lysosomal lumen acidification [GO:0007042]; lysosome organization [GO:0007040]; macromolecule catabolic process [GO:0009057]; membrane raft organization [GO:0031579]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of neuron apoptotic process [GO:0043524]; nervous system development [GO:0007399]; neurotransmitter secretion [GO:0007269]; pinocytosis [GO:0006907]; positive regulation of pinocytosis [GO:0048549]; positive regulation of receptor-mediated endocytosis [GO:0048260]; protein catabolic process [GO:0030163]; protein depalmitoylation [GO:0002084]; protein transport [GO:0015031]; receptor-mediated endocytosis [GO:0006898]; visual perception [GO:0007601]
|
axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; synaptic vesicle [GO:0008021]
|
long-chain fatty acyl-CoA hydrolase activity [GO:0052816]; lysophosphatidic acid binding [GO:0035727]; palmitoyl-(protein) hydrolase activity [GO:0008474]; sulfatide binding [GO:0120146]
|
PF02089;
|
3.40.50.1820;
|
Palmitoyl-protein thioesterase family
|
PTM: Glycosylated. {ECO:0000269|PubMed:9685319}.
|
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651, ECO:0000269|PubMed:9685319}. Secreted {ECO:0000269|PubMed:9685319}.
|
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000250|UniProtKB:P45478};
| null | null | null | null |
FUNCTION: Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons. {ECO:0000250|UniProtKB:P45478}.
|
Mus musculus (Mouse)
|
O88533
|
DDC_MOUSE
|
MDSREFRRRGKEMVDYIADYLDGIEGRPVYPDVEPGYLRPLIPATAPQEPETYEDIIKDIEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPEAFLAGRAGEGGGVIQGSASEATLVALLAARTKVIRQLQAASPEFTQAAIMEKLVAYTSDQAHSSVERAGLIGGIKLKAVPSDGNFSMRASALREALERDKAAGLIPFFVVATLGTTSCCSFDNLLEVGPICNQEGVWLHIDAAYAGSAFICPEFRYLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKRRTDLTGAFNMDPVYLKHSHQDSGFITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVELSHEFESLVRQDPRFEICTEVILGLVCFRLKGSNELNETLLQRINSAKKIHLVPCRLRDKFVLRFAVCARTVESAHVQLAWEHISDLASSVLRAEKE
|
4.1.1.28
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P20711};
|
aminergic neurotransmitter loading into synaptic vesicle [GO:0015842]; amino acid metabolic process [GO:0006520]; carboxylic acid metabolic process [GO:0019752]; catecholamine metabolic process [GO:0006584]; dopamine biosynthetic process [GO:0042416]; gene expression [GO:0010467]; kidney development [GO:0001822]; response to toxic substance [GO:0009636]; serotonin biosynthetic process [GO:0042427]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; synaptic vesicle [GO:0008021]
|
5-hydroxy-L-tryptophan decarboxylase activity [GO:0036467]; amino acid binding [GO:0016597]; aromatic-L-amino-acid decarboxylase activity [GO:0004058]; enzyme binding [GO:0019899]; L-dopa decarboxylase activity [GO:0036468]; protein domain specific binding [GO:0019904]; pyridoxal phosphate binding [GO:0030170]
|
PF00282;
|
3.90.1150.10;1.20.1340.10;3.40.640.10;
|
Group II decarboxylase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + L-dopa = CO2 + dopamine; Xref=Rhea:RHEA:12272, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57504, ChEBI:CHEBI:59905; EC=4.1.1.28; Evidence={ECO:0000250|UniProtKB:P80041}; CATALYTIC ACTIVITY: Reaction=5-hydroxy-L-tryptophan + H(+) = CO2 + serotonin; Xref=Rhea:RHEA:18533, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58266, ChEBI:CHEBI:350546; EC=4.1.1.28; Evidence={ECO:0000250|UniProtKB:P80041};
| null |
PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 2/2. {ECO:0000250|UniProtKB:P80041}.
| null | null |
FUNCTION: Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin. {ECO:0000250|UniProtKB:P80041}.
|
Mus musculus (Mouse)
|
O88536
|
FPR2_MOUSE
|
MESNYSIHLNGSEVVVYDSTISRVLWILSMVVVSITFFLGVLGNGLVIWVAGFRMPHTVTTIWYLNLALADFSFTATLPFLLVEMAMKEKWPFGWFLCKLVHIVVDVNLFGSVFLIALIALDRCICVLHPVWAQNHRTVSLARKVVVGPWIFALILTLPIFIFLTTVRIPGGDVYCTFNFGSWAQTDEEKLNTAITFVTTRGIIRFLIGFSMPMSIVAVCYGLIAVKINRRNLVNSSRPLRVLTAVVASFFICWFPFQLVALLGTVWFKETLLSGSYKILDMFVNPTSSLAYFNSCLNPMLYVFMGQDFRERFIHSLPYSLERALSEDSGQTSDSSTSSTSPPADIELKAP
| null | null |
cellular response to amyloid-beta [GO:1904646]; complement receptor mediated signaling pathway [GO:0002430]; inflammatory response [GO:0006954]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive chemotaxis [GO:0050918]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of superoxide anion generation [GO:0032930]
|
plasma membrane [GO:0005886]
|
amyloid-beta binding [GO:0001540]; complement receptor activity [GO:0004875]; N-formyl peptide receptor activity [GO:0004982]; RAGE receptor binding [GO:0050786]; signaling receptor activity [GO:0038023]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P25090}; Multi-pass membrane protein {ECO:0000305}. Note=Associates with Amyloid-beta protein 42, product of APP, at the cell surface and the complex is then rapidly internalized. {ECO:0000250|UniProtKB:P25090}.
| null | null | null | null | null |
FUNCTION: High affinity receptor for N-formyl-methionyl peptides (FMLP), which are powerful neutrophil chemotactic factors (PubMed:10477558, PubMed:12218158, PubMed:19387439). Stimulates chemotaxis in immune cells to site of infection or tissue damage upon recognition of several ligands, such as FMLP, or ligand involved in cell damage, disease or inflammation (PubMed:10477558, PubMed:19497865). Receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-induced osteoclast differentiation (PubMed:29138422). {ECO:0000269|PubMed:10477558, ECO:0000269|PubMed:12218158, ECO:0000269|PubMed:19387439, ECO:0000269|PubMed:19497865, ECO:0000269|PubMed:29138422}.
|
Mus musculus (Mouse)
|
O88543
|
CSN3_MOUSE
|
MASALEQFVNSVRQLSAQGQMTQLCELINKSGELLAKNLSHLDTVLGALDVQEHSLGVLAVLFVKFSMPSVPDFETLFSQVQLFISTCNGEHIRYATDTFAGLCHQLTNALVERKQPLRGIGILKQAIDKMQMNTNQLTSVHADLCQLCLLAKCFKPALPYLDVDMMDICKENGAYDAKHFLCYYYYGGMIYTGLKNFERALYFYEQAITTPAMAVSHIMLESYKKYILVSLILLGKVQQLPKYTSQIVGRFIKPLSNAYHELAQVYSTNNPSELRNLVSKHSETFTRDNNMGLVKQCLSSLYKKNIQRLTKTFLTLSLQDMASRVQLSGPQEAEKYVLHMIEDGEIFASINQKDGMVSFHDNPEKYNNPAMLHNIDQEMLKCIELDERLKAMDQEITVNPQFVQKSMGSQEDDSGNKPSSYS
| null | null |
in utero embryonic development [GO:0001701]; protein deneddylation [GO:0000338]; regulation of DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:1902162]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
COP9 signalosome [GO:0008180]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]
| null |
PF21215;PF01399;
|
1.25.40.570;
|
CSN3 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UNS2}. Nucleus {ECO:0000250|UniProtKB:Q9UNS2}.
| null | null | null | null | null |
FUNCTION: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes (By similarity). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 (By similarity). The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases (By similarity). CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity). Essential to maintain the survival of epiblast cells and thus the development of the postimplantation embryo (PubMed:12972600). {ECO:0000250|UniProtKB:Q9UNS2, ECO:0000269|PubMed:12972600}.
|
Mus musculus (Mouse)
|
O88551
|
CLD1_MOUSE
|
MANAGLQLLGFILASLGWIGSIVSTALPQWKIYSYAGDNIVTAQAIYEGLWMSCVSQSTGQIQCKVFDSLLNLNSTLQATRALMVIGILLGLIAIFVSTIGMKCMRCLEDDEVQKMWMAVIGGIIFLISGLATLVATAWYGNRIVQEFYDPLTPINARYEFGQALFTGWAAASLCLLGGVLLSCSCPRKTTSYPTPRPYPKPTPSSGKDYV
| null | null |
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; cell junction maintenance [GO:0034331]; cell-cell junction organization [GO:0045216]; cellular response to butyrate [GO:1903545]; cellular response to lead ion [GO:0071284]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; establishment of blood-nerve barrier [GO:0008065]; establishment of endothelial intestinal barrier [GO:0090557]; establishment of skin barrier [GO:0061436]; liver regeneration [GO:0097421]; positive regulation of bicellular tight junction assembly [GO:1903348]; positive regulation of cell migration [GO:0030335]; positive regulation of epithelial cell proliferation involved in wound healing [GO:0060054]; positive regulation of wound healing [GO:0090303]; protein complex oligomerization [GO:0051259]; response to dexamethasone [GO:0071548]; response to ethanol [GO:0045471]; response to interleukin-18 [GO:0070673]; response to lipopolysaccharide [GO:0032496]; response to toxic substance [GO:0009636]; xenobiotic transport across blood-nerve barrier [GO:0061772]
|
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; cell-cell junction [GO:0005911]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; tight junction [GO:0070160]
|
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]; virus receptor activity [GO:0001618]
|
PF00822;
|
1.20.140.150;
|
Claudin family
| null |
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:10562289, ECO:0000269|PubMed:9647647}. Cell membrane {ECO:0000269|PubMed:11889141}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:O95832}. Note=Associates with CD81 and the CLDN1-CD81 complex localizes to the basolateral cell membrane. {ECO:0000250|UniProtKB:O95832}.
| null | null | null | null | null |
FUNCTION: Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions. {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:11889141, ECO:0000269|PubMed:23407391}.
|
Mus musculus (Mouse)
|
O88552
|
CLD2_MOUSE
|
MASLGVQLVGYILGLLGLLGTSIAMLLPNWRTSSYVGASIVTAVGFSKGLWMECATHSTGITQCDIYSTLLGLPADIQAAQAMMVTSSAMSSLACIISVVGMRCTVFCQDSRAKDRVAVVGGVFFILGGILGFIPVAWNLHGILRDFYSPLVPDSMKFEIGEALYLGIISALFSLVAGVILCFSCSPQGNRTNYYDGYQAQPLATRSSPRSAQQPKAKSEFNSYSLTGYV
| null | null |
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell-cell adhesion [GO:0098609]
|
bicellular tight junction [GO:0005923]; membrane [GO:0016020]; plasma membrane [GO:0005886]; tight junction [GO:0070160]
|
channel activity [GO:0015267]; identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]
|
PF00822;
|
1.20.140.150;
|
Claudin family
|
PTM: The disulfide bond is necessary for pore formation, but is not required for correct protein trafficking. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11934881, ECO:0000269|PubMed:32149733}. Cell membrane {ECO:0000269|PubMed:11934881}; Multi-pass membrane protein {ECO:0000269|PubMed:11934881}.
| null | null | null | null | null |
FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000269|PubMed:10508613, ECO:0000269|PubMed:32149733}.
|
Mus musculus (Mouse)
|
O88554
|
PARP2_MOUSE
|
MAPRRQRSGSGRRVLNEAKKVDNGNKATEDDSPPGKKMRTCQRKGPMAGGKDADRTKDNRDSVKTLLLKGKAPVDPECAAKLGKAHVYCEGDDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKTGQHSLVTCSGDLNKAKEIFQKKFLDKTKNNWEDRENFEKVPGKYDMLQMDYAASTQDESKTKEEETLKPESQLDLRVQELLKLICNVQTMEEMMIEMKYDTKRAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALVEACNEFYTRIPHDFGLSIPPVIRTEKELSDKVKLLEALGDIEIALKLVKSERQGLEHPLDQHYRNLHCALRPLDHESNEFKVISQYLQSTHAPTHKDYTMTLLDVFEVEKEGEKEAFREDLPNRMLLWHGSRLSNWVGILSHGLRVAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAQGLLRGKHSTKGMGKMAPSPAHFITLNGSTVPLGPASDTGILNPEGYTLNYNEFIVYSPNQVRMRYLLKIQFNFLQLW
|
2.4.2.-; 2.4.2.30
| null |
base-excision repair [GO:0006284]; decidualization [GO:0046697]; DNA ADP-ribosylation [GO:0030592]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; double-strand break repair [GO:0006302]; extrinsic apoptotic signaling pathway [GO:0097191]; hippocampal neuron apoptotic process [GO:0110088]; positive regulation of cell growth involved in cardiac muscle cell development [GO:0061051]; protein auto-ADP-ribosylation [GO:0070213]; protein poly-ADP-ribosylation [GO:0070212]; response to oxygen-glucose deprivation [GO:0090649]
|
nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of DNA damage [GO:0090734]
|
chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; NAD DNA ADP-ribosyltransferase activity [GO:0140294]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+- protein-aspartate ADP-ribosyltransferase activity [GO:0140806]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; NAD+-protein-glutamate ADP-ribosyltransferase activity [GO:0140807]; NAD+-protein-serine ADP-ribosyltransferase activity [GO:0140805]; nucleosome binding [GO:0031491]; nucleotidyltransferase activity [GO:0016779]; poly-ADP-D-ribose binding [GO:0072572]; poly-ADP-D-ribose modification-dependent protein binding [GO:0160004]
|
PF00644;PF02877;PF05406;
|
3.90.228.10;1.20.142.10;2.20.140.10;
|
ARTD/PARP family
|
PTM: Auto poly-ADP-ribosylated on serine residues, leading to dissociation of the PARP2-HPF1 complex from chromatin (By similarity). Poly-ADP-ribosylated by PARP1 (PubMed:11948190). {ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:11948190}.; PTM: Acetylation reduces DNA binding and enzymatic activity. {ECO:0000269|PubMed:18436469}.; PTM: Proteolytically cleaved by caspase-8 (CASP8) in response to apoptosis, leading to its inactivation. {ECO:0000269|PubMed:12065591}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10364231}. Chromosome {ECO:0000250|UniProtKB:Q9UGN5}. Note=Recruited to DNA damage sites in a PARP1-dependent process: recognizes and binds poly-ADP-ribose chains produced by PARP1 at DNA damage sites via its N-terminus, leading to its recruitment. {ECO:0000250|UniProtKB:Q9UGN5}.
|
CATALYTIC ACTIVITY: Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30; Evidence={ECO:0000269|PubMed:12065591}; CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540, ChEBI:CHEBI:142556; Evidence={ECO:0000250|UniProtKB:Q9UGN5}; CATALYTIC ACTIVITY: Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; Evidence={ECO:0000250|UniProtKB:Q9UGN5}; CATALYTIC ACTIVITY: Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154, ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540; Evidence={ECO:0000250|UniProtKB:Q9UGN5};
| null | null | null | null |
FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:10364231, PubMed:12065591). Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:12065591). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (By similarity). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site (By similarity). PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (By similarity). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains (By similarity). Specifically mediates formation of branched poly-ADP-ribosylation (By similarity). Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (By similarity). {ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:10364231, ECO:0000269|PubMed:12065591}.
|
Mus musculus (Mouse)
|
O88559
|
MEN1_MOUSE
|
MGLKAAQKTLFPLRSIDDVVRLFAAELGREEPDLVLLSLVLGFVEHFLAVNRVIPTNVPELTFQPSPAPDPPGGLTYFPVADLSIIAALYARFTAQIRGAVDLSLYPREGGVSSRELVKKVSDVIWNSLSRSYFKDRAHIQSLFSFITGTKLDSSGVAFAVVGACQALGLRDVHLALSEDHAWVVFGPNGEQTAEVTWHGKGNEDRRGQTVNAGVAERSWLYLKGSYMRCDRKMEVAFMVCAINPSIDLHTDSLELLQLQQKLLWLLYDLGHLERYPMALGNLADLEELEPTPGRPDPLTLYHKGIASAKTYYQDEHIYPYMYLAGYHCRNRNVREALQAWADTATVIQDYNYCREDEEIYKEFFEVANDVIPNLLKEAASLLETGEERTGEQAQGTQGQGSALQDPECFAHLLRFYDGICKWEEGSPTPVLHVGWATFLVQSLGRFEGQVRQKVHIVSREAEAAEAEEPWGDEAREGRRRGPRRESKPEEPPPPKKPALDKGPGSGQSAGSGPPRKTSGTVPGTTRGGQEVGNAAQAPAPAASPPPEGPVLTFQSEKMKGMKELLVATKINSSAIKLQLTAQSQVQMKKQKVSTPSDYTLSFLKRQRKGL
| null | null |
cell division [GO:0051301]; cell population proliferation [GO:0008283]; chromatin remodeling [GO:0006338]; embryonic skeletal system morphogenesis [GO:0048704]; fibroblast apoptotic process [GO:0044346]; fibroblast proliferation [GO:0048144]; hemopoiesis [GO:0030097]; leukocyte homeostasis [GO:0001776]; maternal process involved in female pregnancy [GO:0060135]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell cycle G1/S phase transition [GO:1902807]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of organ growth [GO:0046621]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of stem cell proliferation [GO:2000647]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of type B pancreatic cell proliferation [GO:1904691]; organ growth [GO:0035265]; ossification [GO:0001503]; osteoblast development [GO:0002076]; osteoblast fate commitment [GO:0002051]; positive regulation of cell division [GO:0051781]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fibroblast apoptotic process [GO:2000271]; positive regulation of gene expression [GO:0010628]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of stem cell differentiation [GO:2000738]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of activin receptor signaling pathway [GO:0032925]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of type B pancreatic cell proliferation [GO:0061469]; response to transforming growth factor beta [GO:0071559]; roof of mouth development [GO:0060021]; stem cell differentiation [GO:0048863]; stem cell proliferation [GO:0072089]; transcription initiation-coupled chromatin remodeling [GO:0045815]; type B pancreatic cell differentiation [GO:0003309]; type B pancreatic cell proliferation [GO:0044342]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity [GO:0001216]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]; Y-form DNA binding [GO:0000403]
|
PF05053;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9824159}. Note=May be perinuclear in testis. {ECO:0000269|PubMed:9824159}.
| null | null | null | null | null |
FUNCTION: Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression (By similarity). May be involved in normal hematopoiesis through the activation of HOXA9 expression. May be involved in DNA repair. {ECO:0000250|UniProtKB:O00255, ECO:0000269|PubMed:16415155}.
|
Mus musculus (Mouse)
|
O88561
|
S27A3_MOUSE
|
MAALLLLLPLLLLLPLLLKLDVWPQLRWLPADLAFTVRALRCKRALRARALAAAAADPESSESGCSLAWRLAYLAREQPTHTFLIHGAQRFSYAEAERESNRIARAFLRARGWTGGRRGSGRGSTEEGARVAPPAGDAAARGTTAPPLAPGATVALLLPAGPDFLWIWFGLAKAGLRTAFVPTALRRGPLLHCLRSCGASALVLATEFLESLEPDLPALRAMGLHLWATGPETNVAGISNLLSEAADQVDEPVPGYLSAPQNIMDTCLYIFTSGTTGLPKAARISHLKVLQCQGFYHLCGVHQEDVIYLALPLYHMSGSLLGIVGCLGIGATVVLKPKFSASQFWDDCQKHRVTVFQYIGELCRYLVNQPPSKAECDHKVRLAVGSGLRPDTWERFLRRFGPLQILETYGMTEGNVATFNYTGRQGAVGRASWLYKHIFPFSLIRYDVMTGEPIRNAQGHCMTTSPGEPGLLVAPVSQQSPFLGYAGAPELAKDKLLKDVFWSGDVFFNTGDLLVCDEQGFLHFHDRTGDTIRWKGENVATTEVAEVLETLDFLQEVNIYGVTVPGHEGRAGMAALALRPPQALNLVQLYSHVSENLPPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSVLSDPLYVLDQDIGAYLPLTPARYSALLSGDLRI
|
6.2.1.-; 6.2.1.15; 6.2.1.3
| null |
acyl-CoA metabolic process [GO:0006637]; long-chain fatty acid metabolic process [GO:0001676]
|
endoplasmic reticulum membrane [GO:0005789]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; fatty-acyl-CoA synthase activity [GO:0004321]; long-chain fatty acid transporter activity [GO:0005324]; long-chain fatty acid-CoA ligase activity [GO:0004467]; very long-chain fatty acid-CoA ligase activity [GO:0031957]
|
PF00501;PF13193;
|
3.30.300.30;3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
| null |
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000269|PubMed:15469937}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879, ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000269|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000269|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15469937}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000269|PubMed:15469937}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5K4L6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000250|UniProtKB:Q5K4L6}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651, ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q5K4L6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652; Evidence={ECO:0000250|UniProtKB:Q5K4L6}; CATALYTIC ACTIVITY: Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537; Evidence={ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate + tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640; Evidence={ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031};
| null | null | null | null |
FUNCTION: Mainly functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:15469937, PubMed:15699031). Can mediate the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across membranes (PubMed:15699031). {ECO:0000269|PubMed:15469937, ECO:0000269|PubMed:15699031}.
|
Mus musculus (Mouse)
|
O88563
|
MRP3_RAT
|
MDRLCGSGELGSKFWDSNLTVYTNTPDLTPCFQNSLLAWVPCIYLWAALPCYLFYLRHHRLGYIVLSCLSRLKTALGVLLWCISWVDLFYSFHGLVHGSSPAPVFFITPLLVGITMLLATLLIQYERLRGVRSSGVLIIFWLLCVICAIIPFRSKILLALAEGKILDPFRFTTFYIYFALVLCAFILSCFQEKPPLFSPENLDTNPCPEASAGFFSRLSFWWFTKLAILGYRRPLEDSDLWSLSEEDCSHKVVQRLLEAWQKQQTQASGPQTAALEPKIAGEDEVLLKARPKTKKPSFLRALVRTFTSSLLMGACFKLIQDLSPSSTHSCSASSSGLFRPHGPYWWGFLLAGLMFVSSTMQTLILHQHYHCIFVMALRIRTAIIGVIYRKALTITNSVKREYTVGEMVNLMSVDAQRFMDVSPFINLLWSAPLQVILAIYFLWQILGPSALAGVAVIVLLIPLNGAVSMKMKTYQVQQMKFKDSRIKLMSEILNGIKVLKLYAWEPTFLEQVEGIRQGELQLLRKGAYLQAISTFIWVCTPFMVTLITLGVYVCVDKNNVLDAEKAFVSLSLFNILKIPLNLLPQLISGMTQTSVSLKRIQDFLNQDELDPQCVERKTISPGRAITIHNGTFSWSKDLPPTLHSINIQIPKGALVAVVGPVGCGKSSLVSALLGEMEKLEGAVSVKGSVAYVPQQAWIQNCTLQENVLFGQPMNPKRYQQALETCALLADLDVLPGGDQTEIGEKGINLSGGQRQRVSLARAVYSDANIFLLDDPLSAVDSHVAKHIFDQVIGPEGVLAGKTRVLVTHGISFLPQTDFIIVLADGQITEMGHYSELLQHDGSFANFLRNYAPDENQEANEGVLQHANEEVLLLEDTLSTHTDLTDTEPAIYEVRKQFMREMSSLSSEGEGQNRPVLKRYTSSLEKEVPATQTKETGALIKEEIAETGNVKLSVYWDYAKSVGLCTTLFICLLYAGQNAVAIGANVWLSAWTNDVEEHGQQNNTSVRLGVYATLGILQGLLVMLSAFTMVVGAIQAARLLHTALLHNQIRAPQSFFDTTPSGRILNRFSKDIYVIHEVLAPTILMLFNSFYTSISTIVVIVASTPLFCVVVLPLAVFYGFVQRFYVATSRQLKRLESVSRSPIFSHFSETVTGTSVIRAYGRVQDFKVLSDAKVDSNQKTTYPYIASNRWLGVHVEFVGNCVVLFSALFAVIGRNSLNPGLVGLSVSYALQVTLSLNWMIRTLSDLESNIIAVERVKEYSKTETEAPWVLESNRAPEGWPRSGVVEFRNYSVRYRPGLELVLKNLTLHVQGGEKVGIVGRTGAGKSSMTLCLFRILEAAEGEIFIDGLNVAHIGLHDLRSQLTIIPQDPILFSGTLRMNLDPFGRYSDEDIWRTLELSHLSAFVSSQPTGLDFQCSEGGDNLSVGQRQLVCLARALLRKSRVLVLDEATAAIDLETDDLIQGTIRTQFEDCTVLTIAHRLNTIMDYNRVLVLDKGVVAEFDSPVNLIAAGGIFYGMAKDAGLA
|
7.6.2.-; 7.6.2.2; 7.6.2.3
| null |
bile acid and bile salt transport [GO:0015721]; canalicular bile acid transport [GO:0015722]; leukotriene transport [GO:0071716]; monoatomic anion transmembrane transport [GO:0098656]; response to estradiol [GO:0032355]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014070]; response to organic substance [GO:0010033]; response to organonitrogen compound [GO:0010243]; transmembrane transport [GO:0055085]; xenobiotic transmembrane transport [GO:0006855]; xenobiotic transport [GO:0042908]
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basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
ABC-type bile acid transporter activity [GO:0015432]; ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; glucuronoside transmembrane transporter activity [GO:0015164]; icosanoid transmembrane transporter activity [GO:0071714]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
| null |
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:11897632}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000250|UniProtKB:O15438}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779, ChEBI:CHEBI:456216; EC=7.6.2.3; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10644759}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053; Evidence={ECO:0000305|PubMed:10644759}; CATALYTIC ACTIVITY: Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10644759}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057; Evidence={ECO:0000305|PubMed:10644759}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) + phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10644759}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10644759}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; Evidence={ECO:0000305|PubMed:10644759}; CATALYTIC ACTIVITY: Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=(4Z,15Z)-bilirubin IXalpha C8-beta-D-glucuronoside(in) + ATP + H2O = (4Z,15Z)-bilirubin IXalpha C8-beta-D-glucuronoside(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66180, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:229704, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66181; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=(4Z,15Z)-bilirubin IXalpha C8,C12-beta-D-bisglucuronoside(in) + ATP + H2O = (4Z,15Z)-bilirubin IXalpha C8,C12-beta-D-bisglucuronoside(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66192, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:229706, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66193; Evidence={ECO:0000250|UniProtKB:O15438}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurochenodeoxycholate 3-sulfate(in) = ADP + H(+) + phosphate + taurochenodeoxycholate 3-sulfate(out); Xref=Rhea:RHEA:66176, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:166912, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10644759}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66177; Evidence={ECO:0000305|PubMed:10644759};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.36 uM for ATP (determined by measuring estradiol-17-beta-o-glucuronide transport) {ECO:0000269|PubMed:10644759}; KM=3.06 uM for taurolithocholate sulfate {ECO:0000269|PubMed:10644759}; KM=15.9 uM for taurocholate {ECO:0000269|PubMed:10644759}; Vmax=161.9 pmol/min/mg enzyme for taurolithocholate-3-sulfate {ECO:0000269|PubMed:10644759}; Vmax=50.1 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:10644759};
| null | null | null |
FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (By similarity). Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate). Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (By similarity). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity). {ECO:0000250|UniProtKB:B2RX12, ECO:0000250|UniProtKB:O15438}.
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Rattus norvegicus (Rat)
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O88566
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AXIN2_MOUSE
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MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSDPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVDGVPPYRMGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPAAFAAELISRLEKLKLELESRHSLEERLQQIREDEEKEGSEQALSSRDGAPVQHPLALLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHQHHHHQQCHTLLPTGGKLPPVAACPLLGGKSFLTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVRCLCPGGTDYYCYSKCKSHPKAPEPLPGEQFCGSRGGTLPKRNAKGTEPGLALSARDGGMSSAAGAPQLPGEEGDRSQDVWQWMLESERQSKSKPHSAQSIRKSYPLESACAAPGERVSRHHLLGASGHSRSVARAHPFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPQKQRCCVASQQRDRNHSAAGQAGASPFANPSLAPEDHKEPKKLASVHALQASELVVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWDDETVLPMYEGRILGKVERID
| null | null |
aortic valve morphogenesis [GO:0003180]; bone mineralization [GO:0030282]; canonical Wnt signaling pathway [GO:0060070]; cell development [GO:0048468]; cell population proliferation [GO:0008283]; cellular response to dexamethasone stimulus [GO:0071549]; chondrocyte differentiation involved in endochondral bone morphogenesis [GO:0003413]; dorsal/ventral axis specification [GO:0009950]; intramembranous ossification [GO:0001957]; maintenance of DNA repeat elements [GO:0043570]; mitral valve morphogenesis [GO:0003183]; mRNA stabilization [GO:0048255]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of Wnt signaling pathway [GO:0030178]; odontogenesis [GO:0042476]; osteoblast differentiation [GO:0001649]; osteoblast proliferation [GO:0033687]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein phosphorylation [GO:0001934]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein localization [GO:0008104]; regulation of centromeric sister chromatid cohesion [GO:0070602]; regulation of chondrocyte development [GO:0061181]; regulation of extracellular matrix organization [GO:1903053]; regulation of mismatch repair [GO:0032423]; regulation of Wnt signaling pathway [GO:0030111]; secondary heart field specification [GO:0003139]; somitogenesis [GO:0001756]; stem cell proliferation [GO:0072089]
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beta-catenin destruction complex [GO:0030877]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
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beta-catenin binding [GO:0008013]; I-SMAD binding [GO:0070411]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]; ubiquitin protein ligase binding [GO:0031625]
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PF16646;PF08833;PF00778;PF00615;
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1.10.196.10;2.40.240.130;1.10.167.10;
| null |
PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination and subsequent activation of the Wnt signaling pathway. {ECO:0000250|UniProtKB:Q9Y2T1}.; PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation and subsequent activation of the Wnt signaling pathway. Deubiquitinated by USP34, deubiquitinated downstream of beta-catenin stabilization step: deubiquitination is important Wnt signaling to positively regulate beta-catenin (CTNBB1)-mediated transcription. {ECO:0000250|UniProtKB:Q9Y2T1}.; PTM: Probably phosphorylated by GSK3B and dephosphorylated by PP2A. {ECO:0000250|UniProtKB:O15169}.
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SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2T1}.
| null | null | null | null | null |
FUNCTION: Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B. {ECO:0000250|UniProtKB:O15169}.
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Mus musculus (Mouse)
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O88569
|
ROA2_MOUSE
|
MEKTLETVPLERKKREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGSYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY
| null | null |
G-quadruplex DNA unwinding [GO:0044806]; miRNA transport [GO:1990428]; mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; mRNA splicing, via spliceosome [GO:0000398]; mRNA transport [GO:0051028]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of telomere maintenance via telomere lengthening [GO:1904358]; primary miRNA processing [GO:0031053]; RNA transport [GO:0050658]; telomere capping [GO:0016233]
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Cajal body [GO:0015030]; catalytic step 2 spliceosome [GO:0071013]; chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; neuronal ribonucleoprotein granule [GO:0071598]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; perikaryon [GO:0043204]; postsynaptic cytosol [GO:0099524]; postsynaptic density [GO:0014069]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681]
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DNA polymerase binding [GO:0070182]; G-rich strand telomeric DNA binding [GO:0098505]; miRNA binding [GO:0035198]; molecular condensate scaffold activity [GO:0140693]; mRNA 3'-UTR binding [GO:0003730]; mRNA CDS binding [GO:1990715]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; pre-mRNA intronic binding [GO:0097157]; regulatory region RNA binding [GO:0001069]; RNA binding [GO:0003723]; single-stranded telomeric DNA binding [GO:0043047]
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PF11627;PF00076;
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3.30.70.330;
| null |
PTM: Sumoylated in exosomes, promoting miRNAs-binding. {ECO:0000250|UniProtKB:P22626}.; PTM: Asymmetric dimethylation at Arg-266 constitutes the major methylation site (By similarity). According to a report, methylation affects subcellular location and promotes nuclear localization (By similarity). According to another report, methylation at Arg-266 does not influence nucleocytoplasmic shuttling (By similarity). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626}.
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SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31320558}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P22626}. Cytoplasm {ECO:0000269|PubMed:31320558}. Cytoplasmic granule {ECO:0000250|UniProtKB:P22626}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P22626}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Not found in the nucleolus. Found in exosomes following sumoylation. {ECO:0000250|UniProtKB:P22626}.
| null | null | null | null | null |
FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs. Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (By similarity). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts. Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs. Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (By similarity). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). Also plays a role in the activation of the innate immune response. Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6. In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558). {ECO:0000250|UniProtKB:A7VJC2, ECO:0000250|UniProtKB:P22626, ECO:0000269|PubMed:31320558}.
|
Mus musculus (Mouse)
|
O88572
|
LRP6_MOUSE
|
MGAVLRSLLACSFCVLLRAAPLLLYANRRDLRLVDATNGKENATIVVGGLEDAAAVDFVFGHGLIYWSDVSEEAIKRTEFNKSESVQNVVVSGLLSPDGLACDWLGEKLYWTDSETNRIEVSNLDGSLRKVLFWQELDQPRAIALDPSSGFMYWTDWGEVPKIERAGMDGSSRFVIINTEIYWPNGLTLDYQERKLYWADAKLNFIHKSNLDGTNRQAVVKGSLPHPFALTLFEDTLYWTDWNTHSILACNKYTGEGLREIHSNIFSPMDIHAFSQQRQPNATNPCGIDNGGCSHLCLMSPVKPFYQCACPTGVKLMENGKTCKDGATELLLLARRTDLRRISLDTPDFTDIVLQLEDIRHAIAIDYDPVEGYIYWTDDEVRAIRRSFIDGSGSQFVVTAQIAHPDGIAVDWVARNLYWTDTGTDRIEVTRLNGTMRKILISEDLEEPRAIVLDPMVGYMYWTDWGEIPKIERAALDGSDRVVLVNTSLGWPNGLALDYDEGTIYWGDAKTDKIEVMNTDGTGRRVLVEDKIPHIFGFTLLGDYVYWTDWQRRSIERVHKRSAEREVIIDQLPDLMGLKATSVHRVIGSNPCAEDNGGCSHLCLYRPQGLRCACPIGFELIGDMKTCIVPEAFLLFSRRADIRRISLETNNNNVAIPLTGVKEASALDFDVTDNRIYWTDISLKTISRAFMNGSALEHVVEFGLDYPEGMAVDWLGKNLYWADTGTNRIEVSKLDGQHRQVLVWKDLDSPRALALDPAEGFMYWTEWGGKPKIDRAAMDGSERTTLVPNVGRANGLTIDYAKRRLYWTDLDTNLIESSDMLGLNREVIADDLPHPFGLTQYQDYIYWTDWSRRSIERANKTSGQNRTIIQGHLDYVMDILVFHSSRQAGWNECASSNGHCSHLCLAVPVGGFVCGCPAHYSLNADNRTCSAPSTFLLFSQKSAINRMVIDEQQSPDIILPIHSLRNVRAIDYDPLDKQLYWIDSRQNSIRKAHEDGGQGFNVVANSVANQNLEIQPYDLSIDIYSRYIYWTCEATNVIDVTRLDGRSVGVVLKGEQDRPRAIVVNPEKGYMYFTNLQERSPKIERAALDGTEREVLFFSGLSKPIALALDSKLGKLFWADSDLRRIESSDLSGANRIVLEDSNILQPVGLTVFENWLYWIDKQQQMIEKIDMTGREGRTKVQARIAQLSDIHAVKELNLQEYRQHPCAQDNGGCSHICLVKGDGTTRCSCPMHLVLLQDELSCGEPPTCSPQQFTCFTGDIDCIPVAWRCDGFTECEDHSDELNCPVCSESQFQCASGQCIDGALRCNGDANCQDKSDEKNCEVLCLIDQFRCANGQCVGKHKKCDHSVDCSDRSDELDCYPTEEPAPQATNTVGSVIGVIVTIFVSGTIYFICQRMLCPRMKGDGETMTNDYVVHSPASVPLGYVPHPSSLSGSLPGMSRGKSMISSLSIMGGSSGPPYDRAHVTGASSSSSSSTKGTYFPAILNPPPSPATERSHYTMEFGYSSNSPSTHRSYSYRPYSYRHFAPPTTPCSTDVCDSDYAPSRRMTSVATAKGYTSDVNYDSEPVPPPPTPRSQYLSAEENYESCPPSPYTERSYSHHLYPPPPSPCTDSS
| null | null |
anterior/posterior pattern specification [GO:0009952]; axis elongation [GO:0003401]; axis elongation involved in somitogenesis [GO:0090245]; bone remodeling [GO:0046849]; branching involved in mammary gland duct morphogenesis [GO:0060444]; canonical Wnt signaling pathway [GO:0060070]; cardiac muscle tissue morphogenesis [GO:0055008]; cell migration involved in gastrulation [GO:0042074]; cell-cell adhesion [GO:0098609]; cerebellum morphogenesis [GO:0021587]; cerebral cortex cell migration [GO:0021795]; cerebral cortex development [GO:0021987]; chemical synaptic transmission [GO:0007268]; convergent extension [GO:0060026]; dopaminergic neuron differentiation [GO:0071542]; dorsal/ventral axis specification [GO:0009950]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic limb morphogenesis [GO:0030326]; embryonic pattern specification [GO:0009880]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; establishment of blood-brain barrier [GO:0060856]; establishment of blood-retinal barrier [GO:1990963]; external genitalia morphogenesis [GO:0035261]; face morphogenesis [GO:0060325]; fat cell differentiation [GO:0045444]; forebrain development [GO:0030900]; forebrain generation of neurons [GO:0021872]; forebrain radial glial cell differentiation [GO:0021861]; formation of radial glial scaffolds [GO:0021943]; gastrulation with mouth forming second [GO:0001702]; generation of neurons [GO:0048699]; heart looping [GO:0001947]; limb morphogenesis [GO:0035108]; mammary gland duct morphogenesis [GO:0060603]; mammary placode formation [GO:0060596]; mesenchymal cell proliferation [GO:0010463]; mesodermal cell migration [GO:0008078]; midbrain development [GO:0030901]; midbrain-hindbrain boundary development [GO:0030917]; negative regulation of developmental process [GO:0051093]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of morphogenesis of an epithelium [GO:1905331]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; negative regulation of planar cell polarity pathway involved in cardiac muscle tissue morphogenesis [GO:2000151]; negative regulation of planar cell polarity pathway involved in neural tube closure [GO:2000168]; negative regulation of planar cell polarity pathway involved in outflow tract morphogenesis [GO:2000164]; negative regulation of planar cell polarity pathway involved in pericardium morphogenesis [GO:2000166]; negative regulation of planar cell polarity pathway involved in ventricular septum morphogenesis [GO:2000149]; neural tube closure [GO:0001843]; neural tube development [GO:0021915]; Norrin signaling pathway [GO:0110135]; odontogenesis of dentin-containing tooth [GO:0042475]; outflow tract morphogenesis [GO:0003151]; pericardium morphogenesis [GO:0003344]; positive regulation of apoptotic process [GO:0043065]; positive regulation of bone resorption [GO:0045780]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of neuron projection development [GO:0010976]; positive regulation of ossification [GO:0045778]; positive regulation of stem cell proliferation [GO:2000648]; post-anal tail morphogenesis [GO:0036342]; primitive streak formation [GO:0090009]; receptor-mediated endocytosis involved in cholesterol transport [GO:0090118]; regulation of anatomical structure morphogenesis [GO:0022603]; regulation of cell development [GO:0060284]; regulation of DNA-templated transcription [GO:0006355]; regulation of epithelial cell proliferation [GO:0050678]; response to folic acid [GO:0051593]; retina morphogenesis in camera-type eye [GO:0060042]; roof of mouth development [GO:0060021]; skeletal system morphogenesis [GO:0048705]; somitogenesis [GO:0001756]; stem cell proliferation [GO:0072089]; thalamus development [GO:0021794]; trachea cartilage morphogenesis [GO:0060535]; ventricular septum morphogenesis [GO:0060412]; Wnt signaling pathway involved in forebrain neuroblast division [GO:0021874]; Wnt signaling pathway involved in somitogenesis [GO:0090244]
|
early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
apolipoprotein binding [GO:0034185]; low-density lipoprotein particle receptor activity [GO:0005041]; toxin transmembrane transporter activity [GO:0019534]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
|
PF14670;PF00057;PF00058;
|
4.10.400.10;2.120.10.30;
|
LDLR family
|
PTM: Dual phosphorylation of cytoplasmic PPPSP motifs sequentially by GSK3 and CK1 is required for AXIN1-binding, and subsequent stabilization and activation of beta-catenin via preventing GSK3-mediated phosphorylation of beta-catenin. Phosphorylated, in vitro, by GRK5/6 within and outside the PPPSP motifs. Phosphorylation at Ser-1490 by CDK14 during G2/M phase leads to regulation of the Wnt signaling pathway during the cell cycle. Phosphorylation by GSK3B is induced by RPSO1 binding and inhibited by DKK1. Phosphorylated, in vitro, by casein kinase I on Thr-1479 (By similarity). {ECO:0000250}.; PTM: Undergoes gamma-secretase-dependent regulated intramembrane proteolysis (RIP). The extracellular domain is first released by shedding, and then, through the action of gamma-secretase, the intracellular domain (ICD) is released into the cytoplasm where it is free to bind to GSK3B and to activate canonical Wnt signaling (By similarity). {ECO:0000250}.; PTM: Palmitoylation on the two sites near the transmembrane domain leads to release of LRP6 from the endoplasmic reticulum. {ECO:0000250}.; PTM: Mono-ubiquitinated which retains LRP6 in the endoplasmic reticulum. Ubiquitinated by ZNRF3, leading to its degradation by the proteasome (By similarity). {ECO:0000250}.; PTM: N-glycosylation is required for cell surface location. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum. Membrane raft {ECO:0000250|UniProtKB:O75581}. Note=On Wnt signaling, undergoes a cycle of caveolin- or clathrin-mediated endocytosis and plasma membrane location. Released from the endoplasmic reticulum on palmitoylation. Mono-ubiquitination retains it in the endoplasmic reticulum in the absence of palmitoylation. On Wnt signaling, phosphorylated, aggregates and colocalizes with AXIN1 and GSK3B at the plasma membrane in LRP6-signalosomes (By similarity). Chaperoned to the plasma membrane by MESD. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes. Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation. The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalosomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin. Required for posterior patterning of the epiblast during gastrulation (By similarity). {ECO:0000250, ECO:0000269|PubMed:15142971}.
|
Mus musculus (Mouse)
|
O88574
|
SAP30_MOUSE
|
MNGFTPEEMSRGGDAAAAVAAVVAAAAAAASAGNGNAAGGGAEVPGAGAVSASGPPGAAGPGPGQLCCLREDGERCGRAAGNASFSKRIQKSISQKKVKIELDKSARHLYICDYHKNLIQSVRNRRKRKGSDDDGGDSPVQDIDTPEVDLYQLQVNTLRRYKRHFKLPTRPGLNKAQLVEIVGCHFKSIPVNEKDTLTCFIYSVRNDKNKSDLKADSGVH
| null | null |
modulation by host of symbiont transcription [GO:0052472]; negative regulation of cell migration [GO:0030336]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of stem cell population maintenance [GO:1902459]; regulation of DNA-templated transcription [GO:0006355]; skeletal muscle cell differentiation [GO:0035914]
|
histone deacetylase complex [GO:0000118]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; Sin3-type complex [GO:0070822]
|
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]
|
PF13867;PF13866;
|
6.10.160.20;
|
SAP30 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Involved in the functional recruitment of the Sin3-histone deacetylase complex (HDAC) to a specific subset of N-CoR corepressor complexes. Capable of transcription repression by N-CoR. Active in deacetylating core histone octamers (when in a complex) but inactive in deacetylating nucleosomal histones. {ECO:0000250|UniProtKB:O75446, ECO:0000269|PubMed:9702189}.
|
Mus musculus (Mouse)
|
O88575
|
S620B_MOUSE
|
MESPSAHAVSLPEDEELQPWGGAGGPGQHPGRPRSTECAHPGVVEKVRPKWDNPLQFLLVCISYAVGLGNVWRFPYLCQMYGGGNFLVPYIIMLIVEGMPLLYLELAVGQRMRQGSIGAWRTISPYLSGVGIASLVVSFLASVYFNVINTWALWYLFHSFQDPLPWSVCPLNSNHTGYDEECEKASSTQYFWYRKTLNISPSIQENGGVQWEPALCLTLAWLMVYLCILRGTESTGKVVYFTTSLPYFVLIIYLVRGLTLHGATNGLAYMFTPKIEQLANPKAWINAATQIFFSLGLGCGGLIAFASYNEPSNDCQKHALIVSVINSTTAIFSSIVTFSIYGFKATFNYENCLNKVILLLTNSFDLEDGFLTVSNLEEVKNYLASTYPNKYSEVFPHIRNCSLESELDTAVQGTGLAFIVYTEAIKNMEVSQLWSVLYFFMLLTLGMGSMVGTGTAILTPLTDSKIISSYLPKEAISGLVCLLNCAIGMVFTMEAGNYWFDLFNDYTATLSLLLIVLVETIAVCYVYGLKRFESDLRAMTGRTLSWYWKVMWAFVSPLLIVGLFIFYLSDYILTGTLQYQAWDATQGHVVTKDYPTYALAVIGLLVASSTMCIPLVALGTFVTRHFKIREQFSAA
| null | null |
glycine transport [GO:0015816]; L-proline import across plasma membrane [GO:1904271]; sodium ion transmembrane transport [GO:0035725]
|
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; plasma membrane [GO:0005886]
|
L-proline transmembrane transporter activity [GO:0015193]; proline:sodium symporter activity [GO:0005298]
|
PF00209;
| null |
Sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family, SLC6A20 subfamily
| null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16174864}; Multi-pass membrane protein {ECO:0000269|PubMed:16174864}. Note=Located in the apical brush border membrane of kidney proximal tubule cells.
| null | null | null | null | null |
FUNCTION: Does not show transporter activity with a range of tested amino acids including proline, glutamine, glutamic acid, leucine, alanine, histidine, glycine and arginine. {ECO:0000269|PubMed:15689184}.
|
Mus musculus (Mouse)
|
O88576
|
S6A18_MOUSE
|
MAQASGMDPLVDIEDERPKWDNKLQYLLSCIGFAVGLGNIWRFPYLCQTHGGGAFLIPYFIALVFEGIPLFYIELAIGQRLRRGSIGVWKTISPYLGGVGLGCFSVSFLVSLYYNTVLLWVLWFFLNSFQHPLPWSTCPLDLNRTGFVQECQSSGTVSYFWYRQTLNITSDISNTGTIQWKLFLCLVACWSTVYLCVIRGIESTGKVIYFTALFPYLVLTIFLIRGLTLPGATEGLIYLFTPNMKTLQNPRVWLDAATQIFFSLSLAFGGHIAFASYNPPRNNCEKDAVIIALVNSMTSLYASIAIFSVMGFKASNDYGRCLDRNILSLINEFDLPELSISRDEYPSVLMYLNATQTARVAQLPLKTCHLEDFLDKSASGPGLAFIVFTEAVLHMPGASVWSVLFFGMLFTLGLSSMFGNMEGVITPLLDMGILPKGIPKEVMTGVICFACFLSAICFTLQSGGYWLEIFDSFAASLNLIIFAFMEVVGVIHIYGMKRFCDDIEWMTGRRPGLYWQVTWRVVSPMLLFGIFLSYIVLLIQTPPSYKAWNPQYEHFPSREEKFYPGWVQVTCVLLSFLPSLWVPGVALAQLLSQYKQRWKATHLESGLKLQESRGC
| null | null |
amino acid transmembrane transport [GO:0003333]; amino acid transport [GO:0006865]; neurotransmitter transport [GO:0006836]; neutral amino acid transport [GO:0015804]; renal amino acid absorption [GO:1990297]; sodium ion transmembrane transport [GO:0035725]
|
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; plasma membrane [GO:0005886]
|
neutral L-amino acid transmembrane transporter activity [GO:0015175]; neutral L-amino acid:sodium:chloride symporter activity [GO:0140931]
|
PF00209;
| null |
Sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family, SLC6A18 subfamily
| null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:20377526, ECO:0000269|PubMed:26240152}; Multi-pass membrane protein {ECO:0000255}. Note=In kidneys localizes to the apical membrane in distal segments of the proximal tubule (PubMed:19478081, PubMed:20377526). Cell membrane expression is CLTRN-dependent (PubMed:20377526). {ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526}.
|
CATALYTIC ACTIVITY: Reaction=chloride(out) + L-alanine(out) + 2 Na(+)(out) = chloride(in) + L-alanine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71311, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526, ECO:0000269|PubMed:26240152}; CATALYTIC ACTIVITY: Reaction=chloride(out) + glycine(out) + 2 Na(+)(out) = chloride(in) + glycine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70691, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57305; Evidence={ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526}; CATALYTIC ACTIVITY: Reaction=chloride(out) + L-methionine(out) + 2 Na(+)(out) = chloride(in) + L-methionine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71303, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844; Evidence={ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526}; CATALYTIC ACTIVITY: Reaction=chloride(out) + L-valine(out) + 2 Na(+)(out) = chloride(in) + L-valine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71307, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57762; Evidence={ECO:0000269|PubMed:19478081}; CATALYTIC ACTIVITY: Reaction=chloride(out) + L-isoleucine(out) + 2 Na(+)(out) = chloride(in) + L-isoleucine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71299, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:58045; Evidence={ECO:0000269|PubMed:19478081}; CATALYTIC ACTIVITY: Reaction=chloride(out) + L-serine(out) + 2 Na(+)(out) = chloride(in) + L-serine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71315, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; Evidence={ECO:0000269|PubMed:19478081}; CATALYTIC ACTIVITY: Reaction=chloride(out) + L-leucine(out) + 2 Na(+)(out) = chloride(in) + L-leucine(in) + 2 Na(+)(in); Xref=Rhea:RHEA:71279, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.79 mM for L-alanine (in the presence of CLTRN) {ECO:0000269|PubMed:26240152}; KM=0.14 mM for L-alanine (in the presence of ACE2) {ECO:0000269|PubMed:26240152}; KM=0.99 mM for L-glycine (in the presence of CLTRN) {ECO:0000269|PubMed:26240152}; KM=0.27 mM for L-glycine (in the presence of ACE2) {ECO:0000269|PubMed:26240152}; KM=0.9 mM for L-alanine (in the presence of CLTRN) {ECO:0000269|PubMed:20377526}; KM=2.3 mM for L-glycine (in the presence of CLTRN) {ECO:0000269|PubMed:20377526};
| null | null | null |
FUNCTION: Symporter that transports one amino acid molecule together with two sodium and one chloride ions in kidneys and plays a role in the neutral amino acids reabsorption (PubMed:19478081, PubMed:20377526, PubMed:26240152). Preferentially transports neutral amino acids such as L-glycine and L-alanine but also other neutral amino acids (PubMed:19478081, PubMed:20377526, PubMed:26240152). Required CLTRN for cell surface expression and for its amino acid transporter activity (PubMed:20377526, PubMed:26240152). The transport mechanism is pH-independent (PubMed:19478081). {ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:20377526, ECO:0000269|PubMed:26240152}.
|
Mus musculus (Mouse)
|
O88582
|
SOCS2_RAT
|
MTLRCLEPSGNGADRTRSQWGTAGSPEDQSPEAARLAKALRELSQTGWYWGSMTVNEAKEKLKEAPEGTFLIRDSSHSDYLLTISVKTSAGPTNLRIEYQDGKFRLDSIICVKSKLKQFDSVVHLIDYYVQMCKDKRTGPEAPRNGTVHLYLTKPLYTSAPTLQHFCRLSINKCTGTIRGLPLPTRLKDYLEEYKFQV
| null | null |
cellular response to hormone stimulus [GO:0032870]; growth hormone receptor signaling pathway [GO:0060396]; intracellular signal transduction [GO:0035556]; lactation [GO:0007595]; mammary gland alveolus development [GO:0060749]; negative regulation of multicellular organism growth [GO:0040015]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; positive regulation of neuron differentiation [GO:0045666]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of multicellular organism growth [GO:0040014]; response to estradiol [GO:0032355]; response to peptide hormone [GO:0043434]
|
phosphatidylinositol 3-kinase complex [GO:0005942]
|
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; growth hormone receptor binding [GO:0005131]; insulin-like growth factor receptor binding [GO:0005159]
|
PF00017;PF07525;
|
3.30.505.10;1.10.750.20;
| null |
PTM: Ubiquitinated; mediated by AREL1 and leading to its subsequent proteasomal degradation. Ubiquitination is dependent on phosphorylation at Ser-52, by PKC and is stimulated by LPS. {ECO:0000250|UniProtKB:O35717}.; PTM: Phosphorylation at Ser-52 by PKC facilitates its ubiquitination and proteasomal degradation. {ECO:0000250|UniProtKB:O35717}.
| null | null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS2 appears to be a negative regulator in the growth hormone/IGF1 signaling pathway. Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88583
|
SOCS3_RAT
|
MVTHSKFPAAGMSRPLDTSLRLKTFSSKSEYQLVVNAVRKLQESGFYWSAVTGGEANLLLSAEPAGTFLIRDSSDQRHFFTLSVETQSGTKNLRIQCEGGSFSLQSDPRSTQPVPRFDCVLKLVHHYMPPPGAPSFSLPPTEPSFEVQEQPPAQALPGGTPKRAYYIYSGGEKIPLVLSRPLSSNVATLQHLCRKTVNGHLDSYEKVTQLPGPIREFLDQYDAPL
| null | null |
animal organ regeneration [GO:0031100]; branching involved in labyrinthine layer morphogenesis [GO:0060670]; cell differentiation [GO:0030154]; cellular response to interleukin-17 [GO:0097398]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to thyrotropin-releasing hormone [GO:1905229]; cellular response to type II interferon [GO:0071346]; intracellular signal transduction [GO:0035556]; negative regulation of inflammatory response [GO:0050728]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of receptor signaling pathway via JAK-STAT [GO:0046426]; negative regulation of signal transduction [GO:0009968]; negative regulation of tyrosine phosphorylation of STAT protein [GO:0042532]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; placenta blood vessel development [GO:0060674]; positive regulation of cell differentiation [GO:0045597]; protein ubiquitination [GO:0016567]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of cell growth [GO:0001558]; regulation of protein phosphorylation [GO:0001932]; response to bacterium [GO:0009617]; response to cytokine [GO:0034097]; response to estradiol [GO:0032355]; response to food [GO:0032094]; response to gamma radiation [GO:0010332]; response to glucocorticoid [GO:0051384]; response to hormone [GO:0009725]; response to hypoxia [GO:0001666]; response to insulin [GO:0032868]; response to lipopolysaccharide [GO:0032496]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to progesterone [GO:0032570]; response to xenobiotic stimulus [GO:0009410]; signal transduction [GO:0007165]
|
cytoplasmic side of plasma membrane [GO:0009898]; phosphatidylinositol 3-kinase complex [GO:0005942]
|
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; miRNA binding [GO:0035198]; phosphotyrosine residue binding [GO:0001784]; protein tyrosine kinase inhibitor activity [GO:0030292]
|
PF00017;
|
3.30.505.10;1.10.750.20;
| null |
PTM: Phosphorylated on tyrosine residues after stimulation by the cytokines, IL-2, EPO or IGF1. {ECO:0000250}.
| null | null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells (By similarity). Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). {ECO:0000250|UniProtKB:O14543, ECO:0000250|UniProtKB:O35718}.
|
Rattus norvegicus (Rat)
|
O88587
|
COMT_MOUSE
|
MLLAAVSLGLLLLAFLLLLRHLGWGLVAIGWFEFVQQPVHNLLMGGTKEQRILRHVQQHAKPGDPQSVLEAIDTYCSEKEWAMNVGDAKGQIMDAVIREYRPSLVLELGAYCGYSAVRMARLLPPGARLLTMEINPDYAAITQQMLDFAGLQDKVSILIGASQDLIPQLKKKYDVDTLDMVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVIVPGTPDFLAYVRGSSSFECTHYSSYLEYMKVVDGLEKAVYQGPGSSPVKS
|
2.1.1.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P22734}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P22734};
|
artery development [GO:0060840]; behavioral fear response [GO:0001662]; catecholamine catabolic process [GO:0042424]; catecholamine metabolic process [GO:0006584]; cellular response to cocaine [GO:0071314]; cellular response to phosphate starvation [GO:0016036]; cerebellar cortex morphogenesis [GO:0021696]; cholesterol efflux [GO:0033344]; cognition [GO:0050890]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; developmental process [GO:0032502]; dopamine catabolic process [GO:0042420]; dopamine metabolic process [GO:0042417]; dopamine secretion [GO:0014046]; estrogen metabolic process [GO:0008210]; exploration behavior [GO:0035640]; fear response [GO:0042596]; female pregnancy [GO:0007565]; gene expression [GO:0010467]; glomerulus development [GO:0032835]; glycogen metabolic process [GO:0005977]; habituation [GO:0046959]; kidney development [GO:0001822]; learning [GO:0007612]; learning or memory [GO:0007611]; mastication [GO:0071626]; memory [GO:0007613]; methylation [GO:0032259]; multicellular organism growth [GO:0035264]; multicellular organismal reproductive process [GO:0048609]; multicellular organismal response to stress [GO:0033555]; negative regulation of dopamine metabolic process [GO:0045963]; negative regulation of smooth muscle cell proliferation [GO:0048662]; norepinephrine metabolic process [GO:0042415]; norepinephrine secretion [GO:0048243]; positive regulation of homocysteine metabolic process [GO:0050668]; prostaglandin metabolic process [GO:0006693]; regulation of blood pressure [GO:0008217]; renal albumin absorption [GO:0097018]; renal filtration [GO:0097205]; renal sodium excretion [GO:0035812]; renin secretion into blood stream [GO:0002001]; response to amphetamine [GO:0001975]; response to angiotensin [GO:1990776]; response to corticosterone [GO:0051412]; response to cytokine [GO:0034097]; response to dopamine [GO:1903350]; response to food [GO:0032094]; response to hypoxia [GO:0001666]; response to inorganic substance [GO:0010035]; response to organic substance [GO:0010033]; response to oxidative stress [GO:0006979]; response to pain [GO:0048265]; response to salt [GO:1902074]; response to temperature stimulus [GO:0009266]; response to toxic substance [GO:0009636]; response to wounding [GO:0009611]; response to xenobiotic stimulus [GO:0009410]; short-term memory [GO:0007614]; startle response [GO:0001964]; synaptic transmission, dopaminergic [GO:0001963]; visual learning [GO:0008542]
|
axon [GO:0030424]; cell body [GO:0044297]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; mitochondrion [GO:0005739]; postsynapse [GO:0098794]; postsynaptic membrane [GO:0045211]; vesicle [GO:0031982]
|
catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; magnesium ion binding [GO:0000287]; orcinol O-methyltransferase activity [GO:0102938]
|
PF01596;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family
| null |
SUBCELLULAR LOCATION: [Isoform Soluble]: Cytoplasm {ECO:0000250|UniProtKB:P22734}.; SUBCELLULAR LOCATION: [Isoform Membrane-bound]: Cell membrane {ECO:0000250|UniProtKB:P22734}; Single-pass type II membrane protein {ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:P22734}.
|
CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17878; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-estrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53108, ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136980; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53109; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53104, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87602, ChEBI:CHEBI:136972; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53105; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53100, ChEBI:CHEBI:1156, ChEBI:CHEBI:1189, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53101; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53096, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:62845, ChEBI:CHEBI:136975; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53097; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53092, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:89268; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53093; Evidence={ECO:0000250|UniProtKB:P21964}; CATALYTIC ACTIVITY: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53088, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:28955, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53089; Evidence={ECO:0000250|UniProtKB:P21964};
| null | null | null | null |
FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol. {ECO:0000269|PubMed:18794526}.
|
Mus musculus (Mouse)
|
O88593
|
PGRP1_MOUSE
|
MLFACALLALLGLATSCSFIVPRSEWRALPSECSSRLGHPVRYVVISHTAGSFCNSPDSCEQQARNVQHYHKNELGWCDVAYNFLIGEDGHVYEGRGWNIKGDHTGPIWNPMSIGITFMGNFMDRVPAKRALRAALNLLECGVSRGFLRSNYEVKGHRDVQSTLSPGDQLYQVIQSWEHYRE
| null | null |
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; apoptotic process [GO:0006915]; biological process involved in interaction with host [GO:0051701]; defense response to Gram-positive bacterium [GO:0050830]; detection of bacterium [GO:0016045]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; negative regulation of inflammatory response [GO:0050728]; negative regulation of natural killer cell differentiation involved in immune response [GO:0032827]; negative regulation of type II interferon production [GO:0032689]; peptidoglycan catabolic process [GO:0009253]; response to bacterium [GO:0009617]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; Hsp70 protein binding [GO:0030544]; molecular adaptor activity [GO:0060090]; N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; peptidoglycan binding [GO:0042834]; peptidoglycan immune receptor activity [GO:0016019]; zinc ion binding [GO:0008270]
|
PF01510;
|
3.40.80.10;
|
N-acetylmuramoyl-L-alanine amidase 2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9660837}. Secreted {ECO:0000269|PubMed:14585845, ECO:0000269|PubMed:9660837}. Note=Exists in both soluble and membrane-associated forms.
| null | null | null | null | null |
FUNCTION: Innate immunity protein that plays several important functions in antimicrobial and antitumor defense systems. Acts as a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria and thus provides bactericidal activity (PubMed:12649138, PubMed:9660837, PubMed:9707603). Forms an equimolar complex with heat shock protein HSPA1A and induces programmed cell death through apoptosis and necroptosis in tumor cell lines by activating the TNFR1 receptor on the target cell membrane (PubMed:14585845). In addition, acts in complex with the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce lymphocyte movement. Mechanistically, this complex acts as a ligand of the chemotactic receptors CCR5 and CXCR3 which are present on the cells of the immune system. Promotes also the activation of lymphocytes that become able to kill virus-infected cells as well as tumor cells by modulating the spectrum of their target-cell specificity. Induction of cytotoxicity on monocyte surface requires interaction with TREM1 receptor (By similarity). {ECO:0000250|UniProtKB:O75594, ECO:0000269|PubMed:12649138, ECO:0000269|PubMed:14585845, ECO:0000269|PubMed:9660837, ECO:0000269|PubMed:9707603}.
|
Mus musculus (Mouse)
|
O88597
|
BECN1_MOUSE
|
MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQVRYAQIQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
| null | null |
amyloid-beta metabolic process [GO:0050435]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; cell division [GO:0051301]; cellular response to aluminum ion [GO:0071275]; cellular response to amino acid starvation [GO:0034198]; cellular response to copper ion [GO:0071280]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to glucose starvation [GO:0042149]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to nitrogen starvation [GO:0006995]; cellular response to oxygen-glucose deprivation [GO:0090650]; cytoplasmic pattern recognition receptor signaling pathway [GO:0002753]; defense response to virus [GO:0051607]; early endosome to late endosome transport [GO:0045022]; engulfment of apoptotic cell [GO:0043652]; JNK cascade [GO:0007254]; late endosome to vacuole transport [GO:0045324]; lysosome organization [GO:0007040]; macroautophagy [GO:0016236]; mitophagy [GO:0000423]; mitotic metaphase chromosome alignment [GO:0007080]; negative regulation of apoptotic process [GO:0043066]; negative regulation of autophagosome assembly [GO:1902902]; negative regulation of autophagy [GO:0010507]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of lysosome organization [GO:1905672]; negative regulation of programmed cell death [GO:0043069]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; neuron development [GO:0048666]; p38MAPK cascade [GO:0038066]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; positive regulation of attachment of mitotic spindle microtubules to kinetochore [GO:1902425]; positive regulation of autophagosome assembly [GO:2000786]; positive regulation of autophagy [GO:0010508]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of stress granule assembly [GO:0062029]; protein targeting to lysosome [GO:0006622]; protein-containing complex assembly [GO:0065003]; receptor catabolic process [GO:0032801]; regulation of autophagy [GO:0010506]; regulation of cytokinesis [GO:0032465]; regulation of macroautophagy [GO:0016241]; response to hypoxia [GO:0001666]; response to iron(II) ion [GO:0010040]; response to lead ion [GO:0010288]; response to mitochondrial depolarisation [GO:0098780]; response to other organism [GO:0051707]; response to vitamin E [GO:0033197]; response to xenobiotic stimulus [GO:0009410]; SMAD protein signal transduction [GO:0060395]
|
autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytoplasmic side of mitochondrial outer membrane [GO:0032473]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; membrane [GO:0016020]; nuclear body [GO:0016604]; phagocytic vesicle [GO:0045335]; phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kinase complex, class III [GO:0035032]; phosphatidylinositol 3-kinase complex, class III, type I [GO:0034271]; phosphatidylinositol 3-kinase complex, class III, type II [GO:0034272]; protein-containing complex [GO:0032991]; trans-Golgi network [GO:0005802]
|
GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein kinase binding [GO:0019901]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin protein ligase binding [GO:0031625]
|
PF04111;PF17675;PF15285;
|
6.10.250.3110;1.10.418.40;
|
Beclin family
|
PTM: Phosphorylation at Thr-117 by DAPK1 reduces its interaction with BCL2 and BCL2L1 and promotes induction of autophagy (By similarity). In response to autophagic stimuli, phosphorylated at serine residues by AMPK in an ATG14-dependent manner, and this phosphorylation is critical for maximally efficient autophagy. {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:23332761}.; PTM: Polyubiquitinated by NEDD4, both with 'Lys-11'- and 'Lys-63'-linkages (By similarity). 'Lys-11'-linked polyubiquitination leads to degradation and is enhanced when the stabilizing interaction partner VPS34 is depleted (By similarity). Deubiquitinated by USP10 and USP13, leading to stabilize the PIK3C3/VPS34-containing complexes (By similarity). Polyubiquitinated at Lys-400 with 'Lys-48'-linkages (PubMed:28445460). 'Lys-48'-linked poyubiquitination of Lys-400 leads to degradation (PubMed:28445460). Deubiquitinated by ATXN3, leading to stabilization (PubMed:28445460). Ubiquitinated at Lys-435 via 'Lys-63'-linkage by the DCX(AMBRA1) complex, thereby increasing the association between BECN1 and PIK3C3 to promote PIK3C3 activity (By similarity). 'Lys-48'-linked ubiquitination by RNF216 leads to proteasomal degradation and autophagy inhibition (By similarity). {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:28445460}.; PTM: Proteolytically processed by caspases including CASP8 and CASP3; the C-terminal fragments lack autophagy-inducing capacity and are proposed to induce apoptosis. Thus the cleavage is proposed to be an determinant to switch from autophagy to apoptosis pathways affecting cellular homeostasis including viral infections and survival of tumor cells. {ECO:0000305|PubMed:21364619}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12372286}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome {ECO:0000269|PubMed:25275521}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=Interaction with ATG14 promotes translocation to autophagosomes (By similarity). Expressed in dendrites and cell bodies of cerebellar Purkinje cells. Localized to endosomes in neurons (PubMed:25275521). {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:25275521}.; SUBCELLULAR LOCATION: [Beclin-1-C 35 kDa]: Mitochondrion {ECO:0000269|PubMed:21364619}. Nucleus {ECO:0000250|UniProtKB:Q14457}. Cytoplasm {ECO:0000250|UniProtKB:Q14457}.; SUBCELLULAR LOCATION: [Beclin-1-C 37 kDa]: Mitochondrion {ECO:0000269|PubMed:21364619}.
| null | null | null | null | null |
FUNCTION: Plays a central role in autophagy (PubMed:10604474, PubMed:12372286, PubMed:19270693, PubMed:28445460). Acts as a core subunit of different PI3K complex forms that mediate formation of phosphatidylinositol 3-phosphate and are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis (PubMed:19270693, PubMed:25275521). Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2 (By similarity). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms (PubMed:25275521). Involved in endocytosis including endosome formation in neuronal cells (PubMed:25275521). May play a role in antiviral host defense (By similarity). {ECO:0000250|UniProtKB:Q14457, ECO:0000269|PubMed:10604474, ECO:0000269|PubMed:12372286, ECO:0000269|PubMed:19270693, ECO:0000269|PubMed:25275521, ECO:0000269|PubMed:28445460}.; FUNCTION: Beclin-1-C 35 kDa localized to mitochondria can promote apoptosis; it induces the mitochondrial translocation of BAX and the release of proapoptotic factors (By similarity). {ECO:0000250|UniProtKB:Q14457}.
|
Mus musculus (Mouse)
|
O88600
|
HSP74_RAT
|
MSVVGIDLGFQSCYVAVARAGGIETIANEYSDRCTPACVSFGPKNRSVGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVEAEKSNLAYDIVQLPTGLTGIKVTYMEEERNFTTEQVTAMLLSKLKETAESVLKKPVVDCVVSVPSFYTDAERRSVMDATQIAGLNCLRLMNETTAVALAYGIYKQDLPALEEKPRNVVFVDMGHSAYQVSVCAFNRGKLKVLATAFDTTLGGRKFDEVLVNHFCEEFGKKYKLDIKSKVRALLRLSQECEKLKKLMSANASDLPLSIECFMNDIDVSGTMNRGKFLEMCDDLLARVEPPLRSILDQSKLKKEDIYAVEIVGGATRIPAVKEKISKFFGKELSTTLNADEAVTRGCALQCAILSPAFKVREFSITDVVPYPISLRWNSPAEEGSSDCEVFPKNHAAPFSKVLTFYRKEPFTLEAYYSSPQDLPYPDPAIAQFSVQKVTPQSDGSSSKVKVKVRVNVHGIFSVSSAALVEVHKSEESEEPMETDQNAKEEEKMQVDQEEPHTEEQQPQTPAENKAESEEMETSQAGSKDKKMDQPPQAKKAKVKTSTVDLPIESQLLWQLDREMLGLYTENEGKMIMQDKLEKERNDAKNAVEEYVYEMRDKLSGEYEKFVSEDDRNNFTLKLEDTENWLYEDGEDQPKQVYVDKLAELRTLGQPIKTRFQESEERPKLFEELGKQIQQYMKVISSFKNKEDQYEHLDAADMTKVEKSTNEAMEWMNSKLNLQNKQSLTADPVVKTKEIEAKIKELTNICSPIISKPKPKVEPPKEEPKHAEQNGPVDGQGDNPGTQAAEHGADTAVPSDGDKKLPEMDID
| null | null |
chaperone-mediated protein complex assembly [GO:0051131]; kidney development [GO:0001822]; negative regulation of apoptotic process [GO:0043066]; negative regulation of gene expression [GO:0010629]; negative regulation of protein phosphorylation [GO:0001933]; neuron apoptotic process [GO:0051402]; positive regulation of angiogenesis [GO:0045766]; protein folding [GO:0006457]; protein insertion into mitochondrial outer membrane [GO:0045040]; regulation of microglial cell activation [GO:1903978]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; lipid droplet [GO:0005811]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
adenyl-nucleotide exchange factor activity [GO:0000774]; ATP binding [GO:0005524]; ATP-dependent protein folding chaperone [GO:0140662]; protein-containing complex binding [GO:0044877]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
|
PF00012;
|
1.20.1270.10;3.30.30.30;3.30.420.40;
|
Heat shock protein 70 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null | null | null | null | null |
Rattus norvegicus (Rat)
|
O88602
|
CCG2_MOUSE
|
MGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSSSRSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVHNCIQKDSKDSLHANTANRRTTPV
| null | null |
eye blink reflex [GO:0060082]; membrane depolarization [GO:0051899]; membrane hyperpolarization [GO:0060081]; nervous system process [GO:0050877]; neuromuscular junction development [GO:0007528]; neurotransmitter receptor internalization [GO:0099590]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; neurotransmitter receptor transport, postsynaptic endosome to lysosome [GO:0098943]; positive regulation of protein localization to basolateral plasma membrane [GO:1904510]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; postsynaptic neurotransmitter receptor diffusion trapping [GO:0098970]; protein targeting to membrane [GO:0006612]; regulation of AMPA receptor activity [GO:2000311]; regulation of membrane potential [GO:0042391]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]; regulation of postsynaptic neurotransmitter receptor activity [GO:0098962]; response to calcium ion [GO:0051592]; transmission of nerve impulse [GO:0019226]
|
AMPA glutamate receptor complex [GO:0032281]; cell surface [GO:0009986]; cerebellar mossy fiber [GO:0044300]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; postsynaptic density membrane [GO:0098839]; Schaffer collateral - CA1 synapse [GO:0098685]; somatodendritic compartment [GO:0036477]; voltage-gated calcium channel complex [GO:0005891]
|
channel regulator activity [GO:0016247]; ionotropic glutamate receptor binding [GO:0035255]; voltage-gated calcium channel activity [GO:0005245]
|
PF00822;
|
1.20.140.150;
|
PMP-22/EMP/MP20 family, CACNG subfamily
|
PTM: Phosphorylation of Thr-321 by PKA impairs interaction with DLG1 and DLG4. {ECO:0000269|PubMed:11805122}.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Synapse, synaptosome {ECO:0000250|UniProtKB:Q71RJ2}.
| null | null | null | null | null |
FUNCTION: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity). {ECO:0000250|UniProtKB:Q71RJ2, ECO:0000250|UniProtKB:Q9Y698}.
|
Mus musculus (Mouse)
|
O88609
|
LMX1B_MOUSE
|
MDIATGPESLERCFPRGQTDCAKMLDGIKMEEHALRPGPATLGVLLGSDCPHPAVCEGCQRPISDRFLMRVNESSWHEECLQCAACQQALTTSCYFRDRKLYCKQDYQQLFAAKCSGCMEKIAPTEFVMRALECVYHLGCFCCCVCERQLRKGDEFVLKEGQLLCKGDYEKEKDLLSSVSPDESDSVKSEDEDGDMKPAKGQGSQSKGSGDDGKDPRRPKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLSVRVVQVWFQNQRAKMKKLARRHQQQQEQQNSQRLGQEVLSSRMEGMMASYTPLAPPQQQIVAMEQSPYGSSDPFQQGLTPPQMPGNDSIFHDIDSDTSLTSLSDCFLGSSDVGSLQARVGNPIDRLYSMQSSYFAS
| null | null |
camera-type eye development [GO:0043010]; cell population proliferation [GO:0008283]; central nervous system neuron development [GO:0021954]; cerebellum morphogenesis [GO:0021587]; collagen fibril organization [GO:0030199]; dopaminergic neuron differentiation [GO:0071542]; dorsal/ventral pattern formation [GO:0009953]; embryonic limb morphogenesis [GO:0030326]; limb morphogenesis [GO:0035108]; locomotory behavior [GO:0007626]; memory [GO:0007613]; midbrain development [GO:0030901]; neuron differentiation [GO:0030182]; neuron migration [GO:0001764]; olfactory behavior [GO:0042048]; organ growth [GO:0035265]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of autophagy [GO:0010506]; regulation of gene expression [GO:0010468]; regulation of intracellular transport [GO:0032386]; regulation of transcription by RNA polymerase II [GO:0006357]; synapse organization [GO:0050808]; trabecular meshwork development [GO:0002930]
|
nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00046;PF00412;
|
2.10.110.10;1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcription factor involved in the regulation of podocyte-expressed genes. Essential for the specification of dorsal limb fate at both the zeugopodal and autopodal levels. {ECO:0000250|UniProtKB:O60663}.
|
Mus musculus (Mouse)
|
O88618
|
FTCD_RAT
|
MSQLVECVPNFSEGNNQEVIDAISQAISQTPGCVLLDVDAGPSTNRTVYTFVGQPECVVEGALSAARTASQLIDMRKHKGEHPRMGALDVCPFIPVRGVSMDECVLCAKAFGQRLAEELNVPVYLYGEAAQMPSRQTLPAIRAGEYEALPEKLKQAEWVPDFGPSSFVPSWGATVTGARKFLIAFNINLLSTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLEEKNLAQVSTNLLDFEVTALHTVYEEARREAQELNLPVVGSQLVGLVPLKALLDAAAFYCDKEKLFVLEEEHRIRLVVNRLGLDSLAPFDPKERIIEYLVPDSGPEQSLLDASLRAFVREVGARSAAPGGGSVAAAVAALGAALASMVGQMTYGRRQFDHLDSTMRRLIPPFHAASAQLTSLVDADARAFAACLGAIKLPKNTPEERDRRTCALQEGLRQAVAVPLKLAETVSQLWPALQELAQCGNLSCLSDLQVAAKALETGVFGAYFNVLINLKDMTDDVFKEKTRHRISSLLQEAKTQAALVLGSLEARKE
|
2.1.2.5; 4.3.1.4
| null |
cytoskeleton organization [GO:0007010]; histidine catabolic process to glutamate and formamide [GO:0019556]; histidine catabolic process to glutamate and formate [GO:0019557]
|
centriole [GO:0005814]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum membrane [GO:0030868]
|
folic acid binding [GO:0005542]; formimidoyltetrahydrofolate cyclodeaminase activity [GO:0030412]; glutamate formimidoyltransferase activity [GO:0030409]; intermediate filament binding [GO:0019215]; microtubule binding [GO:0008017]
|
PF02971;PF04961;PF07837;
|
1.20.120.680;3.30.70.670;3.30.990.10;
|
Cyclodeaminase/cyclohydrolase family; Formiminotransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9YH58}. Golgi apparatus {ECO:0000269|PubMed:12160147, ECO:0000269|PubMed:9677387}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O95954}. Note=More abundantly located around the mother centriole. {ECO:0000250|UniProtKB:O95954}.
|
CATALYTIC ACTIVITY: Reaction=5-formimidoyltetrahydrofolate + L-glutamate = (6S)-5,6,7,8-tetrahydrofolate + N-formimidoyl-L-glutamate; Xref=Rhea:RHEA:15097, ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:57456, ChEBI:CHEBI:58928; EC=2.1.2.5; Evidence={ECO:0000269|PubMed:9677387}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15099; Evidence={ECO:0000305|PubMed:9677387}; CATALYTIC ACTIVITY: Reaction=5-formimidoyltetrahydrofolate + 2 H(+) = (6R)-5,10-methenyltetrahydrofolate + NH4(+); Xref=Rhea:RHEA:22736, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57455, ChEBI:CHEBI:57456; EC=4.3.1.4; Evidence={ECO:0000269|PubMed:9677387}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22737; Evidence={ECO:0000305|PubMed:9677387};
| null |
PATHWAY: Amino-acid degradation; L-histidine degradation into L-glutamate; L-glutamate from N-formimidoyl-L-glutamate (transferase route): step 1/1. {ECO:0000305|PubMed:9677387}.
| null | null |
FUNCTION: Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool. {ECO:0000269|PubMed:9677387}.; FUNCTION: Binds and promotes bundling of vimentin filaments originating from the Golgi. {ECO:0000269|PubMed:12160147}.
|
Rattus norvegicus (Rat)
|
O88621
|
FOXH1_MOUSE
|
MASGWDLASTYTPTTPSPQLALAPAQGYLPCMGPRDNSQLRPPEAESLSKTPKRRKKRYLRHDKPPYTYLAMIALVIQAAPFRRLKLAQIIRQVQAVFPFFRDDYEGWKDSIRHNLSSNRCFHKVPKDPAKPQAKGNFWAVDVSLIPAEALRLQNTALCRRWQNRGTHRAFAKDLSPYVLHGQPYQPPSPPPPPREGFSIKSLLGDPGKESTWPQHPGLPGQSTAAQAGTLSKGEEGMGTGPSSSSETPLWPLCSLPGPTIIEGESSQGEVIRPSPVTPDQGSWPLHLLEDSADSRGVPRRGSRASLWGQLPTSYLPIYTPNVVMPLATLPTTSCPQCPSSASPAYWSVGTESQGSQDLLCDLDSLFQGVPPNKSIYDVWVSHPRDLAAPAPGWLLSWYSM
| null | null |
anterior/posterior pattern specification [GO:0009952]; aorta morphogenesis [GO:0035909]; axial mesoderm development [GO:0048318]; cardiac right ventricle morphogenesis [GO:0003215]; cellular response to cytokine stimulus [GO:0071345]; determination of left/right symmetry [GO:0007368]; embryonic heart tube anterior/posterior pattern specification [GO:0035054]; heart looping [GO:0001947]; hepatocyte differentiation [GO:0070365]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of intracellular estrogen receptor signaling pathway [GO:0033147]; negative regulation of transcription by RNA polymerase II [GO:0000122]; outflow tract morphogenesis [GO:0003151]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; secondary heart field specification [GO:0003139]; transforming growth factor beta receptor signaling pathway [GO:0007179]; ventricular trabecula myocardium morphogenesis [GO:0003222]
|
activin responsive factor complex [GO:0032444]; chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
bHLH transcription factor binding [GO:0043425]; co-SMAD binding [GO:0070410]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; nuclear androgen receptor binding [GO:0050681]; protein domain specific binding [GO:0019904]; R-SMAD binding [GO:0070412]; sequence-specific DNA binding [GO:0043565]; SMAD binding [GO:0046332]; transcription cis-regulatory region binding [GO:0000976]
|
PF00250;
|
1.10.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Transcriptional activator. Recognizes and binds to the DNA sequence 5'-TGT[GT][GT]ATT-3'. Required for induction of the goosecoid (GSC) promoter by TGF-beta or activin signaling. Forms a transcriptionally active complex containing FOXH1/SMAD2/SMAD4 on a site on the GSC promoter called TARE (TGF-beta/activin response element). {ECO:0000269|PubMed:10349617, ECO:0000269|PubMed:9702197, ECO:0000269|PubMed:9858566, ECO:0000269|Ref.4}.
|
Mus musculus (Mouse)
|
O88622
|
PARG_MOUSE
|
MSAGPGWEPCTKRPRWGAAGTSAPTASDSRSFPGRQRRVLDPKDAPVQFRVPPSSPACVSGRAGPHRGNATSFVFKQKTITTWMDTKGPKTAESESKENNNTRIDSMMSSVQKDNFYPHKVEKLENVPQLNLDKSPTEKSSQYLNQQQTASVCKWQNEGKHAEQLLASEPPAGTPLPKQLSNANIGQSPHTDDHSDTDHEEDRDNQQFLTPIKLANTKPTVGDGQARSNCKCSGSRQSVKDCTGCQQEEVDVLPESPLSDVGAEDIGTGPKNDNKLTGQESSLGDSPPFEKESEPESPMDVDNSKNSCQDSEADEETSPVFDEQDDRSSQTANKLSSCQAREADGDLRKRYLTKGSEVRLHFQFEGENNAGTSDLNAKPSGNSSSLNVECRSSKQHGKRDSKITDHFMRISKSEDRRKEQCEVRHQRTERKIPKYIPPNLPPEKKWLGTPIEEMRKMPRCGIHLPSLRPSASHTVTVRVDLLRAGEVPKPFPTHYKDLWDNKHVKMPCSEQNLYPVEDENGERTAGSRWELIQTALLNKFTRPQNLKDAILKYNVAYSKKWDFTALVDFWDKVLEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSVTMSQEQIASLLANAFFCTFPRRNAKMKSEYSSYPDINFNRLFEGRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSLEDFPEWERCEKPLTRLHVTYEGTIEGNGRGMLQVDFANRFVGGGVTGAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDGSEKDDWQRRCTEIVAIDALHFRRYLDQFVPEKVRRELNKAYCGFLRPGVPSENLSAVATGNWGCGAFGGDARLKALIQILAAAAAERDVVYFTFGDSELMRDIYSMHTFLTERKLDVGKVYKLLLRYYNEECRNCSTPGPDIKLYPFIYHAVESSAETTDMPGQKAGT
|
3.2.1.143
| null |
ATP generation from poly-ADP-D-ribose [GO:1990966]; carbohydrate metabolic process [GO:0005975]; detection of bacterium [GO:0016045]; DNA damage response [GO:0006974]; nucleotide-sugar metabolic process [GO:0009225]; positive regulation of DNA repair [GO:0045739]; regulation of DNA repair [GO:0006282]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; poly(ADP-ribose) glycohydrolase activity [GO:0004649]
|
PF05028;PF20811;
| null |
Poly(ADP-ribose) glycohydrolase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86W56}. Note=Colocalizes with PCNA at replication foci. Relocalizes to the cytoplasm in response to DNA damage (By similarity). {ECO:0000250|UniProtKB:Q86W56}.
|
CATALYTIC ACTIVITY: Reaction=[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-alpha-D-ribose](n-1) + ADP-D-ribose; Xref=Rhea:RHEA:52216, Rhea:RHEA-COMP:16922, Rhea:RHEA-COMP:16923, ChEBI:CHEBI:15377, ChEBI:CHEBI:57967, ChEBI:CHEBI:142512; EC=3.2.1.143; Evidence={ECO:0000250|UniProtKB:Q86W56};
| null | null | null | null |
FUNCTION: Poly(ADP-ribose) glycohydrolase that degrades poly(ADP-ribose) by hydrolyzing the ribose-ribose bonds present in poly(ADP-ribose). PARG acts both as an endo- and exoglycosidase, releasing poly(ADP-ribose) of different length as well as ADP-ribose monomers. It is however unable to cleave the ester bond between the terminal ADP-ribose and ADP-ribosylated residues, leaving proteins that are mono-ADP-ribosylated. Poly(ADP-ribose) is synthesized after DNA damage is only present transiently and is rapidly degraded by PARG. Required to prevent detrimental accumulation of poly(ADP-ribose) upon prolonged replicative stress, while it is not required for recovery from transient replicative stress. Responsible for the prevalence of mono-ADP-ribosylated proteins in cells, thanks to its ability to degrade poly(ADP-ribose) without cleaving the terminal protein-ribose bond. Required for retinoid acid-dependent gene transactivation, probably by removing poly(ADP-ribose) from histone demethylase KDM4D, allowing chromatin derepression at RAR-dependent gene promoters. Involved in the synthesis of ATP in the nucleus, together with PARP1, NMNAT1 and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. {ECO:0000250|UniProtKB:Q86W56}.
|
Mus musculus (Mouse)
|
O88623
|
UBP2_MOUSE
|
MSQLSSTLKRYTESSRYTDAPYAKPGYGTYTPSSYGANLAASFLEKEKLGFKPVSPTSFLPRPRTYGPSSILDCDRGRPLLRSDIIGSSKRSESQTRGNERPSGSGLNGGSGFSYGVSSNSLSYLPMNARDQGVTLSQKKSNSQSDLARDFSSLRTSDGYRTSDGYRTSEGFRIDPGNLGRSPMLARTRKELCALQGLYQAASRSEYLTDYLENYGRKGSAPQVLTQAPPPSRVPEVLSPTYRPSGRYTLWEKSKGQASGPSRSSSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFMGYNQQDAQEFLRFLLDGLHNEVNRVAARPKASPETLDHLPDEEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
|
3.4.19.12
| null |
cell cycle [GO:0007049]; circadian behavior [GO:0048512]; circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; locomotor rhythm [GO:0045475]; muscle organ development [GO:0007517]; negative regulation of calcium ion transport [GO:0051926]; negative regulation of skeletal muscle tissue development [GO:0048642]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of skeletal muscle tissue development [GO:0048643]; protein deubiquitination [GO:0016579]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
cyclin binding [GO:0030332]; cysteine-type deubiquitinase activity [GO:0004843]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; ubiquitin protein ligase binding [GO:0031625]
|
PF00443;
|
3.90.70.10;
|
Peptidase C19 family, USP2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14686789}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14686789}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250|UniProtKB:Q5U349}. Membrane {ECO:0000269|PubMed:26756164}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:26756164}. Note=Predominantly expressed at membranes. {ECO:0000269|PubMed:26756164}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12;
| null | null | null | null |
FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and isoform 2 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (By similarity). Has no deubiquitinase activity against p53/TP53 (By similarity). Prevents MDM2-mediated degradation of MDM4 (By similarity). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues (PubMed:23213472, PubMed:25238854, PubMed:26756164). Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability (PubMed:23213472). Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and BMAL1 (PubMed:25238854). {ECO:0000250|UniProtKB:O75604, ECO:0000250|UniProtKB:Q5U349, ECO:0000269|PubMed:23213472, ECO:0000269|PubMed:25238854}.; FUNCTION: [Isoform 2]: Circadian clock output effector that regulates Ca(2+) absorption in the small intestine. Probably functions by regulating protein levels of the membrane scaffold protein NHERF4 in a rhythmic manner, and is therefore likely to control Ca(2+) membrane permeability mediated by the Ca(2+) channel TRPV6 in the intestine. {ECO:0000269|PubMed:26756164}.
|
Mus musculus (Mouse)
|
O88627
|
S28A2_MOUSE
|
MEKSKGRKSVSQATVENCMENPGLELMEGGNLEQRYTQEEVTQGHSLEDGLGHSSLWSRRIFQPFTKARSFFERHAGLFRKILLGLLCLAYAAYFLAACILNFQRALALFVITCLVIFILACHFLKKFFPKEQLRCLKPLENTHLNLWAKRVFVGLSVVGLILWLALDTAQRPEQLISFAGICMFILILFACSKHHSAVCWRTVFWGLGLQFIFGILVIRTEPGFNAFQWLGDQIQIFLAYTVEGSSFVFGDTLVQNVFAFQSLPIIIFFGCVMSILYYLGLVQWVIQKVAWFLQITMGTTAAETLAVAGNIFVGMTEAPLLIRPYLADMTISEIHAVMTGGFATIAGTVLGAFISFGIDASSLISASVMAAPCALALSKLVYPEVEESKFKSKEGLKLPRGEERNILEAASNGATDAISLVANVAANLIAFLAVLAFINATLSWLGEMVDIHGLSFQVICSYVLRPMVFMMGVQWADCPLVAEIVGVKFFINEFVAYQQLSQYKNKRLSGVEEWINGEKQWISVKAEIITTFSLCGFANLSSIGITLGGLTSMIPQRKSDLCKIVVRALFTGACVSFISACMAGILYVPRGAETDCVSFLNTNFTNRTYETYVCCRELFQSTSLNGTNMPSFSGPWQDNVSSLRNLASCCDLYTSTVCA
| null | null |
nucleoside transmembrane transport [GO:1901642]; protein localization to cell surface [GO:0034394]; purine nucleoside transmembrane transport [GO:0015860]; retina homeostasis [GO:0001895]
|
apicolateral plasma membrane [GO:0016327]; brush border membrane [GO:0031526]; coated vesicle [GO:0030135]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506]
|
nucleoside transmembrane transporter activity [GO:0005337]; nucleoside:sodium symporter activity [GO:0005415]; purine nucleoside transmembrane transporter activity [GO:0015211]
|
PF07670;PF07662;PF01773;
| null |
Concentrative nucleoside transporter (CNT) (TC 2.A.41) family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O43868}; Multi-pass membrane protein {ECO:0000255}. Apicolateral cell membrane {ECO:0000250|UniProtKB:O43868}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=adenosine(out) + Na(+)(out) = adenosine(in) + Na(+)(in); Xref=Rhea:RHEA:69927, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O43868}; CATALYTIC ACTIVITY: Reaction=inosine(out) + Na(+)(out) = inosine(in) + Na(+)(in); Xref=Rhea:RHEA:69931, ChEBI:CHEBI:17596, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O43868}; CATALYTIC ACTIVITY: Reaction=guanosine(out) + Na(+)(out) = guanosine(in) + Na(+)(in); Xref=Rhea:RHEA:69935, ChEBI:CHEBI:16750, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O43868}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in); Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O43868};
| null | null | null | null |
FUNCTION: Sodium-dependent and purine-selective transporter. Exhibits the transport characteristics of the nucleoside transport system cif or N1 subtype (N1/cif) (selective for purine nucleosides and uridine). Plays a critical role in specific uptake and salvage of purine nucleosides in kidney and other tissues. May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (By similarity). {ECO:0000250|UniProtKB:O43868}.
|
Mus musculus (Mouse)
|
O88632
|
SEM3F_MOUSE
|
MLVTAFILWASLLTGAWPATPIQDQLPATPRVRLSFKELKATGTAHFFNFLLNTTDYRILLKDEDHDRMYVGSKDYVLSLDLHDINREPLIIHWAASPQRIEECILSGKDGNGECGNFVRLIQPWNRTHLYVCGTGAYNPMCTYVNRGRRAQALPWTQMQVVRGRGSRATDGADRPTPTAPRQDYIFYLEPEKLESGKGKCPYDPKLDTASALINEELYAGVYIDFMGTDAAIFRTLGKQTAMRTDQYNSRWLNDPSFIHAELIPDSAERNDDKLYFFFRERSAEAPQNPAVYARIGRICLNDDGGHCCLVNKWSTFLKARLVCSVPGEDGIETHFDELQDVFVQQTQDVRNPVIYAVFTSSGSVFRGSAVCVYSMADIRMVFNGPFAHKEGPNYQWMPFSGKMPYPRPGTCPGGTFTPSMKSTKDYPDEVINFMRTHPLMYQAVYPLQRRPLVVRTGAPYRLTTVAVDQVDAADGRYEVLFLGTDRGTVQKVIVLPKDDQEVEELMLEEVEVFKEPAPVKTMTISSKRQQLYVASAVGVTHLSLHRCQAYGAACADCCLARDPYCAWDGQACSRYTASSKRRSRRQDVRHGNPIRQCRGFNSNANKNAVESVQYGVAGSAAFLECQPRSPQATVKWLFQRDPSDRRREIRAEDRFLRTEQGLLLRALQLGDRGLYSCTATENNFKHIVTRVQLHVLGRDAVHAALFPPLAVSVPPPPGTGPPTPPYQELAQLLAQPEVGLIHQYCQGYWRHVPPRPREAPGALRPPELQDQKKPRNRRHHPPDT
| null | null |
axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; branchiomotor neuron axon guidance [GO:0021785]; facial nerve structural organization [GO:0021612]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; nerve development [GO:0021675]; neural crest cell migration [GO:0001755]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; positive regulation of cell migration [GO:0030335]; regulation of postsynapse organization [GO:0099175]; semaphorin-plexin signaling pathway [GO:0071526]; sympathetic ganglion development [GO:0061549]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; trigeminal nerve structural organization [GO:0021637]; trunk neural crest cell migration [GO:0036484]; ventral trunk neural crest cell migration [GO:0036486]
|
extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]
|
chemorepellent activity [GO:0045499]; semaphorin receptor binding [GO:0030215]
|
PF01403;
|
2.60.40.10;3.30.1680.10;2.130.10.10;
|
Semaphorin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null | null |
Mus musculus (Mouse)
|
O88634
|
PAR4_MOUSE
|
MCWPLLYPLVLGLSISLAEGIQTPSIYDDVESTRGSHEGPLGPTVELKEPKSSDKPNPRGYPGKFCANDSDTLELPASSQALLLGWVPTRLVPALYGLVVAVGLPANGLALWVLATRVPRLPSTILLMNLAVADLLLALVLPPRLAYHLRGQRWPFGEAACRVATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGQRLTTGLCLVAWLSAATLALPLTLHRQTFRLAGSDRMLCHDALPLTEQTSHWRPAFICLAVLGCFVPLLAMGLCYGATLRALAANGQRYSHALRLTALVLFSAVASFTPSNVLLVLHYSNPSPEAWGNLYGAYVPSLALSTLNSCVDPFIYYYVSHEFREKVRAMLCRQPEASSSSQASREAGSRGTAICSSTLL
| null | null |
platelet aggregation [GO:0070527]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of Rho protein signal transduction [GO:0035025]
|
plasma membrane [GO:0005886]
|
G protein-coupled receptor activity [GO:0004930]; protease binding [GO:0002020]; thrombin-activated receptor activity [GO:0015057]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
|
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.
|
Mus musculus (Mouse)
|
O88643
|
PAK1_MOUSE
|
MSNNGVDIQDKPPAPPMRNTSTMIGAGSKDTGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKREKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSKKYMSFTDKSAEDYNSSNTLNVKTVSETPAVPPVSEDDEDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTPFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLQCCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLMHAAKEATKNNH
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13153};
|
actin cytoskeleton organization [GO:0030036]; amygdala development [GO:0021764]; apoptotic process [GO:0006915]; branching morphogenesis of an epithelial tube [GO:0048754]; cell migration [GO:0016477]; cellular response to insulin stimulus [GO:0032869]; cellular response to organic cyclic compound [GO:0071407]; chromatin remodeling [GO:0006338]; dendrite development [GO:0016358]; dendritic spine development [GO:0060996]; DNA damage response [GO:0006974]; establishment of cell polarity [GO:0030010]; exocytosis [GO:0006887]; gamma-aminobutyric acid secretion, neurotransmission [GO:0061534]; glutamate secretion, neurotransmission [GO:0061535]; intracellular signal transduction [GO:0035556]; negative regulation of cell growth involved in cardiac muscle cell development [GO:0061052]; negative regulation of cell proliferation involved in contact inhibition [GO:0060244]; neuromuscular junction development [GO:0007528]; neuron projection morphogenesis [GO:0048812]; observational learning [GO:0098597]; positive regulation of axon extension [GO:0045773]; positive regulation of cell migration [GO:0030335]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of intracellular estrogen receptor signaling pathway [GO:0033148]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of microtubule nucleation [GO:0090063]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of vascular associated smooth muscle cell migration [GO:1904754]; positive regulation of vascular associated smooth muscle cell proliferation [GO:1904707]; protein autophosphorylation [GO:0046777]; protein localization to cytoplasmic stress granule [GO:1903608]; protein phosphorylation [GO:0006468]; receptor clustering [GO:0043113]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of axonogenesis [GO:0050770]; regulation of gene expression [GO:0010468]; regulation of long-term synaptic potentiation [GO:1900271]; regulation of MAPK cascade [GO:0043408]; regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission [GO:0150036]; response to hypoxia [GO:0001666]; response to organic substance [GO:0010033]; transmission of nerve impulse [GO:0019226]; wound healing [GO:0042060]
|
axon [GO:0030424]; cell-cell junction [GO:0005911]; centrosome [GO:0005813]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; focal adhesion [GO:0005925]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; ruffle [GO:0001726]; ruffle membrane [GO:0032587]; Z disc [GO:0030018]
|
ATP binding [GO:0005524]; collagen binding [GO:0005518]; gamma-tubulin binding [GO:0043015]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00786;PF00069;
|
3.90.810.10;1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Autophosphorylated in trans, meaning that in a dimer, one kinase molecule phosphorylates the other one. Activated by autophosphorylation at Thr-423 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation at Thr-423 by BRSK2 and by PDPK1. Phosphorylated by JAK2 in response to PRL; this increases PAK1 kinase activity. Phosphorylated at Ser-21 by PKB/AKT; this reduces interaction with NCK1 and association with focal adhesion sites (By similarity). Upon DNA damage, phosphorylated at Thr-212 and translocates to the nucleoplasm (By similarity). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (PubMed:22685302). {ECO:0000250|UniProtKB:P35465, ECO:0000250|UniProtKB:Q13153, ECO:0000269|PubMed:22685302}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13153}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q13153}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q13153}. Cell membrane {ECO:0000250|UniProtKB:Q13153}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q13153}. Cell projection, invadopodium {ECO:0000250|UniProtKB:Q13153}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q13153}. Chromosome {ECO:0000250|UniProtKB:Q13153}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q13153}. Note=Recruited to the cell membrane by interaction with CDC42 and RAC1 (By similarity). Recruited to focal adhesions upon activation. Colocalized with CIB1 within membrane ruffles during cell spreading upon readhesion to fibronectin. Colocalizes with RUFY3, F-actin and other core migration components in invadopodia at the cell periphery (By similarity). Upon DNA damage, translocates to the nucleoplasm when phosphorylated at Thr-212 where is co-recruited with MORC2 on damaged chromatin (By similarity). Localization to the centrosome does not depend upon the presence of gamma-tubulin (By similarity). Localization of the active, but not inactive, protein to the adhesions and edge of lamellipodia is mediated by interaction with GIT1 (By similarity). {ECO:0000250|UniProtKB:P35465, ECO:0000250|UniProtKB:Q13153}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13153}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13153};
| null | null | null | null |
FUNCTION: Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes (PubMed:10611223, PubMed:12165471, PubMed:12176334, PubMed:15800193, PubMed:22669945, PubMed:23633677). Can directly phosphorylate BAD and protects cells against apoptosis (PubMed:10611223). Activated by interaction with CDC42 and RAC1 (By similarity). Functions as a GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway (By similarity). Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases (By similarity). Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes (By similarity). Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton (PubMed:12176334). Plays a role in the regulation of insulin secretion in response to elevated glucose levels (PubMed:22669945). Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ) (PubMed:12165471). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2 (By similarity). Phosphorylates MYL9/MLC2 (By similarity). Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2 (By similarity). Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus (By similarity). In podocytes, promotes NR3C2 nuclear localization (By similarity). Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed:23633677). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation (By similarity). Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (By similarity). In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling (By similarity). In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in F-actin stabilization (By similarity). In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (PubMed:15800193). Along with GIT1, positively regulates microtubule nucleation during interphase (By similarity). Phosphorylates FXR1, promoting its localization to stress granules and activity (By similarity). {ECO:0000250|UniProtKB:P35465, ECO:0000250|UniProtKB:Q13153, ECO:0000269|PubMed:10611223, ECO:0000269|PubMed:12165471, ECO:0000269|PubMed:12176334, ECO:0000269|PubMed:15800193, ECO:0000269|PubMed:22669945, ECO:0000269|PubMed:23633677}.
|
Mus musculus (Mouse)
|
O88653
|
LTOR3_MOUSE
|
MADDLKRFLYKKLPSVEGLHAIVVSDRDGVPVIKVANDSAPEHALRPGFLSTFALATDQGSKLGLSKNKSIICYYNTYQVVQFNRLPLVVSFIASSSANTGLIVSLEKELAPLFEELIKVVEVS
| null | null |
cellular response to amino acid stimulus [GO:0071230]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of TOR signaling [GO:0032008]; positive regulation of TORC1 signaling [GO:1904263]; protein localization [GO:0008104]; protein localization to cell junction [GO:1902414]; TORC1 signaling [GO:0038202]
|
FNIP-folliculin RagC/D GAP [GO:1990877]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; Ragulator complex [GO:0071986]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; kinase activator activity [GO:0019209]; molecular adaptor activity [GO:0060090]
|
PF08923;
|
3.30.450.30;
|
LAMTOR3 family
| null |
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}; Peripheral membrane protein {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}; Cytoplasmic side {ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:19177150}. Note=Recruited to lysosome and endosome membranes by LAMTOR1. {ECO:0000269|PubMed:19177150}.
| null | null | null | null | null |
FUNCTION: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:15263099). Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane (By similarity). Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated (By similarity). Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2 (PubMed:9733512). {ECO:0000250|UniProtKB:Q9UHA4, ECO:0000269|PubMed:15263099, ECO:0000269|PubMed:9733512}.
|
Mus musculus (Mouse)
|
O88658
|
KIF1B_RAT
|
MSGASVKVAVRVRPFNSRETSKESKCIIQMQGNSTSIINPKNPKEAPKSFSFDYSYWSHTSPEDPCFASQSRVYNDIGKEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGKQEESQAGIIPQLCEELFEKINDNCNEDMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTSYTDIADLMDAGNKARTVAATNMNETSSRSHAVFTIVFTQKKQDPETNLSTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVDNCTSKSKKKKKTDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADRAKQIKCNAVINEDPNAKLVRELKEEVTRLKDLLRAQGLGDIIDIDPLMDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTASMGSLTSSPSSCSLNSQAGLTSVTSIQERIMSTPGGEEAIERLKESEKIIAELNETWEEKLRKTEAIRMEREALLAEMGVAIREDGGTLGVFSPKKTPHLVNLNEDPLMSECLLYYIKDGITRVGQADAERRQDIVLSGAHIKEEHCIFRSERNNTGEVIVTLEPCERSETYVNGKRVAHPVQLRSGNRIIMGKNHVFRFNHPEQARAEREKTPSAETPSEPVDWTFAQRELLEKQGIDMKQEMEKRLQEMEILYKREKEEADLLLEQQRLDYESKLQALQKQVETRSLAAETTEEEEEEEEVPWTQHEFELAQWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQFQFVLLTDTLYSPVPPELLPTEMGKTHEDRPFPRTVVAVEVQDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVGSNAQDDSETTMTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSPTFSTADSDITELADEQQDAMEDFDDEAFVDDTGSDAGTEEGSELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRVAIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKISFDNEYFNQSDFPSAAMTRSGLSLEELRIVEGQGQSSEVISPPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLKLGSAFTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKNNGRGSPLGFYHVQNIAVEVTESFVDYIKTKPIVFEVFGHYQQHPLHLQGQELNSPPQPSRRFFPPPMPLSRPVPATKLNTMNKTSLGQSMSKYDLLVWFEISELEPTGEYIPAVVDHTAGLPCQGTFLLHQGIQRRITVTIIHEKGSELHWKDVRELVVGRIRNKPEVDEAAVDAILSLNIISAKSLKSSHSSSRTFYRFEAVWDSSLHNSLLLNRVTPYGEKIYMTLSAYLELDHCIQPAVITKDVCMVFYSRDAKISPPRSLRNLFGSGYSKSPDSNRVTGIYELSLCKMADTGSPGMQRRRRKVLDTSVAYVRGEENLAGWRPRGDSLILEHQWELEKLELLHEVEKTRHFLLLRERLGDSIPKSMSDSLSPSLSSGTLSTSTSISSQISTTTFESAITPSESSGYDSADIESLVDREKELATKCLQLLTHTFNREFSQVHGSISDCKLSDISPIGRDPSVSSFSSSTLTPSSTCPSLVDSRSSSMDQKTPEANSRASSPCQEFEQFQIIPTVETPYLARAGKNEFLNLVPDIEEVRAGSVVSKKGYLHFKEPLSSNWAKHFVVVRRPYVFIYNSDKDPVERGIINLSTAQVEYSEDQQAMLKTPNTFAVCTKHRGVLLQALNDKDMNDWLYAFNPLLAGTIRSKLSRRCPSQPKY
| null | null |
anterograde axonal transport [GO:0008089]; anterograde neuronal dense core vesicle transport [GO:1990048]; cellular response to nerve growth factor stimulus [GO:1990090]; cytoskeleton-dependent intracellular transport [GO:0030705]; lysosome localization [GO:0032418]; microtubule-based movement [GO:0007018]; mitochondrion transport along microtubule [GO:0047497]; neuromuscular synaptic transmission [GO:0007274]; neuron-neuron synaptic transmission [GO:0007270]; positive regulation of gene expression [GO:0010628]; protein localization to cell periphery [GO:1990778]; response to rotenone [GO:1904647]; retrograde neuronal dense core vesicle transport [GO:1990049]; transport along microtubule [GO:0010970]; vesicle-mediated transport [GO:0016192]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; synaptic vesicle [GO:0008021]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; kinase binding [GO:0019900]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; plus-end-directed microtubule motor activity [GO:0008574]; scaffold protein binding [GO:0097110]
|
PF12473;PF00498;PF12423;PF00225;PF16183;PF00169;
|
2.60.200.20;6.10.250.2520;3.40.850.10;2.30.29.30;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Unc-104 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Mitochondrion {ECO:0000250|UniProtKB:O60333}. Cell projection, axon {ECO:0000250|UniProtKB:Q60575}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:12204119}.
| null | null | null | null | null |
FUNCTION: Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility (By similarity). {ECO:0000250}.; FUNCTION: [Isoform 1]: Mediates the transport of synaptic vesicles in neuronal cells. {ECO:0000269|PubMed:12204119}.; FUNCTION: [Isoform 2]: Involved in the translocation of lysosomes from perinuclear regions to the cell periphery. {ECO:0000269|PubMed:15086790}.
|
Rattus norvegicus (Rat)
|
O88662
|
EMP2_MOUSE
|
MLVILAFIIVFHIVSTALLFISTIDNAWWVGDSFSADLWRVCTNSTNCTEINELTGPEAFEGYSVMQAVQATMILSTILSCISFLIFLLQLFRLKQGERFVLTSIIQLMSCLCVMIGASIYTDRRQDLHQQNRKLYYLLQEGSYGYSFILAWVAFAFTFISGLMYMILRKRK
| null | null |
actin filament organization [GO:0007015]; actin-mediated cell contraction [GO:0070252]; activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; bleb assembly [GO:0032060]; blood vessel endothelial cell migration [GO:0043534]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell-matrix adhesion [GO:0007160]; early endosome to late endosome transport [GO:0045022]; embryo implantation [GO:0007566]; embryonic process involved in female pregnancy [GO:0060136]; heart formation [GO:0060914]; membrane raft assembly [GO:0001765]; natural killer cell proliferation [GO:0001787]; neutrophil migration [GO:1990266]; plasma membrane raft assembly [GO:0044854]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cardiac epithelial to mesenchymal transition [GO:0062043]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; protein localization to cell surface [GO:0034394]; protein localization to plasma membrane [GO:0072659]; regulation of angiogenesis [GO:0045765]; regulation of cell-matrix adhesion [GO:0001952]; regulation of endothelial cell migration [GO:0010594]; regulation of glomerular filtration [GO:0003093]; regulation of kinase activity [GO:0043549]; regulation of vasculogenesis [GO:2001212]; T cell mediated cytotoxicity [GO:0001913]
|
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
integrin binding [GO:0005178]; protein kinase binding [GO:0019901]
|
PF00822;
|
1.20.140.150;
|
PMP-22/EMP/MP20 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16487956, ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12189152}. Apical cell membrane {ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:18400107}. Membrane raft {ECO:0000269|PubMed:12763482, ECO:0000269|PubMed:14978215}. Cytoplasm {ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:18400107, ECO:0000269|PubMed:28295343}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:28295343}. Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney (By similarity). Localizes to the apical cell surface in the luminal epithelium and glandular epithelium (PubMed:16487956). Colocalized with ITGB1 and GPI-anchor proteins on plasma membrane (PubMed:12189152, PubMed:14978215). {ECO:0000250|UniProtKB:Q66HH2, ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16487956}.
| null | null | null | null | null |
FUNCTION: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (PubMed:31550239). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (PubMed:14978215, PubMed:17609206). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (PubMed:14978215). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T-cell mediated cytotoxicity (PubMed:12763482). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (PubMed:12189152). Also regulates many processes through PTK2. Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation (By similarity). Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (PubMed:16216233, PubMed:16487956). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (PubMed:28295343). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (PubMed:30773261). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:P54851, ECO:0000269|PubMed:12189152, ECO:0000269|PubMed:12763482, ECO:0000269|PubMed:14978215, ECO:0000269|PubMed:16216233, ECO:0000269|PubMed:16487956, ECO:0000269|PubMed:17609206, ECO:0000269|PubMed:28295343, ECO:0000269|PubMed:30773261, ECO:0000269|PubMed:31550239}.
|
Mus musculus (Mouse)
|
O88664
|
TAOK1_RAT
|
MPSTNRAGSLKDPEIAELFFKEDPEKLFTDLREIGHGSFGAVYFARDVRTNEVVAIKKMSYSGKQSTEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHTMIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQEAHNGPAVEAQEEEEEQDHGGGRTGTVNSVGSNQSIPSMSISASSQSSSVNSLPDASDDKSELDMMEGDHTVMSNSSVIHLKPEEENYQEEGDPRTRASAPQSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQASMEKEAKVMANEEKKFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQELELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTERIRSLLERQAREIEAFDSESMRLGFSNMVLSNLSPEAFSHSYPGASSWSHNPTGGSGPHWGHPMGGTPQAWGHPMQGGPQPWGHPSGPMQGVPRGSSIGVRNSPQALRRTASGGRTEQGMSRSTSVTSQISNGSHMSYT
|
2.7.11.1
| null |
central nervous system neuron development [GO:0021954]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; execution phase of apoptosis [GO:0097194]; microtubule cytoskeleton organization [GO:0000226]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; negative regulation of microtubule depolymerization [GO:0007026]; neuron cellular homeostasis [GO:0070050]; phosphorylation [GO:0016310]; positive regulation of JNK cascade [GO:0046330]; positive regulation of protein acetylation [GO:1901985]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein autophosphorylation [GO:0046777]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cytoskeleton organization [GO:0051493]; regulation of microtubule cytoskeleton organization [GO:0070507]
|
cytoplasm [GO:0005737]; microtubule cytoskeleton [GO:0015630]; perinuclear region of cytoplasm [GO:0048471]
|
alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; beta-tubulin binding [GO:0048487]; kinase activity [GO:0016301]; myosin V binding [GO:0031489]; protein kinase activator activity [GO:0030295]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activator activity [GO:0043539]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Proteolytically processed by caspase-3 (CASP3). {ECO:0000250}.; PTM: Autophosphorylated (By similarity). Phosphorylated by ATM in response to DNA damage. Phosphorylated by LRRK2 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:14517247}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:14517247};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in various processes such as p38/MAPK14 stress-activated MAPK cascade, DNA damage response and regulation of cytoskeleton stability. Phosphorylates MAP2K3, MAP2K6 and MARK2. Acts as an activator of the p38/MAPK14 stress-activated MAPK cascade by mediating phosphorylation and subsequent activation of the upstream MAP2K3 and MAP2K6 kinases. Involved in G-protein coupled receptor signaling to p38/MAPK14. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of MAP2K3 and MAP2K6. Acts as a regulator of cytoskeleton stability by phosphorylating 'Thr-208' of MARK2, leading to activate MARK2 kinase activity and subsequent phosphorylation and detachment of MAPT/TAU from microtubules. Also acts as a regulator of apoptosis: regulates apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation via activation of the MAPK8/JNK cascade. During fetal development, it plays an essential role in the regulation of neuronal differentiation and migration to the cortical plate (By similarity). {ECO:0000250|UniProtKB:Q5F2E8, ECO:0000269|PubMed:14517247, ECO:0000269|PubMed:17047359}.
|
Rattus norvegicus (Rat)
|
O88665
|
BRD7_MOUSE
|
MGKKHKKHKSDRHFYEEYVEKPLKLVLKVGGSEVTELSTGSSGHDSSLFEDRSDHDKHKDRKRKKRKKGEKQAPGEEKGRKRRRVKEDKKKRDRDRAENEVDRDLQCHVPIRLDLPPEKPLTSSLAKQEEVEQTPLQEALNQLMRQLQRKDPSAFFSFPVTDFIAPGYSMIIKHPMDFSTMKEKIKNNDYQSIEELKDNFKLMCTNAMIYNKPETIYYKAAKKLLHSGMKILSQERIQSLKQSIDFMSDLQKTRKQKERTDACQSGEDSGCWQREREDSGDAETQAFRSPAKDNKRKDKDVLEDKWRSSNSEREHEQIERVVQESGGKLTRRLANSQCEFERRKPDGTTTLGLLHPVDPIVGEPGYCPVRLGMTTGRLQSGVNTLQGFKEDKRNRVTPVLYLNYGPYSSYAPHYDSTFANISKDDSDLIYSTYGEDSDLPNNFSISEFLATCQDYPYVMADSLLDVLTKGGHSRSLQDLDMSSPEDEGQTRALDTAKEAEITQIEPTGRLESSSQDRLTALQAVTTFGAPAEVFDSEEAEVFQRKLDETTRLLRELQEAQNERLSTRPPPNMICLLGPSYREMYLAEQVTNNLKELTQQVTPGDVVSIHGVRKAMGISVPSPIVGNSFVDLTGECEEPKETSTAECGPDAS
| null | null |
cell cycle [GO:0007049]; chromatin remodeling [GO:0006338]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; positive regulation of cell differentiation [GO:0045597]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of T cell differentiation [GO:0045582]; regulation of G0 to G1 transition [GO:0070316]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815]; Wnt signaling pathway [GO:0016055]
|
chromatin [GO:0000785]; kinetochore [GO:0000776]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; RSC-type complex [GO:0016586]
|
histone binding [GO:0042393]; lysine-acetylated histone binding [GO:0070577]; p53 binding [GO:0002039]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]
|
PF00439;PF12024;
|
1.20.920.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10526152, ECO:0000269|PubMed:19909775}. Chromosome {ECO:0000250|UniProtKB:Q9NPI1}.
| null | null | null | null | null |
FUNCTION: Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator for TP53-mediated activation of transcription of a set of target genes. Required for TP53-mediated cell-cycle arrest in response to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase (By similarity). Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR. {ECO:0000250, ECO:0000269|PubMed:12941796, ECO:0000269|PubMed:18809673, ECO:0000269|PubMed:19909775}.
|
Mus musculus (Mouse)
|
O88667
|
RAD_MOUSE
|
MTLNGGSGASGSRGAGGRERDRRRGSTPWGPAPPLHRRSMPVDERDLQAALAPGSLATTAAGTRTQGQRLDWPEGSSDSLSSGGSGSEEGVYKVLLLGAPGVGKSALARIFGGIEDGPEAEAAGHTYDRSITVDGEEASLLVYDIWEEDGGCWLPGHCMAMGDAYVIVYSITDKGSFEKASELRVQLRRARQTDDVPIILVGNKSDLVRSREVSVDEGRACAVVFDCKFIETSAALHHNVQALFEGVVRQIRLRRDSKEDNARRQAGTRRRESLGKKAKRFLGRIVARNSRKMAFRAKSKSCHDLSVL
| null | null |
negative regulation of cell growth [GO:0030308]
|
plasma membrane [GO:0005886]; T-tubule [GO:0030315]
|
calcium channel regulator activity [GO:0005246]; calmodulin binding [GO:0005516]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, RGK family
|
PTM: Phosphorylation at Ser-26, Ser-39, Ser-273 and Ser-301 may be involved in regulating inhibition of voltage-gated L-type Ca(2+) channels. {ECO:0000269|PubMed:36424916}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17525370}.
| null | null | null | null | null |
FUNCTION: May regulate basal voltage-dependent L-type Ca(2+) currents and be required for beta-adrenergic augmentation of Ca(2+) influx in cardiomyocytes, thereby regulating increases in heart rate and contractile force (PubMed:36424916). May play an important role in cardiac antiarrhythmia via the strong suppression of voltage-dependent L-type Ca(2+) currents (PubMed:17525370). Regulates voltage-gated L-type calcium channel subunit alpha-1C trafficking to the cell membrane (PubMed:17525370). Inhibits cardiac hypertrophy through the calmodulin-dependent kinase II (CaMKII) pathway (PubMed:18056528). Inhibits phosphorylation and activation of CAMK2D (By similarity). {ECO:0000250|UniProtKB:P55042, ECO:0000269|PubMed:17525370, ECO:0000269|PubMed:18056528, ECO:0000269|PubMed:36424916}.
|
Mus musculus (Mouse)
|
O88668
|
CREG1_MOUSE
|
MAARAPELARSLLAALLAPALVALLVSPASGRGGRDHGDWDVDRRLPPLPPREDGPRVARFVTHVSDWGSLATISTIKEVRGWPFADIISISDGPPGEGTGEPYMYLSPLQQAVSDLQENPEATLTMSLAQTVYCRNHGFDPQSPLCVHIMMSGTVTKVNKTEEDYARDSLFVRHPEMKHWPSSHNWFFAKLKISRIWVLDYFGGPKVVTPEEYFNVTLQ
| null | null |
autophagy [GO:0006914]; endocytosis [GO:0006897]; lysosomal lumen acidification [GO:0007042]; lysosome organization [GO:0007040]; regulation of DNA-templated transcription [GO:0006355]
|
endosome [GO:0005768]; extracellular space [GO:0005615]; lysosome [GO:0005764]; transcription regulator complex [GO:0005667]
|
insulin-like growth factor receptor binding [GO:0005159]
|
PF13883;
| null |
CREG family
|
PTM: N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O88671
|
DLL3_RAT
|
MVSLQVSSLPQTLILAFLLPQALPAGVFELQIHSFGPGPGPGTPRSPCNARGPCRLFFRVCLKPGVSQEAAESLCALGAALSTSGPVYTEQPGVPAAALSLPDGLVRVPFLDAWPGTFSLIIETWREQLGERAAGPAWNLLARVAGRRRLAAGAPWARDVQRTGAWELHFSYRARCEPPAVGAACARLCRSRSAPSRCGPGLRPCTPFPDECEAPRESLTVCRAGCSPEHGYCEEPDECHCLEGWTGPLCTVPVSTSSCLNSRVSGPAGTGCLLPGPGPCDGNPCANGGSCSETPGSFECACPRGFYGPRCEVSGVTCADGPCFNGGLCVGGEDPDSAYVCHCPPAFQGSNCERRVDRCSLQPCQNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGARRCSCALGFGGRDCRERADPCASRPCAHGGRCYAHFSGLVCACAPGYMGVRCEFAVRPDGADAVPAAPRGLRQADSQRFLLPPALGLLAAAALAGAALLLIHVRRRGPGRDTGTRLLSGTREPSVHTLPDALNNLRLQDGAGDGPTSSADWNHPEDGDSRSIYVIPAPSIYAREA
| null | null |
cell fate determination [GO:0001709]; compartment pattern specification [GO:0007386]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of neurogenesis [GO:0050768]; negative regulation of Notch signaling pathway [GO:0045746]; Notch signaling pathway [GO:0007219]; paraxial mesoderm development [GO:0048339]; positive regulation of neurogenesis [GO:0050769]; skeletal system development [GO:0001501]; somitogenesis [GO:0001756]; tissue development [GO:0009888]
|
plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; Notch binding [GO:0005112]
|
PF00008;PF12661;PF07657;
|
2.60.40.3510;2.10.25.10;
| null |
PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O88673
|
DGKA_MOUSE
|
MAKEKGLISPEDFAQLQKYIEYSTKRVSDVLKVFDDGEMNRFCQGDAIGYLGFEQFMKMYLEMEEVPHHLCWALFWSFHTSQVAAEKTKSKANVICLSDVYCYFTLLEGGRPEDKLEFTFKLYDMDRNGILDSTEVEKIILQMMRVAEYLDWDVSELRPILQEMMREMDQDGSGSVSLDEWVRAGATTVPLLVLLGMDVTMKDDGNHIWRPKRFTRLVYCNLCEQSISLGKQGLSCNFCKYIVHDHCAMKAQPCEVSTYAKSRKDIGVQSHLWVRGGCHSGRCDRCQKKIRTYHSLTGLHCVWCHLEIHDDCLQAVGPECDCGLLRDHILPPCSIYPSVLVSGQECKHKTTDDTSLCTPEAFRIEPVSNTHPLLVFINLKSGGKQGQSVLWKFQYILNPRQVFDLKDGPEPGLRFFKDVPQFRILVCGGDGTVGWVLETIDKANFATVPPVAVLPLGTGNDLARCLRWGRGYEGENLRKILKDIELSKVVYLDRWFLEVIPQQNGEKSDPVPSQIINNYFSIGVDASIAHRFHLMREKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESVTVEICGKLLDLSDLSLEGIAVLNIPSTHGGSNLWGDTKRPHGDTCEINQALGSAAKIITDPDILKTCVPDMSDKRLEVVGIEGAIEMGQIYTRLKSAGHRLAKCSEITFQTTKTLPMQIDGEPWMQAPCTIKITHKNQMPMLMGPPSNSYNFFGFWS
|
2.7.1.107; 2.7.1.93
| null |
diacylglycerol metabolic process [GO:0046339]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; phosphatidic acid biosynthetic process [GO:0006654]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]
|
cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
alkylglycerol kinase activity [GO:0047649]; ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; calcium ion binding [GO:0005509]; phospholipid binding [GO:0005543]
|
PF00130;PF14513;PF00609;PF00781;PF13499;
|
2.60.200.40;3.30.60.20;1.10.238.110;1.10.238.10;
|
Eukaryotic diacylglycerol kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P23743}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-sn-glycerol + ATP = 1-O-alkyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:16937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:30616, ChEBI:CHEBI:58014, ChEBI:CHEBI:456216; EC=2.7.1.93; Evidence={ECO:0000250|UniProtKB:P51556}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16938; Evidence={ECO:0000250|UniProtKB:P51556}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:44072, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52595, ChEBI:CHEBI:73332, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycerol + ATP = 1,2-dihexadecanoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:63324, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63325; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43416, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + ATP = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:63328, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:73990, ChEBI:CHEBI:77593, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63329; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378, ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P20192}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429; Evidence={ECO:0000250|UniProtKB:P20192}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + ATP = 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75936, ChEBI:CHEBI:78385, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P51556}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677; Evidence={ECO:0000250|UniProtKB:P51556}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40403, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77184, ChEBI:CHEBI:77186, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40407, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77185, ChEBI:CHEBI:77187, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P23743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408; Evidence={ECO:0000250|UniProtKB:P23743}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-sn-glycerol + ATP = 1-O-hexadecyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41672, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:34115, ChEBI:CHEBI:77580, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P51556}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673; Evidence={ECO:0000250|UniProtKB:P51556};
| null |
PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000250|UniProtKB:P23743}.
| null | null |
FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro as efficiently as diacylglycerol provided it contains an arachidonoyl group. Also involved in the production of alkyl-lysophosphatidic acid, another bioactive lipid, through the phosphorylation of 1-alkyl-2-acetyl glycerol. {ECO:0000250|UniProtKB:P23743}.
|
Mus musculus (Mouse)
|
O88676
|
MMP23_MOUSE
|
MGCRACLRPEASGAVQGRWLGAALSGLCLLSALALLEWLGAPTETAWRAAQGNVDAPNVGSSTAQVPRLLTMSVTRRRRYTLTPARLRWDHFNLTYRVLSFPRNLLSPEETRRGLAAAFRMWSDVSPFSFREVAPERPSDLKIGFYPVNHTDCLVSAVHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTNLVHVAAHEIGHALGLMHSQQDQALMHLNATLRGWKALSQDELWGLHRLYGCLDRIFVCASWARKGFCDVRQRLMKRLCPRSCDFCYEFPFPTVATTTSPTRTKTRLVREGRNMTFHCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEAQLSIIANAVNEGTYTCVVRRHQRVLSTYSWRVRVRN
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; reproduction [GO:0000003]
|
endoplasmic reticulum membrane [GO:0005789]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF00413;PF01549;
|
1.10.10.1940;3.40.390.10;2.60.40.10;
|
Peptidase M10A family
|
PTM: N-glycosylated. {ECO:0000250}.; PTM: Proteolytic cleavage might yield an active form.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:10471791}; Single-pass type II membrane protein {ECO:0000269|PubMed:10471791}. Note=A secreted form produced by proteolytic cleavage may also exist. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O88680
|
C3AR_CAVPO
|
MESSSAETNSTGLHLEPQYQPETILAMAILGLTFVLGLPGNGLVLWVAGLKMRRTVNTVWFLHLTVADFVCCLSLPFSMAHLALRGYWPYGEILCKFIPTVIIFNMFASVFLLTAISLDRCLMVLKPIWCQNHRNVRTACIICGCIWLVAFVLCIPVFVYRETFTLENHTICTYNFSPGSFDYLDYAYDRDAWGYGTPDPIVQLPGEMEHRSDPSSFQTQDGPWSVTTTLYSQTSQRPSEDSFHMDSAKLSGQGKYVDVVLPTNLCGLPMEENRTNTLHNAAFLSSDLDVSNATQKCLSTPEPPQDFWDDLSPFTHEYRTPRLLKVITFTRLVVGFLLPMIIMVACYTLIIFRMRRVRVVKSWNKALHLAMVVVTIFLICWAPYHVFGVLILFINPESRVGAALLSWDHVSIALASANSCFNPFLYALLGRDLRKRVRQSMKGILEAAFSEDISKSTSFIQAKAFSEKHSLSTNV
| null | null |
calcium-mediated signaling [GO:0019722]; chemotaxis [GO:0006935]; inflammatory response [GO:0006954]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of macrophage chemotaxis [GO:0010759]; positive regulation of neutrophil chemotaxis [GO:0090023]; positive regulation of vascular endothelial growth factor production [GO:0010575]
|
plasma membrane [GO:0005886]
|
complement component C3a receptor activity [GO:0004876]; complement component C5a receptor activity [GO:0004878]; G protein-coupled receptor activity [GO:0004930]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production.
|
Cavia porcellus (Guinea pig)
|
O88689
|
PCDA4_MOUSE
|
MEFSWGSGQESQRLLLSFLLLAIWEAGNSQIHYSIPEEAKHGTFVGRIAQDLGLELTELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPRFPTTQKNLFIAESRPLDTWFPLEGASDADIGINAVLTYRLSPNDYFSLEKPSNDERVKGLGLVLRKSLDREETPEIILVLTVTDGGKPELTGSVQLLITVLDANDNAPVFDRSLYTVKLPENVPNGTLVVKVNASDLDEGVNGDIMYSFSTDISPNVKYKFHIDPVSGEIIVKGYIDFEECKSYEILIEGIDKGQLPLSGHCKVIVQVEDINDNVPELEFKSLSLPIRENSPVGTVIALISVSDRDTGVNGQVTCSLTSHVPFKLVSTFKNYYSLVLDSALDRETTADYKVVVTARDGGSPSLWATASVSVEVADVNDNAPVFAQPEYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLRFQVSARDAGVPALGSNVTLQVFVLDENDNAPTLLEPEAGVSGGIVSRLVSRSVGAGHVVAKVRAVDADSGYNAWLSYELQSSEGNSRSLFRVGLYTGEISTTRILDEADSPRQRLLVLVKDHGDPAMIVTATVLVSLVENGPVPKAPSRVSTSVTHSEASLVDVNVYLIIAICAVSSLLVLTLLLYTALRCSTVPSESVCGPPKPVMVCSSAVGSWSYSQQRRQRVCSGEYPPKTDLMAFSPSLSDSRDREDQLQSAEDSSGKPRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ
| null | null |
cell adhesion [GO:0007155]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]
|
endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synapse [GO:0045202]
|
calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]
|
PF00028;PF08266;PF15974;
|
2.60.40.60;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9655502}; Single-pass type I membrane protein {ECO:0000305|PubMed:27161523, ECO:0000305|PubMed:9655502}. Note=Detected in dendrites and synapses. {ECO:0000269|PubMed:9655502}.
| null | null | null | null | null |
FUNCTION: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination (Probable). Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain (PubMed:27161523). {ECO:0000305|PubMed:27161523}.
|
Mus musculus (Mouse)
|
O88693
|
CEGT_MOUSE
|
MALLDLAQEGMALFGFVLFVVLWLMHFMSIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPAYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGFAATLEQVYFGTSHPRSYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRGWRFSMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVASLIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMTIYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV
|
2.4.1.80
| null |
cell differentiation [GO:0030154]; cornified envelope assembly [GO:1903575]; establishment of skin barrier [GO:0061436]; glucosylceramide biosynthetic process [GO:0006679]; intestinal lipid absorption [GO:0098856]; keratinocyte differentiation [GO:0030216]; leptin-mediated signaling pathway [GO:0033210]; neuron development [GO:0048666]; protein lipidation [GO:0006497]; regulation of signal transduction [GO:0009966]
|
Golgi membrane [GO:0000139]; membrane [GO:0016020]
|
ceramide glucosyltransferase activity [GO:0008120]; dihydroceramide glucosyltransferase activity [GO:0102769]
|
PF13506;
| null |
Glycosyltransferase 2 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:10430909}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R0E0}.
|
CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + UDP-alpha-D-glucose = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP; Xref=Rhea:RHEA:12088, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.80; Evidence={ECO:0000269|PubMed:10430909}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12089; Evidence={ECO:0000269|PubMed:10430909}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + UDP-alpha-D-xylose = a beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP; Xref=Rhea:RHEA:70243, ChEBI:CHEBI:15378, ChEBI:CHEBI:52639, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:189068; Evidence={ECO:0000269|PubMed:33361282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70244; Evidence={ECO:0000269|PubMed:33361282}; CATALYTIC ACTIVITY: Reaction=N-(9Z-octadecenoyl)-sphing-4-enine + UDP-alpha-D-xylose = beta-D-xylosyl-(1<->1')-N-(9Z-octadecenoyl)-sphing-4-enine + H(+) + UDP; Xref=Rhea:RHEA:70247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:77996, ChEBI:CHEBI:189081; Evidence={ECO:0000269|PubMed:33361282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70248; Evidence={ECO:0000269|PubMed:33361282};
| null |
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:10430909, ECO:0000269|PubMed:16109770, ECO:0000269|PubMed:28373486, ECO:0000269|PubMed:33361282}.
| null | null |
FUNCTION: Participates in the initial step of the glucosylceramide-based glycosphingolipid/GSL synthetic pathway at the cytosolic surface of the Golgi. Catalyzes the transfer of glucose from UDP-glucose to ceramide to produce glucosylceramide/GlcCer (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) (PubMed:10430909, PubMed:16109770, PubMed:28373486). Glucosylceramide is the core component of glycosphingolipids/GSLs, amphipathic molecules consisting of a ceramide lipid moiety embedded in the outer leaflet of the membrane, linked to one of hundreds of different externally oriented oligosaccharide structures (PubMed:10430909). Glycosphingolipids are essential components of membrane microdomains that mediate membrane trafficking and signal transduction (PubMed:10430909). They are implicated in many fundamental cellular processes, including growth, differentiation, migration, morphogenesis, cell-to-cell and cell-to-matrix interactions (PubMed:10430909). They are required for instance in the proper development and functioning of the nervous system (PubMed:16109770). As an example of their role in signal transduction, they regulate the leptin receptor/LEPR in the leptin-mediated signaling pathway (PubMed:23554574). They also play an important role in the establishment of the skin barrier regulating keratinocyte differentiation and the proper assembly of the cornified envelope (PubMed:17145749, PubMed:23748427). The biosynthesis of GSLs is also required for the proper intestinal endocytic uptake of nutritional lipids (PubMed:22851168). Catalyzes the synthesis of xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) using UDP-Xyl as xylose donor (PubMed:33361282). {ECO:0000269|PubMed:10430909, ECO:0000269|PubMed:16109770, ECO:0000269|PubMed:17145749, ECO:0000269|PubMed:22851168, ECO:0000269|PubMed:23554574, ECO:0000269|PubMed:23748427, ECO:0000269|PubMed:28373486, ECO:0000269|PubMed:33361282, ECO:0000303|PubMed:10430909}.
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Mus musculus (Mouse)
|
O88696
|
CLPP_MOUSE
|
MWPRVLLGEARVAVDGCRALLSRLAVHFSPPWTAVSCSPLRRSLHGTATRAFPLIPIVVEQTGRGERAYDIYSRLLRERIVCVMGPIDDSVASLVIAQLLFLQSESNKKPIHMYINSPGGVVTAGLAIYDTMQYILNPICTWCVGQAASMGSLLLAAGSPGMRHSLPNSRIMIHQPSGGARGQATDIAIQAEEIMKLKKQLYNIYAKHTKQSLQVIESAMERDRYMSPMEAQEFGILDKVLVHPPQDGEDEPELVQKETATAPTDPPAPTST
|
3.4.21.92
| null |
membrane protein proteolysis [GO:0033619]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]; proteolysis involved in protein catabolic process [GO:0051603]
|
endopeptidase Clp complex [GO:0009368]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
ATP-dependent peptidase activity [GO:0004176]; ATPase binding [GO:0051117]; identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252]
|
PF00574;
| null |
Peptidase S14 family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:10754102, ECO:0000269|PubMed:22710082}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).; EC=3.4.21.92; Evidence={ECO:0000250|UniProtKB:Q16740};
| null | null | null | null |
FUNCTION: Protease component of the Clp complex that cleaves peptides and various proteins in an ATP-dependent process. Has low peptidase activity in the absence of CLPX. The Clp complex can degrade CSN1S1, CSN2 and CSN3, as well as synthetic peptides (in vitro) and may be responsible for a fairly general and central housekeeping function rather than for the degradation of specific substrates. Cleaves PINK1 in the mitochondrion. {ECO:0000250|UniProtKB:Q16740}.
|
Mus musculus (Mouse)
|
O88697
|
STK16_MOUSE
|
MGHALCVCSRGTVIIDNKRYLFVQKLGEGGFSYVDLVEGLHDGHFYALKRILCHEQQDQEEAQREAEMHRLFQHPNILRLMAYSLKERGAKHEAWLLLPFFKKGTLWNEIERLKDQGSFLTEDQILPLLLGISRGLEAIHAKGYAHRDLKPTNILLGDEGQPVLMDLGSMNQACIQVEGSRQALALQDWAAQRCTISYRAPELFSVQSHCVIDERTDVWSLGCVLYAMMFGEGPYDMVFQKGDSVALAVQNELSIPQSPRHSSALRQLLSSMMTVDPQQRPHIPVLLSQLEALQPPAPGQHTTQI
|
2.7.10.2; 2.7.11.1
| null |
cellular response to transforming growth factor beta stimulus [GO:0071560]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of vacuole fusion, non-autophagic [GO:0032889]; vacuolar protein processing [GO:0006624]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
|
PTM: Mainly autophosphorylated on serine/threonine residues. Also autophosphorylated on Tyr-198 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9712705}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Associates with Golgi and Golgi-derived vesicles.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
| null | null | null | null |
FUNCTION: Membrane-associated protein kinase that phosphorylates on serine and threonine residues. In vitro substrates include DRG1, ENO1 and EIF4EBP1. Also autophosphorylates (By similarity). May be involved in secretory vesicle trafficking or intracellular signaling. May have a role in regulating stromal-epithelial interactions that occur during ductal morphogenesis in the mammary gland. May be involved in TGF-beta signaling. Able to autophosphorylate on Tyr residue; it is however unclear whether it has tyrosine-protein kinase toward other proteins. {ECO:0000250, ECO:0000269|PubMed:9878782}.
|
Mus musculus (Mouse)
|
O88700
|
BLM_MOUSE
|
MAAVPLNNLQEQLQRHSARKLNNQPSLSKPKSLGFTFKKKTSEGDVSVTSVSVVKTPALSDKDVNVSEAFSFTESPLHKPKQQAKIEGFFKHFPGRQQSKGTCSEPSLPATVQTAQDTLCTTPKTPTAKKLPVAVFKKLEFSSSADSLSDWADMDDFDMSASDAFASLAKNPATRVSTAQKMKKTKRNFFKPPPRKANAVKTDLTPPSPECLQVDLTKESEEEEEEEEEAEGADCLSRDVICIDNDSASEELTEKDTQESQSLKAHLGAERGDSEKKSHEDEAVFHSVQNTEYFEHNDNDYDIDFVPPSPEEIISTASSSLKCSSMLKDLDDSDKEKGILSTSEELLSKPEEMTTHKSDAGTSKDCDAQQIRIQQQLIHVMEHICKLVDTVPTDELEALNCGTELLQQRNIRRKLLAEAGFNGNDVRLLGSLWRHRPDSLDNTVQGDSCPVGHPNKELNSPYLLSHSPSTEECLPTTTPGKTGFSATPKNLFERPLLNSHLQKSFVSSNWAETPRMENRNESTDFPGSVLTSTTVKAQSKQAASGWNVERHGQASYDIDNFNIDDFDDDDDDDDWENIMHNFPASKSSTATYPPIKEGGPVKSLSERISSAKAKFLPVVSTAQNTNLSESIQNCSDKLAQNLSSKNPKHEHFQSLNFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQREGLAALAYHAGLSDSARDEVQHKWINQDNCQVICATIAFGMGIDKPDVRFVIHASLPKSMEGYYQESGRAGRDGEISHCVLFYTYHDVTRLKRLIMMEKDGNYHTKETHVNNLYSMVHYCENITECRRIQLLAYFGEKGFNPDFCKKYPDVSCDNCCKTKDYKTKDVTDDVKNIIRFVQEHSSSPGTRNIGPAGRFTLNMLVDIFLGSKSAKVKSGIFGKGTTYSRHNAERLFKKLILDKILDEDLYINANDQPIAYVMLGTKAHSVLSGHLKVDFMETENSSSIKKQKALVAKVSQREEVVKKCLGELTEVCKLLGKVFGVHYFNIFNTATLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVIPVLQKYSEWTVPAEDGSPGARGAPEDTEEEEEEAPVSSHYFANQTRNERKRKKMSATHKPKRRRTSYGGFRAKGGSTTCRKTTSKSKFYGVTGSRSASCASQATSSASRKLGIMAPPKPVNRTFLRPSYAFS
|
5.6.2.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P54132}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P54132};
|
alpha-beta T cell differentiation [GO:0046632]; alpha-beta T cell proliferation [GO:0046633]; cellular response to camptothecin [GO:0072757]; cellular response to hydroxyurea [GO:0072711]; cellular response to ionizing radiation [GO:0071479]; cellular response to xenobiotic stimulus [GO:0071466]; chromosome organization [GO:0051276]; DN4 thymocyte differentiation [GO:1904157]; DNA damage response [GO:0006974]; DNA double-strand break processing [GO:0000729]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; G-quadruplex DNA unwinding [GO:0044806]; immature T cell proliferation in thymus [GO:0033080]; mitotic recombination [GO:0006312]; negative regulation of mitotic recombination [GO:0045950]; negative regulation of thymocyte apoptotic process [GO:0070244]; positive regulation of alpha-beta T cell proliferation [GO:0046641]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of immature T cell proliferation in thymus [GO:0033092]; protein complex oligomerization [GO:0051259]; protein homooligomerization [GO:0051260]; regulation of DNA-templated DNA replication [GO:0090329]; replication fork processing [GO:0031297]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414]; resolution of DNA recombination intermediates [GO:0071139]; telomere maintenance [GO:0000723]
|
chromosome [GO:0005694]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; male germ cell nucleus [GO:0001673]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pronucleus [GO:0045120]; RecQ family helicase-topoisomerase III complex [GO:0031422]; replication fork [GO:0005657]; replisome [GO:0030894]
|
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; forked DNA-dependent helicase activity [GO:0061749]; four-way junction DNA binding [GO:0000400]; four-way junction helicase activity [GO:0009378]; isomerase activity [GO:0016853]; protein homodimerization activity [GO:0042803]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270]
|
PF08072;PF16204;PF16202;PF00270;PF00271;PF00570;PF16124;PF09382;
|
1.10.150.80;3.40.50.300;1.10.10.10;
|
Helicase family, RecQ subfamily
|
PTM: Poly-ubiquitinated by TRIM25 at Lys-264. Deubiquitinated by USP37; leading to stabilization in order to sustain the DNA damage response (By similarity). {ECO:0000250|UniProtKB:P54132, ECO:0000269|PubMed:29125140}.; PTM: Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29125140}. Note=Localized to DNA replication forks, especially after DNA damage. {ECO:0000269|PubMed:29125140}.
|
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:9655940}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:9655940};
| null | null | null | null |
FUNCTION: ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction (PubMed:9840919). Participates in DNA replication and repair (By similarity). Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA (PubMed:9840919). Negatively regulates sister chromatid exchange (SCE) (PubMed:27010503, PubMed:9840919). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction (By similarity). Recruited by the KHDC3-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks. {ECO:0000250|UniProtKB:P54132, ECO:0000269|PubMed:27010503, ECO:0000269|PubMed:29125140, ECO:0000269|PubMed:9840919}.
|
Mus musculus (Mouse)
|
O88703
|
HCN2_MOUSE
|
MDARGGGGRPGDSPGTTPAPGPPPPPPPPAPPQPQPPPAPPPNPTTPSHPESADEPGPRARLCSRDSACTPGAAKGGANGECGRGEPQCSPEGPARGPKVSFSCRGAASGPSAAEEAGSEEAGPAGEPRGSQASFLQRQFGALLQPGVNKFSLRMFGSQKAVEREQERVKSAGAWIIHPYSDFRFYWDFTMLLFMVGNLIIIPVGITFFKDETTAPWIVFNVVSDTFFLMDLVLNFRTGIVIEDNTEIILDPEKIKKKYLRTWFVVDFVSSIPVDYIFLIVEKGIDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVMRICNLISMMLLLCHWDGCLQFLVPMLQDFPSDCWVSINNMVNHSWSELYSFALFKAMSHMLCIGYGRQAPESMTDIWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADFRQKIHDYYEHRYQGKMFDEDSILGELNGPLREEIVNFNCRKLVASMPLFANADPNFVTAMLTKLKFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKEMKLSDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLHKVQHDLSSGVFNNQENAIIQEIVKYDREMVQQAELGQRVGLFPPPPPPQVTSAIATLQQAVAMSFCPQVARPLVGPLALGSPRLVRRAPPGPLPPAASPGPPAASPPAAPSSPRAPRTSPYGVPGSPATRVGPALPARRLSRASRPLSASQPSLPHGVPAPSPAASARPASSSTPRLGPAPTARTAAPSPDRRDSASPGAASGLDPLDSARSRLSSNL
| null | null |
cellular response to cAMP [GO:0071320]; cellular response to cGMP [GO:0071321]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transmembrane transport [GO:0071805]; regulation of membrane depolarization [GO:0003254]; regulation of membrane potential [GO:0042391]; sodium ion import across plasma membrane [GO:0098719]; sodium ion transmembrane transport [GO:0035725]
|
axon [GO:0030424]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; dendritic shaft [GO:0043198]; HCN channel complex [GO:0098855]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; somatodendritic compartment [GO:0036477]
|
cAMP binding [GO:0030552]; identical protein binding [GO:0042802]; intracellularly cAMP-activated cation channel activity [GO:0005222]; molecular adaptor activity [GO:0060090]; PDZ domain binding [GO:0030165]; protein-containing complex binding [GO:0044877]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated sodium channel activity [GO:0005248]
|
PF00027;PF00520;PF08412;
|
1.10.287.70;1.10.287.630;2.60.120.10;
|
Potassium channel HCN family
|
PTM: Phosphorylation at Ser-641 by PRKG2 shifts the voltage-dependence to more negative voltages, hence counteracting the stimulatory effect of cGMP on gating. {ECO:0000269|PubMed:21347269}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10962006, ECO:0000269|PubMed:11096117, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12193608, ECO:0000269|PubMed:17562314, ECO:0000269|PubMed:23103389}; Multi-pass membrane protein {ECO:0000269|PubMed:10962006, ECO:0000269|PubMed:11096117, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12193608, ECO:0000269|PubMed:17562314, ECO:0000269|PubMed:23103389}.
| null | null | null | null | null |
FUNCTION: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. {ECO:0000269|PubMed:10962006, ECO:0000269|PubMed:11096117, ECO:0000269|PubMed:11741901, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:12193608, ECO:0000269|PubMed:12968185, ECO:0000269|PubMed:17562314, ECO:0000269|PubMed:23103389}.
|
Mus musculus (Mouse)
|
O88704
|
HCN1_MOUSE
|
MEGGGKPNSASNSRDDGNSVFPSKAPATGPVAADKRLGTPPGGGAAGKEHGNSVCFKVDGGGGEEPAGSFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILSELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIPPINYPQMTALNCTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPIQSPLATRTFHYASPTASQLSLMQQPQQQLPQSQVQQTQTQTQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPQTPGSSTPKNEVHKSTQALHNTNLTKEVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVAAVHSTGLQAGSRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAVQRESPSVLNTDPDAEKPRFASNL
| null | null |
apical protein localization [GO:0045176]; cellular response to cAMP [GO:0071320]; general adaptation syndrome, behavioral process [GO:0051867]; negative regulation of action potential [GO:0045759]; neuronal action potential [GO:0019228]; positive regulation of membrane hyperpolarization [GO:1902632]; potassium ion transmembrane transport [GO:0071805]; protein homotetramerization [GO:0051289]; regulation of membrane depolarization [GO:0003254]; regulation of membrane hyperpolarization [GO:1902630]; regulation of postsynaptic membrane potential [GO:0060078]; response to calcium ion [GO:0051592]; retinal cone cell development [GO:0046549]; sodium ion transmembrane transport [GO:0035725]
|
apical dendrite [GO:0097440]; axon [GO:0030424]; axon terminus [GO:0043679]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; dendritic shaft [GO:0043198]; glutamatergic synapse [GO:0098978]; HCN channel complex [GO:0098855]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic active zone membrane [GO:0048787]; somatodendritic compartment [GO:0036477]
|
cAMP binding [GO:0030552]; identical protein binding [GO:0042802]; intracellular cAMP-activated cation channel activity involved in regulation of presynaptic membrane potential [GO:0140232]; intracellularly cAMP-activated cation channel activity [GO:0005222]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; voltage-gated monoatomic cation channel activity [GO:0022843]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated sodium channel activity [GO:0005248]
|
PF00027;PF00520;PF08412;
|
1.10.287.70;1.10.287.630;2.60.120.10;
|
Potassium channel HCN family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9405696}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11459060, ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}; Multi-pass membrane protein {ECO:0000269|PubMed:22006928}.
|
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:9630217}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:9630217};
| null | null | null | null |
FUNCTION: Hyperpolarization-activated ion channel that are permeable to sodium and potassium ions (PubMed:12034718, PubMed:22006928, PubMed:9630217). Exhibits weak selectivity for potassium over sodium ions (PubMed:11459060). Contributes to the native pacemaker currents in heart (If) and in neurons (Ih) (PubMed:11459060). Participates in cerebellar mechanisms of motor learning (PubMed:14651847). May mediate responses to sour stimuli (PubMed:11675786). {ECO:0000269|PubMed:11459060, ECO:0000269|PubMed:11675786, ECO:0000269|PubMed:12034718, ECO:0000269|PubMed:14651847, ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}.
|
Mus musculus (Mouse)
|
O88705
|
HCN3_MOUSE
|
MEEEARPAAGAGEAATPARETPPAAPAQARAASGGVPESAPEPKRRQLGTLLQPTVNKFSLRVFGSHKAVEIEQERVKSAGAWIIHPYSDFRFYWDLIMLLLMVGNLIVLPVGITFFKEENSPPWIVFNVLSDTFFLLDLVLNFRTGIVVEEGAEILLAPRAIRTRYLRTWFLVDLISSIPVDYIFLVVELEPRLDAEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPMLQDFPSDCWVSMNRMVNHSWGRQYSHALFKAMSHMLCIGYGQQAPVGMPDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADTRQRIHEYYEHRYQGKMFDEESILGELSEPLREEIINFTCRGLVAHMPLFAHADPSFVTAVLTKLRFEVFQPGDLVVREGSVGRKMYFIQHGLLSVLARGARDTRLTDGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDHFNAVLEEFPMMRRAFETVAMDRLRRIGKKNSILQRKRSEPSPGSSGGVMEQHLVQHDRDMARGVRGLAPGTGARLSGKPVLWEPLVHAPLQAAAVTSNVAIALTHQRGPLPLSPDSPATLLARSARRSAGSPASPLVPVRAGPLLARGPWASTSRLPAPPARTLHASLSRTGRSQVSLLGPPPGGGARRLGPRGRPLSASQPSLPQRATGDGSPRRKGSGSERLPPSGLLAKPPGTVQPPRSSVPEPVTPRGPQISANM
| null | null |
cellular response to dopamine [GO:1903351]; potassium ion transmembrane transport [GO:0071805]; regulation of membrane depolarization [GO:0003254]; sodium ion transmembrane transport [GO:0035725]
|
axon [GO:0030424]; cone cell pedicle [GO:0044316]; dendrite [GO:0030425]; HCN channel complex [GO:0098855]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
|
cAMP binding [GO:0030552]; voltage-gated potassium channel activity [GO:0005249]; voltage-gated sodium channel activity [GO:0005248]
|
PF00027;PF00520;PF08412;
|
1.10.287.70;1.10.287.630;2.60.120.10;
|
Potassium channel HCN family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923185, ECO:0000269|PubMed:23382386}; Multi-pass membrane protein {ECO:0000269|PubMed:15923185}.
| null | null | null | null | null |
FUNCTION: Hyperpolarization-activated potassium channel. May also facilitate the permeation of sodium ions. {ECO:0000269|PubMed:15923185}.
|
Mus musculus (Mouse)
|
O88708
|
ORC4_MOUSE
|
MSSRKTKSNAHAECLSQVQRILRERFCHHSPHSNLFGVQVQYKHLIELLKRTAIYGESNSVLIVGPRGSGKTTLLNHALKELMEIEVSENVIQVHLNGLLQTNEKIALKEITRQLNLDNVVEDKVFGSFAENLSFLLEALQKGDRTSSCPVIFILDEFDIFAHQKNQTLLYNLFDISQSAQTPVAVIGLTCRLDILELLEKRVKSRFSHRQIHLMNSFDFPQYLKIFKEQLSLPAEFPDKAFAERWNENVHCLSEDSTVLEVLQKHFSVNKNLQSLHMLLMLALNRVTVSHPFMTSADLMEAQHMCSLDSKANIVHGLSVLEICLIIAMKHLNDIYEEEPFNFQMVYNEFQKFIQRKAHSVYNFEKPVVMKAFEHLQQLELIKPVERTSVNSQREYQLVKLLLDNTQIMNALQKYSNCPTDVRQWATSSLSWL
| null | null |
DNA replication [GO:0006260]; DNA replication initiation [GO:0006270]; polar body extrusion after meiotic divisions [GO:0040038]; protein polymerization [GO:0051258]
|
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear origin of replication recognition complex [GO:0005664]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA replication origin binding [GO:0003688]
|
PF13191;PF14629;
|
3.40.50.300;
|
ORC4 family
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3 (By similarity). Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. {ECO:0000250}.
|
Mus musculus (Mouse)
|
O88712
|
CTBP1_MOUSE
|
MGSSHLLNKGLPLGVRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYSRYPPGVVSVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHTSDQL
|
1.1.1.-
|
COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; Note=Cofactor binding induces a conformational change. {ECO:0000250};
|
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; presynapse to nucleus signaling pathway [GO:0099526]; regulation of cell cycle [GO:0051726]; regulation of transcription by RNA polymerase II [GO:0006357]; synaptic vesicle clustering [GO:0097091]; synaptic vesicle endocytosis [GO:0048488]; white fat cell differentiation [GO:0050872]
|
cytoplasm [GO:0005737]; extrinsic component of presynaptic endocytic zone membrane [GO:0098894]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; presynapse [GO:0098793]; presynaptic active zone cytoplasmic component [GO:0098831]; transcription repressor complex [GO:0017053]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor binding [GO:0140297]; NAD binding [GO:0051287]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; PDZ domain binding [GO:0030165]; protein homodimerization activity [GO:0042803]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713]; transcription coregulator binding [GO:0001221]; transcription corepressor activity [GO:0003714]; transcription corepressor binding [GO:0001222]
|
PF00389;PF02826;
|
3.40.50.720;
|
D-isomer specific 2-hydroxyacid dehydrogenase family
|
PTM: ADP-ribosylated; when cells are exposed to brefeldin A. {ECO:0000250}.; PTM: The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-423 induces proteasomal degradation (By similarity). {ECO:0000250}.; PTM: Sumoylation on Lys-429 is promoted by the E3 SUMO-protein ligase CBX4. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13363}. Nucleus {ECO:0000250|UniProtKB:Q13363}.
| null | null | null | null | null |
FUNCTION: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. {ECO:0000269|PubMed:10369679, ECO:0000269|PubMed:10567582, ECO:0000269|PubMed:16326862, ECO:0000269|PubMed:18483224, ECO:0000269|PubMed:19103759}.
|
Mus musculus (Mouse)
|
O88713
|
KLRG1_MOUSE
|
MADSSIYSTLELPEAPQVQDESRWKLKAVLHRPHLSRFAMVALGLLTVILMSLLMYQRILCCGSKDSTCSHCPSCPILWTRNGSHCYYFSMEKKDWNSSLKFCADKGSHLLTFPDNQGVKLFGEYLGQDFYWIGLRNIDGWRWEGGPALSLRILTNSLIQRCGAIHRNGLQASSCEVALQWICKKVLY
| null | null |
cell surface receptor signaling pathway [GO:0007166]; innate immune response [GO:0045087]
|
intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]
|
PF00059;
|
3.10.100.10;
| null |
PTM: Phosphorylated in response to monoclonal antibody G63 binding and antigenic stimulation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19604491}; Single-pass type II membrane protein {ECO:0000269|PubMed:19604491}.
| null | null | null | null | null |
FUNCTION: Plays an inhibitory role on natural killer (NK) cells and T-cell functions upon binding to their non-MHC ligands. May mediate missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells. {ECO:0000269|PubMed:19604491}.
|
Mus musculus (Mouse)
|
O88721
|
V2R_MOUSE
|
MILVSTTSAVPGALSSPSSPSNSSQEELLDDRDPLLVRAELALLSTIFVAVALSNGLVLGALIRRGRRGRWAPMHVFISHLCLADLAVALFQVLPQLAWDATDRFHGPDALCRAVKYLQMVGMYASSYMILAMTLDRHRAICRPMLAYRHGGGARWNRPVLVAWAFSLLLSLPQLFIFAQRDVGNGSGVFDCWARFAEPWGLRAYVTWIALMVFVAPALGIAACQVLIFREIHASLVPGPSERAGRRRRGHRTGSPSEGAHVSAAMAKTVRMTLVIVIVYVLCWAPFFLVQLWAAWDPEAPLERPPFVLLMLLASLNSCTNPWIYASFSSSVSSELRSLLCCAQRHTTHSLGPQDESCATASSSLMKDTPS
| null | null |
cellular response to hormone stimulus [GO:0032870]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of urine volume [GO:0035811]; positive regulation of blood pressure [GO:0045777]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; positive regulation of intracellular signal transduction [GO:1902533]; positive regulation of systemic arterial blood pressure [GO:0003084]; positive regulation of vasoconstriction [GO:0045907]; regulation of systemic arterial blood pressure by vasopressin [GO:0001992]; response to cytokine [GO:0034097]; telencephalon development [GO:0021537]
|
endocytic vesicle [GO:0030139]; endosome [GO:0005768]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
peptide binding [GO:0042277]; signaling receptor activity [GO:0038023]; vasopressin receptor activity [GO:0005000]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Vasopressin/oxytocin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30518}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P30518}.
| null | null | null | null | null |
FUNCTION: Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption (By similarity). {ECO:0000250|UniProtKB:P30518}.
|
Mus musculus (Mouse)
|
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