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
O70157
TOP3A_MOUSE
MIFPVTLLAFQWHRRPGGRALSRAAMEVAFRGVRKVLCVAEKNDAAKGIADLLSNGRMRRKEGLSKFNKIYEFDYHLYGQNVTMIMTSVSGHLLAHDFQMQFRKWQSCNPLVLFEAEIEKYCPENFIDIKKTLERETHHCQALVIWTDCDREGENIGFEIIHVCKAVKPNLRVLRARFSEITPHAVRTACENLTEPDQRVSDAVDVRQELDLRIGAAFTRFQTLRLQRIFPEVLAEQLISYGSCQFPTLGFVVERFKAIQAFVPEVFHKIKVTHDHKDGTVEFNWKRYRLFNHTACLVLYQLCMEDPMATVVEVRSKPKS...
5.6.2.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
chromosome separation [GO:0051304]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA topological change [GO:0006265]; double-strand break repair via homologous recombination [GO:0000724]; mitochondrial DNA metabolic process [GO:0032042]; resolution of DNA recombination intermediates [GO:0071139]
mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; RecQ family helicase-topoisomerase III complex [GO:0031422]
DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; single-stranded DNA binding [GO:0003697]; zinc ion binding [GO:0008270]
PF01131;PF01751;PF01396;PF06839;
3.40.50.140;3.30.65.10;1.10.460.10;2.70.20.10;1.10.290.10;
Type IA topoisomerase family
null
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q13472}.
CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10131};
null
null
null
null
FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by...
Mus musculus (Mouse)
O70161
PI51C_MOUSE
MELEVPDEAESAEAGAVTAEAAWSAESGAAAGMTQKKAGLAEAPLVTGQPGPGHGKKLGHRGVDASGETTYKKTTSSTLKGAIQLGIGYTVGNLSSKPERDVLMQDFYVVESIFFPSEGSNLTPAHHFQDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCNEPLIELSNPGASGSVFYVTSDDEFIIKTVMHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQSGGKNIRVVVMNNVLPRVVKMHLKFDLKGSTYKRRASKKEKEKSLPTYKDLDFMQDMPEGLLLDSDTFGALVKTLQRDCLVLESFKIMDYSLL...
2.7.1.68
null
axonogenesis [GO:0007409]; chemotaxis [GO:0006935]; exocytosis [GO:0006887]; phagocytosis [GO:0006909]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; platelet ag...
adherens junction [GO:0005912]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynaptic endocytic zone membrane [GO:0098835]; ruffle membrane [GO:00325...
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; ATP binding [GO:0005524]
PF01504;
3.30.810.10;3.30.800.10;
null
PTM: Phosphorylation on Ser-645 negatively regulates binding to TLN2 and is strongly stimulated in mitosis. Phosphorylation on Tyr-644 is necessary for targeting to focal adhesions. Phosphorylation on Ser-645 and Tyr-644 are mutually exclusive. Phosphorylated by SYK and CSK. Tyrosine phosphorylation is enhanced by PTK2...
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q5I6B8}. Endomembrane system {ECO:0000250|UniProtKB:Q5I6B8}. Cytoplasm {ECO:0000269|PubMed:19153220, ECO:0000269|PubMed:20622009}. Cell junction, focal adhesion {ECO:0000269|PubMed:12422220, ECO:0000269|PubMed:1469...
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68; Evide...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37 uM for phosphatidylinositol-4-phosphate/PtdIns(4)P {ECO:0000269|PubMed:9535851}; KM=39 uM for ATP {ECO:0000269|PubMed:9535851}; KM=1.6 uM for 1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4-phosphate {ECO:0000269|PubMed:2...
null
null
null
FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesio...
Mus musculus (Mouse)
O70165
FCN1_MOUSE
MQWPTLWAFSGLLCLCPSQALGQERGACPDVKVVGLGAQDKVVVIQSCPGFPGPPGPKGEPGSPAGRGERGFQGSPGKMGPAGSKGEPGTMGPPGVKGEKGDTGAAPSLGEKELGDTLCQRGPRSCKDLLTRGIFLTGWYTIHLPDCRPLTVLCDMDVDGGGWTVFQRRVDGSIDFFRDWDSYKRGFGNLGTEFWLGNDYLHLLTANGNQELRVDLQDFQGKGSYAKYSSFQVSEEQEKYKLTLGQFLEGTAGDSLTKHNNMSFTTHDQDNDANSMNCAALFHGAWWYHNCHQSNLNGRYLSGSHESYADGINWGTGQGH...
null
null
cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation, lectin pathway [GO:0001867]; G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of interleukin-8 production [GO:0032757]
collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
antigen binding [GO:0003823]; carbohydrate binding [GO:0030246]; carbohydrate derivative binding [GO:0097367]; metal ion binding [GO:0046872]; pattern recognition receptor activity [GO:0038187]; signaling receptor binding [GO:0005102]
PF01391;PF00147;
3.90.215.10;
Ficolin lectin family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O00602}. Cell membrane {ECO:0000250|UniProtKB:O00602}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00602}; Extracellular side {ECO:0000250|UniProtKB:O00602}. Note=Found on the monocyte and granulocyte surface. {ECO:0000250|UniProtKB:O00602}.
null
null
null
null
null
FUNCTION: Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, F...
Mus musculus (Mouse)
O70166
STMN3_MOUSE
MASTVSAYKEKMKELSVLSLICSCFYSQPHPNTIYQYGDMEVKQLDKRASGQSFEVILKSPSDLSPESPVLSSPPKRKDASLEELQKRLEAAEERRKTQEAQVLKQLAERREHEREVLHKALEENNNFSRLAEEKLNYKMELSKEIREAHLAALRERLREKELHAAEVRRNKEQREEMSG
null
null
blastocyst hatching [GO:0001835]; cytoplasmic microtubule organization [GO:0031122]; microtubule depolymerization [GO:0007019]; negative regulation of Rac protein signal transduction [GO:0035021]; neuron projection development [GO:0031175]; regulation of cytoskeleton organization [GO:0051493]; regulation of GTPase acti...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; growth cone [GO:0030426]; neuron projection [GO:0043005]; perinuclear region of cytoplasm [GO:0048471]
protein domain specific binding [GO:0019904]; protein-folding chaperone binding [GO:0051087]; tubulin binding [GO:0015631]
PF00836;
6.10.280.30;
Stathmin family
PTM: N-terminal palmitoylation promotes specific anchoring to the cytosolic leaflet of Golgi membranes and subsequent vesicular trafficking along dendrites and axons. Neuronal Stathmins are substrates for palmitoyltransferases ZDHHC3, ZDHHC7 and ZDHHC15 (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Golgi apparatus. Cell projection, growth cone. Cell projection, axon. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JHU6}.
null
null
null
null
null
FUNCTION: Exhibits microtubule-destabilizing activity, which is antagonized by STAT3. {ECO:0000269|PubMed:16401721}.
Mus musculus (Mouse)
O70167
P3C2G_MOUSE
MAYSWQTEPNRTEPQEDGSDTQQFHHTNQHLSSRQVRLGFDQLVEEINNKTPLSESEKEEDTYFVPDAPNLGSKWPSIYETHPRYFSEFTSQSPDSSQLRFGKLSAIGFNPAVLPTHQLIHEGASWRNPSGKYHGIEYPRFDALPPSSTGQGECNPQGQSGTKHHNYCGEHEGNLPHHHSSYSIDSIPNREKRRSGDVNLVEPSLEFSKDSFLPRTSENVSVESTEPIGCPIEIVEVPQGSNKNLASFCNKVKKIRESYHASDINSNSGKIWAITTAYPSRLFADTKFRVKISIDNSAQLLLLMPHANYLVKDLIAEILL...
2.7.1.137; 2.7.1.154
null
cell migration [GO:0016477]; chemotaxis [GO:0006935]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091]
PF00168;PF00454;PF00792;PF00613;PF00787;
2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10;
PI3/PI4-kinase family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9514948}; Peripheral membrane protein {ECO:0000269|PubMed:9514948}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evid...
null
null
null
null
FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers (PubMed:9514948). May play a role in SDF1A-stimulated chemotaxis. {ECO:0000269|PubMed:20536348, ECO:0000269|PubMed:9514948}.
Mus musculus (Mouse)
O70172
PI42A_MOUSE
MATPGNLGSSVLASKTKTKKKHFVAQKVKLFRASDPLLSVLMWGVNHSINELSHVQIPVMLMPDDFKAYSKIKVDNHLFNKENMPSHFKFKEYCPMVFRNLRERFGIDDQDFQNSLTRSAPLPNDSQARSGARFHTSYDKRYVIKTITSEDVAEMHNILKKYHQYIVECHGVTLLPQFLGMYRLNVDGVEIYVIVTRNVFSHRLSVYRKYDLKGSTVAREASDKEKAKELPTLKDNDFINEGQKIYIDDNNKKIFLEKLKKDVEFLAQLKLMDYSLLVGIHDVERAEQEEVECEENDGEEEGESDSTHPIGTPPDSPGNT...
2.7.1.149
null
1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate biosynthetic process [GO:1902635]; autophagosome-lysosome fusion [GO:0061909]; megakaryocyte development [GO:0035855]; negative regulation of insulin receptor signaling pathway [GO:0046627]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation...
autophagosome [GO:0005776]; cytosol [GO:0005829]; lysosome [GO:0005764]; nucleus [GO:0005634]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
1-phosphatidylinositol-4-phosphate 5-kinase activity [GO:0016308]; 1-phosphatidylinositol-5-phosphate 4-kinase activity [GO:0016309]; ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]
PF01504;
3.30.810.10;3.30.800.10;
null
PTM: Phosphorylated in tyrosines. Phosphorylation is induced by light and increases kinase activity. {ECO:0000250|UniProtKB:Q9R0I8}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20204506}. Nucleus {ECO:0000250|UniProtKB:P48426}. Lysosome {ECO:0000269|PubMed:29727621}. Cytoplasm {ECO:0000269|PubMed:20204506}. Photoreceptor inner segment {ECO:0000305|PubMed:20204506}. Cell projection, cilium, photoreceptor outer segment {ECO:0000305|PubMed:...
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-5-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:12280, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57795, ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.149; Evid...
null
null
null
null
FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Has both ATP- and GTP-dependent kinase activities. May exert its function by regulating the levels of PtdIns5P, which fun...
Mus musculus (Mouse)
O70173
P3C2G_RAT
MAYNWQTEPNRAEPQEGGHDHQQCHHADQHLSSRQVRLGFDQLVEELSNKTPLPEDEKEGTCFVPDTPNLDSKWQSIYGPHPRHFNEFTSQSPHFSQLPFGKASAIGFNPAVLPAHQFIHEGASWRNPTRKYHGGEDPRFSALTPSSTGLDKCHQQGQSGTEHCNYYVEPENNVPHHYSPYSMDSIPDSEEKGSGDADLVEPSLVFSKDSFLPRASENMSVESTEPIGCPLEIVEAPQGSNKSLASFCNNVTKIRGLYHASDTNSNSGKIWAITTAYPSRLFADTQFRVKISTDNSAQLLLLKPPANYLVKDLIAEILLL...
2.7.1.137; 2.7.1.154
null
cell migration [GO:0016477]; chemotaxis [GO:0006935]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886]
1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091]
PF00168;PF00454;PF00792;PF00794;PF00613;PF00787;
2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10;
PI3/PI4-kinase family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9516481}; Peripheral membrane protein {ECO:0000269|PubMed:9516481}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000269...
null
null
null
null
FUNCTION: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers (PubMed:9516481). May play a role in SDF1A-stimulated chemotaxis (By similarity). {ECO:0000250|UniProtKB:O70167, ECO:0000269|PubMed:9516481}.
Rattus norvegicus (Rat)
O70174
ACHA4_MOUSE
MEIGGSGAPPPLLLLPLLLLLGTGLLPASSHIETRAHAEERLLKRLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPGDYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFYDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVSMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFIIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKVTLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVT...
null
null
acetylcholine receptor signaling pathway [GO:0095500]; B cell activation [GO:0042113]; behavioral response to nicotine [GO:0035095]; calcium ion transport [GO:0006816]; exploration behavior [GO:0035640]; inhibitory postsynaptic potential [GO:0060080]; locomotory behavior [GO:0007626]; membrane depolarization [GO:005189...
acetylcholine-gated channel complex [GO:0005892]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; dopaminergic synapse [GO:0098691]; external side of plasma membrane [GO:0009897]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic ...
acetylcholine binding [GO:0042166]; acetylcholine receptor activity [GO:0015464]; acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; heterocyclic compound binding [GO:1901363]; monoatomic ion channel activity [GO:0005216]; protein-containing complex binding [GO:0044877]; quaternary ammonium ...
PF02931;PF02932;
2.70.170.10;1.20.58.390;
Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-4/CHRNA4 sub-subfamily
null
SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
null
null
null
null
null
FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane permeable to sodium ions.
Mus musculus (Mouse)
O70176
PACA_MOUSE
MTMCSGARLALLVYGIIMHSSVSCSPAAGLSFPGIRPEDEAYDQDGNPLQDFYDWDPPGVGSPASALRDAYALYYPADRRDVAHEILNEAYRKVLDQLSARKYLQSVVARGAGENLGGSAVDDPAPLTKRHSDGIFTDSYSRYRKQMAVKKYLAAVLGKRYKQRVKNKGRRIAYL
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; behavioral fear response [GO:0001662]; cAMP-mediated signaling [GO:0019933]; cellular response to glucocorticoid stimulus [GO:0071385]; histamine secretion [GO:0001821]; insulin secretion [GO:0030073]; negative regulation of acute i...
extracellular space [GO:0005615]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; terminal bouton [GO:0043195]
neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428]; pituitary adenylate cyclase activating polypeptide activity [GO:0016521]; pituitary adenylate cyclase-activating polypeptide receptor binding [GO:0031858]
PF00123;
6.10.250.590;
Glucagon family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Binding to its receptor activates G proteins and stimulates adenylate cyclase in pituitary cells (By similarity). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (By similarity). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and ne...
Mus musculus (Mouse)
O70183
BDNF_CAVPO
MTILFLTMVISYFGCMKAAPMKEASVRGPGSLAYPGVRTHGALESATGPKVGARGLTSSSSSSSSSLADTFEHVIEELLVEDQKARPHEESAKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSVSEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR
null
null
memory [GO:0007613]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of neuron apoptotic process [GO:0043524]; nerve development [GO:0021675]; nerve growth factor signaling pathway [GO:0038180]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system development [GO:000742...
axon [GO:0030424]; dendrite [GO:0030425]; extracellular space [GO:0005615]; synaptic vesicle [GO:0008021]
growth factor activity [GO:0008083]; nerve growth factor receptor binding [GO:0005163]
PF00243;
2.10.90.10;
NGF-beta family
PTM: [BDNF precursor form]: N-glycosylated and glycosulfated, contrary to mature BDNF. {ECO:0000250|UniProtKB:P23560}.; PTM: Mature BDNF is produced by proteolytic removal of the propeptide, catalyzed by a FURIN family member. In addition, the precursor form is proteolytically cleaved within the propeptide, but this is...
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P23560}.; SUBCELLULAR LOCATION: [BDNF precursor form]: Secreted {ECO:0000250|UniProtKB:P23560}. Note=A proportion of BDNF is secreted as immature precursor (proBDNF). {ECO:0000250|UniProtKB:P23560}.
null
null
null
null
null
FUNCTION: Important signaling molecule that activates signaling cascades downstream of NTRK2 (By similarity). During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of ...
Cavia porcellus (Guinea pig)
O70191
ATF5_MOUSE
MSLLATLGLELDRALLPASGLGWLVDYGKLPLAPAPLGPYEVLGGALEGGLPGGGEPLAGDGFSDWMTERVDFTALLPLEAPLPPGTLPPPSPAPPDLEAMASLLKKELEQMEDFFLDAPLLPPPSPPPPPPPAAAPSLPLPLPLPTFDLPQPPTLDTLDLLAVYCRSEAGPGDSGLSTLPVPQQPPPLAPLPSPARPAPYPSPASTRGDRKQKKRDQNKSAALRYRQRKRAEGEALEGECQGLEARNRELRERAESVEREIQYVKDLLIEVYKARSQRTRST
null
null
cerebellar granule cell precursor proliferation [GO:0021930]; circadian rhythm [GO:0007623]; fat cell differentiation [GO:0045444]; multicellular organism growth [GO:0035264]; negative regulation of apoptotic process [GO:0043066]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of cel...
centrosome [GO:0005813]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667]
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; heat shock protein binding [GO:0031072]; kinase binding [GO:0019900]; RNA polymerase II transcription regulatory region sequence-specific DNA bin...
PF00170;
1.20.5.170;
BZIP family
PTM: Acetylated at Lys-29 by EP300, the acetylation enhances the interaction with CEBPB, DNA-binding and transactivation activity. {ECO:0000269|PubMed:24216764}.; PTM: Ubiquitinated by CDC34 and UBE2B in order to be degraded by the proteasome. Cisplatin inhibits ubiquitination and proteasome-mediated degradation by inh...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y2D1}. Nucleus {ECO:0000269|PubMed:22095825}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2D1}. Note=Actively transported to the centrosome and accumulated in the pericentriolar material (PCM) during G1 to M phase ...
null
null
null
null
null
FUNCTION: Transcription factor that either stimulates or represses gene transcription through binding of different DNA regulatory elements such as cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), ATF5-specific response element (ARE) (consensus: 5'-C[CT]TCT[CT]CCTT[AT]-3') but also the amino acid response...
Mus musculus (Mouse)
O70194
EIF3D_MOUSE
MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDETSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMVQFNLQTLPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYIN...
null
null
cap-dependent translational initiation [GO:0002191]; formation of cytoplasmic translation initiation complex [GO:0001732]; IRES-dependent viral translational initiation [GO:0075522]; positive regulation of translation [GO:0045727]; translational initiation [GO:0006413]; viral translational termination-reinitiation [GO:...
eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]; synapse [GO:0045202]
mRNA cap binding [GO:0098808]; translation initiation factor activity [GO:0003743]
PF05091;
null
EIF-3 subunit D family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
null
null
null
null
null
FUNCTION: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, e...
Mus musculus (Mouse)
O70196
PPCE_RAT
MLSFQYPDVYRDETSVQDYHGHKICDPYAWLEDPDSEQTKAFVEAQNKITVPFLEQCPIRGLYKERMTELYDYPKYSCHFKKGKRYFYFYNTGLQNQRVLYVQDSLEGEARVFLDPNTLSDDGTVALRGYAFSEDGEYFAYGLSASGSDWVTIKFMKVDGAKELPDVLERVKFTCMAWTHDGKGMFYNSYPQQDGKSDGTETSTNLHQKLCYHVLGTDQSEDVLCAEFPDEPKWMGGAELSDDGRYVLLSIWEGCDPVNRLWYCDLQQGSNGINGILKWVKLIDNFEGEYDYITNEGTVFTFKTNRNSPNYRLINIDFTD...
3.4.21.26
null
protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
endopeptidase activity [GO:0004175]; oligopeptidase activity [GO:0070012]; peptide binding [GO:0042277]; serine-type endopeptidase activity [GO:0004252]
PF00326;PF02897;
3.40.50.1820;2.130.10.120;
Peptidase S9A family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23687}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:10766975};
null
null
null
null
FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long. Has high activity on the succinyl- (suc-) peptide-4-methylcoumaryl-7-amide (MCA) substrates suc-Gly-Pro-Leu-Gly-Pro-MCA, suc-Gly-Pro-MCA and suc-Ala-Ala-Ala-MCA. {ECO:0000269|PubMe...
Rattus norvegicus (Rat)
O70200
AIF1_MOUSE
MSQSRDLQGGKAFGLLKAQQEERLEGINKQFLDDPKYSNDEDLPSKLEAFKVKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKRLIREVSSGSEETFSYSDFLRMMLGKRSAILRMILMYEEKNKEHKRPTGPPAKKAISELP
null
null
actin crosslink formation [GO:0051764]; actin filament bundle assembly [GO:0051017]; actin filament polymerization [GO:0030041]; cellular response to oxidative stress [GO:0034599]; cellular response to type II interferon [GO:0071346]; inflammatory response [GO:0006954]; microglial cell activation [GO:0001774]; negative...
actin filament [GO:0005884]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glial cell projection [GO:0097386]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; phagocytic cup [GO:0001891]; ruffle [GO:0001726]; ruffle m...
actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]
PF21008;
1.10.238.10;
null
PTM: Phosphorylated on serine residues. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10934045}. Cell projection, ruffle membrane {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}; Peripheral membrane protein; Cytoplasmic side. Cell projection, phagocytic cup {ECO:0000269|PubMed:10934045, ECO:0000269|PubMed:14756805}. Note=Associ...
null
null
null
null
null
FUNCTION: Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-l...
Mus musculus (Mouse)
O70201
BIRC5_MOUSE
MGAPALPQIWQLYLKNYRIATFKNWPFLEDCACTPERMAEAGFIHCPTENEPDLAQCFFCFKELEGWEPDDNPIEEHRKHSPGCAFLTVKKQMEELTVSEFLKLDRQRAKNKIAKETNNKQKEFEETAKTTRQSIEQLAA
null
null
apoptotic process [GO:0006915]; cell division [GO:0051301]; establishment of chromosome localization [GO:0051303]; G2/M transition of mitotic cell cycle [GO:0000086]; meiosis I [GO:0007127]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic sp...
apical plasma membrane [GO:0016324]; centriole [GO:0005814]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; interphase microtubule organizing center [GO:0031021]; kinetochore [GO:0000776]; microt...
cysteine-type endopeptidase inhibitor activity [GO:0004869]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; tubulin binding [GO:0015631]; ubiquitin protein ligase activity [GO:0061630]; zinc ion...
PF00653;
null
IAP family
PTM: Ubiquitinated by the Cul9-RING ubiquitin-protein ligase complex, leading to its degradation. Ubiquitination is required for centrosomal targeting. Deubiquitinated by USP35 or USP38; leading to stabilization. {ECO:0000250|UniProtKB:O15392}.; PTM: Acetylation at Lys-129 results in its homodimerization, while deacety...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15392}. Nucleus {ECO:0000250|UniProtKB:O15392}. Chromosome {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere {ECO:0000250|UniProtKB:O15392}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O15392}. Chromosome, centromere, kinetochore {ECO:0000250|UniP...
null
null
null
null
null
FUNCTION: Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:25778398). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (By similarity). Acts as an important regulato...
Mus musculus (Mouse)
O70209
PDLI3_MOUSE
MPQNVVLPGPAPWGFRLSGGIDFNQPLVITRITPGSKAAAANLCPGDVILAIDGFGTESMTHADAQDRIKAASYQLCLKIDRAETRLWSPQVSEDGKAHPFKINLEAEPQEFKPIGTAHNRRAQPFVAAANIDDKRQVVSASYNSPIGLYSTSNIQDALHGQLRGLIPGSLQNEPTASVPPQSDVYRMLHDNRDDPAAPRQSGSFRVLQDLVNDGPDDRPAGTRSVRAPVTKVHGGAGSAQRMPLCDKCGSGIVGAVVKARDKYRHPECFVCADCNLNLKQKGYFFVEGELYCETHARARTRPPEGYDTVTLYPKA
null
null
actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; heart development [GO:0007507]; muscle structure development [GO:0061061]
actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; filamentous actin [GO:0031941]; stress fiber [GO:0001725]; Z disc [GO:0030018]
actin binding [GO:0003779]; actinin binding [GO:0042805]; cytoskeletal protein binding [GO:0008092]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; structural constituent of muscle [GO:0008307]
PF15936;PF00412;PF00595;
2.30.42.10;2.10.110.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250}. Note=Localizes to myofiber Z-lines. {ECO:0000250}.
null
null
null
null
null
FUNCTION: May play a role in the organization of actin filament arrays within muscle cells. {ECO:0000250}.
Mus musculus (Mouse)
O70212
5HT3A_CAVPO
MVLWLQLALLALLLPTSLAQGEVRGKGTAQAHNSTRPALQRLSDHLLADYRKSVRPVRDWRKPTTVSIDAIVYAILSVDEKNQVLTTYIWYRQFWTDEFLQWNPEDFDNITKLSIPTDSIWVPDILINEFVDVGKSPNIPYVYVRHQGEVQNYKPLQVVTACSLDIYNFPFDVQNCSLTFTSWLHTIQDINISLWRLPEKVKSDKSVFMNQGEWELLGVLTEFLEFSDRESRGSFAEMKFYVVIRRRPLFYAVTLLLPSIFLMIVDIVGFYLPPDSGERVSFKITLLLGYSVFLIIVSDTLPATAIGTPLISVYFVVCMA...
null
null
monoatomic cation transport [GO:0006812]
neuron projection [GO:0043005]; postsynaptic membrane [GO:0045211]; synaptic vesicle membrane [GO:0030672]
acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; GABA-A receptor activity [GO:0004890]; serotonin-gated monoatomic cation channel activity [GO:0022850]
PF02931;PF02932;
2.70.170.10;1.20.58.390;
Ligand-gated ion channel (TC 1.A.9) family, 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily, HTR3A sub-subfamily
null
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P46098}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23979}. Cell membrane {ECO:0000250|UniProtKB:P46098}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23979}.
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P46098}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out...
null
null
null
null
FUNCTION: Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation-selective channel complexes, which when activated cause fast, depolarizing responses in neurons. {ECO:0000269|PubMed:9463477}.
Cavia porcellus (Guinea pig)
O70215
NKG2D_RAT
MSKCHNYDLKPAKWDTSQEHQKQRSALPTSRPGENGIIRRRSSIEELKISPLFVVRVLVAAMTIRFTVITLTWLAVFITLLCNKEVSVSSREGYCGPCPNDWICHRNNCYQFFNENKAWNQSQASCLSQNSSLLKIYSKEEQDFLKLVKSYHWMGLVQSPANGSWQWEDGSSLSPNELTLVKTPSGTCAVYGSSFKAYTEDCSNPNTYICMKRAV
null
null
adaptive immune response [GO:0002250]; cell differentiation [GO:0030154]; cellular response to lipopolysaccharide [GO:0071222]; defense response to Gram-positive bacterium [GO:0050830]; natural killer cell activation [GO:0030101]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of natural ki...
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; MHC class I protein binding [GO:0042288]; MHC class Ib receptor activity [GO:0032394]; signaling receptor activity [GO:0038023]
PF00059;
3.10.100.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Colocalized with HCST on the cell surface. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (N...
Rattus norvegicus (Rat)
O70220
FOXQ1_MOUSE
MKLEVFVPRAAHGDKMGSDLEGAGSSDVPSPLSAAGDDSLGSDGDCAANSPAAGSGAGDLEGGGGERNSSGGPSAQDGPEATDDSRTQASAAGPCAGGVGGGEGARSKPYTRRPKPPYSYIALIAMAIRDSAGGRLTLAEINEYLMGKFPFFRGSYTGWRNSVRHNLSLNDCFVKVLRDPSRPWGKDNYWMLNPNSEYTFADGVFRRRRKRLSHRTTVSASGLRPEEAPPGPAGTPQPAPAARSSPIARSPARQEERSSPASKFSSSFAIDSILSKPFRSRRDGDSALGVQLPWGAAPCPPLRAYPALLPAAPGGALLPL...
null
null
anatomical structure morphogenesis [GO:0009653]; cell differentiation [GO:0030154]; hair follicle morphogenesis [GO:0031069]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357...
nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00250;
1.10.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
null
null
null
null
null
FUNCTION: Plays a role in hair follicle differentiation. {ECO:0000269|PubMed:16835220}.
Mus musculus (Mouse)
O70228
ATP9A_MOUSE
MTDSIPLQPVRHKKRVDSRPRAGCCEWLRCCGGGEPRPRTVWLGHPEKRDQRYPRNVINNQKYNFFTFLPGVLFSQFRYFFNFYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTIIREAVEEIRCYVRDKEMNSQVYSRLTSRGTVKVKSSNIQVGDLILVEKNQRVPADMIFLRTSEKNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFLGTFTREDSDPPISESLSIENTLWAGTVIASGTVVGVVLYTGRELRSVMNTSDPRSKIGLFDLEVNCLTKILFGALVVVSLVMVA...
7.6.2.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P40527};
endocytosis [GO:0006897]; negative regulation of exosomal secretion [GO:1903542]; neuron projection morphogenesis [GO:0048812]; phospholipid translocation [GO:0045332]; regulation of endocytic recycling [GO:2001135]; regulation of retrograde transport, endosome to Golgi [GO:1905279]; retrograde vesicle-mediated transpo...
early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]
PF13246;PF00122;PF00702;PF16212;PF16209;
3.40.1110.10;2.70.150.10;3.40.50.1000;
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
null
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000269|PubMed:36604604}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:36604604}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:36604604}. Golgi apparatus, trans-Golgi network membran...
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:O75110};
null
null
null
null
FUNCTION: Plays a role in regulating membrane trafficking of cargo proteins, namely endosome to plasma membrane recycling, probably acting through RAB5 and RAB11 activation (PubMed:36604604). Also involved in endosome to trans-Golgi network retrograde transport (By similarity). In complex with MON2 and DOP1B, regulates...
Mus musculus (Mouse)
O70230
ZN143_MOUSE
MLLAQINRDSQGMTEFPGGGMEAQHVTLCLTEAVTVADGDNLENMEGVSLQAVTLADGSTAYIQHNSKDGRLIDGQVIQLEDGSAAYVQHVPIPKSTGDSLRLEDGQAVQLEDGTTAFIHHTSKDSYDQSSLQAVQLEDGTTAYIHHAVQVPQSDTILAIQADGTVAGLHTGDATIDPDTISALEQYAAKVSIDGSDGVTSTGMIGENEQEKKMQIVLQGHATRVTPKSQQSGEKAFRCKYDGCGKLYTTAHHLKVHERSHTGDRPYQCEHSGCGKAFATGYGLKSHFRTHTGEKPYRCSEDNCTKSFKTSGDLQKHIRT...
null
null
positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
PcG protein complex [GO:0031519]; transcription regulator complex [GO:0005667]
chromatin binding [GO:0003682]; 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 cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00096;
3.30.160.60;
GLI C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Transcriptional activator. Activates the gene for selenocysteine tRNA (tRNAsec). Binds to the SPH motif of small nuclear RNA (snRNA) gene promoters. Participates in efficient U6 RNA polymerase III transcription via its interaction with CHD8 (By similarity). {ECO:0000250, ECO:0000269|PubMed:9535833}.
Mus musculus (Mouse)
O70237
GFI1B_MOUSE
MPRSFLVKSKKAHTYHQPRAQGDELVWPPAVIPVAKEHSQSASPLLSTPLPSQTLDWNTIKQEREMLLNQSLPKMASAPEGPLVTPQPQDGESPLSESPPFYKPSFSWDTLASSYSHSYTQTPSTMQSAFLERSVRLYGSPLVPSTESPLDFRLRYSPGMDTYHCVKCNKVFSTPHGLEVHVRRSHSGTRPFACDVCGKTFGHAVSLEQHTHVHSQERSFECRMCGKAFKRSSTLSTHLLIHSDTRPYPCQFCGKRFHQKSDMKKHTYIHTGEKPHKCQVCGKAFSQSSNLITHSRKHTGFKPFSCELCTKGFQRKVDLR...
null
null
positive regulation of granulocyte differentiation [GO:0030854]; regulation of erythrocyte differentiation [GO:0045646]; regulation of hemopoiesis [GO:1903706]; regulation of transcription by RNA polymerase II [GO:0006357]
nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00096;
3.30.160.60;
null
PTM: Methylation at Lys-8 in the SNAG domain seems required for the recruitment of the corepressor complex. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12594258}. Note=Localized at foci of pericentric heterochromatin.
null
null
null
null
null
FUNCTION: Essential proto-oncogenic transcriptional regulator necessary for development and differentiation of erythroid and megakaryocytic lineages. Component of a RCOR-GFI-KDM1A-HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell developmen...
Mus musculus (Mouse)
O70239
AXIN1_RAT
MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDSVPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSAND...
null
null
adult walking behavior [GO:0007628]; apoptotic process [GO:0006915]; axial mesoderm development [GO:0048318]; axial mesoderm formation [GO:0048320]; canonical Wnt signaling pathway [GO:0060070]; cell development [GO:0048468]; cytoplasmic microtubule organization [GO:0031122]; dorsal/ventral axis specification [GO:00099...
beta-catenin destruction complex [GO:0030877]; cell cortex [GO:0005938]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lateral plasma membrane [GO:0016328]; microtubule cytoskeleton [GO:0015630]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane...
armadillo repeat domain binding [GO:0070016]; beta-catenin binding [GO:0008013]; enzyme binding [GO:0019899]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; p53 binding [GO:0002039]; protein domain specific binding [GO:0019904]; protein homodimerization act...
PF16646;PF08833;PF00778;PF00615;
1.10.196.10;2.40.240.130;1.10.167.10;
null
PTM: Phosphorylation and dephosphorylation of AXIN1 regulates assembly and function of the beta-catenin complex. Phosphorylated by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA. Phosphorylation by CK1 enhances binding of GSK3B to AXIN1. Also phosphorylated by CDK2 which regulates interaction with CTNBB1 (By simi...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15169}. Nucleus {ECO:0000250|UniProtKB:O15169}. Cell membrane {ECO:0000269|PubMed:16815997}. Membrane {ECO:0000250|UniProtKB:O35625}. Note=On UV irradiation, translocates to the nucleus and colocalizes with DAAX (By similarity). MACF1 is required for its transloca...
null
null
null
null
null
FUNCTION: Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning via two opposing effects; down-regulates beta-catenin to inhibit the Wnt signaling pathway and vent...
Rattus norvegicus (Rat)
O70240
AXIN2_RAT
MSSAVLVTLLPDPSSSFREDAPRPPVPGEEGETPPCQPSVGKVQSTKPMPVSSNARRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSVVSKQLKPATKTYIRDGIKKQQIGSVMFDQAQTEIQAVMEENAYQVFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVLCGYLPTLNEEEEWTCADLKCKLSPTVVGLSSKTLRATASVRSTETAENGFRSFKRSEPVNPYHVGSGYVFAPATSANDSELSSDALTDDSMSMTDSSVD...
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]; cellular response to organic cyclic compound [GO:0071407]; chondro...
beta-catenin destruction complex [GO:0030877]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
beta-catenin binding [GO:0008013]; enzyme binding [GO:0019899]; I-SMAD binding [GO:0070411]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]; ubiquitin protein ligase binding [GO:0031625]
PF16646;PF08833;PF00778;PF00615;
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 ac...
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}.
Rattus norvegicus (Rat)
O70244
CUBN_RAT
MSSQFLWGFVTLLMIAELDGKTGKPEQRGQKRIADLHQPRMTTEEGNLVFLTSSTQNIEFRTGSLGKIKLNDEDLGECLHQIQRNKDDIIDLRKNTTGLPQNILSQVHQLNSKLVDLERDFQNLQQNVERKVCSSNPCLNGGTCVNLHDSFVCICPSQWKGLFCSEDVNECVVYSGTPFGCQSGSTCVNTVGSFRCDCTPDTYGPQCASKYNDCEQGSKQLCKHGICEDLQRVHHGQPNFHCICDAGWTTPPNGISCTEDKDECSLQPSPCSEHAQCFNTQGSFYCGACPKGWQGNGYECQDINECEINNGGCSQAPLVP...
null
null
cholesterol metabolic process [GO:0008203]; cobalamin catabolic process [GO:0042366]; cobalamin metabolic process [GO:0009235]; cobalamin transport [GO:0015889]; endocytic hemoglobin import into cell [GO:0020028]; establishment of localization in cell [GO:0051649]; in utero embryonic development [GO:0001701]; lipoprote...
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; brush border [GO:0005903]; brush border membrane [GO:0031526]; clathrin-coated pit [GO:0005905]; coated vesicle [GO:0030135]; cytoplasm [GO:0005737]; endocytic vesicle [GO:0030139]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum [GO:...
calcium ion binding [GO:0005509]; cargo receptor activity [GO:0038024]; cobalamin binding [GO:0031419]; hemoglobin binding [GO:0030492]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
PF00431;PF00008;PF12947;PF07645;PF12661;
2.10.25.10;2.60.120.290;
null
PTM: The precursor is cleaved by a trans-Golgi proteinase furin, removing a propeptide. {ECO:0000250|UniProtKB:O60494}.; PTM: N-glycosylated. {ECO:0000269|PubMed:29402915, ECO:0000269|PubMed:9478979}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29402915}; Peripheral membrane protein {ECO:0000305|PubMed:29402915}. Endosome membrane {ECO:0000269|PubMed:9478979}; Peripheral membrane protein {ECO:0000269|PubMed:9478979}. Lysosome membrane {ECO:0000269|PubMed:9478979}; Peripheral membrane protein {ECO:0000269...
null
null
null
null
null
FUNCTION: Endocytic receptor which plays a role in lipoprotein, vitamin and iron metabolism by facilitating their uptake. Acts together with LRP2 to mediate endocytosis of high-density lipoproteins, GC, hemoglobin, ALB, TF and SCGB1A1. Acts together with AMN to mediate endocytosis of the CBLIF-cobalamin complex. Binds ...
Rattus norvegicus (Rat)
O70247
SC5A6_RAT
MTVASTAAPSYTTSDTNRVISTFSVVDYVVFGLLLVLSLVIGLYHACRGWGRHTVGELLMADRKMGCLPVALSLLATFQSAVAILGGPAEIYRFGTQYWFLGCSYFLGLLIPAHIFIPVFYRLHLTSAYEYLELRFNKAVRICGTVTFIFQMVVYMGVALYAPSLALNAVTGFDLWLSVLALGIVCNIYTALGGLKAVIWTDVFQTLIMFLGQLVVIIVGAAKVGGLGHVWAVASQHGLISGIELDPDPFVRHTFWTLAFGGVFMMLSLYGVNQAQVQRYLSSHSEKAAVLSCYAVFPCQQVALCMSCLIGLVMFAYYKK...
null
null
biotin import across plasma membrane [GO:1905135]; biotin metabolic process [GO:0006768]; biotin transport [GO:0015878]; iodide transmembrane transport [GO:1904200]; pantothenate transmembrane transport [GO:0015887]; sodium ion transport [GO:0006814]; transport across blood-brain barrier [GO:0150104]
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; plasma membrane [GO:0005886]
amide transmembrane transporter activity [GO:0042887]; biotin transmembrane transporter activity [GO:0015225]; iodide transmembrane transporter activity [GO:0015111]; monocarboxylate:sodium symporter activity [GO:0140161]; pantothenate transmembrane transporter activity [GO:0015233]; pantothenate:sodium symporter activ...
PF00474;
1.20.1730.10;
Sodium:solute symporter (SSF) (TC 2.A.21) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y289}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Y289}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=biotin(out) + 2 Na(+)(out) = biotin(in) + 2 Na(+)(in); Xref=Rhea:RHEA:73375, ChEBI:CHEBI:29101, ChEBI:CHEBI:57586; Evidence={ECO:0000269|PubMed:9516450}; CATALYTIC ACTIVITY: Reaction=(R)-pantothenate(out) + 2 Na(+)(out) = (R)-pantothenate(in) + 2 Na(+)(in); Xref=Rhea:RHEA:73371, ChEBI:CHEBI...
null
null
null
null
FUNCTION: Sodium-dependent multivitamin transporter that mediates the electrogenic transport of pantothenate, biotin, lipoate and iodide (PubMed:9516450). Functions as a Na(+)-coupled substrate symporter where the stoichiometry of Na(+):substrate is 2:1, creating an electrochemical Na(+) gradient used as driving force ...
Rattus norvegicus (Rat)
O70249
OGG1_RAT
MLFSSSLSSSMRHRTLTSSPALWASIPCPRSELRLDLVLASGQSFRWREQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDKGQVGRPTLEELETLHKYFQLDVSLTQLYSHWASVDSHFQSVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQAFGPRLVQLDDVTYHGFPNLHALAGPEVETHLRKLGLGYRARYVCASAKAILEEQGGPAWLQQLRVASYEEAHKALCTLPGVGTKVADCICLMALDKPQAVPVDIHVWQIAHRDYGWQPKTSQTKGPSPLANKELGNFFRNLWGPYAGWAQAVLFS...
3.2.2.-; 4.2.99.18
null
base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; negative regulation of apoptotic process [GO:0043066]; negative re...
mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
8-oxo-7,8-dihydroguanine DNA N-glycosylase activity [GO:0034039]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA N-glycosylase activity [GO:0019104]; enzyme binding [GO:0019899]; microtubule binding [GO:0008017]; oxidized purine DNA binding [GO:0032...
PF00730;PF07934;
3.30.310.40;1.10.1670.10;
Type-1 OGG1 family
null
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells. {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RH...
null
null
null
null
FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Rattus norvegicus (Rat)
O70250
PGAM2_MOUSE
MTTHRLVMVRHGESLWNQENRFCGWFDAELSEKGAEEAKRGATAIKDAKIEFDICYTSVLKRAIRTLWTILDVTDQMWVPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDTPPPPMDEKHNYYTSISKDRRYAGLKPEELPTCESLKDTIARALPFWNEEIAPKIKAGQRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELDQNLKPTKPMRFLGDEETVRKAMEAVAAQGKAK
5.4.2.11; 5.4.2.4
null
canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; Notch signaling pathway [GO:0007219]; response to inorganic substance [GO:0010035]; response to mercury ion [GO:0046689]; spermatogenesis [GO:0007283]; striated muscle contraction [GO:0006941]
cytosol [GO:0005829]
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate mutase activity [GO:0004082]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; phosphoglycerate mutase activity [GO:0004619]
PF00300;
3.40.50.1240;
Phosphoglycerate mutase family, BPG-dependent PGAM subfamily
null
null
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P18669}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, C...
null
null
null
null
FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
Mus musculus (Mouse)
O70252
HMOX2_MOUSE
MSSEVETSEGVDESEKNSMAPEKENHTKMADLSELLKEGTKEAHDRAENTQFVKDFLKGNIKKELFKLATTALYFTYSALEEEMDRNKDHPAFAPLYFPTELHRKAALIKDMKYFFGENWEEQVKCSEAAQKYVDRIHYVGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPSTGEGTQFYLFEHVDNAQQFKQFYRARMNALDLNLKTKERIVEEANKAFEYNMQIFSELDQAGSMLARETLEDGLPVHDGKGDIRKCPFYAAQPDKGTLGGSNCPFQTTVAVLRKPSLQLILAASVALVAGLLAWYYM
1.14.14.18
null
heme catabolic process [GO:0042167]; heme oxidation [GO:0006788]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006979]
endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
heme binding [GO:0020037]; heme oxygenase (decyclizing) activity [GO:0004392]; metal ion binding [GO:0046872]
PF01126;
1.20.910.10;
Heme oxygenase family
PTM: A soluble form arises by proteolytic removal of the membrane anchor. {ECO:0000250|UniProtKB:P30519}.; PTM: S-nitrosylated by BLVRB. {ECO:0000250|UniProtKB:P30519}.
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P30519}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:P09601}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P09601}; Single-pass type IV membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|U...
CATALYTIC ACTIVITY: Reaction=heme b + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = biliverdin IXalpha + CO + Fe(2+) + H(+) + 3 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21764, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:1724...
null
null
null
null
FUNCTION: [Heme oxygenase 2]: Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron. {ECO:0000250|UniProtKB:P30519}.; FUNCTION: [Heme oxygenase 2 soluble form]: Catalyze...
Mus musculus (Mouse)
O70255
MPZL2_MOUSE
MYGKSPALVLPLLLSLQLTALCPTEAVEIYTSGALEAVNGTDVRLKCTFSSFAPVGDALTVTWNFRPRDGGREQFVFYYHMDPFRPMSGRFKDRVVWDGNPERYDVSILLWKLQFDDNGTYTCQVKNPPDVDGLVGTIRLSVVHTVPFSEIYFLAVAIGSACALMIIVVIVVVLFQHFRKKRWADRADKAEGTKSKEEEKLNQGNKVSVFVEDTD
null
null
cell-cell adhesion [GO:0098609]; T cell differentiation in thymus [GO:0033077]
plasma membrane [GO:0005886]
null
PF07686;
2.60.40.10;
Myelin P0 protein family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Mediates homophilic cell-cell adhesion.
Mus musculus (Mouse)
O70257
STX7_RAT
MSYTPGIGGDPAQLAQRISSNIQKITQCSAEIQRTLNQLGTPQDTPELRQQLQQEQQYTNQLAKETDKYIKEFGFLPTTPSEQRQRKIQKDRLVAEFTTALTNFQKVQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNFVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDVIDSIEANVESAEVHVQQANQQLSRAANYQRKSRKTLCIIILILVVGIVIIFFIVWGLKG
null
null
endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; organelle assembly [GO:0070925]; organelle localization [GO:0051640]; positive regulation of receptor localization to synapse [GO:1902685]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; regulation of protein l...
azurophil granule [GO:0042582]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; endomembrane system [GO:0012505]; endosome [GO:0005768]; immunological synapse [GO:0001772]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]...
chloride channel inhibitor activity [GO:0019869]; protein-containing complex binding [GO:0044877]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
PF05739;PF14523;
1.20.5.110;1.20.58.70;
Syntaxin family
null
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
O70258
SGCE_MOUSE
MLLFWWWELGDPCAWTGKGRGTLKMSPATTGTFLLTVYTLFSKVHSDRNVYPSAGVLFVHVLEREYFKGEFPPYPKPGEVSNDPITFNTNLMGYPDRPGWLRYIQRTPYSDGVLYGSPTAENVGKPTIIEITAYNRRTFETARHNLIINIMSAEEFPLPYQAEFFIKNMNVEEMLASEVLGDFLGAVKNVWQPERLNAINITSALDRGGRVPLPINDMKEGVYVMVGADVAFSSCLREVENPQNQLRCSQEMEPVITCDKKFRTHFHIDWCKISLVDKTKQVSTYQEVVRGEGILPDGGEYKPPSDSLKSRDYYTDFLVT...
null
null
null
cytoskeleton [GO:0005856]; dendrite membrane [GO:0032590]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; sarcoglycan complex [GO:0016012]; sarcolemma [GO:0042383]
null
PF05510;PF20989;
null
Sarcoglycan alpha/epsilon family
PTM: N-glycosylated. {ECO:0000269|PubMed:17200151}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000269|PubMed:17200151}.
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:17200151}; Single-pass membrane protein {ECO:0000269|PubMed:17200151}. Golgi apparatus {ECO:0000269|PubMed:17200151}. Cell projection, dendrite {ECO:0000269|PubMed:17200151}. Cytoplasm, cytoskeleton {ECO:0000250}.
null
null
null
null
null
FUNCTION: Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Mus musculus (Mouse)
O70260
PIAS3_RAT
MAELGELKHMVMSFRVSELQVLLGFAGRNKSGRKHELLAKALHLLKSSCAPSVQMKIKELYRRRFPRKTLGPSDLSLLSLPPGTSPVGSPSPLASIPPTLLTPGTLLGPKREVDMHPPLPQPVHPDVTMKPLPFYEVYGELIRPTTLASTSSQRFEEAHFTFALTPQQLQQILTSREVLPGAKCDYTIQVQLRFCLCETSCPQEDYFPPNLFVKVNGKLCPLPGYLPPTKNGAEPKRPSRPINITPLARLSATVPNTIVVNWSSEFGRNYSLSVYLVRQLTAGTLLQKLRAKGIRNPDHSRALIKEKLTADPDSEVATTS...
2.3.2.-
null
negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of protein sumoylation [GO:0033234]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive ...
cytoplasm [GO:0005737]; dendrite [GO:0030425]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
ionotropic glutamate receptor binding [GO:0035255]; NF-kappaB binding [GO:0051059]; potassium channel regulator activity [GO:0015459]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription coregulator activity [GO:0003712]; transmembrane transporter binding [GO:0044325]; zinc ion bind...
PF14324;PF02891;
2.60.120.780;1.10.720.30;3.30.40.10;
PIAS family
PTM: Sumoylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O54714}. Nucleus {ECO:0000269|PubMed:9565597}. Nucleus speckle {ECO:0000250|UniProtKB:O54714}. Note=Colocalizes with MITF in the nucleus. Colocalizes with GFI1 in nuclear dots. Colocalizes with SUMO1 in nuclear granules. {ECO:0000250|UniProtKB:O54714}.
null
null
PATHWAY: Protein modification; protein sumoylation.
null
null
FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway and the steroid hormone signaling pa...
Rattus norvegicus (Rat)
O70263
LNX1_MOUSE
MNQPDLADDPDPSPEPLCIVCGQNHSPEENHFYTYTEDVDDDLICHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVDRKPVVLQHCKKSSILVNKLLNKLLVTCPFTEHCTEVLQRCDLQHHFQTSCKGASHYGLTKDRKRRSQDGCPDGCASLMATTLSPEVSAAATISLMTDEPGLDNPAYVSSVEDGEPVANSSDSGRSNRTRARPFERSTMRSRSFKKINRALSALRRTKSGSVVANHVDQGRDNSENTTVPEVFPRLFHLIPDGEITSIKINRADPSESLSIRLVGGSETPLVHIIIQHIYRDGVIARDG...
2.3.2.27
null
protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
cytoplasm [GO:0005737]
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; PDZ domain binding [GO:0030165]; ubiquitin-protein transferase activity [GO:0004842]
PF00595;PF13920;
2.30.42.10;3.30.40.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform...
Mus musculus (Mouse)
O70274
TP4A2_MOUSE
MNRPAPVEISYENMRFLITHNPTNATLNKFTEELKKYGVTTLVRVCDATYDKAPVEKEGIHVLDWPFDDGAPPPNQIVDDWLNLLKTKFREEPGCCVAVHCVAGLGRAPVLVALALIECGMKYEDAVQFIRQKRRGAFNSKQLLYLEKYRPKMRLRFRDTNGHCCVQ
3.1.3.48
null
dephosphorylation [GO:0016311]
cytoplasm [GO:0005737]; early endosome [GO:0005769]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
protein tyrosine phosphatase activity [GO:0004725]
PF00102;
3.90.190.10;
Protein-tyrosine phosphatase family
PTM: Farnesylated. Farnesylation is required for membrane targeting and for interaction with RABGGTB (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10747914}. Early endosome {ECO:0000269|PubMed:10747914}. Cytoplasm {ECO:0000269|PubMed:10747914}.
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;
null
null
null
null
FUNCTION: Protein tyrosine phosphatase which stimulates progression from G1 into S phase during mitosis. Inhibits geranylgeranyl transferase type II activity by blocking the association between RABGGTA and RABGGTB (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O70276
RPE65_RAT
MSIQIEHPAGGYKKLFETVEELSTPLTAHVTGRIPLWLTGSLLRCGPGLFEVGSEPFYHLFDGQALLHKFDFKEGHVTYYRRFIRTDAYVRAMTEKRIVITEFGTCAFPDPCKNIFSRFFSYFRGVEITDNALVNIYPVGEDYYACTETNFITKINPETLETIKQVDLCNYVSVNGATAHPHIESDGTVYNIGNCFGKNFTVAYNIIKIPPLKADKEDPINKSEVVVQFPCSDRFKPSYVHSFGLTPNYIVFVETPVKINLFKFLSSWSLWGANYMDCFESNESMGVWLHVADKKRRKYFNNKYRTSPFNLFHHINTYED...
3.1.1.64; 5.3.3.22
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q28175}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q28175};
camera-type eye development [GO:0043010]; circadian rhythm [GO:0007623]; detection of light stimulus involved in visual perception [GO:0050908]; neural retina development [GO:0003407]; response to light stimulus [GO:0009416]; retina homeostasis [GO:0001895]; retinal metabolic process [GO:0042574]; retinoid metabolic pr...
cell body [GO:0044297]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity [GO:0052885]; all-trans-retinyl-palmitate hydrolase, 11-cis retinol forming activity [GO:0052884]; beta-carotene 15,15'-dioxygenase activity [GO:0003834]; cardiolipin binding [GO:1901612]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872];...
PF03055;
null
Carotenoid oxygenase family
PTM: Palmitoylation by LRAT regulates ligand binding specificity; the palmitoylated form (membrane form) specifically binds all-trans-retinyl-palmitate, while the soluble unpalmitoylated form binds all-trans-retinol (vitamin A). {ECO:0000250|UniProtKB:Q28175}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A9C3R9}. Cell membrane {ECO:0000250|UniProtKB:Q28175}; Lipid-anchor {ECO:0000250|UniProtKB:Q28175}. Microsome membrane {ECO:0000250|UniProtKB:Q28175}. Note=Attached to the membrane by a lipid anchor when palmitoylated (membrane form), soluble when unpalmitoylated. ...
CATALYTIC ACTIVITY: Reaction=an all-trans-retinyl ester + H2O = 11-cis-retinol + a fatty acid + H(+); Xref=Rhea:RHEA:31771, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16302, ChEBI:CHEBI:28868, ChEBI:CHEBI:63410; EC=3.1.1.64; Evidence={ECO:0000250|UniProtKB:Q28175}; CATALYTIC ACTIVITY: Reaction=lutein = (3R,3'S)-...
null
null
null
null
FUNCTION: Critical isomerohydrolase in the retinoid cycle involved in regeneration of 11-cis-retinal, the chromophore of rod and cone opsins. Catalyzes the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol which is further oxidized by 11-cis retinol dehydrogenase to 11-cis-retinal for ...
Rattus norvegicus (Rat)
O70277
TRIM3_RAT
MAKREDSPGPEVQPMDKQFLVCSICLDRYRCPKVLPCLHTFCERCLQNYIPPQSLTLSCPVCRQTSILPEQGVSALQNNFFISSLMEAMQQAPDGAHDPEDPHPLSAVAGRPLSCPNHEGKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSA...
2.3.2.27
null
negative regulation of translation [GO:0017148]; positive regulation of toll-like receptor 3 signaling pathway [GO:0034141]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; protein transport [GO:0015...
cytoplasm [GO:0005737]; dendrite [GO:0030425]; early endosome [GO:0005769]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; postsynapse [GO:0098794]
identical protein binding [GO:0042802]; translation repressor activity [GO:0030371]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
PF00630;PF01436;PF00643;PF00097;
3.30.160.60;2.60.40.10;2.120.10.30;3.30.40.10;
TRIM/RBCC family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75382}. Early endosome {ECO:0000250|UniProtKB:O75382}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9R1R2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9R1R2}. Note=Mainly located in the Golgi apparatus and transported to the early endosomes ...
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:20352094};
null
null
null
null
FUNCTION: E3 ubiquitin ligase that plays essential roles in neuronal functions such as regulation of neuronal plasticity, learning, and memory (PubMed:20352094). In addition to its neuronal functions, participates in other biological processes such as innate immunity or cell cycle regulation. Component of the cytoskele...
Rattus norvegicus (Rat)
O70281
TPST1_MOUSE
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPARLENPKATVRAGLDIKANKTFTYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKEKIRLDEAGVTDEVLDSAMQAFLLEVIVKHGEPAPYLCNKDPFALKSLTYLARLFPNAKFLLMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLHIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALSKWVGKIPPDVLQDMAVIAPM...
2.8.2.20
null
post-translational protein modification [GO:0043687]
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
protein homodimerization activity [GO:0042803]; protein-tyrosine sulfotransferase activity [GO:0008476]
PF13469;
3.40.50.300;
Protein sulfotransferase family
PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60507}.
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O60507}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O60507}.
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]; Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20...
null
null
null
null
FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000269|PubMed:9501187}.
Mus musculus (Mouse)
O70283
WNT2B_MOUSE
MLKLQGEDEAAQLAPRRARVPVPRPTAPDVSPSSARLGLACLLLLLLLTLPARVDTSWWYIGALGARVICDNIPGLVSRQRQLCQRYPDIMRSVGEGAREWIRECQHQFRHHRWNCTTLDRDHTVFGRAMLRSSREAAFVYAISSAGVVHAITRACSQGELSVCSCDPYTRGRHHDQRGDFDWGGCSDNIHYGVRFAKAFVDAKEKRLKDARALMNLHNNRCGRTAVRRFLKLECKCHGVSGSCTLRTCWRALSDFRRTGDYLRRRYDGAVQVTATQDGANFTAARQGYRHATRTDLVYFDNSPDYCVLDKAAGSLGTAG...
null
null
animal organ morphogenesis [GO:0009887]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cell-cell signaling [GO:0007267]; cellular response to starvation [GO:0009267]; chondrocyte differentiation [GO:0002062]; forebrain regionalization [GO:0021871]; hematopoietic stem cell proliferatio...
extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]
cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; signaling receptor binding [GO:0005102]
PF00110;
3.30.2460.20;
Wnt family
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q93097}. Secreted {ECO:0000250|UniProtKB:Q93097}.
null
null
null
null
null
FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt/beta-catenin signaling pathway (PubMed:19686689). Plays a redundant role in embryonic lung development (PubMed:19686689). {ECO:0000269|PubMed:19686689, ECO:0000305}.
Mus musculus (Mouse)
O70291
GRK4_MOUSE
MELENFVANNLLLKARLGFNKQTGRSKKWRELLKFPPVSMCTELRWSIEKDFSSLCDKQPIGRLLFRQFCDTKPDLKRCIEFLDAVAEYEVTIEEEQREFGLAIFSRFFKEKSEVPLPEIPPDIVKECKWNLKQNSPSQNVFEECAGIVCKYLSETPFEEYQESTYFNRFLQWKWLERRPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKLHSRFVVSLAYTYETKDALCLVLTIMNGGDLKYHIYNLGDPGFEEPRAVFYAAELCCGLEDLQRKRIVYRDLKPENILLD...
2.7.11.16
null
desensitization of G protein-coupled receptor signaling pathway [GO:0002029]; G protein-coupled receptor internalization [GO:0002031]; phosphorylation [GO:0016310]; regulation of signal transduction [GO:0009966]; signal transduction [GO:0007165]
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; rhodopsin kinase activity [GO:0050254]
PF00069;PF00615;
1.10.167.10;1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family, GPRK subfamily
PTM: Palmitoylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cell cortex {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=[G-protein-coupled receptor] + ATP = [G-protein-coupled receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:12008, Rhea:RHEA-COMP:11260, Rhea:RHEA-COMP:11261, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.16;
null
null
null
null
FUNCTION: Specifically phosphorylates the activated forms of G protein-coupled receptors.
Mus musculus (Mouse)
O70293
GRK6_MOUSE
MELENIVANTVLLKAREGGGGNRKGKSKKWRQMLQFPHISQCEELRLSLERDYHSLCERQPIGRLLFREFCATRPELTRCTAFLDGVSEYEVTPDEKRKACGRRLMQNFLSHTGPDLIPEVPRQLVSNCAQRLEQGPCKDLFQELTRLTHEYLSTAPFADYLDSIYFNRFLQWKWLERQPVTKNTFRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLD...
2.7.11.16
null
desensitization of G protein-coupled receptor signaling pathway [GO:0002029]; phosphorylation [GO:0016310]; regulation of signal transduction [GO:0009966]; Wnt signaling pathway [GO:0016055]
cytoplasm [GO:0005737]; membrane [GO:0016020]
ATP binding [GO:0005524]; beta-adrenergic receptor kinase activity [GO:0047696]; G protein-coupled receptor kinase activity [GO:0004703]
PF00069;PF00615;
6.10.250.2260;1.10.167.10;1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family, GPRK subfamily
null
SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CATALYTIC ACTIVITY: Reaction=[G-protein-coupled receptor] + ATP = [G-protein-coupled receptor]-phosphate + ADP + H(+); Xref=Rhea:RHEA:12008, Rhea:RHEA-COMP:11260, Rhea:RHEA-COMP:11261, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.16;
null
null
null
null
FUNCTION: Specifically phosphorylates the activated forms of G protein-coupled receptors. Such receptor phosphorylation initiates beta-arrestin-mediated receptor desensitization, internalization, and signaling events leading to their desensitization. Seems to be involved in the desensitization of D2-like dopamine recep...
Mus musculus (Mouse)
O70299
MB211_MOUSE
MIAAQAKLVYHLNKYYNEKCQARKAAIAKTIREVCKVVSDVLKEVEVQEPRFISSLNEMDNRYEGLEVISPTEFEVVLYLNQMGVFNFVDDGSLPGCAVLKLSDGRKRSMSLWVEFITASGYLSARKIRSRFQTLVAQAVDKCSYRDVVKMVADTSEVKLRIRDRYVVQITPAFKCTGIWPRSAAHWPLPHIPWPGPNRVAEVKAEGFNLLSKECHSLAGKQSSAESDAWVLQFAEAENRLQMGGCRKKCLSILKTLRDRHLELPGQPLNNYHMKTLVSYECEKHPRESDWDESCLGDRLNGILLQLISCLQCRRCPHYF...
2.7.7.-
null
camera-type eye development [GO:0043010]; cell population proliferation [GO:0008283]; eye development [GO:0001654]; positive regulation of cell population proliferation [GO:0008284]
nucleus [GO:0005634]
metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; nucleotidyltransferase activity [GO:0016779]
PF03281;PF20266;
1.10.1410.40;3.30.460.90;
Mab-21 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10556287}.
null
null
null
null
null
FUNCTION: Putative nucleotidyltransferase required for several aspects of embryonic development including normal development of the eye, notochord, neural tube and other organ tissues, and for embryonic turning (PubMed:11857508, PubMed:12642482). It is unclear whether it displays nucleotidyltransferase activity in vivo...
Mus musculus (Mouse)
O70302
CIDEA_MOUSE
METARDYAGALIRPLTFMGLQTKKVLLTPLIHPARPFRVSNHDRSSRRGVMASSLQELISKTLDVLVITTGLVTLVLEEDGTVVDTEEFFQTLRDNTHFMILEKGQKWTPGSKYVPVCKQPKKSGIARVTFDLYRLNPKDFLGCLNVKATMYEMYSVSYDIRCTSFKAVLRNLLRFMSYAAQMTGQFLVYAGTYMLRVLGDTEEQPSPKPSTKGWFM
null
null
apoptotic process [GO:0006915]; cellular response to cold [GO:0070417]; lipid droplet fusion [GO:0160077]; lipid metabolic process [GO:0006629]; lipid storage [GO:0019915]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of execution phase of apoptosis [GO:1900118]; negative regulati...
cytoplasm [GO:0005737]; lipid droplet [GO:0005811]; mitochondrial envelope [GO:0005740]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
lipid transfer activity [GO:0120013]; phosphatidic acid binding [GO:0070300]; protein homodimerization activity [GO:0042803]
PF02017;
3.10.20.10;
CIDE family
null
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:18509062, ECO:0000269|PubMed:20810722, ECO:0000269|PubMed:22144693, ECO:0000269|PubMed:26609809}. Nucleus {ECO:0000269|PubMed:22245780}. Note=Enriched at lipid droplet contact sites (PubMed:18509062, PubMed:22144693). Using a GFP-tagged construct, has been shown t...
CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out); Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615; Evidence={ECO:0000305|PubMed:26609809};
null
null
null
null
FUNCTION: Lipid transferase that promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed:18509062, PubMed:22144693, PubMed:26609809, PubMed:36477540). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:18509062, PubMed:22144693, PubMed...
Mus musculus (Mouse)
O70303
CIDEB_MOUSE
MEYLSAFNPNGLLRSVSTVSSELSRRVWNSAPPPQRPFRVCDHKRTVRKGLTAASLQELLDKVLETLLLRGVLTLVLEEDGTAVDSEDFFQLLEDDTCLMVLEQGQSWSPKSGMLSYGLGREKPKHSKDIARITFDVYKQNPRDLFGSLNVKATFYGLYSMSCDFQGVGPKRVLRELLRWTSSLLQGLGHMLLGISSTLRHVVEGADRWQWHGQRHLHS
null
null
apoptotic process [GO:0006915]; COPII-coated vesicle cargo loading [GO:0090110]; execution phase of apoptosis [GO:0097194]; lipid droplet fusion [GO:0160077]; lipid storage [GO:0019915]; positive regulation of apoptotic process [GO:0043065]; regulation of apoptotic process [GO:0042981]; regulation of triglyceride metab...
COPI-coated vesicle [GO:0030137]; COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; lipid droplet [GO:0005811]; perinuclear region of cytoplasm [GO:0048471]
identical protein binding [GO:0042802]; lipid transfer activity [GO:0120013]; molecular adaptor activity [GO:0060090]; phosphatidic acid binding [GO:0070300]
PF02017;
3.10.20.10;
CIDE family
null
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:19187774, ECO:0000269|PubMed:26733203}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19187774, ECO:0000269|PubMed:23297397}; Peripheral membrane protein {ECO:0000269|PubMed:19187774}; Cytoplasmic side {ECO:0000269|PubMed:19187774}. Golgi apparatus {ECO:00002...
null
null
null
null
null
FUNCTION: Lipid transferase specifically expressed in hepatocytes, which promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed:26733203). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:26733203). Localizes on the lipid droplet su...
Mus musculus (Mouse)
O70305
ATX2_MOUSE
MRSSTAAVQRPAAGDPEPRRPAGWAARRSLPRTARRGGRGGAVAYPSAGPPPRGPGAPPRGPRSPPCASDCFGSNGHGASRPGSRRLLGVCGPPRPFVVVLLALAPAATPARACPPGVRASPPRSGVSSSARPAPGCPRPACEPVYGPLTMSLKPQPQPPAPATGRKPGGGLLSSPGAAPASAAVTSASVVPAPAAPVASSSAAAGGGRPGLGRGRNSSKGLPQPTISFDGIYANVRMVHILTSVVGSKCEVQVKNGGIYEGVFKTYSPKCDLVLDAAHEKSTESSSGPKREEIMESVLFKCSDFVVVQFKDTDSSYARR...
null
null
cerebellar Purkinje cell differentiation [GO:0021702]; homeostasis of number of cells [GO:0048872]; negative regulation of multicellular organism growth [GO:0040015]; neuromuscular process [GO:0050905]; neuron projection morphogenesis [GO:0048812]; stress granule assembly [GO:0034063]
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; perinuclear region of cytoplasm [GO:0048471]
mRNA binding [GO:0003729]
PF06741;PF07145;PF14438;
null
Ataxin-2 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9668173}.
null
null
null
null
null
FUNCTION: Involved in EGFR trafficking, acting as negative regulator of endocytic EGFR internalization at the plasma membrane. {ECO:0000269|PubMed:18602463}.
Mus musculus (Mouse)
O70306
TBX15_MOUSE
MSERRRSAVALSSRAHAFSVEALIGSNKKRKLRDWEEKGLDLSMEALSPAGPLGDTDDPATHGLEPHPDSEQSTGSDSEVLTERTSCSFSTHTDLASGAAGPVPAAMSSMEEIQVELQCADLWKRFHDIGTEMIITKAGRRMFPAMRVKITGLDPHQQYYIAMDIVPVDNKRYRYVYHSSKWMVAGNADSPVPPRVYIHPDSLASGDTWMRQVVSFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRKDFSSDLSPTKPVPVGDGVKTFNFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRDSGRNRTGLEAIMETYA...
null
null
cell fate specification [GO:0001708]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic skeletal system morphogenesis [GO:0048704]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA p...
chromatin [GO:0000785]; nucleus [GO:0005634]; RNA polymerase II transcription repressor complex [GO:0090571]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00907;
2.60.40.820;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
null
null
null
null
null
FUNCTION: Probable transcriptional regulator involved in the development of the skeleton of the limb, vertebral column and head. Acts by controlling the number of mesenchymal precursor cells and chondrocytes.
Mus musculus (Mouse)
O70309
ITB5_MOUSE
MPRVPATLYACLLGLCALVPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEYFGNPRSITSRCDLKANLIRNGCEGEIESPASSTHVLRNLPLSSKGSSATGSDVIQMTPQEIAVSLRPGEQTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLENIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLA...
null
null
cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; integrin-mediated signaling pathway [GO:0007229]; stress fiber assembly [GO:0043149]; transforming growth factor beta receptor signaling pathway [GO:0007179]
cell leading edge [GO:0031252]; cell surface [GO:0009986]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; integrin alphav-beta5 complex [GO:0034684]; integrin complex [GO:0008305]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; synaptic membrane [GO:0097060]
integrin binding [GO:0005178]; metal ion binding [GO:0046872]
PF07974;PF18372;PF08725;PF07965;PF00362;PF17205;
4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410;
Integrin beta chain family
null
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand.
Mus musculus (Mouse)
O70310
NMT1_MOUSE
MADESETAVKLPAPSLPLMMEGNGNGHEHCSDCENEEDNSHNRSGLSPANDTGAKKKKKKQKKKKEKGSDMESTQDQPVKMTSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTM...
2.3.1.97
null
cellular ketone metabolic process [GO:0042180]; in utero embryonic development [GO:0001701]; N-terminal peptidyl-glycine N-myristoylation [GO:0018008]; protein localization to membrane [GO:0072657]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
glycylpeptide N-tetradecanoyltransferase activity [GO:0004379]; myristoyltransferase activity [GO:0019107]; peptidyl-lysine N6-myristoyltransferase activity [GO:0018030]
PF01233;PF02799;
3.40.630.170;
NMT family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30419}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P30419}. Membrane {ECO:0000250|UniProtKB:P30419}; Peripheral membrane protein {ECO:0000250|UniProtKB:P30419}. Note=Copurifies with ribosomes. {ECO:0000250|UniProtKB:P30419}.
CATALYTIC ACTIVITY: Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723, ChEBI:CHEBI:133050; EC=2.3.1.97; Evidence={ECO:000026...
null
null
null
null
FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins (PubMed:15753093). Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3' (By similarity). Lysine myristoylation is required to maintain ARF6...
Mus musculus (Mouse)
O70318
E41L2_MOUSE
MTTEVGSASEVKKGSDQAGADASKEKAKEVENEQTPVSEPEEEKGSQPGPPVERQSTPRLRKRGKDPSENRGISRFIPPWLKKQRSYNLVVAKDGGDKKEPTQADVEDQILGKEESLPEEESRAKGDAEEMAQRKHLEVQVEVREAKPALKSSVETQPAEEVRKDKEETIQDTQEEKLEGGAAKRETKEVQTSELKAEVASQKATKKTKTVLAKVTLLDGTEYSCDLEKRAKGQVLFDRVCEHLNLLEKDYFGLLFQDHPEQKNWLDPAKEIKRQLKNLPWLFTFNVKFYPPDPSQLTEDITRYFLCLQLRQDIASGRLP...
null
null
actin cytoskeleton organization [GO:0030036]; actomyosin structure organization [GO:0031032]; cell cycle [GO:0007049]; cell division [GO:0051301]; cortical actin cytoskeleton organization [GO:0030866]; positive regulation of protein localization to cell cortex [GO:1904778]; regulation of cell shape [GO:0008360]
actin cytoskeleton [GO:0015629]; cell cortex [GO:0005938]; cell junction [GO:0030054]; COP9 signalosome [GO:0008180]; cytoskeleton [GO:0005856]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
actin binding [GO:0003779]; PH domain binding [GO:0042731]; spectrin binding [GO:0030507]; structural molecule activity [GO:0005198]
PF05902;PF08736;PF09380;PF00373;PF09379;PF04382;
1.20.80.10;2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:O43491}. Cell membrane {ECO:0000250|UniProtKB:O43491}.
null
null
null
null
null
FUNCTION: Required for dynein-dynactin complex and NUMA1 recruitment at the mitotic cell cortex during anaphase. {ECO:0000250|UniProtKB:O43491}.
Mus musculus (Mouse)
O70320
PLB1_CAVPO
MGLQPGVLLVGLLLLGQGITQIHTSSGKSTLEGQLWPETKKNFPFSCSPKKLGLNMPSESVHTLTPADIKLIAAIGDMETPPDSGAVNLDTSERTEKEPWRGCMGMMTVLSDIISHFNPSVLLPTCPPWRSAAVRGGVEELRTQAEELVSSLKKNPQLDFQQDWKLINVFFSNASLCYLCPSAHENGPLMSNMDKLAGILHYLHQEVPRAFVNLVDLFEVVAMPRWHQGTMLSRPSPEACGCSGETSKLDTVVMQWSYQETWDSLLASSSFNDQESFAVVFQPFFYEVSSPVEEPPSQDPTTLALSLWNNMMKPVGQKDE...
3.1.1.3; 3.1.1.4; 3.1.1.5
null
phospholipid metabolic process [GO:0006644]
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]
lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545]; phospholipase A2 activity [GO:0004623]; retinyl-palmitate esterase activity [GO:0050253]; triglyceride lipase activity [GO:0004806]
PF00657;
3.40.50.1110;
'GDSL' lipolytic enzyme family, Phospholipase B1 subfamily
PTM: Undergoes proteolytic cleavage in the ileum. {ECO:0000269|PubMed:9593672}.
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:O54728}; Single-pass type I membrane protein {ECO:0000255}. Note=Present in the intestinal brush border membranes. {ECO:0000269|PubMed:9593672}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:O54728}; Physiologica...
null
null
null
null
FUNCTION: Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (PubMed:2722844). Has dual phospholipase and lysophospholipase activities toward diacylpho...
Cavia porcellus (Guinea pig)
O70324
MOT8_MOUSE
MALPSPASEEAEGPCQEANQEYQEPVCSPVPEPEPEPEPEPEPDPEPVPVPPPEPQPEPEPQPLPDPAPLPELGFEAEPVQEPEPTPTVETRGTARGFQPPEGGFGWIVVFAATWCNGSIFGIHNSVGILYSMLLEEEKEKNRQVEFQAAWVGALAMGMIFFCSPIVSIFTDRLGCRITATTGAAVAFIGLHTSSFTSSLSLRYFTYGILFGCGCSFAFQPSLVILGHYFQRRLGLANGVVSAGSSIFSMSFPFLIKMLGDKIKLAQTFQVLSTFMFVLTLLSLTYRPLLPSSQDTPSKRGAHTLRQRFLVQFRKYFNMR...
null
null
amino acid import across plasma membrane [GO:0089718]; amino acid metabolic process [GO:0006520]; hormone transport [GO:0009914]; negative regulation of neural precursor cell proliferation [GO:2000178]; thyroid hormone generation [GO:0006590]; thyroid hormone transport [GO:0070327]; thyroid-stimulating hormone secretio...
apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]
amino acid transmembrane transporter activity [GO:0015171]; identical protein binding [GO:0042802]; monocarboxylic acid transmembrane transporter activity [GO:0008028]; thyroid hormone transmembrane transporter activity [GO:0015349]
PF07690;
1.20.1250.20;
Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18687783}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:18687783}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=3,3',5-triiodo-L-thyronine(out) = 3,3',5-triiodo-L-thyronine(in); Xref=Rhea:RHEA:71811, ChEBI:CHEBI:533015; Evidence={ECO:0000269|PubMed:31436139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71812; Evidence={ECO:0000305|PubMed:31436139}; PhysiologicalDirection=right-to-left; Xref=...
null
null
null
null
FUNCTION: Specific thyroid hormone transmembrane transporter, that mediates both uptake and efflux of thyroid hormones across the cell membrane independently of pH or a Na(+) gradient (PubMed:31436139). Major substrates are the iodothyronines T3 and T4 and to a lesser extent rT3 and 3,3-diiodothyronine (3,3'-T2). Acts ...
Mus musculus (Mouse)
O70325
GPX4_MOUSE
MSWGRLSRLLKPALLCGALAAPGLAGTMCASRDDWRCARSMHEFSAKDIDGHMVCLDKYRGFVCIVTNVASQUGKTDVNYTQLVDLHARYAECGLRILAFPCNQFGRQEPGSNQEIKEFAAGYNVKFDMYSKICVNGDDAHPLWKWMKVQPKGRGMLGNAIKWNFTKFLIDKNGCVVKRYGPMEEPQVIEKDLPCYL
1.11.1.12; 1.11.1.9
null
arachidonic acid metabolic process [GO:0019369]; cellular response to oxidative stress [GO:0034599]; chromatin organization [GO:0006325]; lipoxygenase pathway [GO:0019372]; negative regulation of ferroptosis [GO:0110076]; protein polymerization [GO:0051258]; response to estradiol [GO:0032355]; response to oxidative str...
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
glutathione peroxidase activity [GO:0004602]; identical protein binding [GO:0042802]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; selenium binding [GO:0008430]
PF00255;
3.40.30.10;
Glutathione peroxidase family
null
SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:12566075, ECO:0000269|PubMed:22207760}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:12566075}.; SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus {ECO:0000269|PubMed:11344099}.
CATALYTIC ACTIVITY: Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O; Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019; EC=1.11.1.12; Evidence={ECO:0000269|PubMed:29...
null
null
null
null
FUNCTION: Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (PubMed:29290465). Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells f...
Mus musculus (Mouse)
O70326
GREM1_MOUSE
MNRTAYTVGALLLLLGTLLPTAEGKKKGSQGAIPPPDKAQHNDSEQTQSPPQPGSRTRGRGQGRGTAMPGEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQPPTKKKRVTRVKQCRCISIDLD
null
null
angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [GO:0060379]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell morphogenesis [GO:0000902]; cell-cell signaling [GO:0007267]; collagen fib...
cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; heparan sulfate proteoglycan binding [GO:0043395]; protein homodimerization activity [GO:0042803]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; vascular endothelial growth factor receptor ...
PF03045;
2.10.90.10;
DAN family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
null
null
null
null
null
FUNCTION: Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as BMP a antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop (PubMed:12808456, PubMed:15201225). Down-regulates the BMP4 signaling in a dose-dependent manner (...
Mus musculus (Mouse)
O70333
CRIPT_MOUSE
MVCEKCEKKLGRVITPDTWKDGARNTTESGGRKLNENKALTSKKARFDPYGKNKFSTCRICKSSVHQPGSHYCQGCAYKKGICAMCGKKVLDTKNYKQTSV
null
null
cytoplasmic microtubule organization [GO:0031122]; establishment of protein localization [GO:0045184]; mRNA processing [GO:0006397]; protein localization to microtubule [GO:0035372]; regulation of postsynaptic density assembly [GO:0099151]; regulation of postsynaptic density protein 95 clustering [GO:1902897]; RNA spli...
cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; spliceosomal complex [GO:0005681]
microtubule binding [GO:0008017]; PDZ domain binding [GO:0030165]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]
PF10235;
null
CRIPT family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Colocalizes with DLG4 in asymmetric synapses. {ECO:0000250}.
null
null
null
null
null
FUNCTION: As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (By similarity). Involved in the cytoskeletal anchoring of DLG4 in excitatory synapses (By similarity). {ECO:0000250|UniProtKB:Q792Q4, ECO:0000250|UniProtKB:Q9P021}.
Mus musculus (Mouse)
O70337
BIK_MOUSE
MSEARLMARDVIKTVPHDQVPQPPVASETPSMKEPVRDVDLMECVEGRNQVALRLACIGDEMDLCLRSPRLVQLPGIAIHRLAVTYSRTGVRGIFRSLIRSLTNLRENIWSWRVLTPGAWVSPDQDPGQLFPMVLLVFLLLGGAWYLQLQ
null
null
apoptotic mitochondrial changes [GO:0008637]; male gonad development [GO:0008584]; regulation of apoptotic process [GO:0042981]; spermatogenesis [GO:0007283]
Bcl-2 family protein complex [GO:0097136]; endomembrane system [GO:0012505]; mitochondrial envelope [GO:0005740]; mitochondrial membrane [GO:0031966]
BH domain binding [GO:0051400]; protein-containing complex binding [GO:0044877]
PF12201;
null
null
PTM: Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage is a necessary step prior its degradation by the proteosome-dependent mechanism (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Mitochondrion membrane {ECO:0000269|PubMed:9525867}; Single-pass membrane protein {ECO:0000269|PubMed:9525867}. Note=Around the nuclear envelope, and in cytoplasmic membranes. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Accelerates programmed cell death. Binding to the apoptosis repressors Bcl-X(L), BHRF1 or Bcl-2 suppresses this death-promoting activity. {ECO:0000269|PubMed:9525867}.
Mus musculus (Mouse)
O70342
NPY5R_MOUSE
MEVKLEEHFNKTFVTENNTAASQNTASPAWEDYRGTENNTSAARNTAFPVWEDYRGSVDDLQYFLIGLYTFVSLLGFMGNLLILMAVMKKRNQKTTVNFLIGNLAFSDILVVLFCSPFTLTSVLLDQWMFGKAMCHIMPFLQCVSVLVSTLILISIAIVRYHMIKHPISNNLTANHGYFLIATVWTLGFAICSPLPVFHSLVELKETFGSALLSSKYLCVESWPSDSYRIAFTISLLLVQYILPLVCLTVSHTSVCRSISCGLSHKENRLEENEMINLTLHPSKKSRDQAKPPSTQKWSYSFIRKHRRRYSKKTACVLPA...
null
null
cardiac left ventricle morphogenesis [GO:0003214]; chemical synaptic transmission [GO:0007268]; eating behavior [GO:0042755]; G protein-coupled receptor signaling pathway [GO:0007186]; generation of ovulation cycle rhythm [GO:0060112]; negative regulation of acute inflammatory response to antigenic stimulus [GO:0002865...
GABA-ergic synapse [GO:0098982]; membrane [GO:0016020]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
neuropeptide binding [GO:0042923]; neuropeptide Y receptor activity [GO:0004983]; pancreatic polypeptide receptor activity [GO:0001602]; peptide YY receptor activity [GO:0001601]
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 neuropeptide Y and peptide YY. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity. Seems to be associated with food intake. Could be involved in feeding disorders (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O70343
PRGC1_MOUSE
MAWDMCSQDSVWSDIECAALVGEDQPLCPDLPELDLSELDVNDLDTDSFLGGLKWCSDQSEIISNQYNNEPANIFEKIDEENEANLLAVLTETLDSLPVDEDGLPSFDALTDGAVTTDNEASPSSMPDGTPPPQEAEEPSLLKKLLLAPANTQLSYNECSGLSTQNHAANHTHRIRTNPAIVKTENSWSNKAKSICQQQKPQRRPCSELLKYLTTNDDPPHTKPTENRNSSRDKCASKKKSHTQPQSQHAQAKPTTLSLPLTPESPNDPKGSPFENKTIERTLSVELSGTAGLTPPTTPPHKANQDNPFKASPKLKPSCK...
null
null
adipose tissue development [GO:0060612]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to oxidative stress [GO:0034599]; cellular response to thyroid hormone stimulus [GO:0097067]; cellular response to transforming growth factor beta stimulus [GO:0071560]; circadian regulati...
apical dendrite [GO:0097440]; chromatin [GO:0000785]; cytosolic ribosome [GO:0022626]; euchromatin [GO:0000791]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
alpha-tubulin binding [GO:0043014]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; lncRNA binding [GO:0106222]; nuclear estrogen receptor binding [GO:0030331]; nuclear receptor coactivator activity [GO:0030374]; peroxisome proliferator activated receptor binding [GO:004297...
PF00076;
3.30.70.330;
null
PTM: Phosphorylation by AMPK in skeletal muscle increases activation of its own promoter (PubMed:17609368). Phosphorylated by CLK2 (PubMed:20074525). {ECO:0000269|PubMed:17609368, ECO:0000269|PubMed:20074525}.; PTM: Heavily acetylated by KAT2A/GCN5 under conditions of high nutrients, leading to inactivation of PPARGC1A...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22886304, ECO:0000269|PubMed:23217713}. Nucleus, PML body {ECO:0000269|PubMed:22886304}.
null
null
null
null
null
FUNCTION: Transcriptional coactivator for steroid receptors and nuclear receptors (PubMed:12754525, PubMed:15744310, PubMed:23217713, PubMed:9529258). Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter (PubMed:12754525, PubMed:15744310, PubMed:2321771...
Mus musculus (Mouse)
O70344
KCNQ1_CAVPO
MAAASSPPRTERKRGGWGRLLGSRRGSASLAKKCPFSLELAEGGPAGGTLYAPVAPPGALSPGSPAPPASPAAPPAGLELGPRPPVSLDPRVSIYSARRPLLARTHIQGRVYNFLERPTGWKCFVYHFAVFLIVLACLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGIWGRLRFARKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIGYGDKV...
null
null
adrenergic receptor signaling pathway [GO:0071875]; auditory receptor cell development [GO:0060117]; cellular response to cAMP [GO:0071320]; cellular response to epinephrine stimulus [GO:0071872]; cellular response to xenobiotic stimulus [GO:0071466]; cochlea development [GO:0090102]; corticosterone secretion [GO:00359...
apical plasma membrane [GO:0016324]; basolateral part of cell [GO:1990794]; basolateral plasma membrane [GO:0016323]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; late endosome [GO:0005770]; lumenal side of...
calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; outward rectifier potassium channel activity [GO:0015271]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase A regulatory subunit binding [GO:0034...
PF00520;PF03520;
1.10.287.70;6.10.140.1910;1.20.120.350;
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.1/KCNQ1 sub-subfamily
PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier potassium channel activity of the KCNQ1-KCNE1 complex through a macromolecular complex that includes PKA, PP1, and the targeting protein AKAP9. {ECO:0000250|UniProtKB:P51787}.; PTM: Ubiquitinated by NEDD4L; promotes internalization. The ubiquitinylated ...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51787}. Early endosome {ECO:0000250|UniProtKB:P51787}. Membrane raft {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum {ECO:0000250|Uni...
null
null
null
null
null
FUNCTION: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selectiv...
Cavia porcellus (Guinea pig)
O70348
DXO_MOUSE
MEPRGTKRKAEKTEVEKPLNKLPRAVPSLRTQPSLYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPINGPGPDFDLRDGYPDRYQPRDEEVQERLDHLLRWVLEHRNQLEGGPGWLAGATVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPAARAQRLARPPLLRELMYMGYKFEQYMCADKPGGSPDPSGEVNTNVAYCSVLRSRLGNHPLLFSGEVDCLNPQAPCTQPPSCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPHVVAGFRNPEGFVCSLKTFPTMEMFENVRNDRE...
3.1.13.-; 3.6.1.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947}; Note=Binds 2 magnesium ions. {ECO:0000269|PubMed:23523372, ECO:0000269|PubMed:30180947};
mRNA catabolic process [GO:0006402]; NAD-cap decapping [GO:0110155]; nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process [GO:0000956]; nucleic acid metabolic process [GO:0090304]; RNA destabilization [GO:0050779]
cytosol [GO:0005829]; nucleus [GO:0005634]
5'-3' exonuclease activity [GO:0008409]; magnesium ion binding [GO:0000287]; mRNA 5'-diphosphatase activity [GO:0034353]; mRNA binding [GO:0003729]; nucleotide binding [GO:0000166]; RNA NAD-cap (NAD-forming) hydrolase activity [GO:0110152]
PF08652;
null
DXO/Dom3Z family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O77932}.
CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + diphosphate + H(+); Xref=Rhea:RHEA:78683, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:138282, ChEBI:CHEBI:167618; Evidence={ECO:0...
null
null
null
null
FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed:28283058, PubMed:32374864). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (PubMed:2...
Mus musculus (Mouse)
O70351
HCD2_RAT
MAAAVRSVKGLVAVITGGASGLGLSTAKRLVGQGATAVLLDVPNSEGETEAKKLGGNCIFAPANVTSEKEVQAALTLAKEKFGRIDVAVNCAGIAVAIKTYHEKKNQVHTLEDFQRVINVNLIGTFNVIRLVAGVMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIVGMTLPIARDLAPIGIRVVTIAPGLFATPLLTTLPDKVRNFLASQVPFPSRLGDPAEYAHLVQMVIENPFLNGEVIRLDGAIRMQP
1.1.1.159; 1.1.1.178; 1.1.1.239; 1.1.1.35; 1.1.1.53; 1.1.1.62
null
androgen metabolic process [GO:0008209]; bile acid biosynthetic process [GO:0006699]; brexanolone metabolic process [GO:0062173]; C21-steroid hormone metabolic process [GO:0008207]; estrogen metabolic process [GO:0008210]; fatty acid beta-oxidation [GO:0006635]; fatty acid metabolic process [GO:0006631]; isoleucine cat...
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial nucleoid [GO:0042645]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739]; tRNA methyltransferase complex [GO:0043527]
17-beta-hydroxysteroid dehydrogenase (NAD+) activity [GO:0044594]; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity [GO:0047015]; 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; acetoacetyl-CoA reductase activity [GO:0018454]; amyloid-beta binding [GO:0001540]; androstan-3-alpha,17-beta-diol dehydrogenase ac...
PF00106;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99714}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q99714}.
CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:...
null
PATHWAY: Amino-acid degradation; L-isoleucine degradation. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000250|UniProtKB:Q9971...
null
null
FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism. Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation cycle, namely the...
Rattus norvegicus (Rat)
O70355
BTNL2_MOUSE
MVDCPRYSLSGVAASFLFVLLTIKHPDDFRVVGPNLPILAKVGEDALLTCQLLPKRTTAHMEVRWYRSDPDMPVIMYRDGAEVTGLPMEGYGGRAEWMEDSTEEGSVALKIRQVQPSDDGQYWCRFQEGDYWRETSVLLQVAALGSSPNIHVEGLGEGEVQLVCTSRGWFPEPEVHWEGIWGEKLMSFSENHVPGEDGLFYVEDTLMVRNDSVETISCFIYSHGLRETQEATIALSERLQTELASVSVIGHSQPSPVQVGENIELTCHLSPQTDAQNLEVRWLRSRYYPAVHVYANGTHVAGEQMVEYKGRTSLVTDAIH...
null
null
negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of T cell proliferation [GO:0042102]; regulation of cytokine production [GO:0001817]; T cell receptor signaling pathway [GO:0050852]
external side of plasma membrane [GO:0009897]
signaling receptor binding [GO:0005102]
PF08205;PF07686;
2.60.40.10;
Immunoglobulin superfamily, BTN/MOG family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: Negative regulator of T-cell proliferation. {ECO:0000269|PubMed:16751379, ECO:0000269|PubMed:17237401}.
Mus musculus (Mouse)
O70361
PER3_MOUSE
MDPCGDPAVPGGDCPQTRGPGLQGASGQEGPLQGTCVDSSHSEHEDRNRMSEELIMVVQEMKKYFPAERHTKPSTLDALNYALRCVHSVQANSDFFQSLGPRGAHQADVTVYSLEDLTALASEHTSKNTDTFAAVFSFLSGRLVHISEQAALILNSKRGFLKSVHFVDLLAPQDVRAFYAHTAPTQLPFWNNWTQRASQYECAPAKPFFCRICGGGDREKRHYSPFRILPYLVHVHSSAQPEPEPCCLTLVEKIHSGYEAPRIPVDKRIFTTTHTPGCVFLEVDERAVPLLGYLPQDLIGTSILTYLHPEDRPLMVAIHQ...
null
null
circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein stabilization [GO:0050821]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
kinase binding [GO:0019900]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor binding [GO:0001222]; ubiquitin protein ligase binding [GO:0031625]
PF08447;PF21353;PF12114;
3.30.450.20;
null
PTM: Phosphorylation by CSNK1E is weak and appears to require association with PER1 and translocation to the nucleus. {ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:11865049}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}. Nucleus {ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:11591712, ECO:0000269|PubMed:11865049, ECO:0000269|PubMed:14701732}. Note=Mainly cytoplasmic. Translocates to the...
null
null
null
null
null
FUNCTION: Originally described as 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. I...
Mus musculus (Mouse)
O70362
PHLD_MOUSE
MSAGRLWSSLLLLLPLFCSKSSSCGLSTHVEIGHRALEFLRLQDGRINYKELILEHQDAYQAGTVFPDAFYPSICKRGKYHDVSERTHWTPFLNASIHYIRENYPLPWEKDTEKLVAFLFGITSHMVADLSWHNLGFLRTMGAIDFYNSYSDAHSAGDFGGDVLSQFEFNFNYLSRRWYVPVRDLLRIYDNLYGRKVITKDVLVDCTYLQFLEMHGEMFAVSKLYSTYSTKSPFLVEQFQDYFLGGLDDMAFWSTNIYRLTSFMLENGTSDCNLPENPLFISCDGRNHTLSGSKVQKNDFHRNLTMFISRDIRKNLNYTE...
3.1.4.50
null
cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to calcium ion [GO:0071277]; cellular response to cholesterol [GO:0071397]; cellular response to inorganic substance [GO:0071241]; cellular response to insulin stimulus [GO:0032869]; cellular response to iron(II) ion [GO:0071282]; cellula...
cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intracellular membrane-bounded organelle [GO:0043231]
glycosylphosphatidylinositol phospholipase D activity [GO:0004621]; phospholipase D activity [GO:0004630]; sodium channel regulator activity [GO:0017080]
PF01839;PF00882;
2.130.10.130;
GPLD1 family
null
SUBCELLULAR LOCATION: Secreted. Note=Associated with the High-Density Lipoproteins (HDL). {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1D-myo-inositol + a 1,2-diacyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:10832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57997, ChEBI:CHEBI:58608, ChEBI:CHEBI:58700; EC=3.1...
null
null
null
null
FUNCTION: This protein hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol glycans (GPI-anchor) thus releasing these proteins from the membrane. {ECO:0000269|PubMed:9716655}.
Mus musculus (Mouse)
O70370
CATS_MOUSE
MRAPGHAAIRWLFWMPLVCSVAMEQLQRDPTLDYHWDLWKKTHEKEYKDKNEEEVRRLIWEKNLKFIMIHNLEYSMGMHTYQVGMNDMGDMTNEEILCRMGALRIPRQSPKTVTFRSYSNRTLPDTVDWREKGCVTEVKYQGSCGACWAFSAVGALEGQLKLKTGKLISLSAQNLVDCSNEEKYGNKGCGGGYMTEAFQYIIDNGGIEADASYPYKATDEKCHYNSKNRAATCSRYIQLPFGDEDALKEAVATKGPVSVGIDASHSSFFFYKSGVYDDPSCTGNVNHGVLVVGYGTLDGKDYWLVKNSWGLNFGDQGYIR...
3.4.22.27
null
antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; basement membrane disassembly [GO:0034769]; bone resorption [GO:0045453]; immune response [GO:0006955]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cation channel activity [GO:2001...
cell surface [GO:0009986]; early endosome lumen [GO:0031905]; extracellular space [GO:0005615]; lysosome [GO:0005764]; membrane [GO:0016020]; phagocytic vesicle [GO:0045335]
cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; peptidase activity [GO:0008233]
PF08246;PF00112;
3.90.70.10;
Peptidase C1 family
null
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P25774}. Secreted {ECO:0000250|UniProtKB:P25774}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:P25774}.
CATALYTIC ACTIVITY: Reaction=Similar to cathepsin L, but with much less activity on Z-Phe-Arg-|-NHMec, and more activity on the Z-Val-Val-Arg-|-Xaa compound.; EC=3.4.22.27;
null
null
null
null
FUNCTION: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L. {ECO:0000250|UniProtKB:P25774}.
Mus musculus (Mouse)
O70372
TERT_MOUSE
MTRAPRCPAVRSLLRSRYREVWPLATFVRRLGPEGRRLVQPGDPKIYRTLVAQCLVCMHWGSQPPPADLSFHQVSSLKELVARVVQRLCERNERNVLAFGFELLNEARGGPPMAFTSSVRSYLPNTVIETLRVSGAWMLLLSRVGDDLLVYLLAHCALYLLVPPSCAYQVCGSPLYQICATTDIWPSVSASYRPTRPVGRNFTNLRFLQQIKSSSRQEAPKPLALPSRGTKRHLSLTSTSVPSAKKARCYPVPRVEEGPHRQVLPTPSGKSWVPSPARSPEVPTAEKDLSSKGKVSDLSLSGSVCCKHKPSSTSLLSPPR...
2.7.7.49
null
cellular response to hypoxia [GO:0071456]; DNA strand elongation [GO:0022616]; establishment of protein localization to telomere [GO:0070200]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cellular senescence [GO:2000773]; negative regulation of e...
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; plasma membrane [GO:0005886]; PML body [GO:0016605]; telomerase catalytic core complex [GO:0000333]; telomerase ho...
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; telomerase activity [GO:0003720]; telomerase RNA binding [GO:0070034]; telomerase RNA reverse transcriptase activi...
PF00078;PF12009;PF21399;
1.10.132.70;1.10.357.90;3.30.70.2630;
Reverse transcriptase family, Telomerase subfamily
PTM: Phosphorylation at Tyr-697 under oxidative stress leads to translocation of TERT to the cytoplasm and reduces its antiapoptotic activity. Dephosphorylated by SHP2/PTPN11 leading to nuclear retention. Phosphorylation by the AKT pathway promotes nuclear location. Phosphorylation at the G2/M phase at Ser-447 by DYRK2...
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O14746}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus. Chromosome, telomere. Cytoplasm {ECO:0000250}. Nucleus, PML body {ECO:0000250}. Note=Shuttling between nuclear and cytoplasm depends on cell cycle, phosphorylation states, transformation and DNA damage....
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
null
null
null
null
FUNCTION: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of t...
Mus musculus (Mouse)
O70373
XIRP1_MOUSE
MADAQMQVAPTPTIQMRTEEDLSLPHPSAPEGLPPPPPKETFSKFQQQRQASELRRLYKHIHPELRKNLEEAVAEDLAEVLGSEEPTEGDVQCMRWIFENWRLDAIGDHERPAAREPVSGGNVQATSRKFEEGSFTNSSDQEPEGLRPSGGDVQAARQMFETKPLDALRGQEEATQTTMREPAATGDVQGTRKLFETRPLDRLGSRPSIQEQSPLELRSEIQELKGDVKKTVKLFQTEPLCAIQDAEGTIHEVKAACREEIQSNAVRSARWLFETRPLDAFNQDPSQVRVIRGISLEEGALPDVSATRWIFETQPLDAIR...
null
null
actin filament organization [GO:0007015]; cardiac muscle cell development [GO:0055013]; heart morphogenesis [GO:0003007]; negative regulation of cell population proliferation [GO:0008285]; Notch signaling pathway [GO:0007219]; regulation of membrane potential [GO:0042391]; sarcomere organization [GO:0045214]
adherens junction [GO:0005912]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; intercalated disc [GO:0014704]; stress fiber [GO:0001725]
actin filament binding [GO:0051015]; filamin binding [GO:0031005]
PF08043;
null
Xin family
null
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:Q5PZ43}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q5PZ43}. Note=Colocalizes with actin stress fibers. {ECO:0000250|UniProtKB:Q702N8}.
null
null
null
null
null
FUNCTION: Protects actin filaments from depolymerization (By similarity). Required for correct cardiac intercalated disk ultrastructure via maintenance of cell-cell adhesion stability, and as a result maintains cardiac organ morphology, conductance and heat beat rhythm (PubMed:17766470). {ECO:0000250|UniProtKB:Q702N8, ...
Mus musculus (Mouse)
O70374
MTG8R_MOUSE
MVGVPGAAAFQLGCEKRVPAMPGSPVEVKIQSRSSPPIMPPLPPINPGGPRPVSFTPTALSNGINHSPPTLNGAPSPPQRFSNGPASSTSSALTNQQLPATCGARQLSKLKRFLTTLQQFGNDISPEIGEKVRTLVLALVNSTVTIEEFHCKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARAAKQTPSQYLAQHEHLLLNTSIASPADSSELLMEVHGNGKRPSPERRDENNFERDTVPPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPLQHYTLEDIATSHLYREPNKMLEHREVRERHHNLSLNGG...
null
null
DNA-templated transcription [GO:0006351]; epithelial cell differentiation [GO:0030855]; intestinal epithelial cell differentiation [GO:0060575]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neuron projection development [GO:0010977]; negative regulation of Notch signaling path...
nucleus [GO:0005634]
metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]
PF08788;PF07531;PF01753;
6.10.140.2220;6.10.250.230;1.20.120.1110;
CBFA2T family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440}.
null
null
null
null
null
FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Via association with PRDM14 is involved in regulation of embryonic stem cell (ESC) pluripotency. Involved in ...
Mus musculus (Mouse)
O70377
SNP23_RAT
MDDLSPEEIQLRAHQVTDESLESTRRILGLAIESQDAGIKTITMLDEQGEQLNRIEEGMDQINKDMREAEKTLTELNKCCGLCVCPCNRTKNFESGKNYKATWGDGGDSSPSNVVSKQPSRITNGQPQQTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKNMALDMGNEIDAQNQQIQKITEKADTNKNRIDIANTRAKKLIDS
null
null
exocytic insertion of neurotransmitter receptor to postsynaptic membrane [GO:0098967]; exocytosis [GO:0006887]; histamine secretion by mast cell [GO:0002553]; membrane fusion [GO:0061025]; protein-containing complex assembly [GO:0065003]; regulation of exocytosis [GO:0017157]; synaptic vesicle fusion to presynaptic act...
adherens junction [GO:0005912]; azurophil granule [GO:0042582]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; SN...
SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075]
PF00835;
1.20.5.110;
SNAP-25 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Mainly localized to the plasma membrane. ...
null
null
null
null
null
FUNCTION: Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion. {ECO:0000250}.
Rattus norvegicus (Rat)
O70394
I27RA_MOUSE
MNRLRVARLTPLELLLSLMSLLLGTRPHGSPGPLQCYSVGPLGILNCSWEPLGDLETPPVLYHQSQKYHPNRVWEVKVPSKQSWVTIPREQFTMADKLLIWGTQKGRPLWSSVSVNLETQMKPDTPQIFSQVDISEEATLEATVQWAPPVWPPQKVLICQFRYKECQAETWTRLEPQLKTDGLTPVEMQNLEPGTCYQVSGRCQVENGYPWGEWSSPLSFQTPFLDPEDVWVSGTVCETSGKRAALLVWKDPRPCVQVTYTVWFGAGDITTTQEEVPCCKSPVPAWMEWAVVSPGNSTSWVPPTNLSLVCLAPESAPCDV...
null
null
cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-positive bacterium [GO:0050830]; negative regulation of cellular extravasation [GO:0002692]; negative regulation of interleukin-17 production [GO:0032700]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of neur...
cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
cytokine binding [GO:0019955]; interleukin-27 receptor activity [GO:0045509]
null
2.60.40.10;
Type I cytokine receptor family, Type 2 subfamily
null
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Receptor for IL27. Requires IL6ST/GP130 to mediate signal transduction in response to IL27. This signaling system acts through STAT3 and STAT1. Involved in the regulation of Th1-type immune responses. Also appears to be involved in innate defense mechanisms.
Mus musculus (Mouse)
O70397
P2RX2_CAVPO
MAATHPKAPTAQRLRQGWSAFWDYETPKVIVVRNRPLGVVYRAVQLLILLYFVWYVFIVQKSYQDSETGPESSIITKVKGITQSEHKVWDVEEYVKPPEGGSVFSIITRIEVTPFQTLGACPESIRVPNTTCHLDADCTAGELDMLGNGLRTGRCVPYYHGEAKTCEVSGWCPVEDGAAVSHFLGKMAPNFTILIKNSIHYPKFQFSKGNIAHRDMTYLRRCTFDQGFDPYCPIFRLGFIVEQAGENFTELAHRGGVIGVIINWDCDLDLPSSHCNPKYSFRRLDPKHVPASSGYNFRFAKYYRVNSTTTRTLIKAYGIR...
null
null
calcium ion transmembrane transport [GO:0070588]; response to ATP [GO:0033198]; sensory perception of sound [GO:0007605]
apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; receptor complex [GO:0043235]
ATP binding [GO:0005524]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; extracellularly ATP-gated monoatomic cation channel activity [GO:0004931]; purinergic nucleotide receptor activity [GO:0001614]
PF00864;
1.10.287.940;2.60.490.10;
P2X receptor family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UBL9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}.
CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9UBL9}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P49653}; CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out...
null
null
null
null
FUNCTION: ATP-gated nonselective transmembrane cation channel permeable to potassium, sodium and calcium (By similarity). Activation by extracellular ATP induces a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of...
Cavia porcellus (Guinea pig)
O70400
PDLI1_MOUSE
MTTQQIVLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAAIANLCIGDLITAIDGEDTSSMTHLEAQNKIKGCADNMTLTVSRSEQKIWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPAPSTRVITNQYNSPTGLYSSENISNFNNAVESKTSASGEEANSRPVVQPHPSGSLIIDKDSEVYKMLQEKQELNEPPKQSTSFLVLQEILESDGKGDPNKPSGFRSVKAPVTKVAASVGNAQKLPICDKCGTGIVGVFVKLRDHHRHPECYVCTDCGINLKQKGHFFVEDQIYCEKHARERVTPPEGYD...
null
null
actin cytoskeleton organization [GO:0030036]; establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; fibroblast migration [GO:0010761]; heart development [GO:0007507]; maintenance of cell polarity [GO:0030011]; muscle structure development [GO:0061061]; regulation of transcription by RNA polymerase I...
actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; cytoplasm [GO:0005737]; filamentous actin [GO:0031941]; stress fiber [GO:0001725]; transcription regulator complex [GO:0005667]; Z disc [GO:0030018]
actin binding [GO:0003779]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; transcription coactivator activity [GO:0003713]
PF15936;PF00412;PF00595;
2.30.42.10;2.10.110.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11596114}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O00151}. Note=Associates with the actin stress fibers (PubMed:11596114).
null
null
null
null
null
FUNCTION: Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton (By similarity). Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration and ...
Mus musculus (Mouse)
O70404
VAMP8_MOUSE
MEEASGSAGNDRVRNLQSEVEGVKNIMTQNVERILSRGENLDHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVIICVIVLIIVILIILFATGTIPT
null
null
autophagosome maturation [GO:0097352]; cellular response to type II interferon [GO:0071346]; defense response to virus [GO:0051607]; establishment of localization in cell [GO:0051649]; membrane fusion [GO:0061025]; mucus secretion [GO:0070254]; positive regulation of pancreatic amylase secretion [GO:1902278]; protein t...
basal part of cell [GO:0045178]; basolateral part of cell [GO:1990794]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764...
SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]
PF00957;
1.20.5.110;
Synaptobrevin family
null
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:27628032}; Single-pass type IV membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:Q9WUF4}; Single-pass type IV membrane prote...
null
null
null
null
null
FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE ...
Mus musculus (Mouse)
O70405
ULK1_MOUSE
MEPGRGGVETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHTMRTLSEDTVRLFLQQIAGAMRLLHSKGIIHRDLKPQNILLSNPGGRRANPSNIRVKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTLVPAIPRETSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASTPIKKSPPVPVPSYPSSGSGSSSSSSSASHLASPPSLGE...
2.7.11.1
null
autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; axon extension [GO:0048675]; axonogenesis [GO:0007409]; cellular response to amino acid starvation [GO:0034198]; cellular response to nutrient levels [GO:0031669]; cerebellar granule cell differentiation [GO:0021707]; collateral sprouting [GO:0048668]; establ...
Atg1/ULK1 kinase complex [GO:1990316]; autophagosome [GO:0005776]; axon [GO:0030424]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; phagophore assembly site [GO:0000407]; phagophore assembl...
ATP binding [GO:0005524]; Hsp90 protein binding [GO:0051879]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF12063;PF21127;PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily
PTM: Autophosphorylated. Phosphorylated under nutrient-rich conditions; dephosphorylated during starvation or following treatment with rapamycin. In response to nutrient limitation, phosphorylated and activated by AMPK, leading to activate autophagy. Under nutrient sufficiency, phosphorylated by MTOR/mTOR, disrupting t...
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19258318}. Preautophagosomal structure {ECO:0000269|PubMed:19258318}. Note=Under starvation conditions, is localized to puncate structures primarily representing the isolation membrane that sequesters a portion of the cytoplasm resulting in the formation of a...
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:0000305|PubMed:22539723, ECO:000030...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:10624947, PubMed:19258318, PubMed:21205641, PubMed:21258367, PubMed:21460634, PubMed:25040165, PubMed:25723488). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precu...
Mus musculus (Mouse)
O70418
RN112_RAT
MPRPVLSVTAFCHRLGKRESKRSFMGNSSNSWSHASFPKLELGLGQRPSPPRESPTCSICLERLREPISLDCGHDFCIRCFSTHRIPGCELPCCPECRKICKQKKGLRSLGERMKLLPQRPLPPALQETCAVRAERLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLDHLLRGLPGLESGDSTRPRAEGSLPGIRWGANGLTRGIWMWSHPFLLGKEGKKVAVFLVDTGDVMSPELSRETRVKLCALTMMLSSYQILNTSQELKDTDLGYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSS...
2.3.2.27
null
embryonic brain development [GO:1990403]; endoplasmic reticulum organization [GO:0007029]; G1 to G0 transition involved in cell differentiation [GO:0070315]; neuron differentiation [GO:0030182]; positive regulation of glial cell differentiation [GO:0045687]; positive regulation of neuron differentiation [GO:0045666]; p...
cell body [GO:0044297]; cytoplasm [GO:0005737]; endosome [GO:0005768]; membrane [GO:0016020]; neuron projection [GO:0043005]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; postsynaptic density [GO:0014069]; synaptic vesicle [GO:0008021]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein self-association [GO:0043621]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF02263;PF00097;
3.40.50.300;3.30.40.10;
TRAFAC class dynamin-like GTPase superfamily, GB1/RHD3 GTPase family, GB1 subfamily
PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q96DY5}.
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q96DY5}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q96DY5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96DY5}. Cytoplasm {ECO:0000250|UniProtKB:Q96DY5}. Nucleus {ECO:0000250|UniProtKB:Q96DY5}. Nucleus, nuclear body {ECO:0000...
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
null
null
FUNCTION: E3 ubiquitin-protein ligase that plays an important role in neuronal differentiation, including neurogenesis and gliogenesis, during brain development. During embryonic development initiates neuronal differentiation by inducing cell cycle arrest at the G0/G1 phase through up-regulation of cell-cycle regulator...
Rattus norvegicus (Rat)
O70421
FZD1_MOUSE
MAEEAAPSESRAAGRLSLELCAEALPGRREEVGHEDTASHRRPRADPRRWASGLLLLLWLLEAPLLLGVRAQAAGQVSGPGQQAPPPPQPQQSGQQYNGERGISIPDHGYCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTVLEQALPPCRSLCERARQGCEALMNKFGFQWPDTLKCEKFPVHGAGELCVGQNTSDKGTPTPSLLPEFWTSNPQHGGGGYRGGYPGGAGTVERGKFSCPRALRVPSYLNYHFLGEKDCGAPCEPTKVYGLMYFGPEELRFSRTWIGI...
null
null
astrocyte-dopaminergic neuron signaling [GO:0036520]; autocrine signaling [GO:0035425]; canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pathway involved in mesenchymal stem cell differentiation [GO:0044338]; cell-cell signaling [GO:0007267]; endothelial cell differentiation [GO:0045446]; hard pala...
cell surface [GO:0009986]; plasma membrane [GO:0005886]
frizzled binding [GO:0005109]; G protein-coupled receptor activity [GO:0004930]; identical protein binding [GO:0042802]; PDZ domain binding [GO:0030165]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
PF01534;PF01392;
1.10.2000.10;1.20.1070.10;
G-protein coupled receptor Fz/Smo family
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15923619}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Receptor for Wnt proteins (PubMed:15923619). Activated by WNT7B (PubMed:15923619). Activated by WNT3A, WNT3, WNT1 and to a lesser extent WNT2, but apparently not by WNT4, WNT5A, WNT5B, WNT6, WNT7A or WNT7B (By similarity). Contradictory results showing activation by WNT7B have been described for mouse (PubMed...
Mus musculus (Mouse)
O70423
AOC3_MOUSE
MTQKTTLVLLALAVITIFALVCVLLAGRSGDGGGLSQPLHCPSVLPSVQPRTHPSQSQPFADLSPEELTAVMSFLTKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGPLPHPSYMRDVTVERHGGPLPYYRRPVLDREYQDIEEMIFHRELPQASGLLHHCCFYKHQGQNLLTMTTAPRGLQSGDRATWFGLYYNLSGAGFYPHPIGLELLIDHKALDPALWTIQKVFYQGRYYESLTQLEDQFEAGLVNVVLVPNNGTGGSWSLKSSVPPGPAPPLQFHPQG...
1.4.3.21
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q16853}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q16853}; COFA...
amine metabolic process [GO:0009308]; cell adhesion [GO:0007155]; eating behavior [GO:0042755]; leukocyte migration involved in inflammatory response [GO:0002523]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of...
cell surface [GO:0009986]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; microvillus [GO:0005902]; plasma membrane [GO:0005886]
aliphatic amine oxidase activity [GO:0052595]; calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; primary amine oxidase activity [GO:0008131]; protein heterodimerization activity [GO:0046982]; quinone binding [GO:0048038]
PF01179;PF02727;PF02728;
3.10.450.40;2.70.98.20;
Copper/topaquinone oxidase family
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:Q16853}.; PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q16853}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16853}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16853}.
CATALYTIC ACTIVITY: Reaction=H2O + methylamine + O2 = formaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:59420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:28938, ChEBI:CHEBI:59338; Evidence={ECO:0000250|UniProtKB:Q16853}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59421;...
null
null
null
null
FUNCTION: Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia. Has a preference for the primary monoamines methylamine and benzylamine. Could also act on 2-phenylethylamine but much less efficiently. At endothelial cells s...
Mus musculus (Mouse)
O70433
FHL2_MOUSE
MTERFDCHHCNESLYGKKYILKEENPHCVACFEELYANTCEECGTPIGCDCKDLSYKDRHWHEGCFHCSRCGSSLVDKPFAAKEEQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFTCQRCQQPIGTKSFIPKENQNFCVPCYEKQYALQCVQCKKPITTGGVTYREQPWHKECFVCTACKKQLSGQRFTARDEFPYCLTCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI
null
null
atrial cardiac muscle cell development [GO:0055014]; heart trabecula formation [GO:0060347]; negative regulation of apoptotic process [GO:0043066]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast differentiation [...
M band [GO:0031430]; nucleus [GO:0005634]; Z disc [GO:0030018]
bHLH transcription factor binding [GO:0043425]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134]
PF00412;
2.10.110.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14192}. Nucleus {ECO:0000269|PubMed:20013826}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22851699}.
null
null
null
null
null
FUNCTION: May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 wit...
Mus musculus (Mouse)
O70435
PSA3_MOUSE
MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSANDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDVVKEVAKIIYIVHDEVKDKAFELELSWVGELTKGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM
null
null
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773]; synapse [GO:0045202]
ubiquitin protein ligase binding [GO:0031625]
PF00227;PF10584;
3.60.20.10;
Peptidase T1A family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25788}. Nucleus {ECO:0000250|UniProtKB:P25788}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:P25788}.
null
null
null
null
null
FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus p...
Mus musculus (Mouse)
O70436
SMAD2_RAT
MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTANTVDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFSLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVN...
null
null
activin receptor signaling pathway [GO:0032924]; adrenal gland development [GO:0030325]; anatomical structure morphogenesis [GO:0009653]; anterior/posterior pattern specification [GO:0009952]; aortic valve morphogenesis [GO:0003180]; cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; cell population ...
activin responsive factor complex [GO:0032444]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; heteromeric SMAD protein complex [GO:0071144]; homomeric SMAD protein complex [GO:0071142]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; SMAD protein complex [GO:0071141]; transcription regulator complex [G...
chromatin binding [GO:0003682]; co-SMAD binding [GO:0070410]; disordered domain specific binding [GO:0097718]; 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 activit...
PF03165;PF03166;
2.60.200.10;3.90.520.10;
Dwarfin/SMAD family
PTM: In response to TGF-beta, phosphorylated on the C-terminal SXS motif by TGF-beta and activin type 1 receptor kinases, phosphorylation declines progressively in a KMT5A-dependent manner. Phosphorylation in this motif is required for interaction with a number of proteins including SMURF2, SNON and SMAD4 in response t...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15796}. Nucleus {ECO:0000250|UniProtKB:Q15796}. Note=Cytoplasmic and nuclear in the absence of TGF-beta (By similarity). On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4 or with IPO7 (By similarity). On dephosphorylation by phosphatase PP...
null
null
null
null
null
FUNCTION: Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the S...
Rattus norvegicus (Rat)
O70437
SMAD4_RAT
MDNMSITNTPTSNDACLSIVHSLMCHRQGGESETFAKRAIESLVKKLKEKKDELDSLITAITTNGAHPSKCVTIQRTLDGRLQVAGRKGFPHVIYARLWRWPDLHKNELKHVKYCQYAFDLKCDSVCVNPYHYERVVSPGIDLSGLTLQSNAPPSMLVKDEYVHDFEGQPSLPTEGHSIQTIQHPPSNRASTETYSAPALLAPSESNATSTTNFPNIPVASTSQPASILAGSHSEGLLQIASGPQPGQQQNGFTAQPATYHHNSTTTWTGSRTAPYTPNLPHHQNGHLQHHPPMPPHPGHYWPVHNELAFQPPISNHPAP...
null
null
adrenal gland development [GO:0030325]; anatomical structure morphogenesis [GO:0009653]; anterior/posterior pattern specification [GO:0009952]; atrioventricular canal development [GO:0036302]; atrioventricular valve formation [GO:0003190]; axon guidance [GO:0007411]; BMP signaling pathway [GO:0030509]; brainstem develo...
activin responsive factor complex [GO:0032444]; centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heteromeric SMAD protein complex [GO:0071144]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator...
chromatin binding [GO:0003682]; collagen binding [GO:0005518]; 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]; fila...
PF03165;PF03166;
2.60.200.10;3.90.520.10;
Dwarfin/SMAD family
PTM: Phosphorylated by PDPK1. {ECO:0000250}.; PTM: Monoubiquitinated on Lys-519 by E3 ubiquitin-protein ligase TRIM33. Monoubiquitination hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade. Deubiquitination by USP9X restores its competence to me...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13485}. Nucleus {ECO:0000250|UniProtKB:Q13485}. Note=In the cytoplasm in the absence of ligand. Migration to the nucleus when complexed with R-SMAD. PDPK1 prevents its nuclear translocation. {ECO:0000250|UniProtKB:Q13485}.
null
null
null
null
null
FUNCTION: Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling. Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA a...
Rattus norvegicus (Rat)
O70439
STX7_MOUSE
MSYTPGIGGDSAQLAQRISSNIQKITQCSVEIQRTLNQLGTPQDSPELRQLLQQKQQYTNQLAKETDKYIKEFGSLPTTPSEQRQRKIQKDRLVAEFTTSLTNFQKAQRQAAEREKEFVARVRASSRVSGGFPEDSSKEKNLVSWESQTQPQVQVQDEEITEDDLRLIHERESSIRQLEADIMDINEIFKDLGMMIHEQGDMIDSIEANVESAEVHVQQANQQLSRAADYQRKSRKTLCIIIFILVVRIVIICLIVWGLKG
null
null
endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; vesicle docking [GO:0048278]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]
early endosome membrane [GO:0031901]; endomembrane system [GO:0012505]; endosome [GO:0005768]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; perinuclear region of cytoplasm [GO:0048471]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
protein-containing complex binding [GO:0044877]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]
PF05739;PF14523;
1.20.5.110;1.20.58.70;
Syntaxin family
null
SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O70441
SYN3_RAT
MNFLRRRLSDSSFVANLPNGYMPDLQRPESSSSSPASPATERRHPQPLAASFSSPGSSLFSSFSSAMKQTPQAPTGLMEPPTPVTPVVQRPRILLVIDDAHTDWSKYFHGKKVNGDIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKIVRSFKPDFILVRQHAYSMALAEDYRSLVIGLQYGGLPAVNSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMLTAPNFPVVIKLGHAHAGMGKIKVENQHDYQDITSVVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSA...
null
null
neurotransmitter secretion [GO:0007269]; synaptic vesicle clustering [GO:0097091]; synaptic vesicle cycle [GO:0099504]
extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
ATP binding [GO:0005524]
PF02078;PF02750;PF10581;
3.40.50.20;3.30.1490.20;3.30.470.20;
Synapsin family
PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Peripheral membrane protein localized to the cytoplasmic surface of synaptic vesicles.
null
null
null
null
null
FUNCTION: May be involved in the regulation of neurotransmitter release and synaptogenesis. Binds ATP with high affinity and ADP with a lower affinity. This is consistent with a catalytic role of the C-domain in which ADP would be dissociated by cellular ATP after bound ATP was hydrolyzed.
Rattus norvegicus (Rat)
O70443
GNAZ_MOUSE
MGCRQSSEEKEAARRSRRIDRHLRSESQRQRREIKLLLLGTSNSGKSTIVKQMKIIHSGGFNLDACKEYKPLIIYNAIDSLTRIIRALAALKIDFHNPDRAYDAVQLFALTGPAESKGEITPELLGVMRRLWADPGAQACFGRSSEYHLEDNAAYYLNDLERIAAPDYIPTVEDILRSRDMTTGIVENKFTFKELTFKMVDVGGQRSERKKWIHCFEGVTAIIFCVELSGYDLKLYEDNQTSRMAESLRLFDSICNNNWFINTSLILFLNKKDLLAEKIRRIPLSVCFPEYKGQNTYEEAAVYIQRQFEDLNRNKETKEI...
null
null
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; G protein-coupled receptor signaling pathway [GO:0007186]; G protein-coupled serotonin receptor signaling pathway [GO:0098664]; negative regulat...
cell body [GO:0044297]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; heterotrimeric G-protein complex [GO:0005834]; membrane [GO:0016020]; plasma membrane [GO:0005886]
adenylate cyclase inhibitor activity [GO:0010855]; G protein-coupled receptor binding [GO:0001664]; G protein-coupled serotonin receptor binding [GO:0031821]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]
PF00503;
1.10.400.10;3.40.50.300;
G-alpha family, G(i/o/t/z) subfamily
null
SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
null
null
null
null
null
FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Mus musculus (Mouse)
O70444
PIM3_RAT
MLLSKFGSLAHLCGPGGVDHLPVKILQPAKADKESFEKVYQVGAVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGSLGGMAVPLEVVLLRKVGAAGGARGVIRLLDWFERPDGFLLVLERPEPAQDLFDFITERGALDEPLARRFFAQVLAAVRHCHNCGVVHRDIKDENLLVDLRSGELKLIDFGSGAVLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLFFRRRVSPECQQLIEWCLSLRPSERPSLDQIAAHPWMLGTEGSVPENCDLRLCALDTDDGASTT...
2.7.11.1
null
apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cellular response to forskolin [GO:1904322]; negative regulation of apoptotic process [GO:0043066]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; protein phosphorylation [GO:0006468]; regulation of mitoti...
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, PIM subfamily
PTM: Ubiquitinated, leading to proteasomal degradation. {ECO:0000250}.; PTM: Phosphorylated. Interaction with PPP2CA promotes dephosphorylation (By similarity). Autophosphorylated (in vitro). {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; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Proto-oncogene with serine/threonine kinase activity that can prevent apoptosis and promote cell survival and protein translation. May contribute to tumorigenesis through: the delivery of survival signaling through phosphorylation of BAD which induces release of the anti-apoptotic protein Bcl-X(L), the regula...
Rattus norvegicus (Rat)
O70445
BARD1_MOUSE
MPRRPPRVCSGNQPAPVPAMEPATDGLWAHSRAALARLEKLLRCSRCANILKEPVCLGGCEHIFCSGCISDCVGSGCPVCYTPAWILDLKINRQLDSMIQLSSKLQNLLHDNKDSKDNTSRASLFGDAERKKNSIKMWFSPRSKKVRYVVTKVSVQTQPQKAKDDKAQEASMYEFVSATPPVAVPKSAKTASRTSAKKHPKKSVAKINREENLRPETKDSRFDSKEELKEEKVVSCSQIPVMERPRVNGEIDLLASGSVVEPECSGSLTEVSLPLAEHIVSPDTVSKNEETPEKKVCVKDLRSGGSNGNRKGCHRPTTST...
2.3.2.27
null
cellular response to ionizing radiation [GO:0071479]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA strand resection involved in replication fork processing [GO:0110025]; homologous recombination [GO:0035825]; mitotic G2/M transition checkpoint [GO:0044818]; negative regulation of apoptotic process [GO...
BRCA1-A complex [GO:0070531]; BRCA1-B complex [GO:0070532]; BRCA1-BARD1 complex [GO:0031436]; BRCA1-C complex [GO:0070533]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; nuclear speck [GO:0016607]; nuclear ubiquitin ligase complex [GO:0000152]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA binding [GO:0003723]; ubiquitin-protein transferase activity [GO:0004842]
PF12796;PF14835;
1.25.40.20;3.40.50.10190;3.30.40.10;
null
PTM: Processed during apoptosis. The homodimer is more susceptible to proteolytic cleavage than the BARD1/BRCA1 heterodimer. {ECO:0000250|UniProtKB:Q99728}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15077185}. Cytoplasm {ECO:0000269|PubMed:15077185}. Note=Can translocate to the cytoplasm. Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. {ECO:0000250|UniProtKB:Q99728}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q99728};
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase. The BRCA1-BARD1 heterodimer specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Plays a central role ...
Mus musculus (Mouse)
O70451
MOT2_MOUSE
MPSEPSAPLPQPLPPDGGWGWVVVCASFISIGFSYAFPKAVTVFFKDIQEIFNTTSSQIAWISSIMLAVMYAGGPISSVLVNNYGSRPVVIVGGLLCCIGMILASYSNSVIELYLTVGFIGGLGLAFNLQPALTIIGKYFYRRRPLANGCAMAGSPVFLSTLAPFNQYLFNNYGWKGSFLILGGIFLHSCVAGCLMRPVGPSPNTKKSKSKVGSRHDSTLKKASKVSTAQKVNRFLDFSLFMHRGFLIYLSGNVILFLGIFAPIIFLAQYAKHIGVDDYNSAFLLSVMAFIDMFARPSVGLIANTSLIRPRIQYLFSSAI...
null
null
lactate transmembrane transport [GO:0035873]; plasma membrane lactate transport [GO:0035879]; pyruvate transmembrane transport [GO:1901475]
basolateral plasma membrane [GO:0016323]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; nucleoplasm [GO:0005654]; parallel fiber to Purkinje cell synapse [GO:0098688]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; Schaffer coll...
identical protein binding [GO:0042802]; lactate transmembrane transporter activity [GO:0015129]; pyruvate transmembrane transporter activity [GO:0050833]; symporter activity [GO:0015293]
PF07690;
1.20.1250.20;
Major facilitator superfamily, Monocarboxylate porter (TC 2.A.1.13) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60669}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Cytoplasm {ECO:0000269|PubMed:21792931}. Basolateral cell membrane {ECO:0000250|UniProtKB:P53988}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60669}. Note=Requires the ancillary prote...
CATALYTIC ACTIVITY: Reaction=(S)-lactate(in) + H(+)(in) = (S)-lactate(out) + H(+)(out); Xref=Rhea:RHEA:29415, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651; Evidence={ECO:0000269|PubMed:21792931}; CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate(out) + H(+)(out) = 3-methyl-2-oxobutanoate(in) + H(+)(in); Xref=Rhea:RHEA:71783...
null
null
null
null
FUNCTION: Proton-coupled monocarboxylate symporter (PubMed:21792931). Catalyzes the rapid transport across the plasma membrane of monocarboxylates such as L-lactate, pyruvate and ketone bodies, acetoacetate, beta-hydroxybutyrate and acetate. Dimerization is functionally required and both subunits work cooperatively in ...
Mus musculus (Mouse)
O70456
1433S_MOUSE
MERASLIQKAKLAEQAERYEDMAAFMKSAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPEVKEYREKVETELRGVCDTVLGLLDSHLIKGAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWTADSAGEEGGEAPEEPQS
null
null
establishment of skin barrier [GO:0061436]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; keratinization [GO:0031424]; keratinocyte development [GO:0003334]; keratinocyte differentiation [GO:0030216]; keratinocyte proliferation [GO:0043616]; negative regulation of innate immune response ...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]
identical protein binding [GO:0042802]; phosphoprotein binding [GO:0051219]; phosphoserine residue binding [GO:0050815]; protein kinase binding [GO:0019901]; protein sequestering activity [GO:0140311]
PF00244;
1.20.190.20;
14-3-3 family
PTM: Ubiquitinated. Ubiquitination by RFFL induces proteasomal degradation and indirectly regulates p53/TP53 activation. {ECO:0000250|UniProtKB:P31947}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16710422}. Nucleus {ECO:0000269|PubMed:16710422}. Secreted {ECO:0000250|UniProtKB:P31947}. Note=May be secreted by a non-classical secretory pathway. {ECO:0000250|UniProtKB:P31947}.
null
null
null
null
null
FUNCTION: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (By similarity). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (By similarity). Binding generally results in the modulation of the acti...
Mus musculus (Mouse)
O70458
OSMR_MOUSE
MAFSVVLHPAFLLAVLSLRASRSEVLEEPLPLTPEIHKVSFQLKLQEVNLEWTVPALTHEELNMIFQIEISRLNISNTIWVENYSTTVKREEAVRWNWTSDIPLECVKHFIRIRALVDDTKSLPQSSWGNWSSWKEVNAKVSVEPDKSLIFPKDKVLEEGSNVTICLMYGQNVYNVSCKLQDEPIHGEQLDSHVSLLKLNNVVFLSDTGTNINCQATKGPKRIFGTVLFVSKVLEEPKNVSCETRDFKTLDCSWEPGVDTTLTWRKQRFQNYTLCESFSKRCEVSNYRNSYTWQITEGSQEMYNFTLTAENQLRKRSVNI...
null
null
cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; positive regulation of cell population proliferation [GO:0008284]
external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
ciliary neurotrophic factor receptor binding [GO:0005127]; cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; oncostatin-M receptor activity [GO:0004924]
PF00041;PF21177;PF17971;
2.60.40.10;
Type I cytokine receptor family, Type 2 subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Associates with IL31RA to form the IL31 receptor (PubMed:9920829). Binds IL31 to activate STAT3 and possibly STAT1 and STAT5 (By similarity). Capable of transducing OSM-specific signaling events (By similarity). {ECO:0000250|UniProtKB:Q99650, ECO:0000269|PubMed:9920829}.
Mus musculus (Mouse)
O70460
CCL19_MOUSE
MAPRVTPLLAFSLLVLWTFPAPTLGGANDAEDCCLSVTQRPIPGNIVKAFRYLLNEDGCRVPAVVFTTLRGYQLCAPPDQPWVDRIIRRLKKSSAKNKGNSTRRSPVS
null
null
cell maturation [GO:0048469]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; dendritic cell chemotaxis [GO:0002407]; establishment of T cell polarity [GO:00...
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]
CCR chemokine receptor binding [GO:0048020]; CCR7 chemokine receptor binding [GO:0031732]; chemokine activity [GO:0008009]; chemokine receptor binding [GO:0042379]
PF00048;
2.40.50.40;
Intercrine beta (chemokine CC) family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Strongly chemotactic for naive (L-selectinhi) CD4 T-cells and for CD8 T-cells and weakly attractive for resting B-cells and memory (L-selectinlo) CD4 T-cells. May play a role in promoting encounters between recirculating T-cells and dendritic cells and in the migration of activated B-cells into the T-zone of ...
Mus musculus (Mouse)
O70467
ANM3_RAT
MCSLAAGNGQGAELGPEPLELSDSGDDAGWEDEDADAEPAQGRQHTPCLFCDRLFRSAEETFSHCKLEHQFNIDGMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWDKDEYLKPVLEDDLLLQFDVEDLYEPVSAPFTYPNGLSENTSAVEKLKLMEARALSAEAALARAREDLQKMKQFAQDFVMNVDVRTCSSTTTIADLQEDEDGVYFSSYGHYGIHEEMLKDKVRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVIAVDQSEILYQAMDIIRLNKLEDTIVLIKGKIEEVSLPVEKV...
2.1.1.319
null
dendritic spine morphogenesis [GO:0060997]; methylation [GO:0032259]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of retinoic acid biosynthetic process [GO:1900053]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; modified amino acid binding [GO:0072341]; protein-arginine N-methyltransferase activity [GO:0016274]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; protein-arginine omega-N monomethyltransferase activity [GO:0035241]...
PF21137;PF21336;PF06325;
2.70.160.11;3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, Protein arginine N-methyltransferase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9642256}.
CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + S-adenosyl-L-methionine = H(+) + N(omega)-methyl-L-arginyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48100, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11990, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65280; Evidence={...
null
null
null
null
FUNCTION: Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (PubMed:10899106, PubMed:15334060, PubMed:9642256). May regulate retinoi...
Rattus norvegicus (Rat)
O70468
MYPC3_MOUSE
MPEPGKKPVSAFNKKPRSAEVTAGSAAVFEAETERSGVMVRWQRDGSDITANDKYGLAAEGKRHTLTVRDASPDDQGSYAVIAGSSKVKFDLKVTEPAPPEKAESEVAPGAPEEVPAPATELEESVSSPEGSVSVTQDGSAAEHQGAPDDPIGLFLMRPQDGEVTVGGSIVFSARVAGASLLKPPVVKWFKGKWVDLSSKVGQHLQLHDSYDRASKVYLFELHITDAQTTSAGGYRCEVSTKDKFDSCNFNLTVHEAIGSGDLDLRSAFRRTSLAGAGRRTSDSHEDAGTPDFSSLLKKRDSFRRDSKLEAPAEEDVWEI...
null
null
cardiac muscle contraction [GO:0060048]; cell adhesion [GO:0007155]; heart morphogenesis [GO:0003007]; muscle contraction [GO:0006936]; myosin filament assembly [GO:0031034]; regulation of heart contraction [GO:0008016]; regulation of heart rate [GO:0002027]; sarcomere organization [GO:0045214]; ventricular cardiac mus...
A band [GO:0031672]; cytoskeleton [GO:0005856]; myofibril [GO:0030016]; sarcomere [GO:0030017]; striated muscle myosin thick filament [GO:0005863]
actin binding [GO:0003779]; metal ion binding [GO:0046872]; myosin heavy chain binding [GO:0032036]; structural constituent of cytoskeleton [GO:0005200]
PF00041;PF07679;PF18362;
2.60.40.10;
Immunoglobulin superfamily, MyBP family
PTM: Substrate for phosphorylation by PKA and PKC. Reversible phosphorylation appears to modulate contraction (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q14896}.
null
null
null
null
null
null
FUNCTION: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
Mus musculus (Mouse)
O70469
DOK2_MOUSE
MVRMEEPAVKQGFLHLQQQQTFGKKWRRFAAVLYGESGCALARLELQDVPEKTRRGEATRKVVRLSDCLRVAEVGSEASSPRDTSAFILETKERLYLLAAPSAERSDWIQAICLLAFPGQRKGSPGLEEKSGSPCMEENELYSSSTTGLCKEYMVTIRPTEASERCRLRGSYTLRTGVSALELWGGPEPGTQLYDWPYRFLRRFGRDKATFSFEAGRRCLSGEGNFEFETRHGNEIFQALEKVIAVQKNATPSGPPSLPATGPMMPTVLPRPESPYSRPHDSLPSPSPGTLVPGMRPGAPEGEYAVPFDTVAHSLRKSFR...
null
null
negative regulation of MAPK cascade [GO:0043409]; positive regulation of MAPK cascade [GO:0043410]; Ras protein signal transduction [GO:0007265]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
cytoplasm [GO:0005737]
transmembrane receptor protein tyrosine kinase adaptor activity [GO:0005068]
PF02174;PF00169;
2.30.29.30;
DOK family, Type A subfamily
PTM: On immunoreceptor stimulation, phosphorylated on C-terminal tyrosine residues. Phosphorylation on Tyr-351 is required for binding to the SH2 domain of NCK. Phosphorylation on both Tyr-276 and Tyr-304 is required for interaction with RASGAP. Phosphorylated on tyrosine residues by TEK/TIE2. {ECO:0000269|PubMed:10508...
null
null
null
null
null
null
FUNCTION: DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK2 may modulate the cellular proliferation induced by IL-4, as well as IL-2 and IL-3. May be involved in modulating Bcr-Abl signaling. Attenuates EGF-...
Mus musculus (Mouse)
O70473
AK1A1_CRIGR
MASCVLLHTGQKMPLIGLGTWKSNPGQVKAAIKYALSVGYRHIDCAAVYGNEIEIGEALKENVGPGKAVPREELFVTSKLWNTKHHPEDVEAALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNDDGTIRYDSTHYKETWKALEALVAKGLVKALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRHPDEPVLLEEPVVLALAEKHGRSPAQILLRWQVQRKVVCIPKSITPSRILQNIQVFDFTFSPEEMKQLDALNKHWRYIVPMITVDGKSVPRDAGHPLYPF...
1.1.1.19; 1.1.1.2; 1.1.1.20; 1.1.1.372; 1.1.1.54; 1.6.-.-
null
aldehyde catabolic process [GO:0046185]; cellular detoxification of aldehyde [GO:0110095]; D-glucuronate catabolic process [GO:0042840]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; glucuronate catabolic process to xylulose 5-phosphate [GO:0019640]; L-ascorbic acid biosynthet...
apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; synapse [GO:0045202]
alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; glucuronolactone reductase activity [GO:0047941]; glycerol dehydrogenase [NADP+] activity [GO:0047956]; L-glucuronate reductase activity [GO:0047939]; methylglyoxal reductase (NADPH-dependent, acetol producing) [GO:...
PF00248;
3.20.20.100;
Aldo/keto reductase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JII6}. Apical cell membrane {ECO:0000250|UniProtKB:Q9JII6}.
CATALYTIC ACTIVITY: Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2; Evidence={ECO:0000250|UniProtKB:P14550}; CATALYTIC ACTIVITY: Reaction=L-gulonate + NADP(+) = aldehydo-D-...
null
null
null
null
FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged sub...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O70475
UGDH_MOUSE
MVEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNEARINAWNSPTLPIYEPGLKEVVESCRGKNLFFSTNIDDAIREADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNSNGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLIGGDETPEGQKAVRALCAVYEHWVPKEKILTTNTWSSELSKLAANAFLAQRISSINSISALCEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYWQQVIDMNDYQRRRFASRIID...
1.1.1.22
null
chondroitin sulfate biosynthetic process [GO:0030206]; gastrulation with mouth forming second [GO:0001702]; glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; neuron development [GO:0048666]; protein hexamerization [GO:0034214]; UDP-glucuronate biosynthe...
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
identical protein binding [GO:0042802]; NAD binding [GO:0051287]; UDP-glucose 6-dehydrogenase activity [GO:0003979]
PF00984;PF03720;PF03721;
1.20.5.100;3.40.50.720;
UDP-glucose/GDP-mannose dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate; Xref=Rhea:RHEA:23596, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58885; EC=1.1.1.22; Evidence={ECO:0000269|PubMed:9737970};
null
PATHWAY: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1. {ECO:0000269|PubMed:9737970}.
null
null
FUNCTION: Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:9737970). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (PubMed:14505572). Required for ...
Mus musculus (Mouse)
O70477
PKNX1_MOUSE
MMATQTLSIDSYQDGQQMQVVTELKTEQDPNCSDPDAEGVSPPPIESQTPMDADKQAIYRHPLFPLLALLFEKCEQSTQGSEGTTSASFDVDIENFVRKQEKDGKPFFCEDPETDNLMVKAIQVLRIHLLELEKVNELCKDFCSRYIACLKTKMNSETLLSGEPGSPYSPVQSQQIQSAITGTLSPQGIVVPASALQQGNVTMATVAGGTVYQPVTVVTPQGQVVTQALSPGTIRIQNSQLQLQLNQDLSILHQEDGSSKNKRGVLPKHATNVMRSWLFQHIGHPYPTEDEKKQIAAQTNLTLLQVNNWFINARRRILQP...
null
null
angiogenesis [GO:0001525]; camera-type eye development [GO:0043010]; erythrocyte differentiation [GO:0030218]; hemopoiesis [GO:0030097]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase ...
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
PF05920;PF16493;
1.10.10.60;
TALE/MEIS homeobox family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Activates transcription in the presence of PBX1A and HOXA1. {ECO:0000269|PubMed:29465778}.; FUNCTION: (Microbial infection) In complex with PBX1, binds to the 5'-TGATTGAC-3' consensus sequence in the U5 region of Moloney murine leukemia virus and promotes viral transcription. {ECO:0000269|PubMed:12529389}.
Mus musculus (Mouse)
O70480
VAMP4_MOUSE
MPPKFKRHLNDDDVTGSVKSERRNLLEDDSDEEEDFFLRGPSGPRFGPRNDKIKHVQNQVDEVIDVMQENITKVIERGERLDELQDKSESLSDNATAFSNRSKQLRRQMWWRGCKIKAIMALAAAILLLMIIILIVVKFRT
null
null
cellular response to type II interferon [GO:0071346]; Golgi ribbon formation [GO:0090161]; Golgi to plasma membrane protein transport [GO:0043001]; regulation of Golgi to plasma membrane protein transport [GO:0042996]; regulation of synaptic vesicle endocytosis [GO:1900242]; SNARE complex assembly [GO:0035493]; synapti...
Golgi apparatus [GO:0005794]; phagocytic vesicle [GO:0045335]; presynaptic endosome membrane [GO:0098954]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802]
null
PF00957;
1.20.5.110;
Synaptobrevin family
PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum neurotoxin type X (BoNT/X) which hydrolyzes the 87-Arg-|-Ser-88 bond and probably inhibits neurotransmitter release (PubMed:28770820). It remains unknown whether BoNT/X is ever produced, or what organisms it targets. {ECO:0000269|PubMed:28770820}.
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with trans Golgi network (TGN) and newly formed immature secretory granules (ISG). Not found on the mature secretory organelles (By similarity). {ECO:0000250}.
null
null
null
null
null
FUNCTION: Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O70481
UBR1_MOUSE
MADEEMDGAERMDVSPEPPLAPQRPASWWDQQVDFYTAFLHHLAQLVPEIYFAEMDPDLEKQEESVQMSILTPLEWYLFGEDPDICLEKLKHSGAFQLCGKVFKSGETTYSCRDCAIDPTCVLCMDCFQSSVHKNHRYKMHTSTGGGFCDCGDTEAWKTGPFCVDHEPGRAGTTKESLHCPLNEEVIAQARRIFPSVIKYIVEMTIWEEEKELPPELQIREKNERYYCVLFNDEHHSYDHVIYSLQRALDCELAEAQLHTTAIDKEGRRAVKAGVYATCQEAKEDIKSHSENVSQHPLHVEVLHSVVMAHQKFALRLGSW...
2.3.2.27
null
cellular response to leucine [GO:0071233]; negative regulation of TOR signaling [GO:0032007]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]; ubiquitin-dependent protein catabolic process via the N-end rule pathway [GO:0071596]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; proteasome complex [GO:0000502]; ubiquitin ligase complex [GO:0000151]
leucine binding [GO:0070728]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
PF02617;PF18995;PF02207;
2.10.110.30;3.30.1390.10;
UBR1 family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leu...
Mus musculus (Mouse)
O70490
ACSM2_RAT
MHWLWKIPRLCTFWGTEMFHRTFHMNIKKLMPIQWGHQEVPAKFNFASDVIDHWASLEKAGKRSPGPALWWMNGSGEELKWNFRELSEISKQTANVLTGACGLQRGDRVAVVLPRVPEWWLVTLGCMRSGLVFMPGTTQMKSTDILYRLQSSKARAIVAGDEVVQEVDAVAPDCSFLKIKLLVSEKNREGWLNFKALLKDASPIHQCVETVSQESAAIYFTSGTSGPPKMAEHSHCSLGLKAKMDAGWTGLGPSDTMWTISDTGWILNILGSFLEPWVLGTCIFVHLLPKFDPQTVLKVLSSYPINTLLGAPLIYRMLLQ...
6.2.1.2; 6.2.1.25
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q68CK6}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q68CK6};
acyl-CoA metabolic process [GO:0006637]; fatty acid biosynthetic process [GO:0006633]; medium-chain fatty-acyl-CoA metabolic process [GO:0036112]
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
ATP binding [GO:0005524]; benzoate-CoA ligase activity [GO:0018858]; butyrate-CoA ligase activity [GO:0047760]; decanoate-CoA ligase activity [GO:0102391]; fatty acid ligase activity [GO:0015645]; fatty-acyl-CoA synthase activity [GO:0004321]; metal ion binding [GO:0046872]
PF00501;PF13193;
3.30.300.30;3.40.50.12780;
ATP-dependent AMP-binding enzyme family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q68CK6}.
CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2; Evidence={ECO:0000250|UniProtKB:Q68CK6}; Physiologi...
null
null
null
null
FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an acyl-CoA, the first step in fatty acid metabolism (By similarity). Capable of activating medium-chain fatty acids (e.g. butyric (C4) to decanoic (C10) acids), and certain carboxylate-containing xenobiotics, e.g. benzoate (By similarity). {ECO:000025...
Rattus norvegicus (Rat)
O70491
STRA6_MOUSE
MESQASENGSQTSSGVTDDYSSWYIEEPLGAEEVQPEGVIPLCQLTAPPALLHACLASLSFLVLLLLALLVRRRRLWPRCGHRGLGLPSPVDFLAGDLSWTVPAAVFVVLFSNLCLLLPDENPLPFLNLTAASSPDGEMETSRGPWKLLALLYYPALYYPLAACASAGHQAAFLLGTVLSWAHFGVQVWQKAECPQDPKIYKHYSLLASLPLLLGLGFLSLWYPVQLVQSLRHRTGAGSQGLQTSYSEKYLRTLLCPKKLDSCSHPASKRSLLSRAWAFSHHSIYTPQPGFRLPLKLVISATLTGTATYQVALLLLVSVV...
null
null
camera-type eye development [GO:0043010]; establishment of localization in cell [GO:0051649]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; retinol transport [GO:0034633]; vitamin A import into cell [GO:0071939]
plasma membrane [GO:0005886]
retinal binding [GO:0016918]; retinol binding [GO:0019841]; retinol transmembrane transporter activity [GO:0034632]; signaling receptor activity [GO:0038023]
PF14752;
null
null
PTM: Phosphorylated on tyrosine residues in response to RBP4 binding (PubMed:21368206). Phosphorylation requires the presence of LRAT, suggesting it may be triggered by the uptake of retinol that is then metabolized within the cell to retinoids that function as signaling molecules (By similarity). {ECO:0000250|UniProtK...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9203140}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0V8E7}. Note=In the retinal pigment epithelium localizes to the basolateral membrane (PubMed:22467576, PubMed:24852372). Plasma membrane of the basal pole of Sertoli cells, absent in plasma membrane of ...
null
null
null
null
null
FUNCTION: Functions as a retinol transporter (PubMed:23839944, PubMed:24852372). Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1. Retinol uptake is enhanced b...
Mus musculus (Mouse)
O70492
SNX3_MOUSE
MAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKTNLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRHVPFRGDDGIFDDNFIEERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA
null
null
endocytic recycling [GO:0032456]; heme biosynthetic process [GO:0006783]; hemoglobin biosynthetic process [GO:0042541]; late endosome to Golgi transport [GO:0034499]; negative regulation of phagocytosis [GO:0050765]; positive regulation of neuron projection development [GO:0010976]; protein to membrane docking [GO:0022...
clathrin-coated vesicle [GO:0030136]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; early phagosome [GO:0032009]; endosome membrane [GO:0010008]; retromer complex [GO:0030904]
phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; retromer complex binding [GO:1905394]
PF00787;
3.30.1520.10;
Sorting nexin family
PTM: Ubiquitinated, leading to its proteasomal degradation. Deubiquitinated by USP10. {ECO:0000269|PubMed:18632802}.
SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:23416069}. Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:O60493}. Note=Colocalizes to clathrin-coated endosomal vesicles morphologically distinct from retromer-decorated non-branched endosomal tubule structures. Colocalizes with EEA1 on nascent phagosomes...
null
null
null
null
null
FUNCTION: Phosphoinositide-binding protein required for multivesicular body formation. Specifically binds phosphatidylinositol 3-phosphate (PtdIns(P3)). Can also bind phosphatidylinositol 4-phosphate (PtdIns(P4)), phosphatidylinositol 5-phosphate (PtdIns(P5)) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2) (Pu...
Mus musculus (Mouse)