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
E9Q3T6
PRD14_MOUSE
MALPPSGETQSQDKANYLPQSNPHHLTTYYAHAPGYSHFRNLATTEEEFQPWKLAAAVLESQAMAPLDAFRMTAPLLNPGLAVQSEPLYNLPWYKLSPWNRIPQFTPEVPRFLDSTEHRSSGSSNQNLVLGGGGGQISGQRWEAENLLLPSPVIASLLPDGIKSSQSISVPQTLNQEGKLPFCGFNFTEEELSFVLYGAIASPEHPTDLQHAISGILVPTESSGSNHLHKTLDKDSLQLPEGLCLMQTSFGDVPHFGVFCSDFIAKGVRFGPFRGRVVNASEVKAHRDNSRMWEIFEDGHLSHFIDGKGSGNWMSYVNCA...
2.1.1.-
null
cell fate specification [GO:0001708]; cell morphogenesis [GO:0000902]; embryo implantation [GO:0007566]; epigenetic regulation of gene expression [GO:0040029]; fertilization [GO:0009566]; fibroblast growth factor receptor signaling pathway [GO:0008543]; germ cell development [GO:0007281]; germ-line stem cell population...
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin DNA binding [GO:0031490]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; RNA binding [GO:0003723]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
PF21549;PF00096;
3.30.160.60;2.170.270.10;
Class V-like SAM-binding methyltransferase superfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Transcription factor that has both positive and negative roles on transcription (By similarity). Plays a role in cellular pluripotency. Essential for germ cell development at 2 levels: the reacquisition of potential pluripotency, including SOX2 up-regulation, and successful epigenetic reprogramming, character...
Mus musculus (Mouse)
E9Q401
RYR2_MOUSE
MADAGEGEDEIQFLRTDDEVVLQCTATIHKEQQKLCLAAEGFGNRLCFLESTSNSKNVPPDLSICTFVLEQSLSVRALQEMLANTVEKSEGQVDVEKWKFMMKTAQGGGHRTLLYGHAILLRHSYSGMYLCCLSTSRSSTDKLAFDVGLQEDTTGEACWWTIHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSYGNSSWHVDAAFQQTLWSVAPISSGSEAAQGYLIGGDVLRLLHGHMDECLTVPSGEHGEEQRRTVHYEGGAVSVHARSLWRLETLRVAWSGSHIRWGQPFRLRHVTTGKYLSLMEDKNLLLMDKE...
null
null
calcium ion transmembrane import into cytosol [GO:0097553]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; calcium ion transport into cytosol [GO:0060402]; calcium-mediated signaling [GO:0019722]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cardiac ...
A band [GO:0031672]; calcium channel complex [GO:0034704]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; protein-containing complex [GO:0032991]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; sarcoplasmic reticulum [GO:0016529]; sarcopl...
calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; intracellularly gated calcium channel activity [GO:0015278]; organic cyclic compound bindi...
PF13499;PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622;
1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;1.10.238.10;1.25.10.30;
Ryanodine receptor (TC 1.A.3.1) family, RYR2 subfamily
PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2807 and Ser-2813 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca(2+) levels. {ECO:0000269|PubMed:17693412, ECO:0000269|PubMed:2043105...
SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000305|PubMed:10473538}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10473538, ECO:0000269|PubMed:33536282};
null
null
null
null
FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered ...
Mus musculus (Mouse)
E9Q414
APOB_MOUSE
MGPRKPALRTPLLLLFLLLFLDTSVWAQDEVLENLSFSCPKDATRFKHLRKYVYNYEAESSSGVQGTADSRSATKINCKVELEVPQICGFIMRTNQCTLKEVYGFNPEGKALMKKTKNSEEFAAAMSRYELKLAIPEGKQIVLYPDKDEPKYILNIKRGIISALLVPPETEEDQQELFLDTVYGNCSTQVTVNSRKGTVPTEMSTERNLQQCDGFQPISTSVSPLALIKGLVHPLSTLISSSQTCQYTLDPKRKHVSEAVCDEQHLFLPFSYKNKYGIMTRVTQKLSLEDTPKINSRFFSEGTNRMGLAFESTKSTSSPK...
null
null
artery morphogenesis [GO:0048844]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; establishment of localization in cell [GO:0051649]; fertilization [GO:0009566]; flagellated sperm motility [GO:0030317]; in utero embr...
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; lipid droplet [GO:0005811]; low-density lip...
cholesterol transfer activity [GO:0120020]; heparin binding [GO:0008201]; lipase binding [GO:0035473]; low-density lipoprotein particle receptor binding [GO:0050750]; phospholipid binding [GO:0005543]
PF12491;PF06448;PF09172;PF01347;
2.20.80.10;1.25.10.20;
null
PTM: Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}. Secreted {ECO:0000250|UniProtKB:P04114}. Lipid droplet {ECO:0000250|UniProtKB:P04114}.
null
null
null
null
null
FUNCTION: Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor.
Mus musculus (Mouse)
E9Q4F7
ANR11_MOUSE
MPKGGCSKTPQQEDFALSNDMVEKQTGKKDKDKVSLTKTPKLDRSDGGKEVRERATKRKLPFTVGANGEQKDSDTEKQGPERKRIKKEPVARKSGLLFGMGLSGIRAGYPLSERQQVALLMQMTAEESANSPVDTTPKHPSQSTVCQKGTPNSASKTKDKVNKRNERGETRLHRAAIRGDARRIKELISEGADVNVKDFAGWTALHEACNRGYYDIAKQLLAAGAEVNTKGLDDDTPLHDAANNGHYKVVKLLLRYGGNPQQSNRKGETPLKVANSPTMVNLLLGKGTYTSSEESSTESSEEEDAPSFAPSSSVDGNNTD...
null
null
anatomical structure morphogenesis [GO:0009653]; bone development [GO:0060348]; face morphogenesis [GO:0060325]; head morphogenesis [GO:0060323]; in utero embryonic development [GO:0001701]; multicellular organism growth [GO:0035264]; odontogenesis of dentin-containing tooth [GO:0042475]; skeletal system morphogenesis ...
nucleus [GO:0005634]
null
PF12796;
1.25.40.20;
null
PTM: Subject to proteasomal degradation which is probably essential to regulate its activity. {ECO:0000269|PubMed:25413698}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25413698}. Note=Localizes to chromatin during prometaphase (By similarity). {ECO:0000250|UniProtKB:Q6UB99}.
null
null
null
null
null
FUNCTION: Chromatin regulator which modulates histone acetylation and gene expression in neural precursor cells (PubMed:25556659). May recruit histone deacetylases (HDACs) to the p160 coactivators/nuclear receptor complex to inhibit ligand-dependent transactivation (By similarity). Has a role in proliferation and devel...
Mus musculus (Mouse)
E9Q4J9
AGRF2_MOUSE
MIPAHWLYCLMLLLPIESCRILCQASSKSKEKVTSRPHDVCDGVCNNNGTPCFQSCPPDSEGNMKFACKAKKWHKVTETCHTLNTHSIFEEDKELYSVQSSDSTIRTHMFHRELKTIMDTLMEKCPKDLSCVIKGIERSPRMPGNIAVVVQLLHNISTTLTKDVNEEKMQSYSAMANHILNSKSISNWTFIQDRNSSCVLLQSIHSFASKLFMKEHLINISHVFIHTLGTVVSRGSLGKNFTFSMRINETSDKVTGRLLLSPEELQKVPSAFQVISIAFPTLGAILEASLLENVTVNGLVLSVILPEELKNISLIFEKIR...
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]
membrane [GO:0016020]
G protein-coupled receptor activity [GO:0004930]
PF00002;PF01825;
2.60.220.50;1.20.1070.10;
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Orphan receptor.
Mus musculus (Mouse)
E9Q4N7
ARI1B_MOUSE
MAARAAAAARARAGSGERRAPSGPRPAPGARDLETGARGAVAAPGPILGGGDGGLNNVHHHPLHPRHDLNMAHSASAAAAASSNSAQSGRSEAALKEGGSAAALSSSAAVAASSSSAGPGSTMETGLLPNHKLKAVGEAPAAPPHQQHHHHHAHHHHHHHAHHLHHLHHHHALQQQLNQFQQPQPPQPQQQQPPPPPQQQHPTANNSLGGAGGGAPQPGPDMEQPQHGGAKDSVAGNQADPQGQPLLSKPGDEDDAPPKMGEPAGSRYEHPGLGAQQQPAPVAVPGGGGGPAAVSEFNNYYGSAAPASGGPGGRAGPCFD...
null
null
chromatin remodeling [GO:0006338]; dendritic cell dendrite assembly [GO:0097026]; dendritic spine development [GO:0060996]; neuron-neuron synaptic transmission [GO:0007270]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]
brahma complex [GO:0035060]; nBAF complex [GO:0071565]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]; synapse [GO:0045202]
DNA binding [GO:0003677]; nucleosome binding [GO:0031491]
PF01388;PF12031;
1.10.150.60;1.25.10.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NFD5, ECO:0000255|PROSITE-ProRule:PRU00355}.
null
null
null
null
null
FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome ...
Mus musculus (Mouse)
E9Q4S1
PDE8B_MOUSE
MGCAPSIHVSQSGVIYCRDSDESNSPRQTSSVSQGPTAPLHGLFVQTDAADAMPPSRAAGPPGAVRVRRSRAELGSGSSTGSSGPATTTCRGRRRHCCSSAEAETQTSYTSVKVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQSRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKE...
3.1.4.53
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250};
behavioral fear response [GO:0001662]; cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; negative regulation of insulin secretion [GO:0046676]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of steroid hormone biosynt...
cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872]
PF13426;PF08629;PF00233;
1.10.1300.10;3.30.450.20;
Cyclic nucleotide phosphodiesterase family, PDE8 subfamily
null
null
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53;
null
PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
null
null
FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
E9Q4Z2
ACACB_MOUSE
MVLLLFLTCLVFSCLTFSWLKIWGKMTDSKPLTNSKVEANLLSSEESLSASELSGEQLQEHGDHSCLSYRGPRDASQQRNSLPSSCQRPPRNPLSSNDTWPSPELQTNWTAAPGPEVPDANGLSFPARPPSQRTVSPSREDRKQAHIKRQLMTSFILGSLDDNSSDEDPSAGSFQNSSRKSSRASLGTLSQEAALNTSDPESHAPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGNRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADQYVPVPGGPNNNNYA...
6.4.1.2
COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250|UniProtKB:O00763}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|P...
acetyl-CoA metabolic process [GO:0006084]; energy homeostasis [GO:0097009]; fatty acid biosynthetic process [GO:0006633]; fatty acid oxidation [GO:0019395]; glucose import [GO:0046323]; intracellular aspartate homeostasis [GO:0090459]; intracellular glutamate homeostasis [GO:0090461]; lactic acid secretion [GO:0046722]...
mitochondrial fatty acid beta-oxidation multienzyme complex [GO:0016507]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin binding [GO:0009374]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]
PF08326;PF21385;PF02785;PF00289;PF00364;PF01039;PF02786;
2.40.50.100;3.40.50.20;3.30.1490.20;3.30.470.20;2.40.460.10;3.90.1770.10;
null
PTM: The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity. {ECO:0000250|UniProtKB:O00763}.; PTM: Phosphorylated by AMPK at Ser-212 inactivates the enzyme (PubMed:24913514). Required for the maintenance of skeletal muscle lipid and glucose homeostas...
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677481}.
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000250|UniProtKB:O00763}; Physi...
null
PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:O00763}.
null
null
FUNCTION: Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (By similarity). Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the tra...
Mus musculus (Mouse)
E9Q555
RN213_MOUSE
MECPQCGHVSSEKAPKFCSECGQKLPSAATVQGDLKNDNTLVVSSTPEGKTEQGAVLREEEVLLSSTDPGKELEKPEESDSNASWTTQMSKKEKRRRKRQGTISSSEAPSSGLWSLDMPPSPGSHNSALPQNQAQQGGAASQPGHPLDTENMPMEDGFVHTEGSGSPLQGQAAERTDAQSNLAPSDLAEVKDLNTSKPSVDKGLPLDGGPALSAFKGHPKMTDASQKAPLPESKGETSGQEKKVPPIDAAASPVKTAGKETGEDVRKPKPSPVSPVASKHGDQEAELKGKLATPVRKSNEGGNTQPEDQRKPGEGRNFAA...
2.3.2.-; 2.3.2.27; 3.6.4.-
null
angiogenesis [GO:0001525]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; lipid droplet formation [GO:0140042]; lipid ubiquitination [GO:0120323]; negative regulation of non-canonical Wnt signaling pathway [GO:2000051]; protein autoubiquitination [GO:0051865]; protein K63-linked ubiquit...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; nucleolus [GO:0005730]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
PF00097;PF20173;
3.40.50.300;3.30.40.10;
AAA ATPase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}.
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:Q63HN8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) ...
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}.
null
null
FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:32573437). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacter...
Mus musculus (Mouse)
E9Q557
DESP_MOUSE
MSCNGGSHPRINTLGRMTRAESGPDLRYEMTYSGGGGGGGGGGGGGTSRTFYSHSRRCTVNDQNSDGYCQTGTMSRHQNQNTIQEMLQNCSDCLMRAELIAQPELKFGEGMQLAWNRELDEYFTQANDQMEIIDGLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISVPRVRRASSKGAGGYTCQSGSGWDEFTKRLTGECLGWMRQQREEMDLMAWGVDAGSVEQHINSHRSIHNTIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSDKNTNIAQK...
null
null
adherens junction organization [GO:0034332]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell-cell adhesion [GO:0098609]; desmosome organization [GO:0002934]; epithelial cell-cell adhesion [GO:0090136]; intermediate filament cytoskeleton organization [GO:0045104]; intermedi...
adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; fascia adherens [GO:0005916]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886]
protein kinase C binding [GO:0005080]; scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198]
PF00681;PF17902;PF18373;PF21019;
1.20.58.1060;1.20.58.60;3.30.160.780;3.90.1290.10;2.30.30.40;
Plakin or cytolinker family
null
SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000269|PubMed:15479741, ECO:0000269|PubMed:22515648}. Cell membrane {ECO:0000269|PubMed:21285247, ECO:0000269|PubMed:22515648, ECO:0000269|PubMed:26403541}. Note=Localizes at the intercalated disk in cardiomyocytes. {ECO:0000269|PubMed:15479741, ECO:0000269|PubMed:26...
null
null
null
null
null
FUNCTION: Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250|UniProtKB:F1LMV6}.
Mus musculus (Mouse)
E9Q5C9
NOLC1_MOUSE
MADTGLRRVVPSDLYPLVLRFLRDSQLSEVASKFAKATGATQQDANASSLLDIYSFWLNRSTKAPKVKLQSNGPVTKKAKKETSSSDSSEDSSEDEDKKAQGLPTQKAAAQVKRASVPQHAGKAAAKASESSSSEESSEEEEEDKKKKPVQQKAAKPQAKAVRPPAKKAESSESDSDSDSDSSSEEETPQTQKPKAAVAAKAQTKAEAKPGTPAKAQPKVANGKAAASSSSSSSSDDSEEEKKAAAPPKKTVPKKQVVAKAPVKVAAAPTQKSSSSEDSSSEEEEGQRQPMKKKAGPYSSVPPPSVPLPKKSPGTQAPKK...
null
null
box H/ACA RNA metabolic process [GO:0033979]; neural crest cell development [GO:0014032]; neural crest formation [GO:0014029]; nucleolus organization [GO:0007000]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of protein im...
box C/D RNP complex [GO:0031428]; box H/ACA snoRNP complex [GO:0031429]; Cajal body [GO:0015030]; cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small nuclear ribonucleoprotein complex [GO:0030532]
box C/D RNA binding [GO:0034512]; box C/D snoRNP complex binding [GO:0062064]; box H/ACA snoRNA binding [GO:0034513]; box H/ACA snoRNP complex binding [GO:0062065]; nuclear localization sequence binding [GO:0008139]; protein domain specific binding [GO:0019904]; protein heterodimerization activity [GO:0046982]; protein...
PF05022;
null
NOLC1 family
PTM: Undergoes rapid and massive phosphorylation/dephosphorylation cycles on CK2 and PKC sites. NOLC1 is one of the mostly phosphorylated proteins in the cell. {ECO:0000250|UniProtKB:Q14978}.; PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-IP7) (PubMed:15604408). Serine pyrophosphorylation is achie...
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q14978}. Cytoplasm {ECO:0000250|UniProtKB:Q14978}. Note=Shuttles between the nucleolus and the cytoplasm. At telophase it begins to assemble into granular-like pre-nucleolar bodies which are subsequently relocated to nucleoli at the early G1-phase. {ECO:00...
null
null
null
null
null
FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification (By similarity). Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with TCOF1 and acts as ...
Mus musculus (Mouse)
E9Q5F9
SETD2_MOUSE
MKPLPSQQPPPKMGDFYDPEHPTPEEEENEAKIENVQKTGFIKGPVFKGVASSRFLPKGTKTKVNLEEQGRQKVSFSFSFTKKTLQNRFLTALSNEKQSDSPNSPAPPLQVDSNPKVKMDAGDTFPATEESSPPKSRVELGRIHFKKHLLHVTSRPQLAASTTAASPLPPTTQLPAVLAESMIDSPPSSPPPPPPPPQASSPSPPAQISEPVALPQPPATALMTSPPGPLPGDVAVRAQKESPVKSGPEVLEVDTKQDIVSNSLEEHTVQTLKEQADHLLQKEDSHIGKEEEVSDGSKISLSSKKASSKKKSSQFEGTFL...
2.1.1.-; 2.1.1.359
null
angiogenesis [GO:0001525]; cell migration involved in vasculogenesis [GO:0035441]; coronary vasculature morphogenesis [GO:0060977]; defense response to virus [GO:0051607]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic organ development [GO:0048568]; embryonic placenta morphogenesis [GO:0060669]; endo...
chromosome [GO:0005694]; nucleus [GO:0005634]
alpha-tubulin binding [GO:0043014]; histone H3K36 methyltransferase activity [GO:0046975]; histone H3K36 trimethyltransferase activity [GO:0140955]; metal ion binding [GO:0046872]; protein-lysine N-methyltransferase activity [GO:0016279]
PF17907;PF00856;PF08236;PF00397;
2.20.70.10;1.20.930.10;2.170.270.10;1.10.1740.100;
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, SET2 subfamily
PTM: May be automethylated. {ECO:0000250|UniProtKB:Q9BYW2}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18157086}. Chromosome {ECO:0000269|PubMed:18157086}.
CATALYTIC ACTIVITY: Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI...
null
null
null
null
FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:18157086, PubMed:20133625). It is capable of trimethylating unmethylated H3K36 (H3K36me0) in vitro (By similarity). Represents the main enzyme generating H3K3...
Mus musculus (Mouse)
E9Q5G3
KIF23_MOUSE
MKSAKAKTVRKPVIKKGSQTNLKDPVGVYCRVRPLSFPDQECCVEVINSTTLQLHTPEGYRLNRNGDYKETQYSFKRVFGTHTTQKELFDVVANPLVDDLIHGKNGLLFTYGVTGSGKTYTMTGSPGSGGLLPRCLNMIFNSIGSFQAKRYVFKSNDRNSMEIQCEVDALLERQKREALPIPKTPSSKRQADPEFADMINVQEFCKAEEVDEDSVYGVFVSYIEIYNNYIYDLLEEVQFDPIKPKLPQSKTLREDKNHNMYVAGCTEVEVKSTEEAFEVFWRGQKKRRIANTHLNRESSRSHSVFSIKLVQAPLDADGDN...
null
null
microtubule-based movement [GO:0007018]; mitotic cytokinesis [GO:0000281]; mitotic spindle midzone assembly [GO:0051256]
centrosome [GO:0005813]; cytoplasm [GO:0005737]; Flemming body [GO:0090543]; intercellular bridge [GO:0045171]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]
PF00225;PF16540;
3.40.850.10;2.60.40.4330;
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family
PTM: Ubiquitinated. Deubiquitinated by USP8/UBPY (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Midbody, Midbody ring {ECO:0000269|PubMed:19020301}. Note=Localizes to the interzone of mitotic spindles (By similarity). Detected at the midbody during later stages of mitotic cytokinesis. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Essential for cytokinesis in Rho-mediated signaling. Required for the localization of ECT2 to the central spindle. Pl...
Mus musculus (Mouse)
E9Q5G7
OOG1_MOUSE
MVICLHCPDQDDSLEEVTEECYSPPTLQNLAIQSLLRDEALAISALTDLPQSLFPVIFEEAFTDGYIGILKAMIPVWPFPYLSLGKQINNCNLETLKAMLEGLDILLAQKVQTSRCKLRVINWREDDLKIWAGSHEGEGLPDFRTEKQPIENSAGCEVKKELKVTTEVLRMKGRLDESTTYLLQWAQQRKDSIHLFCRKLLIEGLTKASVIEIFKTVHADCIQELILRCICIEELAFLNPYLKLMKSLFTLTLDHIIGTFSLGDSEKLDEETIFSLISQLPTLHCLQKLYVNDVPFIKGNLKEYLRCLKKPLETLCISNC...
null
null
negative regulation of apoptotic process [GO:0043066]; negative regulation of cell differentiation [GO:0045596]; negative regulation of DNA-templated transcription [GO:0045892]; oocyte development [GO:0048599]; positive regulation of cell population proliferation [GO:0008284]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
null
null
3.80.10.10;
PRAME family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12890732, ECO:0000269|PubMed:16580637}. Cytoplasm {ECO:0000269|PubMed:12890732, ECO:0000269|PubMed:16580637}. Note=In early one-cell embryos, exists only in the cytoplasm and gradually moves to the nucleus at the middle one-cell stage. At the late one-cell and early two...
null
null
null
null
null
FUNCTION: May down-regulate the expression of spermatogenesis-associated genes in female germ cells allowing their normal differentiation into oocytes (PubMed:29731491). May act as a Ras-mediated signaling protein in early embryogenesis. {ECO:0000269|PubMed:29731491, ECO:0000305|PubMed:16580637}.
Mus musculus (Mouse)
E9Q5K4
CP2CN_MOUSE
MELLGLPTLALLVLVMSLSLLSVWTKMRTGGRLPPGPTPLPIIGNILQLDLKDIPASLSKLAKEYGPVYTLYFGSWPTVVLHGYDVVKEALLNQGDEFLGRGPLPIIEDSQKGHGIVFSEGERWKLLRRFSLMTLKNFGMGKRSLEERVQEEARCLVEELHKTEAQPFDPTFILACAPCNVICSILFNERFPYNDKTFLNLMDLLNKNFYQLNSIWIQMYNLWPTIMKYIPGKHREFSKRLGGVKNFILEKVKEHQESLDPANPRDYIDCFLSKIEEEKHNLKSDFNLENLAICGSNLFTAGTETTSTTLRFGLLLLVKH...
1.14.14.-
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P33261};
epoxygenase P450 pathway [GO:0019373]; icosanoid biosynthetic process [GO:0046456]; xenobiotic metabolic process [GO:0006805]
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]
arachidonic acid 11,12-epoxygenase activity [GO:0008405]; arachidonic acid 14,15-epoxygenase activity [GO:0008404]; arachidonic acid epoxygenase activity [GO:0008392]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with in...
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15084647}. Microsome membrane {ECO:0000269|PubMed:15084647}.
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:49884, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:...
null
PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000305|PubMed:15084647}.
null
null
FUNCTION: A cytochrome P450 monooxygenase involved in polyunsaturated fatty acids (PUFAs) metabolism and signaling (PubMed:15084647). Catalyzes preferentially the epoxidation of double bonds of PUFAs (PubMed:15084647). Converts arachidonic acid (ARA, C20:4(n-6)) primarily to stereospecific products 8R,9S-epoxyeicosatri...
Mus musculus (Mouse)
E9Q5K9
YTDC1_MOUSE
MAADSREEKDGELNVLDDILTEVPEQDDELYNPESEQDKNEKKGSKRKSERMESTDTKRQKPSIHSRQLISKPLSSSVSNNKRIVSTKGKSVTEYKNEEYQRSERNKRLDADRKIRLSSSSSREPYKSQPEKTCLRKRDSERRAKSPTPDGSERIGLEVDRRASRSSQSSKEEVNSEDYGSDHETGSSGSSEQGNNTENEEEGGEEDVEEDEEVDEDAEDDEEVDEDAEEEEEEDEEEEEDEDEDEEEEEYEQDERDQKEEGNDYDTRSEASDSGSESVSFTDGSVRSGSGTDGSDEKKKERKRARGISPIVFDRSGSSA...
null
null
dosage compensation by inactivation of X chromosome [GO:0009048]; in utero embryonic development [GO:0001701]; mRNA alternative polyadenylation [GO:0110104]; mRNA export from nucleus [GO:0006406]; mRNA splice site recognition [GO:0006376]; mRNA splicing, via spliceosome [GO:0000398]; post-transcriptional regulation of ...
nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; RNA binding [GO:0003723]
PF04146;
3.10.590.10;
null
PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q9QY02}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29799838}. Nucleus speckle {ECO:0000250|UniProtKB:Q96MU7}. Note=Localizes to a novel subnuclear structure, the YT bodies. {ECO:0000250|UniProtKB:Q9QY02}.
null
null
null
null
null
FUNCTION: Regulator of alternative splicing that specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs (PubMed:29262316, PubMed:29799838). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in the efficiency of mRNA splicing, processing and stability ...
Mus musculus (Mouse)
E9Q5R7
NAL12_MOUSE
MLPSTARDGLYRLSTYLEELEAGELKKFKLFLGIAEDLSQDKIPWGRMEKAGPLEMAQLMVAHMGTREAWLLALSTFQRIHRKDLWERGQGEDLVRVTPNNGLCLFESQSACPLDVSPNAPRKDLQTTYKDYVRRKFQLMEDRNARLGECVNLSNRYTRLLLVKEHSNPIWTQQKFVDVEWERSRTRRHQTSPIQMETLFEPDEERPEPPHTVVLQGAAGMGKSMLAHKVMLDWADGRLFQGRFDYVFYISCRELNRSHTQCSVQDLISSCWPERGISLEDLMQAPDRLLFIIDGFDKLHPSFHDAQGPWCLCWEEKQPT...
null
null
cellular response to cytokine stimulus [GO:0071345]; dendritic cell migration [GO:0036336]; ERK1 and ERK2 cascade [GO:0070371]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of inflammatory response [GO:0050728...
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; protein-macromolecule adaptor activity [GO:0030674]
PF14484;PF13516;PF05729;PF17776;PF17779;PF02758;
1.10.533.10;3.40.50.300;3.80.10.10;
NLRP family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P59046}.
null
null
null
null
null
FUNCTION: Plays an essential role as an potent mitigator of inflammation (PubMed:26521018, PubMed:30559449). Primarily expressed in dendritic cells and macrophages, inhibits both canonical and non-canonical NF-kappa-B and ERK activation pathways (PubMed:30559449). Functions as a negative regulator of NOD2 by targeting ...
Mus musculus (Mouse)
E9Q612
PTPRO_MOUSE
MGHLPRGTLGGRRLLPLLGLFVLLKIVTTFHVAVQDDNNIVVSLEASDIVSPASVYVVRVAGESKNYFFEFEEFNSTLPPPVVFKATYHGLYYIITLVVVNGNVVTKPSRSITVLTKPLPVTSVSIYDYKPSPETGVLFEIHYPEKYNVFSRVNISYWEGRDFRTMLYKDFFKGKTVFNHWLPGLCYSNITFQLVSEATFNKSTLVEYSGVSHEPKQHRTAPYPPRNISVRFVNLNKNNWEEPSGSFPEDSFIKPPQDSIGRDRRFHFPEETPETPPSNVSSGSPPSNVSSAWPDPNSTDYESTSQPFWWDSASAAPENE...
3.1.3.48
null
axon guidance [GO:0007411]; cell morphogenesis [GO:0000902]; glomerulus development [GO:0032835]; lamellipodium assembly [GO:0030032]; monocyte chemotaxis [GO:0002548]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of glomerular filtration [GO:0003105]; peptidyl-tyrosine depho...
apical plasma membrane [GO:0016324]; dendritic spine [GO:0043197]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]
cadherin binding [GO:0045296]; protein homodimerization activity [GO:0042803]; protein tyrosine phosphatase activity [GO:0004725]; Wnt-protein binding [GO:0017147]
PF00041;PF00102;
2.60.40.10;3.90.190.10;
Protein-tyrosine phosphatase family, Receptor class 3 subfamily
null
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044};
null
null
null
null
FUNCTION: Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function. {ECO:0000269|PubMed:11086029}.
Mus musculus (Mouse)
E9Q634
MYO1E_MOUSE
MGSKGAYRYHWQSHNVKHSGVDDMVLLSKITESSIVENLKKRYMDDYIFTYIGSVLISVNPFKQMPYFGEKEVEMYQGAAQYENPPHIYALADSMYRNMIIDRENQCVIISGESGAGKTVAAKYIMSYVSRVSGGGPKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSPGGEPDGGKISNFLLEKSRVVMRNPGERSFHIFYQLIEGASPEQKQSLGITSMDYYYYLSLSGSYKVDDIDDKRDFQETLHAMNVIGIFSEEQTLVLQIVAGILHLGNISFKEVGNYAAVESEEFLAFPAYLLGINQDRLK...
null
null
actin filament organization [GO:0007015]; endocytosis [GO:0006897]; glomerular basement membrane development [GO:0032836]; glomerular filtration [GO:0003094]; glomerulus development [GO:0032835]; hemopoiesis [GO:0030097]; in utero embryonic development [GO:0001701]; kidney development [GO:0001822]; platelet-derived gro...
actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; brush border [GO:0005903]; clathrin-coated endocytic vesicle [GO:0045334]; cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; microvillus [GO:0005902]; myosin complex [GO:0016459]; plasma membrane [GO:0005886]; protein-contai...
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; phosphatidylinositol binding [GO:0035091]; protein-containing complex binding [GO:0044877]
PF00063;PF06017;PF00018;
1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;2.30.30.40;
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19005011}. Cell junction {ECO:0000269|PubMed:19005011}. Cytoplasmic vesicle {ECO:0000305|PubMed:19005011}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:19005011}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19005011}. Note=In podocytes, it localize...
null
null
null
null
null
FUNCTION: Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain (By sim...
Mus musculus (Mouse)
E9Q649
GCNT4_MOUSE
MKIFRCCFKYTLQQKLFILLLTLWLFSLLKLLNVGRLLFPQRDIYLVEYSLSTSPFVRNRFPESGDAARDNVNCSGVYEHEPLEIGKSLEIRRRSIIDLEDGDVVAMTSDCDVYQTLRQYHEKLVSREEEDFPIAYSLVVHKDAIMVERLIRAIYNQHNLYCIHYDLKSPDTFKAAMNNLAKCFPNIFIASKLETVEYAHISRLQADWNCLSDLLKSSVQWKYVINLCGQDFPLKSNFELVTELKSLQGRNMLETVRPPSAKTERFTYHHELRQVPYDYMKLPVKTNVSKGAPPHNIQVFVGSAYFVLSRAFVKYIFNSS...
2.4.1.102
null
inter-male aggressive behavior [GO:0002121]; kidney morphogenesis [GO:0060993]; neutrophil homeostasis [GO:0001780]; protein glycosylation [GO:0006486]; thyroid hormone metabolic process [GO:0042403]; tissue morphogenesis [GO:0048729]
Golgi membrane [GO:0000139]
acetylglucosaminyltransferase activity [GO:0008375]; beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity [GO:0003829]
PF02485;
null
Glycosyltransferase 14 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13...
null
PATHWAY: Protein modification; protein glycosylation.
null
null
FUNCTION: Glycosyltransferase that mediates core 2 O-glycan branching, an important step in mucin-type biosynthesis. Does not have core 4 O-glycan or I-branching enzyme activity. {ECO:0000250|UniProtKB:Q9P109}.
Mus musculus (Mouse)
E9Q6W4
ZN296_MOUSE
MSRRKAGRVPRRVDPDTDTDIEMPDLVMDVKPDLDLRSLAQGPWIARDMPISDVKRQLQTASRPLGAPSTCAPRMPLSSKSSDRQPWTDKHPDLLTCGRCGKIFPLGAIIAFMDHKKQGCQLLQVSDPISESKELKALSCLQCGRQYTSPWKLLCHAQWDHGLCIYQTQHLDTPEAPLLGLAEVAAAMSAVAVVAPVESKPPPVSSAARRSPTCDVCKKTLSSFSNLKVHMRSHTGERPYSCDQCSYACAQSSKLNRHKKTHRQLAPGSPSTSASSRGVSPAAPPEPAAYAAAPASTLPSQTVEKAGAAATAGVQEPGAP...
null
null
negative regulation of dendrite development [GO:2000171]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283]
nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00096;
3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24161396}.
null
null
null
null
null
FUNCTION: May be a transcriptional corepressor with KLF4. {ECO:0000269|PubMed:24161396}.
Mus musculus (Mouse)
E9Q784
ZC3HD_MOUSE
MSKIRRKVTVENTKTISESTSRRPSVFERLGPSTGSTTETQCRNWLKTGSCLYGNTCRFIHGPSPRGKGYSSNYRRSPERPTGDLRERMKNKRQDVDSESQKRNTEEPSSPVRKESSRGRHRDKEDIKIVKERTPESEEENVEWETNRDDSDNGDINYDYVHELSLEMKRQKIQRELMKLEQENMDKREEIIIQKEVSPEVVRSKLSPSPSLRKSSKSPKRKSSPKASSAGKKERKAAVVASPLLDQQRNSKGNQSKKKGPRTPSPPPPILEDIILGKKYKEKYKVKDRIEEKPRDGKDRGRDFEKQREKRDKPRSSSPG...
null
null
mRNA methylation [GO:0080009]; mRNA processing [GO:0006397]; regulation of stem cell population maintenance [GO:2000036]; RNA splicing [GO:0008380]
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA N6-methyladenosine methyltransferase complex [GO:0036396]
metal ion binding [GO:0046872]
PF00642;
4.10.1000.10;
ZC3H13 family
null
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q5T200}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}.
null
null
null
null
null
FUNCTION: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29535189, PubMed:29547716). Acts as a key regulator of m6A methylation by promoting m6A methylation of m...
Mus musculus (Mouse)
E9Q7D5
ARHG5_MOUSE
MEAEEPEYGVSTEVPDIEELKTIPEGIMRSSQIPALDPEAQEDRDPSYKWTDGHRPVMNQSKVLRDMGDHTPNSMAIFFKKESSDMETSQEILLAEACNTPDQQEAVIQSLKDRLSRTIAAPELLACAVQEEWLDIPSKLDNRVGAELQSELMSLTLAVSKEKEEEETSPDTSIPRGSWPPCKTHPGETEQTQGSGSELLRQGKQLQLEATQENQGQEGFLQSQEAQGLEEQEGQEVEIQEEGTLNEGICFGGLLGEQEEVEEGFNGNEEEQKQGQIQSYMLLGGQWENEGLSGELEGLNYSERGQENRERRVWVLRDSE...
null
null
actin cytoskeleton organization [GO:0030036]; hematopoietic stem cell homeostasis [GO:0061484]; intracellular signal transduction [GO:0035556]; myeloid dendritic cell chemotaxis [GO:0002408]; positive regulation of podosome assembly [GO:0071803]; positive regulation of protein import [GO:1904591]; positive regulation o...
anchoring junction [GO:0070161]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; podosome [GO:0002102]
guanyl-nucleotide exchange factor activity [GO:0005085]; lipid binding [GO:0008289]
PF15441;PF00169;PF00621;PF00018;
1.20.900.10;2.30.29.30;2.30.30.40;
null
PTM: Activation of SRC induces tyrosine phosphorylation of ARHGEF5. {ECO:0000269|PubMed:21525037}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12774}. Cytoplasm {ECO:0000250|UniProtKB:Q12774}. Cell projection, podosome {ECO:0000269|PubMed:21525037}.
null
null
null
null
null
FUNCTION: Guanine nucleotide exchange factor which activates Rho GTPases (PubMed:19713215, PubMed:21525037). Strongly activates RHOA (PubMed:19713215, PubMed:21525037). Also strongly activates RHOB, weakly activates RHOC and RHOG and shows no effect on RHOD, RHOV, RHOQ or RAC1 (PubMed:19713215). Involved in regulation ...
Mus musculus (Mouse)
E9Q7E2
ARID2_MOUSE
MANSTGKAPPDERRKGLAFLDELRQFHHSRGSPFKKIPAVGGKELDLHGLYTRVTTLGGFAKVSEKNQWGEIVEEFNFPRSCSNAAFALKQYYLRYLEKYEKVHHFGEDDDEVPPGNPKPQLPIGAIPSSYNYQQHSVSDYLRQSYGLSMDFNSPNDYNKLVLSLLSGLPNEVDFAINVCTLLSNESKHVMQLEKDPKIITLLLANAGVFDDTLGSFSSVFGEEWREKTDRDFVKFWKDIVDDNEVRDLISDRNKAHEDTPGEWIWESLFHPPRKLGINDIEGQRVLQIAVILRNLSFEESNVKLLAANRTCLRFLLLSA...
null
null
cardiac muscle cell proliferation [GO:0060038]; chromatin remodeling [GO:0006338]; circulatory system development [GO:0072359]; coronary artery morphogenesis [GO:0060982]; embryonic organ development [GO:0048568]; heart morphogenesis [GO:0003007]; homeostatic process [GO:0042592]; negative regulation of cell migration ...
chromatin [GO:0000785]; kinetochore [GO:0000776]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514]; transcription regulator complex [GO:0005667]
DNA binding [GO:0003677]; metal ion binding [GO:0046872]
PF01388;PF02257;
1.10.150.60;1.10.10.10;
RFX family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00858}.
null
null
null
null
null
FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). May be involved in targeting the complex to different genes. May be involved in regula...
Mus musculus (Mouse)
E9Q7F2
RN169_MOUSE
MAAAGPSTRASSAAAAAALSRRGRRGRCDEMAAAKAGAPGPASSPALLVLRSAPRPEESGCTGCLETPGEVAALPCSHSRCRGCASRAAGPGCRRCRPRGSGWARRRARDDGQAAAELMGERARRGQPEPCRPRRDGGAAASGPRPEPEPLAEPEFIFRTPIKLSKPGELSEEYGCLRKLRGEKLQEEKDCDDQIHKLLQEDSEMGKRKADEQKKRDEAVVLKTSLEQCPARLSDSENEEPSRGQMMQTHRSAFVSKNSSCSLAFLAGKLNTKVQRSQSCSDTVQDRVRSRLRTAPPNRAKITTITPGSTPIIGVLLSTQ...
2.3.2.27
null
DNA damage response [GO:0006974]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; negative regulation of double-strand break repair [GO:2000780]; protein ubiquitination [GO:0016567]
cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; nucleosome binding [GO:0031491]; ubiquitin modification-dependent histone binding [GO:0061649]; ubiquitin-protein transferase activity [GO:0004842]
null
3.30.40.10;
RNF169 family
PTM: Phosphorylated by DYRK1A; phosphorylation increases RNF169 ability to block accumulation of TP53BP1 at the DSB sites. {ECO:0000250|UniProtKB:Q8NCN4}.
SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8NCN4}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8NCN4}. Note=Localizes to sites of double-strand breaks (DSBs) following DNA damage. Recruited to DSBs via recognition of RNF168-dependent ubiquitin products. {ECO:0000250|UniProtKB:Q8NCN4}.
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: Probable E3 ubiquitin-protein ligase that acts as a regulator of double-strand breaks (DSBs) repair following DNA damage. Functions in a non-canonical fashion to harness RNF168-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization. Once ...
Mus musculus (Mouse)
E9Q7G0
NUMA1_MOUSE
MTLHATRAATLLSWVNSLHVADPVETVLQLQDCSIFIKIINTIHDTKEGQQILQQPLPERLDFVCSFLQKNRKHPSSTQCLVSVQKVIEGSEMELAKMIMLFLYQSTMSSRNLRDWEQFEYGVQAELAVILKFMLDHEESLNLTEDLESFLEKVPYTHASTLSEELSPPSHQTKRKIRFLEIQRIASSSSENNFLSGSPSSPMGDILQTPQFQMRRLKKQLADERSNRDDLELELSESLKLLTEKDAQIAMMQQRIDHLALLNEKQAASSQEPSELEELRGKNESLTVRLHETLKQCQNLKTEKSQMDRKISQLSEENGD...
null
null
anastral spindle assembly [GO:0055048]; astral microtubule organization [GO:0030953]; cell division [GO:0051301]; establishment of mitotic spindle orientation [GO:0000132]; meiotic cell cycle [GO:0051321]; microtubule bundle formation [GO:0001578]; positive regulation of BMP signaling pathway [GO:0030513]; positive reg...
cell cortex region [GO:0099738]; centrosome [GO:0005813]; chromosome [GO:0005694]; cortical microtubule [GO:0055028]; cytoplasmic microtubule bundle [GO:1905720]; cytosol [GO:0005829]; dendrite [GO:0030425]; lateral cell cortex [GO:0097575]; lateral plasma membrane [GO:0016328]; microtubule bundle [GO:0097427]; microtu...
disordered domain specific binding [GO:0097718]; dynein complex binding [GO:0070840]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; microtubule plus-end binding [GO:0051010]; phosphatidylinositol binding [GO:0035091]; tubulin binding [GO:0015631]
PF21670;
null
null
PTM: Phosphorylation and dephosphorylation on Thr-2037 regulates the extent of cortical NUMA1 and the dynein-dynactin complex localization during mitotic metaphase and anaphase. In metaphase, phosphorylation on Thr-2037 occurs in a kinase CDK1-dependent manner; this phosphorylation maintains low levels of cortical dyne...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19255246}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14980}. Nucleus matrix {ECO:0000250|UniProtKB:Q14980}. Chromosome {ECO:0000250|UniProtKB:Q14980}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26765568}. Cytoplasm, cytoskeleton, microtubule organizing center, centr...
null
null
null
null
null
FUNCTION: Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:19255246, PubMed:24109598, PubMed:26765568). Functions to tether the minus ends of MTs at the spindle poles, which...
Mus musculus (Mouse)
E9Q7R9
CFA43_MOUSE
MSQDPERDDVTASATASASASAPASASAHYSGSSLSVRWVQGFPSQNVHFVNDQTICYPSGNFVIFINLETKKKTVLQCINGIVGVMATNVPSEVVAFSDRRFKPVIYIYSFPSLTRKNKLKGDILLDYTLLCFSYCGTYLASYSSLPEFELALWNWEASAILCKKSNPGMDVSQMSFNPMNWHQMCLSSSSAMSVWTIERSNQEHHFRIRSVKLPLEDATFLNEPDMLFPTTLPKDLIYGPVLPLSAIAGLVGEEAETFRPKDDIYPLLHPTMHCWTPSSDLYVGCEEGHLLMINTETLKVTVLQKAEEFPLPDGAPLI...
null
null
brain development [GO:0007420]; cerebrospinal fluid circulation [GO:0090660]; cilium assembly [GO:0060271]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localization in cell [GO:0051649]; flagellated sperm motility [GO:0030317]; motile cilium assembly [GO:0044458]; ...
9+2 motile cilium [GO:0097729]; axoneme [GO:0005930]; extracellular region [GO:0005576]
null
null
2.130.10.10;
CFAP43 family
null
SUBCELLULAR LOCATION: Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q57WH1}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:Q57WH1}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:31884020}.
null
null
null
null
null
FUNCTION: Flagellar protein involved in sperm flagellum axoneme organization and function (PubMed:28552195, PubMed:29449551, PubMed:31884020). Involved in the regulation of the beating frequency of motile cilia on the epithelial cells of the respiratory tract (PubMed:31884020). {ECO:0000269|PubMed:28552195, ECO:0000269...
Mus musculus (Mouse)
E9Q7X6
HEG1_MOUSE
MATPRAPRWPPPSLLLLLLLPLLLLPPAAPGARGSLPSPAHRTLLPVAGPLSPPGAGHTAPGPGVATRRGRSGRVPRGVSAAAARNRWLESNNPEPHIGCSPSYQSQEDHSGSRKGVTAQNARMSHSSSEGPENPPLLPETSAEWSNMASSHRADIAGLRRGPSPEITTAPTAHSSLLSLESLPESPSSSRSQRRITPSQTESGTSLGFLERTRELPEEGTVHTQVAGTWVSRQASHPALEPGEPTVLSQKRNSSGQEHSGPPFSWSQSHPPPSDHPSSSGSIKNGNNFTALQNPSVTQTKSMLITDTYTNGVPRTLRSL...
null
null
cardiac atrium morphogenesis [GO:0003209]; cardiac muscle tissue growth [GO:0055017]; cell-cell junction organization [GO:0045216]; endothelial cell development [GO:0001885]; endothelial cell morphogenesis [GO:0001886]; heart development [GO:0007507]; in utero embryonic development [GO:0001701]; lung development [GO:00...
cell surface [GO:0009986]; cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]
calcium ion binding [GO:0005509]
PF00008;PF07645;
2.10.25.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000269|PubMed:19151727}.
null
null
null
null
null
FUNCTION: Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May be acting by stabilizing endothelial cell junctions. {ECO:0000269|PubMed:19151727}.
Mus musculus (Mouse)
E9Q7X7
NRX2A_MOUSE
MALGSRWQPPPQLPPLLLLLALAAGVRGLEFGGGPGQWARYARWAGAASTGELSFSLRTNATRALLLYLDDGGDCDFLELLLVDGRLRLRFTLSCAEPATLQLDTPVADDRWHMVLLTRDARRTALAVDGEARAAEVRSKRREMQVASDLFVGGIPPDVRLSALTLSTVKYEPPFRGLLANLKLGERPPALLGSQGLRGAAADPLCAPARNPCANGGLCTVLAPGEVGCDCSHTGFGGKFCSEEEHPMEGPAHLTLNSEVGSLLFSEGGAGRGGAGDVHQPTKGKEEFVATFKGNEFFCYDLSHNPIQSSTDEITLAFRT...
null
null
adult behavior [GO:0030534]; cell adhesion [GO:0007155]; chemical synaptic transmission [GO:0007268]; gephyrin clustering involved in postsynaptic density assembly [GO:0097116]; neuroligin clustering involved in postsynaptic membrane assembly [GO:0097118]; neurotransmitter secretion [GO:0007269]; postsynaptic density p...
cell projection [GO:0042995]; glutamatergic synapse [GO:0098978]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991]
calcium channel regulator activity [GO:0005246]; cell adhesion molecule binding [GO:0050839]; metal ion binding [GO:0046872]; neuroligin family protein binding [GO:0097109]; transmembrane signaling receptor activity [GO:0004888]
PF02210;
2.60.120.200;2.10.25.10;
null
PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate attachment is required for synapse development by mediating interactions with neuroligins. {ECO:0000269|PubMed:30100184}.
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9CS84}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling. {ECO:0000250|UniProtKB:Q63374}.
Mus musculus (Mouse)
E9Q816
CP2W1_MOUSE
MALLLLGVWGILLLLGLWGLLQGCTRSPSLAPRWPPGPRPLPFLGNLHLLGVTQQDRALMELSERYGPMFTIHLGSQKTVVLSGYEVVREALVGTGHELADRPPIPIFQHIQRGGGIFFSSGARWRAGRQFTVRTLQSLGVQQPSMVGKVLQELACLKGQLDSYGGQPLPLALLGWAPCNITFTLLFGQRFDYQDPVFVSLLSLIDQVMVLLGSPGIQLFNTFPRLGAFLRLHRPVLSKIEEVRTILRTLLETRRPPLPTGGPAQSYVEALLQQGQEDDPEDMFGEANVLACTLDMVMAGTETTAATLQWAVFLMVKHPH...
1.14.14.-
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:Q6VVX0};
aflatoxin metabolic process [GO:0046222]; organic acid metabolic process [GO:0006082]; phospholipid metabolic process [GO:0006644]; retinoic acid catabolic process [GO:0034653]; xenobiotic metabolic process [GO:0006805]
cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]
all-trans retinal binding [GO:0005503]; all-trans-retinol binding [GO:1904768]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of o...
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8TAV3}. Cell membrane {ECO:0000250|UniProtKB:Q8TAV3}. Microsome membrane {ECO:0000250|UniProtKB:Q8TAV3}.
CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:352...
null
null
null
null
FUNCTION: A cytochrome P450 monooxygenase that may play a role in retinoid and phospholipid metabolism. Catalyzes the hydroxylation of saturated carbon hydrogen bonds. Hydroxylates all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may regulate atRA clearance. Other retinoids such as all-trans retinol and all-tra...
Mus musculus (Mouse)
E9Q876
ABCAC_MOUSE
MASQFHQLRILVWKNWLGVKRQPLWTLVLILWPVIIFIILAITRTKFPPTAKPTCYLAPRNLPSAGFFPFLQTLLCDTDSKCKDTPYGPRDLLRRKGIDGPLFKESEILKKPSNPKRDSNLSLRSTQVPERSHTSLATVPPRPSYDLEGTGTENFNGSQLLTRILGLEKLLKQNSTPEDIRRELCESYPGYTADYAFSWVTLGKNVFNKFCLSNMTLLESSLQELKYQVSQMSSDPDNQKRVFRGLVQVLSFFSQVQQQREVWQLLSSLPDVFQNGTSLSSLFGVLQKANRVLLVVQKVYPRVQTDEGFSTLQKSVKHLL...
7.6.2.1
null
ceramide metabolic process [GO:0006672]; ceramide transport [GO:0035627]; cholesterol efflux [GO:0033344]; corneocyte desquamation [GO:0003336]; establishment of localization in cell [GO:0051649]; establishment of skin barrier [GO:0061436]; intracellular protein transport [GO:0006886]; keratinization [GO:0031424]; kera...
cytosol [GO:0005829]; epidermal lamellar body membrane [GO:0097234]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; plasma membrane [GO:0005886]; transport vesicle membrane [GO:0030658]
ABC-type transporter activity [GO:0140359]; apolipoprotein A-I receptor binding [GO:0034191]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; ATPase-coupled transmembrane transporter activity [GO:0042626]; lipid transporter activity [...
PF12698;PF00005;
3.40.50.300;
ABC transporter superfamily, ABCA family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q86UK0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q86UK0}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q86UK0}. Note=Localizes in the limiting membrane of the lamellar granules (LGs). Trafficks from the Golgi appa...
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:Q86UK0}; CATALYTIC ACTIVITY: Reaction=ATP + beta-D-glucosylceramide(in) + H2O = ADP + beta-D-glucosylceramide(out) + H(+) + phosphate; Xref=Rhea:RHEA:66660, ChEBI:CHEBI:15377,...
null
null
null
null
FUNCTION: Transports lipids such as glucosylceramides from the outer to the inner leaflet of lamellar granules (LGs) membrane, whereby the lipids are finally transported to the keratinocyte periphery via the trans-Golgi network and LGs and released to the apical surface of the granular keratinocytes to form lipid lamel...
Mus musculus (Mouse)
E9Q8I9
FRY_MOUSE
MASQQDSGFFEISIKYLLKSWSNASPVGNGYIKPPVPPASGTHREKGPPAMLPINVDPDSKPGEYVLKSLFVNFTTQAERKIRIIMAEPLEKPLTKSLQRGEDPQFDQVISSMSSLSEYCLPSILRTLFDWYKRQNGIEDESHEYRPRTSNKSKSDEQQRDYLMERRDLAIDFIFSLVLIEVLKQIPLHPVIDSLIHDIINLAFKHFKYKEGYLGPNTGNMHIVADLYAEVIGVLAQAKFPAVKKKFMAELKELRHKEQSPYVVQSIISLIMGMKFFRIKMYPVEDFEASLQFMQECAHYFLEVKDKDIKHALAGLFVEI...
null
null
cell morphogenesis [GO:0000902]; negative regulation of tubulin deacetylation [GO:1904428]; neuron projection development [GO:0031175]
cell cortex [GO:0005938]; centrosome [GO:0005813]; site of polarized growth [GO:0030427]; spindle pole [GO:0000922]
enzyme inhibitor activity [GO:0004857]
PF19421;PF14225;PF14228;PF14222;
null
Furry protein family
PTM: Phosphorylated by AURKA, CDK1 and PLK1. {ECO:0000269|PubMed:22753416}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Distributed diffusely throughout the cytoplasm in interphase. Localizes to the separating centrosomes in prophase, to the spindle pol...
null
null
null
null
null
FUNCTION: Plays a crucial role in the structural integrity of mitotic centrosomes and in the maintenance of spindle bipolarity by promoting PLK1 activity at the spindle poles in early mitosis. May function as a scaffold promoting the interaction between AURKA and PLK1, thereby enhancing AURKA-mediated PLK1 phosphorylat...
Mus musculus (Mouse)
E9Q8Q6
CC141_MOUSE
MSCKESPHVGASTTTVSSVAVHAGDSKIVIAVVKCGKWVRLQLAESQPNLLEIGSSQDETKKLLHDHELLLAKLKALEDRVWELLREADRTAEANKAQSQVYDAMAQTLGEAWATLVSMLERRRELLGLTSEFFQSALEFAIKIDQAEAFLQNPHEFESTEALQSLLLLHDRHAKELLERSLDLLNKSQQLTDFIEKFKCEGSTMNSELIQGAQSSCLKIDSLLELLQDRRRQLDKYLQQQRQELSQVLQLCLWDQQENQVSSWFQKAIRDLQEQSLGASLSDNRELICKHEDLIVKAKEWDSAVEKLKSQALGILLSKD...
null
null
brain development [GO:0007420]; centrosome localization [GO:0051642]; cerebral cortex radially oriented cell migration [GO:0021799]
centrosome [GO:0005813]; cytoplasm [GO:0005737]
null
PF07679;
1.20.58.60;2.60.40.10;
null
PTM: Ubiquitinated and degradated by the CDC20-APC/C pathway. During brain development, CDC20-APC/C complex degrades CCDC141 after centrosome translocation into the dilated area. CCDC141 is restabilized in the dilation until the centrosome enters the dilation, at which point it is once again immediately destabilized by...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20956536}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20956536, ECO:0000269|PubMed:34298015}. Note=Co-localized with DISC1 at/around the centrosome. Localizes to the centrosome, at least in part, in a DISC1-dependent manner ...
null
null
null
null
null
FUNCTION: Plays a critical role in cortical radial and GnRH neurons migration during brain development (PubMed:20956536, PubMed:27014940). Regulates cortical radial migration by negatively controlling the activity of histone deacetylase 6 (HDAC6) and promotes centrosome maturation (PubMed:27737934). CAMDI is required f...
Mus musculus (Mouse)
E9Q8Q8
SACA6_MOUSE
MTSQRSLSSPQTRRPSVMGLISLVGSIVLLFLLIFRASTWACLFCFTTYEERLRVCQLFVGREETKINLCRNELEGAFEDLKDMKINYDERSYLHDEFTQMTVSLQEKAARRREPFWLAFKDAAAKLKRTIEHLKKAPACIPPCGLQEVARLFHCSGCFSKLCDLPLDCPVQDMLVNRGDQALFSCIVAFELPESEITYSWKFVGGVRTKDVTYFRDMPGAHGYLARIRPVQPKHGGTFSCVILHDQRPLARLYFYLNVTGPPPPEDTELQVTFREVMNRTPAEPEMIQPWSPSLGELLTNPQALTLGNLFLLAATAALG...
null
null
fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]
acrosomal membrane [GO:0002080]; acrosomal vesicle [GO:0001669]; membrane [GO:0016020]
null
null
null
SPACA6 family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:32393636}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Sperm protein required for fusion of sperm with the egg membrane during fertilization. {ECO:0000269|PubMed:24275887, ECO:0000269|PubMed:32210282, ECO:0000269|PubMed:32393636}.
Mus musculus (Mouse)
E9Q8T2
PRD15_MOUSE
MCPPTIWEKGGQVGARWSLRAPEVSAMAEDGSEEIMFIWCEDCSQYHDSECPELGPVVMVKDSFVLSRARSSLPSNLEIRRLDDGAEGVFAVTQLVKRTQFGPFESRRVAKWEKESAFPLKVFQKDGHPVCFDTSNEDDCNWMMLVRPALEPGHQNLTAYQHGSDVYFTTSKDIPAGTELRVWYAAFYAKKMDKPMLKQACSSVQAAGTPEPSVSVEPERGQWVCKVCSNTFLELQLLNEHLLGHLEQAKSLPAGGQQHEAASEKEPDAPRMEPPTAAESKSIQSVMVTKEPKKKPRRGRKPKASKVEQPLVIIKDKEPS...
2.1.1.-
null
cell fate commitment [GO:0045165]; methylation [GO:0032259]; negative regulation of MAPK cascade [GO:0043409]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of stem cell division [GO:2000035]; regulation of transcr...
cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleus [GO:0005634]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific...
PF21549;PF00096;PF13894;
3.30.160.60;2.170.270.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28740264}.
null
null
null
null
null
FUNCTION: Sequence-specific DNA-binding transcriptional regulator. Plays a role as a molecular node in a transcriptional network regulating embryonic development and cell fate decision. Stimulates the expression of upstream key transcriptional activators and repressors of the Wnt/beta-catenin and MAPK/ERK pathways, res...
Mus musculus (Mouse)
E9Q8T7
DYH1_MOUSE
MEECNKEGPSSSSQGPGYCPVKVPESHDLEKILQESNYHPERNPLNPDPKTPPLPLTDLRQPRKSPLTGTDKKYPLMKQRGFYSDILSPGTLDKLGNVCCGPYMSQNLIRQADLDKFTPKVDSFVIPEDFQERVEQQIIGATTRLLTQTDFPLQSYEPKVQVPFQVLPGQCPRKIEIERRKQQYLRLDIEQLLTSEGIDSNKLMPRHPDLQHPQTIEQGRDPLFPIYLPLKVFDNEEFDCRTPTEWLNMGLEPGSQNRKPVPGKALLPTDDDLGHEDPKNQELDYRWCEVGVLDYDEEKKLYLVQKTDKRGLVRDEMGMP...
null
null
cilium movement involved in cell motility [GO:0060294]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; flagellated sperm motility [GO:0030317]; inner dynein arm assembly [GO:0036159]; sperm axoneme assembly [GO:0007288]
extracellular region [GO:0005576]; inner dynein arm [GO:0036156]; microtubule [GO:0005874]; sperm flagellum [GO:0036126]
ATP binding [GO:0005524]; dynein intermediate chain binding [GO:0045505]; dynein light intermediate chain binding [GO:0051959]; microtubule motor activity [GO:0003777]; minus-end-directed microtubule motor activity [GO:0008569]
PF12774;PF12775;PF12780;PF12781;PF17857;PF18198;PF08393;PF17852;PF18199;PF03028;PF12777;
1.10.287.2620;1.10.472.130;1.10.8.1220;1.10.8.710;1.20.1270.280;1.20.58.1120;1.20.920.20;1.20.920.30;3.10.490.20;6.10.140.1060;1.20.140.100;3.20.180.20;3.40.50.300;1.10.8.720;
Dynein heavy chain family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9P2D7}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:11371505}.
null
null
null
null
null
FUNCTION: Force generating protein of cilia required for sperm flagellum motility (PubMed:11371505). Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP (By similarity). Required in spermatozoa for the formation of the...
Mus musculus (Mouse)
E9Q912
GDS1_MOUSE
MDNLSDTLKKLKITAADRTEGSLEGCLDCLLQALAQNNAETSEKIQGSGILQLFANLLTPQASCTAKVADIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDSHEGRSAVDQAGGAQIVIDHLRSLCGRTDPASEKLMTVFCGMLMNYSNENDSLQAQLISMGVIPTLVKLLGIHCHNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDKREMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSNKEDDVAELKTASDLMVLLLLGDESMQKLFEGGKGSVFQR...
null
null
angiotensin-activated signaling pathway involved in heart process [GO:0086098]; CAAX-box protein maturation [GO:0080120]; cardiac muscle hypertrophy [GO:0003300]; myosin filament assembly [GO:0031034]; negative regulation of endoplasmic reticulum calcium ion concentration [GO:0032471]; positive regulation of mitochondr...
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
GTPase regulator activity [GO:0030695]; guanyl-nucleotide exchange factor activity [GO:0005085]
PF00514;
1.25.10.10;
null
PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000250|UniProtKB:O55143}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P52306}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P52306}. Mitochondrion {ECO:0000250|UniProtKB:P52306}. Nucleus {ECO:0000250|UniProtKB:P52306}. Note=Nuclear import is dependent on complexing with a GTPase containing a C-terminal polybasic region. {ECO...
null
null
null
null
null
FUNCTION: Acts as a GEF (guanine nucleotide exchange factor) for the Rho family of small GTP-binding proteins (G proteins) that stimulates the dissociation of GDP to enable subsequent binding of GTP. Additionally, appears to chaperone the processing and/or trafficking of small GTPases containing a C-terminal polybasic ...
Mus musculus (Mouse)
E9Q956
MCMD2_MOUSE
METLQMKEAALVYLDRSGGLQKFIDDCKSYNDSKQSYAVYRFSILIDPCDVVELDADLGNHILHHPLKAARVFQSVCFVAVKTLSLIGQLQTETQINIVLKLTHLPALPSYTLDLCEFPLNYASQRFYMMQGIVIAMTTITKYTQGARFLCSDGVCPLSKGFQYVRVHVPGATESATVRNDFLCSLCSSSLQEDRKFRVLGDKQIVEIITTKMFHAFQGDSKNQPFRFQSLGIFLRDELVNKMKIGNEYKIIGIPVCVKTSQTALCVEANNITPHTAKVPLGISDNFRRLLSLTSSSCWKFTAMLANVFASQIVAPGTYN...
null
null
double-strand break repair involved in meiotic recombination [GO:1990918]; double-strand break repair via break-induced replication [GO:0000727]; late meiotic recombination nodule assembly [GO:0042140]; meiotic recombination nodule assembly [GO:0007146]; oogenesis [GO:0048477]; spermatogenesis [GO:0007283]; synaptonema...
null
ATP binding [GO:0005524]; DNA binding [GO:0003677]; single-stranded DNA helicase activity [GO:0017116]
PF17855;
3.40.50.300;
null
null
null
null
null
null
null
null
FUNCTION: Plays an important role in meiotic recombination and associated DNA double-strand break repair. {ECO:0000269|PubMed:27760146, ECO:0000269|PubMed:27986806}.
Mus musculus (Mouse)
E9Q9A9
OAS2_MOUSE
MGNWLTGNWSSDRSSGYSSGWSPGGSSGVPSGPVHKLEKSIQANLTPNENCLKQIAVSSVPSQKLEGYIQENLKPNRESLKQIDQAVDAIWDLLRSQIPVKEVAKGGSYGRETALRGCSDGTLVLFMDCFQQFQDQIKYQDAYLDVIELWLKIHEKKSVKHEHALVVQVSVPGQRILLQLLPVFNPLRSNENPSSCVYVDLKKSMDQVRASPGEFSDCFTTLQQRFFKKYPQRLKDLILLVKHWYEQCQEKWKTPPPQPLLYALELLTVYAWEQGCQAEDFDMAQGVRTVLRLIQRPTELCVYWTVNYNFEDETVRNILL...
2.7.7.84
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P29728};
defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; interleukin-27-mediated signaling pathway [GO:0070106]; negative regulation of viral genome replication [GO:0045071]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of tumor necrosis factor productio...
cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]
2'-5'-oligoadenylate synthetase activity [GO:0001730]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]
PF01909;PF10421;PF18144;
1.10.1410.20;3.30.460.10;
2-5A synthase family
PTM: Myristoylation is not essential for its activity. {ECO:0000250|UniProtKB:P29728}.; PTM: Glycosylated. Glycosylation is essential for its activity. {ECO:0000250|UniProtKB:P29728}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29728}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P29728}.
CATALYTIC ACTIVITY: Reaction=3 ATP = 5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 diphosphate; Xref=Rhea:RHEA:34407, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:67143; EC=2.7.7.84; Evidence={ECO:0000269|PubMed:15865429, ECO:0000269|PubMed:29117179};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for ATP {ECO:0000269|PubMed:15865429}; Note=kcat is 6.4 sec(-1) for ATP. {ECO:0000269|PubMed:15865429};
null
null
null
FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:12396720, PubMed:29117179). Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactiv...
Mus musculus (Mouse)
E9Q9D5
RBL2A_MOUSE
MAGDRNRHCELEQEKYDTHENVKIICLGDSAVGKSKLMERFLMDGFQPQQLSTYALTLYKHTATVDGKTILVDFWDTAGQERFQSMHASYYHKAHACIMVFDVQRKITYKNLGTWYAELREFRPEIPCILVANKIDADIQMTQKNFSFAKKFSLPLYFVSAADGTNVVKLFNDAIRLAVAYKESSQDFMDEVLQELENFKLEQKEEDTSGQEQSDTTKSPSPS
null
null
cilium assembly [GO:0060271]; flagellated sperm motility [GO:0030317]; intracellular protein transport [GO:0006886]; photoreceptor cell morphogenesis [GO:0008594]; regulation of exocytosis [GO:0017157]; single fertilization [GO:0007338]
endomembrane system [GO:0012505]; intraciliary transport particle B [GO:0030992]; sperm midpiece [GO:0097225]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]
PF00071;
3.40.50.300;
Small GTPase superfamily, Rab family
null
null
null
null
null
null
null
FUNCTION: Plays an essential role in male fertility, sperm intra-flagellar transport, and tail assembly. Binds, in a GTP-regulated manner, to a specific set of effector proteins including key proteins involved in cilia development and function and delivers them into the growing sperm tail. {ECO:0000269|PubMed:23055941}...
Mus musculus (Mouse)
E9Q9F6
CTSRD_MOUSE
MLVLMLAAAVATMVRAHTLCRVHTVRTGKVFKSNIQLQGDPLFYAFPNTFVLKNVCKADISVYLGQKVFLTIDNFESSLLPLTVPKSLAVGVPSITSAHFVSGSLVLFVISGKGYSYDYYENTWRKLEGISEPVSHISGDVCCFKGSFCLELSNNLFAYLRGGQIPGTNIYFSDNGGFSFQLMNTDKLSHLTGTLGGIFHLHSMSQVGVLMVENNLGTFHYMEYPLNHSMGIAFSYKNLLEVIMKPYQRGFMVLWNQKSILVSSNSGQIVEHVRLIDQKIFTDLDVEHANINIYSVASNAYELAFLVAEDHLYYGSQSYM...
null
null
flagellated sperm motility [GO:0030317]; sperm capacitation [GO:0048240]; spermatogenesis [GO:0007283]
CatSper complex [GO:0036128]; sperm principal piece [GO:0097228]
null
PF15020;
null
CATSPERD family
null
SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:34225353}; Single-pass type I membrane protein {ECO:0000255}. Note=Specifically located in the principal piece of sperm tail. {ECO:0000269|PubMed:21224844, ECO:0000269|PubMed:34225353}.
null
null
null
null
null
FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:34225353). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:21224844). Required for CATSPER1 stability before intraflagellar...
Mus musculus (Mouse)
E9Q9F7
CC146_MOUSE
MEYNSKDAEEETEDEEEGLKEAEGEEQEKEEVTATSETDDDQEDLPSVLVPTVNIREERLINLAETPAFLCLHELHSKGKLPGTRMAELKAKYTLLHDTVVSTQESEVQLLENAKRFTEQIQQQQVCLQQAEDFPNVFTTEVCKLREQLLKYQNEYTAAQEREYNIQYRLTSLTEEKSIILKEFEKIPKPGEIEKKTRLLKESTEELRKEVIQRRLEIKNLREDVVLKQKQLVREQKELEELMEYQVGLKDDVVHHQSVPVQITKEIEKMTRKKVETEKKNIVLESELKELSDSLKKLENKVNTLAEERDDIMKEVEGKR...
null
null
manchette assembly [GO:1905198]; sperm axoneme assembly [GO:0007288]; sperm flagellum assembly [GO:0120316]; spermatid development [GO:0007286]
centriole [GO:0005814]; centrosome [GO:0005813]; cytoskeleton [GO:0005856]; sperm connecting piece [GO:0097224]
null
null
null
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8IYE0}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:38038747}. Note=In sperm cells, localized to only one centriole identified as the mother centriole by co-staining with CEP164 (By sim...
null
null
null
null
null
FUNCTION: Essential for sperm flagellum biogenesis and male fertility. {ECO:0000269|PubMed:38038747}.
Mus musculus (Mouse)
E9Q9K5
TRDN_MOUSE
MTEITAEGNASTTTTVIDNKNGCIPKSPGKVLKRSVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVNDAVEETTDWIYGFFSLLSDIISSEGDEDDEDADEDIDKGEIEEPPLKRKEIHQEKAEKEEKPEKKIQTKASHREREKGKEKLKGEKPEKTATHKEKLEKKERPETKMMAKEDKKIKTKEKTEEKAKKEMKVGKQEKVKPTAAKAKETPKTPPKARKKDDKEMPAVHEQKDQYAFCRYMIDMFVHGDLKPGQSPVMPPPSLTPSKPALSTTALEEKEKEEKKKMEKKD...
null
null
cytoplasmic microtubule organization [GO:0031122]; endoplasmic reticulum membrane organization [GO:0090158]; establishment of localization in cell [GO:0051649]; heart contraction [GO:0060047]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of release of sequestered calcium ion into cytosol [GO:...
calcium channel complex [GO:0034704]; cytosol [GO:0005829]; junctional membrane complex [GO:0030314]; junctional sarcoplasmic reticulum membrane [GO:0014701]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; sarcoplasmic reticulum [GO:0016529]
signaling receptor binding [GO:0005102]
PF05279;
null
null
PTM: Phosphorylated by CaMK2. {ECO:0000250|UniProtKB:Q28820}.; PTM: N-glycosylated. {ECO:0000269|PubMed:19383796}.
SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11707337}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28820}.
null
null
null
null
null
FUNCTION: Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae...
Mus musculus (Mouse)
E9Q9M8
PWP2B_MOUSE
MEPRAGCRLPVRVEQVVNGALVVTVSCGERSFAGILLDCTKKSGLFGLSPSTLLPLADNSSAVSCHGQAPEEGTGEVMQLETGPLHPHHKDPEKDQPPKTAVSEPPPPLIPPVPAGNLPPFPPYFEGAPFPHPLWLRNTYQQWVPQPPPRTIKRTRRRLSRNRDPGRLILSTIRLRPRQVLCEKCKSTVSPQEASPSPLNTPKPRRRLGSGPDSEHRKPEEPEDSAVIATAAPRRSKREKREEDRVAGERVPRSPVIKISYSTPQGKGEVVKIPSRVHGSVEPFCPQQSLQNGSQDSEVSRDVEPRGGGDRPPSGSSASI...
null
null
chromatin remodeling [GO:0006338]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; regulation of cold-induced thermogenesis [GO:0120161]
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
NuRD complex binding [GO:0120325]
PF00855;
2.30.30.140;
null
PTM: Deubiquitinated by BRCC3; leading to its stabilization. {ECO:0000269|PubMed:34180153}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:34180153}.
null
null
null
null
null
FUNCTION: Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260). Competes with CHD4 and MBD3 for interaction with ...
Mus musculus (Mouse)
E9Q9R9
DLG5_MOUSE
MEPQRRELLAQCQQSLAQAMTEVEAVLGLLEAAGALSPGERRQLDEEAGGAKAELLLQLLLAKEQDHFQDLRAALEKTQPHLLPILYLNGVVGPPQSTEGAGSTYSVLSIMPSDSESSSSLSSVGTTGKAPSPPPLLTEQQANDTVENLSIQLRLMTRERNELRKRLAFATHGATFDKRPYHRLNPDYERLKIQCVRAMSDLQSLQNQHTNALKRCEEVAKETDFYHTLHSRLLSDQTQLKDDVDMLRRENGKLRRERNLLQQSWEDMKRLREEDQKEIGDLRAQQQQVLKHNGSSEILNKLYDTAMDKLEVVKKDYDAL...
null
null
apical protein localization [GO:0045176]; epithelial to mesenchymal transition [GO:0001837]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; maintenance of cell polarity [GO:0030011]; metanephric collecting duct d...
adherens junction [GO:0005912]; cell junction [GO:0030054]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]
beta-catenin binding [GO:0008013]; cytoskeletal protein binding [GO:0008092]
PF16610;PF00625;PF00595;PF04822;
2.30.42.10;1.10.533.10;3.40.50.300;2.30.30.40;
MAGUK family
null
SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:Q8TDM6}. Cell membrane {ECO:0000250|UniProtKB:Q8TDM6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8TDM6}. Postsynaptic density {ECO:0000269|PubMed:25232112}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:25644602}. Note=Localized at si...
null
null
null
null
null
FUNCTION: Acts as a regulator of the Hippo signaling pathway. Negatively regulates the Hippo signaling pathway by mediating the interaction of MARK3 with STK3/4, bringing them together to promote MARK3-dependent hyperphosphorylation and inactivation of STK3 kinase activity toward LATS1 (PubMed:28087714). Positively reg...
Mus musculus (Mouse)
E9Q9U0
U17PB_MOUSE
MVVALSFPEADPAMSPPSAPELHQDEAQVVEELAANGKHSLSWESPQGPGCGLQNTGNSCYLNAALQCLTHTPPLADYMLSQEHSQTCCSPEGCKMCAMEAHVTQSLLHTHSGDVMKPSQNLTSAFHKRKQEDAHEFLMFTLETMHESCLQVHRQSEPTSEDSSPIHDIFGGWWRSQIKCHHCQGTSYSYDPFLDIPLDISSVQSVKQALQDTEKAEELCGENSYYCGRCRQKKPASKTLKLYSAPKVLMLVLKRFSGSMGKKLDRKVSYPEFLDLKPYLSQPTGGPLPYALYAVLVHEGATCHSGHYFCCVKAGHGKWY...
3.4.19.12
null
proteolysis [GO:0006508]; regulation of apoptotic process [GO:0042981]
cytosol [GO:0005829]; nucleus [GO:0005634]
cysteine-type deubiquitinase activity [GO:0004843]
PF00443;
3.90.70.10;
Peptidase C19 family, USP17 subfamily
PTM: Ubiquitinated. {ECO:0000269|PubMed:14583620}.
null
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:14583620};
null
null
null
null
FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. {ECO:0000269|PubMed:14583620}.
Mus musculus (Mouse)
E9Q9W4
S27A6_MOUSE
MLLSWLTGLGAGLLSLHFLQKLLFPYFWDDFWYLLKVVRYGIQMEMYKLRGELVTVLDKFLSHTRKQPRKAFIIYEGDVYTYEDVDKRSNRIAHALLNHSSLKRGDVVALLMSNEPDFVHVWFGLAKLGCVVAFLNSNLRFDSLLHCINTCEPTAVVVGGDLLGSIEEILPSLPKHVRVWGMKDSVPEGIDSLQEKLSLASDEPVPPSHHVTSSLKSTCLYIFTSGTTGLPKAAVISQLQVLKGSVGLWAFGCTADDIIYITLPLYHSSGSLLGIGGCVELGATCVLKKKFSASQFWNDCKKYNVTVFQYIGELCRYLCK...
6.2.1.-; 6.2.1.15; 6.2.1.3
null
long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]
arachidonate-CoA ligase activity [GO:0047676]; fatty acid transmembrane transporter activity [GO:0015245]; long-chain fatty acid transporter activity [GO:0005324]; long-chain fatty acid-CoA ligase activity [GO:0004467]; nucleotide binding [GO:0000166]; oleate transmembrane transporter activity [GO:1901480]; very long-c...
PF00501;PF13193;
3.30.300.30;3.40.50.12780;
ATP-dependent AMP-binding enzyme family
null
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9Y2P4}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305|PubMed:15699031}; Multi-pass membrane protein {ECO:0000255}. Note=In heart is exclusively located on the sarcolemma in areas juxtaposed with small blood vessels where it ...
CATALYTIC ACTIVITY: Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879, ChEBI:CHEBI:28868; Evidence={ECO:0000250|UniProtKB:Q9Y2P4}; CATALYTIC ACTIVITY: Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256, ChEBI:CHEBI:7896; Evidence={ECO:0000250|UniProtKB:Q9Y2P4}; CATALYTIC ACTIVITY: R...
null
null
null
null
FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport at the plasma membrane (By similarity). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:1569...
Mus musculus (Mouse)
E9Q9W7
PDZD7_MOUSE
MARGFTVGFDPLGLGELSSGSLSSVSSRGHLGSDSGSTATRYLLRKQQRLLNGPSRGIRASSPMGRVILINSPIEANSDESDIIHAVRVEKSPSGRLGFSVRGGSEHGLGIFVSKVEEGSSAERAGLCVGDKITEVNGLSLESTTMGSAVRLLTSSSCLHMMVRRMGRVPGIKFSKEKTTWVDVVNRRLVVEKCSSTPSDRSSEDGVRRIVHLYTTSDDFCLGFNIRGGKEFGLGIYVSKVDHGGLAEENGIKVGDQVLAANGVRFDDISHSQAVEVLKGQTHIMLTIKETGRYPAYKEMVSEYCWLDRLSNGVLQQLSP...
null
null
auditory receptor cell development [GO:0060117]; auditory receptor cell stereocilium organization [GO:0060088]; detection of mechanical stimulus involved in sensory perception of sound [GO:0050910]; establishment of localization in cell [GO:0051649]; establishment of protein localization [GO:0045184]; inner ear recepto...
cilium [GO:0005929]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; stereocilia ankle link [GO:0002141]; stereocilia ankle link complex [GO:0002142]; stereocilium [GO:0032420]; stereocilium tip [GO:0032426]; USH2 complex [GO:1990696]
identical protein binding [GO:0042802]
PF00595;
1.20.1160.20;2.30.42.10;
null
null
SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q9H5P4}. Nucleus {ECO:0000250|UniProtKB:Q9H5P4}. Cell projection, stereocilium {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485}. Note=Localizes at the ankle region of the stereocilia. {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:27525485...
null
null
null
null
null
FUNCTION: In cochlear developing hair cells, essential in organizing the USH2 complex at stereocilia ankle links (PubMed:24334608). Blocks inhibition of adenylate cyclase activity mediated by ADGRV1 (PubMed:24962568). {ECO:0000269|PubMed:24334608, ECO:0000269|PubMed:24962568}.
Mus musculus (Mouse)
E9QA28
CEA16_MOUSE
MKMPLTWYSWFLLSAWILNTGAEISITPEPAQPAEGDNVTLVVHGLSGELLAYNWYAGPTLSLTFLVASYIVSTGDETPGPAHTGREAVRPDGSLDIHGALPGHTGTYILQTLNRQFQTEVGYGHMQVYEILAPPTVMANDTALVERRDTLRLVCSSPSPAEVRWFFNGDALPVAVRLGMSPDGRMLTRHGVRREEAGAYQCEVWNPVSVSRSEPLNLTVYFGPERVAILQDSTTRTGCTIKVDFNMSLTLWCVARSCPEPEYVWAFNGKALKNGQDHLNISSMTAAHEGTYTCIAKNSKTLLSGSASVVVKLSAAAVAM...
null
null
sensory perception of sound [GO:0007605]
extracellular space [GO:0005615]; stereocilium tip [GO:0032426]
identical protein binding [GO:0042802]
PF13927;PF07686;
2.60.40.10;
Immunoglobulin superfamily, CEA family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21368133}. Note=Localizes at the tip of cochlear outer hair cells and to the tectorial membrane. {ECO:0000269|PubMed:21368133}.
null
null
null
null
null
FUNCTION: Required for proper hearing, plays a role in maintaining the integrity of the tectorial membrane. {ECO:0000269|PubMed:25080593}.
Mus musculus (Mouse)
E9QA62
LMOD3_MOUSE
MSGHSRNSEQEDTLSEELDEDELLANLSPEELKELQSEMEVMAPDPHLPVGMIQKDQTDKAPTGNFNHKSLVDYMYLQKASRRMLEDERVPVSFVQSEKNTQNQREVGDKGIKNMPQFLKEKLNSEILAKKRESNGSNNVQEAEDDDEDEEEEEEDDEDEEEEEEDEEDDEGEEDEDGEQANREKNDAKEQIHNNPGTYQQLATKTAHEQKDTSETKEKGEKKIAKLDPKKLALDTSFLKVSARPSGNQTDLDGSLRRVRQNDPDMKELNLNNIENIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLREN...
null
null
actin filament organization [GO:0007015]; actin nucleation [GO:0045010]; muscle contraction [GO:0006936]; myofibril assembly [GO:0030239]; pointed-end actin filament capping [GO:0051694]; positive regulation of skeletal muscle fiber development [GO:0048743]; skeletal muscle fiber development [GO:0048741]; skeletal musc...
A band [GO:0031672]; cytoskeleton [GO:0005856]; M band [GO:0031430]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865]
actin monomer binding [GO:0003785]; tropomyosin binding [GO:0005523]
PF03250;
3.80.10.10;
Tropomodulin family
PTM: Ubiquitinated, leading to its degradation. Interaction with KLHL40 negatively regulates ubiquitination and degradation. {ECO:0000269|PubMed:24960163}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q0VAK6}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:24960163}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:Q0VAK6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q0VAK6}. Note=Highly expressed in nonstriated areas of developing ...
null
null
null
null
null
FUNCTION: Essential for the organization of sarcomeric actin thin filaments in skeletal muscle (PubMed:25774500, PubMed:26035871). Increases the rate of actin polymerization (By similarity). {ECO:0000250|UniProtKB:Q0VAK6, ECO:0000269|PubMed:26035871}.
Mus musculus (Mouse)
E9QAG8
ZN431_MOUSE
MVDALTYDDVYVNFTQEEWALLNPSQKSLYKDVMLETYRNLNAVGYNWEDSNIEEHCESSRRHGRHERNHTGEKPYEGIQYGEAFVHHSSLQMRKIIHTGEKRYKCNQCDKAYSRHSILQIHKRTHSGEKPYECNQCGKAFTQHSHLKIHMVTHTGEKPYKCDQCGKAFAFHSTLQVHKRTHTGEKPYECNQCSKAFAHHCHLRVHKRIHTGEKPYKCDQCGKAFVGQNDLKRHERVHTGEKPYKCNECGKAFVCNASLRTHKTTHTGVKPYECKQCTKSFASHGQLQKHERIHTGEKPYKCDQCGKAFASHDKFQKHER...
null
null
cell differentiation [GO:0030154]; negative regulation of DNA-binding transcription factor activity [GO:0043433]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF01352;PF00096;PF13894;PF13465;
6.10.140.140;3.30.160.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21177534}.
null
null
null
null
null
FUNCTION: Sequence-specific DNA binding transcriptional repressor. Represses target gene transcription by recruiting HDAC1 and HDAC2 histone deacetylases. Acts as a specific transcriptional repressor for PTCH1 during embryonic development. Required for osteoblast differentiation and sonic hedgehog/SHH signaling respons...
Mus musculus (Mouse)
E9QAM5
HELZ2_MOUSE
MASVGCSLRSASTSATNGPSLAGLCAKVDLYLGCSRCTQCLNESTYILREVEHTCPREILLARFKQAAESKIWRKVGRRPSFPTPMRYQVCHYYRPGLGCRRHWNRCTFARSPEEALVWTFELKNNLPRLKLKEAVQGTRAPDRLQTPADTIRAEFGGHFQLLCAICFTCCPPCLCPVDPRGHCPKHQICPTLLIHVIVEGLKRQFVEVRPLPQRRHPLNYCMYVGRGVPCRHGASRCEYAHSAVEMAVWKAEQLDGLQRGDLLTYPLFGENKWKASPNPNPPVTKLYCHACLVTCNSQEAFENHCSSLEHAQMVAFDQA...
3.1.13.1; 3.6.4.13
null
regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; P granule [GO:0043186]
5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; exoribonuclease II activity [GO:0008859]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
PF13086;PF13087;PF00773;
3.40.50.300;
DNA2/NAM7 helicase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYK8}.
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.13.1; Evidence={ECO:0000250|UniProtKB:Q9BYK8}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:...
null
null
null
null
FUNCTION: Can degrade highly structured RNAs through its concerted ATP-dependent RNA helicase and 3' to 5' exoribonuclease activities (By similarity). Shows a strong preference for pyrimidine over purine residues for its nuclease activity (By similarity). Acts as a transcriptional coactivator for a number of nuclear re...
Mus musculus (Mouse)
E9QAT4
SC16A_MOUSE
MQPPPQAVPSGVAGPPPAGNPRSMFWANSPYRKPANNAPVAPITRPLQPVTDPFAFNRQTLQNTPVGSSSKSSLPNLPGPALSVFSQWPGLPVTPTNAGDSSTGLHEPLSGTLSQPRADASLFPPASTPSSLPGLEVSRNAEADPSSGHEVQMLPHSAHYIPGVGPEQPLGGQMNDSGSGPDQPMNRHAPHDGAVTHAASPFLPQPQMPGQWGPAQGGPQPSYQHHSPYLEGPVQNMGLQAASLPHFPPPSSLHQGPGHESHAPQTFTPASLASGEGNEIVHQQSKNHPLSSFPPKHTFEQNSRIGNMWASPELKQNPGV...
null
null
autophagy [GO:0006914]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum organization [GO:0007029]; Golgi organization [GO:0007030]; Golgi to plasma membrane transport [GO:0006893]; protein exit from endoplasmic reticulum [GO:0032527]; protein localization to endoplasmic reticulum exit site [GO:0070973]; prote...
cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; organelle membrane [GO:0031090]; perinuclear region of cytoplasm [GO:0048471]
null
PF12932;PF12931;
1.25.40.1030;
SEC16 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein. Golgi apparatus membrane {ECO:0000250|UniProtKB:O15027}; Peripheral membrane protein {ECO:0000250|UniProtKB:O15027}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:27354378}. Cytoplasm, cytosol {ECO:0000...
null
null
null
null
null
FUNCTION: Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo tr...
Mus musculus (Mouse)
E9QAU8
ARK2C_MOUSE
MVLVHVGYLVLPVFGSVRNRGAPFQRSQHPHATSCRHFHLGPPQPQQLAPDFPLAHPVQSQPGLSAHMAPAHQHSGTLHQSLTPLPTLQFQDVTGPSFLPQALHQQYLLQQQLLEAQHRRLVSHPRRNQDRVSVHPHRLHPSFDFGHQLQTPQPRYLAEGTDWDLSVDAGLSPAQFQVRPIPQHYQHYLATPRMHHFPRNSSSTQMVVHEIRNYPYPQLHFLALQGLNPSRHTSAVRESYEELLQLEDRLGNVTRGAVQNTIERFTFPHKYKKRRPQDSKGKKDEGEESDTDEKCTICLSMLEDGEDVRRLPCMHLFHQL...
2.3.2.27
null
axonogenesis [GO:0007409]; forelimb morphogenesis [GO:0035136]; innervation [GO:0060384]; limb development [GO:0060173]; motor neuron axon guidance [GO:0008045]; muscle structure development [GO:0061061]; positive regulation of BMP signaling pathway [GO:0030513]; protein catabolic process [GO:0030163]; protein polyubiq...
nucleus [GO:0005634]; protein-containing complex [GO:0032991]
ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF13639;
3.30.40.10;
Arkadia family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23610558}.
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:23610558};
null
null
null
null
FUNCTION: E3 ubiquitin-protein ligase that acts as a regulator of motor axon elongation (PubMed:23610558). Required for efficient motor axon extension in the dorsal forelimb by enhancing the transcriptional responses of the SMAD1/SMAD5/SMAD8 effectors, which are activated downstream of BMP (PubMed:23610558). Acts by me...
Mus musculus (Mouse)
E9QBI7
OMA1_DANRE
MQQTCIRLVKLDMLSTLTRFRTHSAIRCCAQRLFHCRPSLFISARTYFIKIDSSSLPKLKGSVSFSASCVSLGSSRLGLCSSSFKTGAPAALRAPVVFQRTRGFHTSGRRRALPALPLLWMVLKPLQKIMAIILGRSIRKWWVALPANKKQLFREWSWRRRWHFLGAGTGLLFIASLFFFTHLDESPITGRTRLLVFSRKNFRELAQFNADAFMEEFKDSLIASSDPRHKVVEQVVQILAQRNQDIAEISAVPWTVHVVDSPTMNAFVLPNGEIFVFTGMLNAVTDIHQLTFILGHEMAHALIGHAAEQASLSHVVELLS...
3.4.24.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O75844}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:O75844};
diet induced thermogenesis [GO:0002024]; energy homeostasis [GO:0097009]; glucose metabolic process [GO:0006006]; HRI-mediated signaling [GO:0140468]; integrated stress response signaling [GO:0140467]; lipid metabolic process [GO:0006629]; mitochondrial protein processing [GO:0034982]; mitochondrial respiratory chain c...
mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
PF01435;
3.30.2010.10;
Peptidase M48 family
PTM: Autocatalytically cleaved in response to mitochondrial depolarization both at the N-terminus and C-terminus to generate the short active form (S-OMA1). The S-OMA1 form is unstable. {ECO:0000250|UniProtKB:Q9D8H7}.; PTM: May form a redox-dependent disulfide bond (By similarity). Exists in a semi-oxidized state and i...
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9D8H7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D8H7}.
null
null
null
null
null
FUNCTION: Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as opa1 and dele1 (By similarity). Involved in the fusion of the mitochondrial inner membranes b...
Danio rerio (Zebrafish) (Brachydanio rerio)
E9QDC5
HWA_DANRE
MSQLGSAVPSSNLPEGLPVSSLALLILVLIPCVLLLLLLNCLFVGYKLFRMTRRKRDRYGSEMSLMHSSYSTRQRITRFSDEPPVAPNRKTNYVSVSEPMLAPPITSSLTSSAERRATGQRAMFLRPDGATYAGSESLRVPHWRTSAPVLVQSSDSDMERVNTVPPNSPVLRVTPNGFSVPMTSLRRSSTMELESTSLDKIHVECESASIIPQENSCYVVSSSSSARGSGLDSDFGASAGVSLRILSMDSDGFPGSAWASALEWDYYDPSYVTQNHVPKHRPQAPPITTKQYWV
null
null
dorsal/ventral pattern formation [GO:0009953]; embryonic axis specification [GO:0000578]; positive regulation of Wnt signaling pathway involved in dorsal/ventral axis specification [GO:2000055]; protein destabilization [GO:0031648]; regulation of canonical Wnt signaling pathway [GO:0060828]
plasma membrane [GO:0005886]
null
null
null
Huluwa family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30467143}; Single-pass membrane protein {ECO:0000255}. Note=Enriched on the plasma membrane of blastomeres only in a small region in which the dorsal organizer will form. {ECO:0000269|PubMed:30467143}.
null
null
null
null
null
FUNCTION: Key maternal determinant of the dorsal organizer and body axis formation in vertebrates that acts by promoting stabilization of beta-catenin (ctnnb1) (PubMed:30467143). Localizes on the plasma membrane of the future dorsal blastomeres in early blastulas and binds to and promotes the tankyrase-mediated degrada...
Danio rerio (Zebrafish) (Brachydanio rerio)
E9QG68
UBP45_DANRE
MRLKDPFSLKTADMTKRSNKPKKPRDEDSSDEVGGLTCQHVSRAVDLSSVKKAVTGSLWSVCSDCLKERNVLEGETAGAHDILVCLKCGFQGCNQAEVQHSTKHQQAHHSDSHCITISLTTWKAWCFECKEELSTHCNKKALAQTLDFLQKQSAKATSGTSSKLIKLREEPAEYVDTQRGKSPVNSTLIPVKGINNLGNTCFFNAVMQNLSQTHMLNDLIQDVKEKGHKMKISPSTETNLGSLTVTLPSPEPLTSAMFLFLQSMKESGKGPVSPKILFNQLCQKAPRFKGYQQQDSQELLHYLLDSMRVEETKRIKAGIL...
3.4.19.12
null
cell migration [GO:0016477]; neural retina development [GO:0003407]; photoreceptor cell maintenance [GO:0045494]; proteolysis [GO:0006508]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; photoreceptor inner segment [GO:0001917]
cysteine-type deubiquitinase activity [GO:0004843]; zinc ion binding [GO:0008270]
PF00443;PF02148;
3.90.70.10;3.30.40.10;
Peptidase C19 family
null
SUBCELLULAR LOCATION: Photoreceptor inner segment {ECO:0000269|PubMed:30573563}. Cytoplasm {ECO:0000250|UniProtKB:Q70EL2}. Nucleus {ECO:0000250|UniProtKB:Q70EL2}.
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000250|UniProtKB:Q70EL2};
null
null
null
null
FUNCTION: Catalyzes the deubiquitination of SPDL1 (By similarity). Plays a role in the repair of UV-induced DNA damage via deubiquitination of ERCC1, promoting its recruitment to DNA damage sites (By similarity). May be involved in the maintenance of photoreceptor function (PubMed:30573563). May play a role in normal r...
Danio rerio (Zebrafish) (Brachydanio rerio)
E9QI36
HARS1_DANRE
MADKAQLQEAIKTQGEVVRKLKSEKASKEQIDEEVARLLQLKAQLGGDEGKHVFVLKTAKGTRDYNPKQMAIREKVFNIIINCFKRHGAETIDSPVFELKETLTGKYGEDSKLIYDLKDQGGELLSLRYDLTVPFARYLAMNKITNIKRYHIAKVYRRDNPAMTRGRYREFYQCDFDIAGQYDAMIPDAECLKLVYEILSELDLGDFRIKVNDRRILDGMFAICGVPDEKFRTICSTVDKLDKLAWEEVKKEMVNEKGLSEEVADRIRDYVSMQGGKDLAERLLQDPKLSQSKQACAGITDMKLLFSYLELFQITDKVVF...
6.1.1.21
null
histidyl-tRNA aminoacylation [GO:0006427]; mitochondrial translation [GO:0032543]; nematode larval development [GO:0002119]; regulation of vasculature development [GO:1901342]; sprouting angiogenesis [GO:0002040]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
ATP binding [GO:0005524]; histidine-tRNA ligase activity [GO:0004821]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]
PF03129;PF13393;PF00458;
3.40.50.800;1.10.287.10;
Class-II aminoacyl-tRNA synthetase family
null
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:28934368}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000269|PubMed:28934368}.
CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;...
null
null
null
null
FUNCTION: Catalyzes the aminoacylation of histidyl-tRNA. {ECO:0000250|UniProtKB:P12081}.
Danio rerio (Zebrafish) (Brachydanio rerio)
E9QJ30
KL40B_DANRE
MALPIDPMEEPRMYQQTLLQDGLYDLLESDMMVDCVLKIKDKEFPCHRLVLAACSSYFRAFFKSGVEESKQREIVLEDVEPGVMGIILKYLYTSNINVTEQNVQDIFALSNMLQIPSIFTVCVSFLQKRLSLSNCLAIFRLGLMLDCPRLAISARNFACERFQFITRDEEFLQLTPSELAAVLASDSLNVETEQDVFEALIKWVGHDQENRIGDLPDLLDCIRLRLVPRDYFVKNVEKHEWLSSNPEITKKLQLVKDAHAGKLPELKKTKNKKSPSEEGQKKGDEEEVEEEEEQEERLPGILNDNLRFGMFLRELIFLIN...
null
null
muscle structure development [GO:0061061]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein ubiquitination [GO:0031398]; skeletal muscle fiber development [GO:0048741]; skeletal muscle fiber differentiation [GO:0098528]; swimming [GO:0036268]
A band [GO:0031672]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; I band [GO:0031674]
null
PF07707;PF00651;PF01344;
1.25.40.420;2.120.10.80;
KLHL40 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000250|UniProtKB:Q9D783}. Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:Q9D783}.
null
null
null
null
null
FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex (By similarity). Required for skeletal muscle development (PubMed:23746549). {ECO:0000250|UniProtKB:Q9D783, ECO:0000269|PubMed:23746549}.
Danio rerio (Zebrafish) (Brachydanio rerio)
E9QJ73
CXR32_DANRE
MDNSTTAAEVSAPTDYDYNSTSYDDDNPYAAPCSLTETWNFLGRFAPVAYILVFILALVGNILVLCVIRRYRQSRHSPCSFSLTDTFLLHLAVSDLLLAATLPFFAVEWISEWVFGKVMCKITGALFSLNVYCGVLFLACISFDRYLAIVHAINISWRRKTCHAQLACAFIWVICLGLSMVDMHFRDLVEIPGMNRMVCQIVYSEQYSKQWQIGMQLVSMVLGFILPLLVMLYCYLHIFKALCHATRRQKRRSLRLIISLVIVFVISWAPYNALRMTDSLQMLGVIVKSCALNNVLDVGILVTESLGLAHCALNPLLYGL...
null
null
calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; chemokine-mediated signaling pathway [GO:0070098]; immune response [GO:0006955]; innate immune response [GO:0045087]; leukocyte migration involved in immune response [GO:0002522]; macrophage activation involved in immune response [GO:0002281]; macro...
external side of plasma membrane [GO:0009897]
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25573892}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Receptor for the C-X-C chemokines cxcl11.1 and cxcl11.6 (PubMed:25573892). Promotes macrophage chemotaxis to sites of bacterial infection (PubMed:20424185, PubMed:25573892). {ECO:0000269|PubMed:20424185, ECO:0000269|PubMed:25573892}.
Danio rerio (Zebrafish) (Brachydanio rerio)
E9QY26
CP51B_ASPFU
MGLIAFILDGICKHCSTQSTWVLVGIGLLSILAVSVIINVLQQLLFKNPHEPPVVFHWFPFIGSTISYGIDPYKFFFDCRAKYGDIFTFILLGKKTTVYLGTKGNDFILNGKLRDVCAEEVYSPLTTPVFGRHVVYDCPNAKLMEQKKFVKYGLTSDALRSYVPLITDEVESFVKNSPAFQGHKGVFDVCKTIAEITIYTASRSLQGKEVRSKFDSTFAELYHNLDMGFAPINFMLPWAPLPHNRKRDAAQRKLTETYMEIIKARRQAGSKKDSEDMVWNLMSCVYKNGTPVPDEEIAHMMIALLMAGQHSSSSTASWIV...
1.14.14.154
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:26269599};
bile acid biosynthetic process [GO:0006699]; cholesterol homeostasis [GO:0042632]; ergosterol biosynthetic process [GO:0006696]; methylation [GO:0032259]
endoplasmic reticulum membrane [GO:0005789]
heme binding [GO:0020037]; iron ion binding [GO:0005506]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; oxysterol 7-alpha-hydroxylase activity [GO:0008396]; steroid 7-alpha-hydroxylase activity [GO:0008387]; sterol 14-demethylase activity [GO:0008398]
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=a 14alpha-methyl steroid + 3 O2 + 3 reduced [NADPH--hemoprotein reductase] = a Delta(14) steroid + formate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:54028, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.8 uM for eburicol {ECO:0000269|PubMed:26269599}; KM=3.78 uM for obtusifoliol {ECO:0000269|PubMed:26269599};
PATHWAY: Steroid metabolism; ergosterol biosynthesis. {ECO:0000269|PubMed:18191972, ECO:0000269|PubMed:26269599, ECO:0000269|PubMed:28461309}.
null
null
FUNCTION: Sterol 14alpha-demethylase, encoded by cyp51A and cyp51B, that plays a critical role in the third module of ergosterol biosynthesis pathway, being ergosterol the major sterol component in fungal membranes that participates in a variety of functions (PubMed:18191972, PubMed:26269599, PubMed:26459890, PubMed:29...
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
E9QYP0
SIDA_ASPFU
MESVERKSESSYLGMRNMQPEQRLSLDPPRLRSTPQDELHDLLCVGFGPASLAIAIALHDALDPRLNKSASNIHAQPKICFLERQKQFAWHSGMLVPGSKMQISFIKDLATLRDPRSSFTFLNYLHQKGRLIHFTNLSTFLPARLEFEDYMRWCAQQFSDVVAYGEEVVEVIPGKSDPSSSVVDFFTVRSRNVETGEISARRTRKVVIAIGGTAKMPSGLPQDPRIIHSSKYCTTLPALLKDKSKPYNIAVLGSGQSAAEIFHDLQKRYPNSRTTLIMRDSAMRPSDDSPFVNEIFNPERVDKFYSQSAAERQRSLLADK...
1.14.13.196
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:22928747}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:22928747};
cellular response to iron ion starvation [GO:0010106]; ergosterol biosynthetic process [GO:0006696]; ferrichrome biosynthetic process [GO:0031169]; intracellular iron ion homeostasis [GO:0006879]; secondary metabolite biosynthetic process [GO:0044550]; siderophore biosynthetic process [GO:0019290]; siderophore-dependen...
null
iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP+ binding [GO:0070401]; ornithine N5-monooxygenase activity [GO:0031172]
PF13434;
3.50.50.60;
Lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family
null
null
CATALYTIC ACTIVITY: Reaction=L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine + NADP(+); Xref=Rhea:RHEA:41508, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78275; EC=1.14.13.196; Evidence={ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894}; C...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 mM for L-ornithine (in the presence of 1 mM NADH) {ECO:0000269|PubMed:20614882}; KM=1.7 mM for L-ornithine (in the presence of 1 mM NADPH) {ECO:0000269|PubMed:20614882}; KM=0.49 mM for L-ornithine (at 37 degrees Celsius) {ECO:0000269|PubMed:20650894}; KM=0.58 m...
PATHWAY: Siderophore biosynthesis; ferrichrome biosynthesis. {ECO:0000269|PubMed:15504822, ECO:0000269|PubMed:16113265, ECO:0000269|PubMed:17845073, ECO:0000269|PubMed:20614882, ECO:0000269|PubMed:20650894, ECO:0000269|PubMed:22465572}.
null
null
FUNCTION: L-ornithine N(5)-monooxygenase; part of the siderophore biosynthetic pathway (PubMed:15504822, PubMed:16113265, PubMed:17845073, PubMed:20614882, PubMed:20650894, PubMed:22465572). Aspergillus fumigatus produces four types of siderophores, low-molecular-mass iron chelators, including excreted fusarinine C (Fs...
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
E9R5S0
RHBA_ASPFU
MPAAPKQRKIAIVGSRSVGKSSLTVRFVEHHFVESYYPTIENTFSRIIKYNGQDFATEIVDTAGQDEYSILNSKHFIGIHGYIIVYSVASRQSFDMVRVIRDKILNHLGADHVPLVVVGNKSDLKSEQRQVSLDEGRQLGEEFQCAFTEASARLDYNVTKAFDLMIGEIEKSQNPSQPAGGSKCILM
3.6.5.-
null
asexual sporulation resulting in formation of a cellular spore [GO:0043936]; cellular response to nitrogen starvation [GO:0006995]; negative regulation of asexual sporulation resulting in formation of a cellular spore [GO:0043944]; small GTPase-mediated signal transduction [GO:0007264]
plasma membrane [GO:0005886]
GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
PF00071;
3.40.50.300;
Small GTPase superfamily, Rheb family
PTM: Farnesylation is important for efficiently activating mTORC1-mediated signaling. {ECO:0000250|UniProtKB:Q15382}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15382}; Lipid-anchor {ECO:0000250|UniProtKB:Q15382}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15382}.
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q15382}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:Q1538...
null
null
null
null
FUNCTION: Small GTPase that acts as an allosteric activator of the canonical TOR pathway, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12135576, PubMed:12704156). Plays a role in virulence ...
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
E9RAH5
GLIT_ASPFU
MSIGKLLSNGALLVDVLIIGAGPAGLSTATGLARQLHTAVVFDSGVYRNAKTQHMHNVLGWDHRNPAELRAAGRADLTTRYSTIQFQNSTIEAIRQVETNQLFEARDNEGHSWYGRKVVLATGVRDIPLDIEGYSECWANGIYHCLFCDGYEERGQETVGVLALGPIANPARALHLARMALRLSESVTIYTNGNEQLAKEIQQAAEESPVGASGLKFEARPIRRFEKGDVAKTVIVHLGESESKTEGFLVYNPQTEVNGPFAKQLALNMTEGGDILTTPPFYETSVPGVFAVGDCATPLKAVTPAVSMGSLAAGGLVAQL...
1.8.1.-
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:24446392}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:24446392};
cell redox homeostasis [GO:0045454]; cellular response to mycotoxin [GO:0036146]; gliotoxin biosynthetic process [GO:2001310]; mycotoxin biosynthetic process [GO:0043386]
null
flavin adenine dinucleotide binding [GO:0050660]; thioredoxin-disulfide reductase (NADP) activity [GO:0004791]
PF07992;
3.50.50.60;
Class-II pyridine nucleotide-disulfide oxidoreductase family
null
null
null
null
PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:20548963}.
null
null
FUNCTION: Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide (PubMed:15979823, PubMed:21612254). The first step in gliotoxin biosynthesis is the condensation o...
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
E9RBG1
ABCC_ASPFU
MSLLGTINPNINPERTVAGRGTQEEEGEIARVEHNHHNNAASVSTDETVLERSKEIGDEDVAVEEVTRLARQLTRQSTRFSTSGNVENPFLETKEDSTLNPLSPNFKAKNWMKNLLALSSRDPERYPKRVAGVAFKNLSVHGYGSPTDYQKDVFNSVLEVGTLVRRIMGTGKQKIQILRDFDGLVKSGEMLVVLGRPGSGCSTFLKTISGEMNGIYMDEKSYLNYQGISSKQMRKQFRGEAIYTAETDVHFPQLTVGDTLKFAALARAPRNRLPGVSREQYAVHMRDVVMAMLGLTHTMNTRVGNDFVRGVSGGERKRVS...
null
null
xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961]
plasma membrane [GO:0005886]
ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]
PF01061;PF19055;PF00005;PF14510;PF06422;
3.40.50.300;
ABC transporter superfamily, ABCG family, PDR (TC 3.A.1.205) subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24123268}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=ATP + fluconazole(in) + H2O = ADP + fluconazole(out) + H(+) + phosphate; Xref=Rhea:RHEA:61916, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:46081, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:32209680}; PhysiologicalDirection=left-to-right; Xre...
null
null
null
null
FUNCTION: Pleiotropic ABC efflux transporter that shows a strong substrate specificity for the azole class of drugs such as lotrimazole (CLT), fluconazole (FLC), itraconazole (ITC), ketoconazole (KTC), posaconazole (POS), tebuconazole (TEBZ), and voriconazole (VRC) (Probable) (PubMed:22509997, PubMed:23580559, PubMed:2...
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
E9RBR0
ABR2_ASPFU
MWYQSASLLGVAAVAQAATVHYSLDLTWETGSPNGVSREMIFVNGQFPGPAIILNEGDEAIIDVTNHLPFNTSIHFHGIEQKNTPWADGVVGLSQWAIQPGQSYTYQWRADTYGTYWYHAHDKAEIMDGLYGPVHIRPRPNRDSPFSMISDDPADIRAMKQAERNGKLVMLSDWDHLTGQEYMKAMEETGYDIFCSDSVLINGRGSVFCHDPEELTQMVPPPELAILNSSLTDKGCLPFVPPIQGNWEHHPDKVPPGLNEGCHPSTTQETIFTVDAAHQWASFHFISAASLKVLVVSIDEHPMYVYEVDGRYIEPQLAHS...
1.10.3.-
null
melanin biosynthetic process [GO:0042438]; pigment biosynthetic process [GO:0046148]
cell surface [GO:0009986]
copper ion binding [GO:0005507]; hydroquinone:oxygen oxidoreductase activity [GO:0052716]; oxidoreductase activity [GO:0016491]
PF00394;PF07731;PF07732;
2.60.40.420;
Multicopper oxidase family
null
SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:26972005}.
null
null
PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:10515939, ECO:0000269|PubMed:19156203}.
null
null
FUNCTION: Laccase; part of the gene cluster that mediates the biosynthesis of dihydroxynaphthalene (DHN)-melanin, a bluish-green pigment and a structural component of the conidial wall (PubMed:10515939, PubMed:14970241, PubMed:19156203). The first step of the pathway is the production of the heptaketide naphtopyrone YW...
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
E9RCK4
VEA_ASPFU
MATRPPLMPPANETESSVSRISREGKKITYKLSVMQQPERARACGAGAKSSADRRPVDPPPVVELRIFESDPNDDLHKTDITFAYNANFFLFATLETARPMAQGRLTGPPTCPVLTGVPVAGVAYLDRPQQAGYFIFPDLSVRHEGRYRLSFHLYEEIKDIKDADKDTPMPDLNSSTNLTKPSAPKAHLNFRLEVKSVPFTVYSAKKFPGLATSTSLSRIIAEQGCRVRIRRDVRMRRRGEKRTDDYDFDDERAFATRSDRYTTPDMYAANSAERARSTSISTTADTSFPYGSDAQRRPSAGDYGFQGAQPYQRSMPAAS...
null
null
asexual sporulation resulting in formation of a cellular spore [GO:0043936]; conidiophore development [GO:0070787]; negative regulation of conidiophore development [GO:0070794]; negative regulation of sexual sporulation resulting in formation of a cellular spore [GO:0043942]; positive regulation of asexual sporulation ...
cytoplasm [GO:0005737]; nucleus [GO:0005634]
null
PF11754;
2.60.40.3960;
Velvet family, VeA subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C8VTV4}. Cytoplasm {ECO:0000250|UniProtKB:C8VTV4}. Note=Enriched in the nucleus in the dark (By similarity). {ECO:0000250|UniProtKB:C8VTV4}.
null
null
null
null
null
FUNCTION: Component of the velvet transcription factor complex that controls sexual/asexual developmental ratio in response to light, promoting sexual development in the darkness while stimulating asexual sporulation under illumination (By similarity). The velvet complex hat acts as a global regulator for secondary met...
Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
F0JAI6
KEBAB_DROME
MSSMAKSPDMRTPGCCSPLRTKELLERQRSSRCTPAKGYLTPRNCQSPKHPEMRIPSIFVTDADYGLERPKQLLQRLERSLYRSSSASKVPPKHSLLASQNRQRTWEGPKTPEFRSRTNKTIPASEPRPRRAKELLEDLRSKHQGTPATKIPSQRNPKENQELSKSHTCIPSSEPQPIRPKLILERERQESITNRLASTSIDRLKTKPPRSSFTSSRLLVPQMGFSYPKDPKRLHESDKGIKLTTSKRKLDFKTELGTDWLRRELEKIGKEWRKKTDYQLRQLISGFVKQLVRLLPFNGITFSHLSRDCYVQQMVEALQQ...
null
null
null
kinetochore [GO:0000776]; perinuclear region of cytoplasm [GO:0048471]; spindle microtubule [GO:0005876]
kinetochore binding [GO:0043515]; microtubule binding [GO:0008017]
null
1.10.418.30;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21912673}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21912673}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:21912673}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:21912673}. Note=During metaphase expressed in the kinetochores. During anaph...
null
null
null
null
null
null
Drosophila melanogaster (Fruit fly)
F0NDL2
HELS_SULIR
MSLELEWMSIDDLKLPSNVIDIIKNRGIKKLNPPQTEAVKKGLLDGNRLLLTSPTGSGKTLIAEMGIISFLLKNGGKAIYVTPLRALTNEKYLTFKDWESIGFKVAMTSGDYDTDDAWLKNYDIIITTYEKLDSLWRHRPDWLNEANYFVLDELHYLNDPERGPVVESVTIRAKRRNLLALSATISNYKQIAKWLGAEPVATNWRPVPLMEGVMYPERKKKEYTILFRDNTTRKVHGDDAIIAYTLDSLSKNGQVLVFRNSRKMAESTALKIANYMNFVSLDEKAISEILNQLDDIEEGGSDEKELLKSLISKGVAYHHA...
5.6.2.3; 5.6.2.4
null
DNA repair [GO:0006281]
null
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; isomerase activity [GO:0016853]
PF00270;PF00271;PF21280;
1.10.3380.30;1.10.150.20;3.40.50.300;
Helicase family, Hel308 subfamily
null
null
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:29846688}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, Ch...
null
null
null
null
FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:29846688}.; FUNCTION: Has predominantly 3'-5' helicase activity but also a weak 5'-3' helicase activity (PubMed:29846688). Has the ability to unwind rep...
Sulfolobus islandicus (strain REY15A)
F0NHH1
ALBA1_SULIR
MSSGTPTPSNVVLIGKKPVMNYVLAALTLLNQGVSEIVIKARGRAISKAVDTVEIVRNRFLPDKIEIKEIRVGSQVVTSQDGRQSRVSTIEIAIRKK
3.1.-.-
null
chromosome condensation [GO:0030261]
chromosome [GO:0005694]; cytoplasm [GO:0005737]
double-stranded DNA binding [GO:0003690]; nuclease activity [GO:0004518]; RNA binding [GO:0003723]
PF01918;
3.30.110.20;
Histone-like Alba family
PTM: Acetylated (PubMed:29679495). Acetylation at Lys-16 by the Pat acetylase decreases DNA-binding affinity (By similarity). Deacetylation at Lys-16 by the CobB deacetylase increases DNA-binding affinity (By similarity). Acetylation at Ser-2 is involved in the regulation of the turnover of the protein (PubMed:29679495...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01122}. Chromosome {ECO:0000255|HAMAP-Rule:MF_01122}.
null
null
null
null
null
FUNCTION: Binds double-stranded DNA tightly but without sequence specificity (By similarity). Involved in DNA compaction (By similarity). Possesses DNA endonuclease activity (By similarity). Prevents transcription after DNA binding (By similarity). Binds single-stranded DNA and RNA in vitro (By similarity). Binds rRNA ...
Sulfolobus islandicus (strain REY15A)
F0NID4
PINA_SULIR
MNDLMLDKSALLFGVSKYLEKGIITGNVLIHKSLLAELERESNDGLVSAEIALDEVKKLKDITERILVNFEIVGDDSKKGEANELSREYCLEKGCIIVTADETQKKICDAMGIQYNFLQPLKQGLSFESFFDDETMSLHIKEDTVPRAKKGKPGNWKFVNLSDKPMLSTDVRMIANEIINAVRLIKGSFVEIERRGSLIIQLGNYRVVITRPPLSDGWEITITRPVVRKRLEDYNLDERLIKRLEERAEGIIIAGAPGMGKTTFAQALAEYYMRLGKIVKTIESPRDMHLPPEITQYSKNYAEIGELHDILLLSRPDYTV...
3.6.4.12
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:28238763}; Note=Ca(2+) stimulates ATPase activity more than Mn(2+) or Mg(2+). {ECO:0000269|PubMed:28238763};
DNA recombination [GO:0006310]; DNA repair [GO:0006281]
null
ATP binding [GO:0005524]; DNA binding [GO:0003677]; four-way junction helicase activity [GO:0009378]; hydrolase activity [GO:0016787]
PF00437;
3.40.50.1010;3.40.50.300;
null
null
null
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:28238763};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0 for ATPase activity. {ECO:0000269|PubMed:28238763};
null
FUNCTION: Promotes Holliday junction (HJ) branch migration and unwinds Y-shaped DNA (but not replication forks or dsDNA) in an ATP hydrolysis-dependent manner (PubMed:28238763). Stimulates cleavage by HJ resolvase Hjc (PubMed:28238763). Unwinds Y-shaped and 3'-flap DNA substrates. In the absence of other proteins stabi...
Sulfolobus islandicus (strain REY15A)
F0T4D1
KDTA_CHLP6
MIKGRRTKLHTFLYDCFLIFAFMVGLPRILYKRFVHGKYTKSLGIRFGFKKPEVPGTGPVAWFHGASVGETALLLPLLKRFMKEYPEWRCVVTSCTESGHENAHRLFGPLGVTTFILPLDLSIIIKPVVRAISPSLLVFSEGDCWLNFIEEAKRLGATAVIINGKLSANSCKRFTILKRFGRNYFSPVDGFLLQDEQHKARFLQLGVDKEKIQVTGNIKTYTETLSENNQRDYWREKLQLAQDTELLVLGSVHPKDVEVWLPVVRELRRNLKVLWVPRHIERSKELEALLSKENISYGLWSKEATFAQHDAIIVDAIGWL...
2.4.99.12; 2.4.99.13; 2.4.99.14; 2.4.99.15
null
lipid A biosynthetic process [GO:0009245]; lipopolysaccharide core region biosynthetic process [GO:0009244]
plasma membrane [GO:0005886]
Kdo transferase activity [GO:0043842]
PF04413;
3.40.50.11720;3.40.50.2000;
Glycosyltransferase group 1 family, Glycosyltransferase 30 subfamily
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+); Xref=Rhea:RHEA:28066, ChEBI:CHEBI:15378, ChEBI:CHEBI:58603, ChEBI:CHEBI:60364, ChEBI:CHEBI:60377, ChEBI:CHEBI:85987; EC=2.4.99.12; Evidence={ECO:0000269|PubMed:10951204, ECO:0000...
null
PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
null
null
FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of predominantly four 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A. Thus generates the genus-specific LPS epitope of Chlamydia, composed of the...
Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia psittaci)
F1C7I4
MDHC_TAESO
MPGPLRVLITGAAGQIAYNLSNMVANGNLFGKDQKIILHLLDIPEAKTVLEGVVMELQDCAFTVLEGIVPTHCLKEAFTDIDVALMVGAMPRKQGMERRDLLSSNVKIFKDQGEALEKYAKKTVKVLVVGNPANTNCLIMSKYAPSIPKENFTALSRLDHNRAIYQVAAKVGVPSECVKNVCIWGNHSNKQFPDLAHAVVTKGGKQHPAKELINDEKWVKEVFTPCVQNRGAAVIGLRKLSSAASAAKAIVDQMHDWWFGTKEGEWVSMSVYSTGEHYGAPKDIYFSFPVTIKNGHYKVVDGLAMDEWGKGLFKITADEL...
1.1.1.37
null
malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
L-malate dehydrogenase activity [GO:0030060]; NAD binding [GO:0051287]; protein homodimerization activity [GO:0042803]
PF02866;PF00056;
3.90.110.10;3.40.50.720;
LDH/MDH superfamily, MDH type 2 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19277715}.
CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000269|PubMed:19277715, ECO:0000269|PubMed:21439955};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=100 uM for L-malate (at pH 9.6) {ECO:0000269|PubMed:21439955}; KM=42 uM for NAD (at pH 9.6) {ECO:0000269|PubMed:21439955}; KM=44 uM for oxaloacetate (at pH 8) {ECO:0000269|PubMed:21439955}; KM=167 uM for NADH (at pH 8) {ECO:0000269|PubMed:21439955}; KM=215 uM for L...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.6 for oxaloacetate reduction and 9.6 for malate oxidation (PubMed:19277715, PubMed:21439955). Stable between pH 6.8-8.5 for the forward reaction (PubMed:19277715). {ECO:0000269|PubMed:19277715, ECO:0000269|PubMed:21439955};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Has highest activity between 5-40 degrees Celsius. No activity at 60 degrees Celsius. {ECO:0000269|PubMed:21439955};
FUNCTION: Malate dehydrogenase. Has no activity with NADPH as substrate. Does not show lactate dehydrogenase activity. {ECO:0000269|PubMed:21439955}.
Taenia solium (Pork tapeworm)
F1CKI6
3CAR1_PICSI
MSVISIVPLASKPCLYKSFISSTHEPKALRRPISTVGLCRRAKSVTASMSMSSSTALSDDGVQRRIGNHHSNLWDDNFIQSLSSPYGASSYAERAERLIGEVKEIFNRISMANGELVSHVDDLLQHLSMVDNVERLGIDRHFQTEIKVSLDYVYSYWSEKGIGPGRDIVCADLNTTALGFRLLRLHGYTMFPDVFEQFKDQMGRIACSTNQTERQISSILNLFRASLIAFPWEKVMEEAEIFSTAYLKEALQTIPVSSLSREIQYVLDYRWHSDLPRLETRTYIDILRENATNETLDMKTEKLLELAKVEFNIFNSLQQN...
4.2.3.107
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7}; Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:A0A1C9J6A7};
gibberellin biosynthetic process [GO:0009686]; green leaf volatile biosynthetic process [GO:0010597]; monoterpene biosynthetic process [GO:0043693]; monoterpenoid biosynthetic process [GO:0016099]; response to jasmonic acid [GO:0009753]
chloroplast [GO:0009507]
lyase activity [GO:0016829]; magnesium ion binding [GO:0000287]; terpene synthase activity [GO:0010333]
PF01397;PF03936;
1.10.600.10;1.50.10.130;
Terpene synthase family, Tpsd subfamily
null
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate = (+)-car-3-ene + diphosphate; Xref=Rhea:RHEA:32539, ChEBI:CHEBI:7, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.107; Evidence={ECO:0000269|PubMed:21323772};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6.88 uM for geranyl diphosphate {ECO:0000269|PubMed:21323772}; Vmax=32.1 pmol/sec/ug enzyme with geranyl diphosphate as substrate {ECO:0000269|PubMed:21323772}; Note=kcat is 2.21 sec(-1) with geranyl diphosphate as substrate. {ECO:0000269|PubMed:21323772};
PATHWAY: Terpene metabolism; oleoresin biosynthesis. {ECO:0000269|PubMed:21323772}.
null
null
FUNCTION: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores (e.g. insect attack by white pine weevil P.strobi) and pathogens (PubMed:21323...
Picea sitchensis (Sitka spruce) (Pinus sitchensis)
F1CMX0
KSHA1_RHORH
MSLGTSEQSEIREIVAGSAPARFARGWHCLGLAKDFKDGKPHSVHAFGTKLVVWADSNDEIRILDAYCRHMGGDLSQGTVKGDEIACPFHDWRWGGNGRCKNIPYARRVPPIAKTRAWHTLDQDGLLFVWHDPQGNPPPADVTIPRIAGATSDEWTDWVWYTTEVDTNCREIIDNIVDMAHFFYVHYSFPVYFKNVFEGHVASQFMRGQAREDTRPHANGQPKMIGSRSDASYFGPSFMIDDLVYEYEGYDVESVLINCHYPVSQDKFVLMYGMIVKKSDRLEGEKALQTAQQFGNFIAKGFEQDIEIWRNKTRIDNPLL...
1.14.15.30
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|...
cholesterol metabolic process [GO:0008203]; lipid catabolic process [GO:0016042]
null
2 iron, 2 sulfur cluster binding [GO:0051537]; 3-ketosteroid 9-alpha-monooxygenase activity [GO:0036200]; iron ion binding [GO:0005506]
PF19298;PF00355;
2.102.10.10;
null
null
null
CATALYTIC ACTIVITY: Reaction=androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:32199, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, Ch...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for 1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=2 uM for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=2.2 uM for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius...
null
null
null
FUNCTION: May be involved in the degradation of cholic acid, a steroid acid found predominantly in the bile (PubMed:21642460). In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androste...
Rhodococcus rhodochrous
F1CMY8
KSHA5_RHORH
MSIDTARSGSDDDVEIREIQAAAAPTRFARGWHCLGLLRDFQDGKPHSIEAFGTKLVVFADSKGQLNVLDAYCRHMGGDLSRGEVKGDSIACPFHDWRWNGKGKCTDIPYARRVPPIAKTRAWTTLERNGQLYVWNDPQGNPPPEDVTIPEIAGYGTDEWTDWSWKSLRIKGSHCREIVDNVVDMAHFFYIHYSFPRYFKNVFEGHTATQYMHSTGREDVISGTNYDDPNAELRSEATYFGPSYMIDWLESDANGQTIETILINCHYPVSNNEFVLQYGAIVKKLPGVSDEIAAGMAEQFAEGVQLGFEQDVEIWKNKAP...
1.14.15.30
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628, ECO:0000269|PubMed:25049233}; COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|...
cholesterol catabolic process [GO:0006707]
null
2 iron, 2 sulfur cluster binding [GO:0051537]; 3-ketosteroid 9-alpha-monooxygenase activity [GO:0036200]; iron ion binding [GO:0005506]
PF19298;PF00355;
2.102.10.10;
null
null
null
CATALYTIC ACTIVITY: Reaction=androsta-1,4-diene-3,17-dione + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:32199, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, Ch...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 uM for 1,4-BNC as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=0.5 uM for testosterone as substrate (at pH 7.0 and 22 degrees Celsius) {ECO:0000269|PubMed:25049233}; KM=0.8 uM for AD as substrate (at pH 7.0 and 22 degrees Celsi...
PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:25049233}.
null
null
FUNCTION: Probably involved in the degradation of cholesterol (PubMed:21642460). In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-...
Rhodococcus rhodochrous
F1DBA9
MPAC_PENBR
MNFHKGQPKEDLRVLFGPQCPDITDSITHIRDAISKDPTGLGFLTNILDELPSLWPTIAGAWPALKNVEGESQLLALGRLFEHESEDRVEASNLMMTPITVMRHIVDFWNLQDVATHPAFPSSSLSETEMPRIVDTQGFCVGLLAAIAVACSRNTQEFQYVASNAIRLSLCVGALVDLDEILCGSTTSLAVSAERVKQEIHDHGLRTKQLSLRGRFHHEAHREGIQHIMKLCTNDSRFKLPRSDALLTPLRSSQGGEIFQQEALLHTVALDSILCAKANWYDVVSALINSTEMTVDQSHLLSIGPEEFVPRSARSRSVAR...
2.3.1.-
null
fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; mycophenolic acid biosynthetic process [GO:0140722]; proteolysis [GO:0006508]; terpenoid biosynthetic process [GO:0016114]
cytosol [GO:0005829]
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; phosphopantetheine binding [GO:0031177]; serine-type peptidase activity [GO:0008236]
PF00698;PF20434;PF18558;PF00109;PF02801;PF08242;PF00326;PF21089;PF00550;PF14765;PF16073;
3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.10.129.110;3.40.50.150;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:A0A0B5KU17}.
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + 3 malonyl-CoA + S-adenosyl-L-methionine = 5-methylorsellinate + 3 CO2 + 4 CoA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:63056, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHE...
null
PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis. {ECO:0000269|PubMed:21398490}.
null
null
FUNCTION: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of mycophenolic acid (MPA), the first isolated antibiotic natural product in the world obtained from a culture of Penicillium brevicompactum in 1893 (PubMed:21398490, PubMed:21398493). MpaC catalyzes the synthesis of 5-m...
Penicillium brevicompactum
F1LM81
TM1L1_RAT
MAFGKSHRDPYATSLGHLIEKATFAGVQTEDWGQFMHICDIINTTQDGPKDAVKALKKRISKNYNHKEIQLSLSLIDMCMQNCGPSFQSLIVKKEFVKDTLVKLLNPRYTLPLETQNRILSFIKMWSQGFPGGVDVSEVKEVYLDLLKKGVQFPPLDGEPETKQEAGQISPSRPTSVPTAPALSSIIAPKNPTISLVPEQIGKLHSELDMVKMNVKVMTAILMENTPGSENHEDIELLRKLYKTGREMQERIMDLLVVVENEDVTVELIQVNEDLNNAILGYERFTRNQQRLLEQKRNPTEANQTSSEPSAPSCDLLNLG...
null
null
negative regulation of mitotic nuclear division [GO:0045839]; positive regulation of protein autophosphorylation [GO:0031954]; protein transport [GO:0015031]; signal transduction [GO:0007165]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; endosome membrane [GO:0010008]; Golgi stack [GO:0005795]; membrane [GO:0016020]
clathrin binding [GO:0030276]; phosphatidylinositol binding [GO:0035091]; protein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; ubiquitin binding [GO:0043130]
PF03127;PF00790;
1.20.58.160;1.25.40.90;
TOM1 family
PTM: Phosphorylated on tyrosines by FYN and LYN. {ECO:0000269|PubMed:17977829}.
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack {ECO:0000250}. Endosome membrane {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:17977829}. Membrane {ECO:0000269|PubMed:17977829}; Peripheral membrane protein {ECO:0000269|PubMed:17977829}; Cytoplasmic side {ECO:0000269|PubMed:17977829}. Note=A small proportion is membra...
null
null
null
null
null
FUNCTION: Probable adapter protein involved in signaling pathways. Interacts with the SH2 and SH3 domains of various signaling proteins when it is phosphorylated. May promote FYN activation, possibly by disrupting intramolecular SH3-dependent interactions (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
F1LM93
YES_RAT
MGCIKSKENKSPAIKYTPENPTEPVNTSAGHYGVEHATAATTSSTKGASANFNSLSMTPFGGSSGVTPFGGASSSFSVVPSSYPTSLTGGVTIFVALYDYEARTTEDLSFKKGERFQIINNTEGDWWEARSIATGKNGYIPSNYVAPADSIQAEEWYFGKMGRKDAERLLLNPGNQRGIFLVRESETTKGAYSLSIRDWDEVRGDNVKHYKIRKLDNGGYYITTRAQFDTLQKLVKHYTEHADGLCHKLTTVCPTVKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTKVAIKTLKPGTMMPEAFLQEAQ...
2.7.10.2
null
cell differentiation [GO:0030154]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; positive regulatio...
actin filament [GO:0005884]; centrosome [GO:0005813]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; postsynaptic specialization, intracellular component [GO:0099091]
ATP binding [GO:0005524]; enzyme binding [GO:0019899]; epidermal growth factor receptor binding [GO:0005154]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102]; transme...
PF07714;PF00017;PF00018;
3.30.505.10;2.30.30.40;1.10.510.10;
null
PTM: Phosphorylation by CSK on the C-terminal tail maintains the enzyme in an inactive state. Autophosphorylation at Tyr-424 maintains enzyme activity by blocking CSK-mediated inhibition (By similarity). {ECO:0000250}.; PTM: Palmitoylation at Cys-3 promotes membrane localization. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1709169}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytosol {ECO:0000269|PubMed:1709169}. Note=Newly synthesized protein initially accumulates in the Golgi region and traffics to the plasma membrane through the ex...
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100...
null
null
null
null
FUNCTION: Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphoryl...
Rattus norvegicus (Rat)
F1LMN3
E2F8_RAT
MENQKENLFSEPHKRGLVKSPLQESSKANVVLAEIQPDLGPLTTPTKPKEVSQGEPWTPTANLKMLISAVSPEIRSRDQKRGLSDNRSGLPEARDCLHEPQAKTNEKSQPSRKEKSLGLLCHKFLARYPKYPNPAVNNDICLDEVAEELDVERRRIYDIVNVLESLHMVSRLAKNRYTWHGRHNLTKTLGTLKSVGEENKYAEQIMMIKRKEHEQEFDFIKSCGLEDHHVIKSTAGQNGHSDMCFVELPGVEFRAASANSRKDKSLRVMSQKFVMLFLVSTPQIVSLEIAAKILIGEDHVEDLDKSKFKTKIRRLYDIAN...
null
null
cell cycle comprising mitosis without cytokinesis [GO:0033301]; chorionic trophoblast cell differentiation [GO:0060718]; fibroblast proliferation [GO:0048144]; hepatocyte differentiation [GO:0070365]; negative regulation of cytokinesis [GO:0032466]; negative regulation of transcription by RNA polymerase II [GO:0000122]...
nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; DNA-binding transcription rep...
PF02319;
1.10.10.10;
E2F/DP family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Atypical E2F transcription factor that participates in various processes such as angiogenesis and polyploidization of specialized cells. Mainly acts as a transcription repressor that binds DNA independently of DP proteins and specifically recognizes the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represse...
Rattus norvegicus (Rat)
F1LMV6
DESP_RAT
MSCNGGSHPRINTLGRMTRAESGPDLRYEMTYSGGGGGGGGGGGGTSRMYYSRRCTVNDQNSDGYCQTGTMSRHQNQNTIQELLQNCADCLMRAELIAQPELKFGEGIQLAWNRELDEYFTQANDQMEIIDGLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISAPRVRRASSKGGYTCQSGSGWDEFTKRLTGECLGWMRQQRAEMDLMAWGVDSGSVEQHINSHRSIHNAIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSDKNTNIAQKQEAFS...
null
null
adherens junction organization [GO:0034332]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell-cell adhesion [GO:0098609]; desmosome organization [GO:0002934]; epithelial cell-cell adhesion [GO:0090136]; intermediate filament cytoskeleton organization [GO:0045104]; intermedi...
adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; fascia adherens [GO:0005916]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886]
protein kinase C binding [GO:0005080]; scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198]
PF00681;PF17902;PF18373;PF21019;
1.20.58.1060;1.20.58.60;3.30.160.780;3.90.1290.10;2.30.30.40;
Plakin or cytolinker family
null
SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:P15924}. Cell membrane {ECO:0000250|UniProtKB:E9Q557}. Note=Localizes at the intercalated disk in cardiomyocytes. {ECO:0000250|UniProtKB:E9Q557}.
null
null
null
null
null
FUNCTION: Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (PubMed:26858265). {ECO:0000269|PubMed:26858265}.
Rattus norvegicus (Rat)
F1LMY4
RYR1_RAT
MGDGGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFILEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSCCEEGFVTGGHVLRLFHGHMDECLTISPSDSDDQRRLVYYEGGPVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALTEDQGLVVVDASKAHTKATSFCFRIS...
null
null
calcium ion transport [GO:0006816]; cellular response to ATP [GO:0071318]; cellular response to caffeine [GO:0071313]; cellular response to calcium ion [GO:0071277]; muscle contraction [GO:0006936]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; ossification involved in ...
calcium channel complex [GO:0034704]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; I band [GO:0031674]; junctional membrane complex [GO:0030314]; membrane [GO:0016020]; organelle membrane [GO:...
ATP binding [GO:0005524]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; protease binding [GO:0002020]; ryanodine-sensitive calcium-release channel activity [GO:0005219]; voltag...
PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622;
1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;6.20.350.10;1.25.10.30;
Ryanodine receptor (TC 1.A.3.1) family
PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2840 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2840. {ECO:0000250|UniProtKB:P21817}.; PTM: Activated by reversible S-nitrosylation (By similarity). Repeated very high-level exercise incr...
SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11316255}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P11716}. Note=The number of predicted transmembrane domains varies between orthologs. Both N-terminus and C-terminus are cytoplasmic. {ECO:0000250|UniProtKB:P11716}.
CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:11316255};
null
null
null
null
FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:11316255). Repeated very high-level exercise increases the open probabili...
Rattus norvegicus (Rat)
F1LN46
CPT1C_RAT
MAEAHQASSLLSSLSSDGAEVELSSSVWQEIYLSALRSWKRNLWRVWNDFLAGVVPATPLSWLFLFSTIQLACLLQLDPSLGLMEKIKELLPDWGGQHHQLQGLLAAAVFASCLWGTLIFTLHVALRLLLSHHGWLLEPHGTMSSPTKTWLALVRIFSGRHPRLFSFQRALPRQPVPGAQETVRKYLESMRPVLRDDAFDSVVALANDFLRLQAPRLQLYLQLKSWCASNYVSDWWEEFVYLRSRGSLVNSTYYMMDFLYVTPTPLQAARAGNAVHTLLLYRHLLNRQEIPPTLLMGMRPLCSAQYERMFNTTRIPGVEK...
3.1.2.22
null
carnitine metabolic process [GO:0009437]; fatty acid metabolic process [GO:0006631]; regulation of postsynaptic membrane neurotransmitter receptor levels [GO:0099072]
AMPA glutamate receptor complex [GO:0032281]; axon [GO:0030424]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; postsynapse [GO:0098794]
carnitine O-palmitoyltransferase activity [GO:0004095]; palmitoyl-(protein) hydrolase activity [GO:0008474]
PF00755;PF16484;
6.10.250.1760;3.30.559.10;3.30.559.70;
Carnitine/choline acetyltransferase family
null
SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8BGD5}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BGD5}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18192268}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the soma and dendritic ...
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000250|UniPr...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25.35 mM for palmitoyl-CoA {ECO:0000269|PubMed:18192268}; KM=58.53 mM for carnitine {ECO:0000269|PubMed:18192268}; Vmax=0.09 nmol/min/mg enzyme (towards carnitine) {ECO:0000269|PubMed:18192268}; Vmax=0.095 nmol/min/mg enzyme (towards palmitoyl-CoA) {ECO:0000269|Pub...
null
null
null
FUNCTION: Palmitoyl thioesterase specifically expressed in the endoplasmic reticulum of neurons. Modulates the trafficking of the glutamate receptor, AMPAR, to plasma membrane through depalmitoylation of GRIA1 (By similarity). Also regulates AMPR trafficking through the regulation of SACM1L phosphatidylinositol-3-phosp...
Rattus norvegicus (Rat)
F1LNJ2
U520_RAT
MADVTARSLQYEYKANSNLVLQADRSLIDRTRRDEPTGEVLSLVGKLEGTRMGDKAQRTKPQMQEERRAKRRKRDEDRHDINKMKGYTLLSEGIDEMVGIIYKPKTKETRETYEVLLSFIQAALGDQPRDILCGAADEVLAVLKNEKLRDKERRREIDLLLGQTDDTRYHVLVNLGKKITDYGGDKEIQNMDDNIDETYGVNVQFESDEEEGDEDVYGEVREEASDDDMEGDEAVVRCTLSANLVASGELMSSKKKDLHPRDIDAFWLQRQLSRFYDDAIVSQKKADEVLEILKTASDDRECENQLVLLLGFNTFDFIKV...
3.6.4.13
null
mRNA splicing, via spliceosome [GO:0000398]; spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) [GO:0000388]
catalytic step 2 spliceosome [GO:0071013]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U2-type catalytic step 1 spliceosome [GO:0071006]; U2-type precatalytic spliceosome [GO:0071005]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; helicase activity [GO:0004386]; identical protein binding [GO:0042802]; nucleic acid binding [GO:0003676]; RNA helicase activity [GO:0003724]
PF21188;PF00270;PF00271;PF18149;PF02889;
1.10.150.20;2.60.40.150;3.40.50.300;1.10.3380.10;1.10.10.10;
Helicase family, SKI2 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75643}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:O75643};
null
null
null
null
FUNCTION: Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes. As a component of the minor spliceosome, involved in th...
Rattus norvegicus (Rat)
F1LP64
TRIPC_RAT
MSNRPNNNPGGSLRRSQRNTAGAQPQDDSIGGRSCSSSSAVIVPQPEDPDRANTSERQKTGQVPKKDNSRGVKRSASPDYNRTNSPSSAKKPRAFQHIESLSETNKPPSKSKKRHLDQEQQLKSAQLPSTSKAHTRKSVAAGSSRSQKRKRTESSCVKSGSGSESTGAEERSAKPTKLASKSATSAKAGCSTITDSSSAASTSSSSSAVASASSTVPAGARVKQGKDQNKARRSRSASSPSPRRSSREKEQSKTGGSSKFDWAARFSPKVSLPKTKLSLPGSSKSETSKPGPSGLQAKLASLRKSTKKRSESPPAELPSL...
2.3.2.26
null
DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; heterochromatin boundary formation [GO:0033696]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of embryonic development...
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]
nuclear thyroid hormone receptor binding [GO:0046966]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF00632;PF02825;
3.30.720.50;3.30.2410.10;3.90.1750.10;1.25.10.10;
UPL family, K-HECT subfamily
null
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q14669}.
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=2.3.2.26; Evidence={ECO:0000250|UniProtKB:Q14669};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q14669}.
null
null
FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion degradation (UFD) pathway and regulation of DNA repair. Part of the ubiquitin fusion degradation (UFD) pathway, a process that mediates ubiquitination of protein at their N-terminus, regardless of the presence of lysine residues in target proteins. Acts...
Rattus norvegicus (Rat)
F1LP90
MINK1_RAT
MGDPAPARQSDFIFLVALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFTDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQLKDHIDRSRKKRGEKEETE...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
actin cytoskeleton organization [GO:0030036]; brain development [GO:0007420]; chemical synaptic transmission [GO:0007268]; dendrite morphogenesis [GO:0048813]; MAPK cascade [GO:0000165]; negative thymic T cell selection [GO:0045060]; neuron cellular homeostasis [GO:0070050]; neuron projection morphogenesis [GO:0048812]...
axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; Golgi apparatus [GO:0005794]; postsynaptic density [GO:0014069]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00780;PF00069;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:21048137}. Cell projection, axon {ECO:0000269|PubMed:21048137}. Cell projection, dendrite {ECO:0000269|PubMed:21048137}.
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: Serine/threonine kinase which acts as a negative regulator of Ras-related Rap2-mediated signal transduction to control neuronal structure and AMPA receptor trafficking (PubMed:21048137). Required for normal synaptic density, dendrite complexity, as well as surface AMPA receptor expression in hippocampal neuro...
Rattus norvegicus (Rat)
F1LQ48
HNRPL_RAT
MSRRLLPRAEKRRRRLEQRQQPDEQLRRAGAMVKMAAAGGGGGGGRYYGGGNEGGRAPKRLKTENAGDQHGGGGGGGSGAAGGGGGENYDDPHKTPASPVVHIRGLIDGVVEADLVEALQEFGPISYVVVMPKKRQALVEFEDVLGACNAVNYAADNQIYIAGHPAFVNYSTSQKISRPGDSDDSRSVNSVLLFTILNPIYSITTDVLYTICNPCGPVQRIVIFRKNGVQAMVEFDSVQSAQRAKASLNGADIYSGCCTLKIEYAKPTRLNVFKNDQDTWDYTNPNLSGQGDPGSNPNKRQRQPPLLGDHPAEYGEGRGF...
null
null
cellular response to amino acid starvation [GO:0034198]; circadian rhythm [GO:0007623]; mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of translation [GO:0045727]; regulation of altern...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; pronucleus [GO:0045120]; ribonucleoprotein complex [GO:1990904]; ribonucleoprotein granule [GO:0035770]; synapse [GO:0045202]
mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; mRNA CDS binding [GO:1990715]; pre-mRNA intronic binding [GO:0097157]; RNA binding [GO:0003723]; transcription cis-regulatory region binding [GO:0000976]
PF00076;PF13893;PF11835;
3.30.70.330;
null
PTM: Several isoelectric forms of the L protein are probably the results of post-translational modifications. {ECO:0000250|UniProtKB:P14866}.; PTM: Phosphorylation at Ser-578 by CaMK4 enhances interaction with a CaMK4-responsive RNA element (CaRRE1), and prevents inclusion of the stress axis-regulated exon (STREX) of t...
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P14866}. Cytoplasm {ECO:0000269|PubMed:18161049}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. These granules are not identical with P bodies or stress granules. {ECO:0000250|UniProtKB:P14866}.
null
null
null
null
null
FUNCTION: Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements. Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts. Associates, togethe...
Rattus norvegicus (Rat)
F1LQ70
LOX12_RAT
MGRYRVRVVTGAWLFSGSVNLVRLWLVGAHREARLELQLRPARGKEEEFDFDVAEDLGPLQFVKLHKEHTVVDDAWFCNLITVQGPGMSAEAVFPCYRWVQGEGILRLPEGTARLAGDNALDVFQKHREKELKERQQTYRWATWKQGLPQTIAADCKDDLPPNMRFHEEKRLDFEWTLKAGVLEMGLKRVYTLLRSWNRLEDFDQIFWGQKSALAEKVHRCWQEDELFGYQFLNGANPMLLRRSTSLPSRLVLPPGTEELQAQLEKELKDGCLFEADFILLDGIPANVIRGEQQYLAAPLVMLRMDPSGKLLPMAIQIQP...
1.13.11.-; 1.13.11.31; 1.13.11.33; 3.3.2.-
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726};
arachidonic acid metabolic process [GO:0019369]; cellular response to lipid [GO:0071396]; establishment of skin barrier [GO:0061436]; fatty acid oxidation [GO:0019395]; hepoxilin biosynthetic process [GO:0051122]; leukotriene A4 metabolic process [GO:1901751]; linoleic acid metabolic process [GO:0043651]; lipid metabol...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; sarcolemma [GO:0042383]
arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; hydrolase activity [GO:0016787]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165]
PF00305;PF01477;
3.10.450.60;2.60.60.20;
Lipoxygenase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane {ECO:0000250}. Note=Membrane association is stimulated by EGF. {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444; EC=1.13.11.31; Evidence={ECO:0000269|PubMed:23382512}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10429; Evi...
null
PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:23382512}.
null
null
FUNCTION: Catalyzes the regio and stereo-specific incorporation of molecular oxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:23382512). Mainly converts arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to...
Rattus norvegicus (Rat)
F1LQQ7
SCN7A_RAT
MLTSPEPKGLVPFTAESLELIKNHIAKKCNEEHEEEDLKPSWGLEAGKKLPFAYGTLPQGTVSEPLEDVDPYYYVKRNTFMVLNRNRVIFRFNAVSILCTLSPLSSLRRAVIKVLVHPLFRLLILISVLTDSILMCMSNLPEWILAVENTLLGIYTFEILVKVIARGIWAGSFSFLGDLWNWLDFSVTLFELITRSSPLSSLPMFKTIRTLRILKIIPLNHGLQSIVVTLVQCLKKLLGAIALALFFLTVSSLFGMGLFMGNLKHKCVRWPQEDGNDVMYNGTGSQYHILERENFYYMEGARYALLCGNKTDAGLCPEGY...
null
null
cellular homeostasis [GO:0019725]; membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; osmosensory signaling pathway [GO:0007231]; response to bacterium [GO:0009617]; sodium ion homeostasis [GO:0055078]; sodium ion transmembrane transport [GO:0035725]; sodium ion transp...
axon [GO:0030424]; glial cell projection [GO:0097386]; plasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518]
osmolarity-sensing monoatomic cation channel activity [GO:1990760]; sodium channel activity [GO:0005272]; transmembrane transporter binding [GO:0044325]; voltage-gated sodium channel activity [GO:0005248]
PF00520;PF06512;
1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350;
Sodium channel (TC 1.A.1.10) family, SCN7A subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01118}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:21084682};
null
null
null
null
FUNCTION: Sodium leak channel functioning as an osmosensor regulating sodium ion levels in various tissues and organs. While most sodium channels are voltage-gated, SCN7A is not and lets sodium flow through membrane along its concentration gradient (PubMed:21084682, PubMed:9001394). In glial cells of the central nervou...
Rattus norvegicus (Rat)
F1LQX4
RHG44_RAT
MKKQFNRMRQLANQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLGKMLKLCGETEDELAQELIHFELRVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAGAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSFGKPLEEHLMISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADP...
null
null
exocytosis [GO:0006887]; modification of dendritic spine [GO:0098886]; modification of postsynaptic structure [GO:0099010]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of filopodium assembly [GO:0051490]; negative regulation of Rac protein signal transduction [GO:0035021]; neurotransm...
dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; leading edge membrane [GO:0031256]; postsynapse [GO:0098794]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; recycling endosome [GO:0055037]
GTPase activator activity [GO:0005096]; phospholipid binding [GO:0005543]; small GTPase binding [GO:0031267]
PF03114;PF00620;
1.20.1270.60;1.10.555.10;
null
null
SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000269|PubMed:23739967, ECO:0000269|PubMed:25498153}. Recycling endosome {ECO:0000250|UniProtKB:Q5SSM3}. Presynapse {ECO:0000269|PubMed:23739967}. Cell projection, dendrite {ECO:0000269|PubMed:25498153}. Note=In CA1 hippocampal synapses, detected at both pres...
null
null
null
null
null
FUNCTION: GTPase-activating protein (GAP) that stimulates the GTPase activity of Rho-type GTPases. Thereby, controls Rho-type GTPases cycling between their active GTP-bound and inactive GDP-bound states. Acts as a GAP at least for CDC42 and RAC1 (PubMed:25498153). In neurons, is involved in dendritic spine formation an...
Rattus norvegicus (Rat)
F1LQY6
NECA2_RAT
MCERAARLCRAGAHRLLREPPPQGRALGGLLRWVGARMGEPRAPLVPDIPAADPDPGPAAPRGGTAVILDIFRRADKNDDGKLSLEEFQLFFADGVLNEKELEGLFHTIDSDNTNHVDTKELCDYFVEHMGDYEDVLASLETLNHSVLKAMGYTKKVYEGGNNVDQFVTRFLLKETANQIQSLLSSVESAVEAIEEQTSQIRQDHCKPSPGVNESRYGGPTPPYIPNHKLVVPEPVKSLPVAIGEPKEEGLEVQISRLAELIGRLESKTLSFDLQQRLSDEEGTNMYLQLVRQEMAVCPEQLGEFLDSLRQYLRSTAEER...
null
null
calcium-mediated signaling [GO:0019722]; negative regulation of G protein-coupled receptor internalization [GO:1904021]; positive regulation of adenosine receptor signaling pathway [GO:0060168]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of glutamate receptor signaling pathway [GO:19...
axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; plasma membrane [GO:0005886]
A2A adenosine receptor binding [GO:0031687]; calcium ion binding [GO:0005509]; type 5 metabotropic glutamate receptor binding [GO:0031802]
PF03992;PF13499;
3.30.70.100;1.10.238.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17689978}. Cell projection, dendrite {ECO:0000269|PubMed:17689978}. Cell projection, axon {ECO:0000269|PubMed:17689978}. Cell membrane {ECO:0000250|UniProtKB:Q7Z6G3}. Note=Colocalizes with ADORA2A and/or mGluR5/GRM5 at the plasma membrane (By similarity). Found in neu...
null
null
null
null
null
FUNCTION: May act as a signaling scaffold protein that senses intracellular calcium. Can modulate ligand-induced internalization of ADORA2A and coupling efficiency of mGluR5/GRM5; for both receptors may regulate signaling activity such as promoting MAPK1/3 (ERK1/2) activation. {ECO:0000250|UniProtKB:Q7Z6G3}.
Rattus norvegicus (Rat)
F1LR10
LIMA1_RAT
MESTPFNRRQWTSLSLRVTAKELSLVNKNKSSTIVEIFSKYQKAAEEANMERKKNNTESLPQHFRRGTLSVLKKKWENPVAGAESHTDSLPNSSSDGGHTADHPPAEVTAKAAPGARADREEHTQPRSRFGSRPEAVTQCRYPRSEDSHDFKAQATESQNMENCLGDSRHEAEKPEMSENTETSGKIEKYNVPLNRLKMMFEKGEHSQNKSPWTQGRNAGGRRLSENSCSLDDLEIGAGHLSSSAFNSEKNESKRNLELPRLSETSIKDRMAKYQAAVSKQSSPASYASELKPSESKTHKWEQKENVPPGPEACSIHQEG...
null
null
actin filament bundle assembly [GO:0051017]; cell migration [GO:0016477]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; intestinal cholesterol absorption [GO:0030299]; negative regulation of actin filament depolymerization [GO:0030835]; ruffle organization [GO:0031529]
actin cytoskeleton [GO:0015629]; brush border [GO:0005903]; brush border membrane [GO:0031526]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; stress fiber [GO:0001725]
actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; metal ion binding [GO:0046872]
PF00412;
2.10.110.10;
null
PTM: Phosphorylation of the C-terminal region by MAPK1/MAPK3 reduces its association with F-actin and contributes to actin filament reorganization and enhanced cell motility. {ECO:0000250|UniProtKB:Q9ERG0}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UHB6}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9UHB6}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UHB6}. Cell membrane {ECO:0000250|UniProtKB:Q9ERG0}. Note=This cytoskeletal protein colocalizes with actin stress fibers and focal adhesion plaqu...
null
null
null
null
null
FUNCTION: Actin-binding protein involved in actin cytoskeleton regulation and dynamics. Increases the number and size of actin stress fibers and inhibits membrane ruffling. Inhibits actin filament depolymerization. Bundles actin filaments, delays filament nucleation and reduces formation of branched filaments (By simil...
Rattus norvegicus (Rat)
F1LRS8
CD2AP_RAT
MVDYIVEYDYDAVHDDELTIRVGEIIRNVKKLQEEGWLEGELNGRRGMFPDNFVKEIKRETEPKDDNLPIKRERPGNVASLVQRISTYGLPAGGIQPHPQTKAMKKKTKKRQCKVLFEYSPQNEDELELTVGDVIDVIEEVEEGWWSGTLNNKLGLFPSNFVKELESTDDGEMHDAQEESEVSLTGPTSPMPSPGNGSEPAPGSVTQPKKIRGVGFGDIFKEGSVKLRTRTSSSETEEKKSEKPLILQSLGSRTQNVEVTKPDIDGKIKAKEYCKTVFPYTGTNEDELTFREGEIIHLISKETGEAGWWKGELNGKEGVF...
null
null
actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; adipose tissue development [GO:0060612]; apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell division [GO:0051301]; cell migration [GO:0016477]; cell population proliferation [GO:0008283]; ...
actin filament [GO:0005884]; axon [GO:0030424]; cell leading edge [GO:0031252]; cell periphery [GO:0071944]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endocytic vesicle [GO:0030139]; filamentous actin [GO:0031941]; growth cone [GO:0030426]; late endosome [GO:0005770]; neuromuscular...
actin binding [GO:0003779]; actin filament binding [GO:0051015]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; clathrin binding [GO:0030276]; identical protein binding [GO:0042802]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; protein-containing complex binding [GO:0044877]...
PF00018;PF14604;
2.30.30.40;
null
PTM: Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-Src. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9Y5K6}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9Y5K6}. Cell junction {ECO:0000250|UniProtKB:Q9Y5K6}. Note=Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles (By similarity). Located at podocyte slit diaphragm between podocyte foo...
null
null
null
null
null
FUNCTION: Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (By similarity). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhib...
Rattus norvegicus (Rat)
F1LTE0
TANC2_RAT
MFRNSLKMLLTGGKSSRKNRSSDGGSEEPPDRRQSSVDSRQSRSGPGGISTESDCAFEPDYAVPALPVSEGDVEQELGPPPSVDEAANTLMTRLGFLLGEKVTEVQPGDQYSMEVQDENQTSAITQRISPCSTLTSSTASPPASSPCSTLPPVSTNATAKDCSYGAVTSPTSTLESRDSGIIATLTNYSENMERTKYVGEAGKELGSGGNLKPWQSQKSSMDSCLYRVDENMAASTYSLNKIPERNLETVLSQSVQSIPLYLMPRPNSVAATSSAHLEDLAYLDEQRHTPLRTSLRMPRQSMSGARTQQDLRVRFAPYRP...
null
null
dense core granule cytoskeletal transport [GO:0099519]; in utero embryonic development [GO:0001701]; regulation of dendritic spine development [GO:0060998]; regulation of dendritic spine morphogenesis [GO:0061001]
axon [GO:0030424]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; postsynaptic density, intracellular component [GO:0099092]
null
PF12796;PF13181;
1.25.40.20;1.25.40.10;
TANC family
null
SUBCELLULAR LOCATION: Cell projection, dendritic spine {ECO:0000269|PubMed:30021165}.
null
null
null
null
null
FUNCTION: Scaffolding protein in the dendritic spines which acts as immobile postsynaptic posts able to recruit KIF1A-driven dense core vesicles to dendritic spines. {ECO:0000269|PubMed:30021165}.
Rattus norvegicus (Rat)
F1LVW7
DIAP3_RAT
MEKHRARALGRDSKASRRKGLPSAPPAGPYELGEKRPKLHLNIRTLTDDMLDKFASIRIPKGSKKERPPLPQLKTVSGSSDYSSVSSETMENNPKSLSENEVLKLFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTGSLRSSRQISPQEFIHELKMGYTGERLFTYLESLRVSLTSNPVSWVQNFGHEGLGLLLDILEKLINGQIQEKVVKKTQHKVIQCLRALMNTQYGLERIMSDERSLSLLAKAMDPKQPSMMADVVKLLSAVCIVGEESILEEVLEALTSAGEERKIDRFFSIVEGLRHNSVQLQVA...
null
null
actin crosslink formation [GO:0051764]; actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; actin filament organization [GO:0007015]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; autophagosome-lysosome fusion [GO:0061909]; cell projection organization...
actin filament [GO:0005884]; actin filament bundle [GO:0032432]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; ESCRT I complex [GO:0000813]; filamentous actin [GO:0031941]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; ribbon synapse [GO:0097470]; spindle pole [GO:0000922]; stereocilia tip-l...
actin binding [GO:0003779]; cytoskeletal protein binding [GO:0008092]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267]
PF06367;PF06371;PF02181;
1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10;
Formin homology family, Diaphanous subfamily
PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9Z207}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18651670}. Nucleus {ECO:0000269|PubMed:18651670}. Note=During mitosis, co-localizes with the actin-rich cleavage furrow and with the microtubule-rich central spindle during cytokinesis (By similarity). Shuttles between the cytoplasm and the nucleus (By similarity). {E...
null
null
null
null
null
FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers. Required for cytokinesis, stress fiber formation and transcriptional activation of the serum response factor. Binds to GTP-bound form of Rho and to profilin: acts in a Rho-dependent ...
Rattus norvegicus (Rat)
F1LX07
S2512_RAT
MAVKVHTTKRGDPHELRNIFLQYASTEVDGEHYMTPEDFVQRYLGLYNDPNSNPKIVQLLAGVADQTKDGLISYQEFLAFESVLCAPDSMFIVAFQLFDKSGNGEVTFENVKEIFGQTIIHHHIPFNWDCEFIRLHFGHNRKKHLNYVEFTQFLQELQLEHARQAFALKDKSKSGMISGLDFSDVMVTIRSHMLTPFVEENLVSAAGGSTSHQVSFSYFNAFNSLLNNMELVRKIYSTLAGTRKDIEVTKEEFASAITYGVVTPINVGILYFINNVHISTGRLTLADIERIAPLAEGALPYNLAELQRQQSPGLGRPIWL...
null
null
aspartate transmembrane transport [GO:0015810]; glutamate biosynthetic process [GO:0006537]; L-glutamate transmembrane transport [GO:0015813]; malate-aspartate shuttle [GO:0043490]; negative regulation of glucose catabolic process to lactate via pyruvate [GO:1904024]; positive regulation of ATP biosynthetic process [GO...
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
3-sulfino-L-alanine: proton, glutamate antiporter activity [GO:0000514]; acidic amino acid transmembrane transporter activity [GO:0015172]; aspartate:glutamate, proton antiporter activity [GO:0000515]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; L-aspartate transmembrane transporter activi...
PF00153;
1.10.238.10;1.50.40.10;
Mitochondrial carrier (TC 2.A.29) family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:4436323, ECO:0000305|PubMed:486467}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-aspartate(in) + L-glutamate(out) = H(+)(in) + L-aspartate(out) + L-glutamate(in); Xref=Rhea:RHEA:70783, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:4436323}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine(out) + H(+)(in) + L-glutamat...
null
null
null
null
FUNCTION: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (PubMed:4436323). Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. C...
Rattus norvegicus (Rat)
F1LXF1
BCR_RAT
MVDSVGFAEAWRAQFPDSEPPRMELRSVGDIEQELERCKASIRRLEQEVNQERFRMIYLQTLLAKEKKSYDRQRWGFRRAAQPPDGAAEPRASAPRLPPAPADGADPAPVEESEARPDGEGSPSKGRPATARRPAAAAPADRDDRGPPTSVAALRSNFEKIRKGPAQPGSADAEKPFYVNVEFHHERGLVKVNDKEVSDRISSLGSQAMQMERKKSQQSAGQGLGEAPRPHYRGRSSESSCGLDGDYEDAELNPRFLKDNLINANGGNRPPWPPLEYQPYQSIYVGGMMVEGEGKSPLLRSQSTSEQEKRLTWPRRSYSP...
2.7.11.1
null
actin cytoskeleton organization [GO:0030036]; brain development [GO:0007420]; cell migration [GO:0016477]; cellular response to lipopolysaccharide [GO:0071222]; definitive hemopoiesis [GO:0060216]; establishment of localization in cell [GO:0051649]; focal adhesion assembly [GO:0048041]; homeostasis of number of cells [...
axon [GO:0030424]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density, intracellular component [GO:0099092]; protein-containing complex [GO:0032991]; Schaffer collateral - CA...
ATP binding [GO:0005524]; enzyme binding [GO:0019899]; GTPase activator activity [GO:0005096]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF09036;PF00168;PF19057;PF00620;PF00621;
4.10.280.30;2.60.40.150;1.20.900.10;2.30.29.30;1.10.555.10;
null
PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine residues, leading to down-regulation of the BCR kinase activity. Phosphorylation by HCK is important for interaction with GRB2. {ECO:0000250|UniProtKB:P11274}.
SUBCELLULAR LOCATION: Postsynaptic density {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q6PAJ1}. Cell projection, axon {ECO:0000250|UniProtKB:Q6PAJ1}. Synapse {ECO:0000269|PubMed:20962234}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P11274}; Physiolo...
null
null
null
null
FUNCTION: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein (GAP) domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-re...
Rattus norvegicus (Rat)
F1LYL9
SOX9_RAT
MNLLDPFMKMTDEQEKGLSGAPSPTMSEDSAGSPCPSGSGSDTENTRPQENTFPKGEPDLKKESEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAEEATEQTHISPNAIFKALQADSPHSSSGMSEVHSPGEHSGQSQGPPTPPTTPKTDVQAGKVDLKREGRPLAEGGRQPPIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVSYTGSYG...
null
null
anterior head development [GO:0097065]; aortic valve morphogenesis [GO:0003180]; apoptotic process [GO:0006915]; astrocyte fate commitment [GO:0060018]; bone mineralization [GO:0030282]; branching involved in ureteric bud morphogenesis [GO:0001658]; bronchus cartilage development [GO:0060532]; cAMP-mediated signaling [...
nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667]
beta-catenin binding [GO:0008013]; bHLH transcription factor binding [GO:0043425]; chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription ...
PF00505;PF12444;
1.10.30.10;
null
PTM: Acetylated; acetylation impairs nuclear localization and ability to transactivate expression of target genes. Deacetylated by SIRT1. {ECO:0000250|UniProtKB:Q04887}.; PTM: Phosphorylation at Ser-64 and Ser-211 by PKA increases transcriptional activity and may help delay chondrocyte maturation downstream of PTHLH/PT...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04887, ECO:0000255|PROSITE-ProRule:PRU00267}.
null
null
null
null
null
FUNCTION: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development (By similarity). Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding g...
Rattus norvegicus (Rat)
F1LYQ8
FARP1_RAT
MGEIEQKPTPASRLGAPENSGISTLERGQKPPPTPSGKLMTVKIQMLDDTQEAFEVPQRAPGKVLFDAVCNHLNLVEGDYFGLEFPDHRKIVVWLDLLKPIVKQIRRPKHVLVKFVVKFFPPDHTQLQEELTRYLFALQVKQDLAQGRLTCNDTSAALLISHIVQSEIGDFDEALDREHLAKNKYVPQQDALEDKIVEFHHSHIGQTPAESDFQLLEVARRLEMYGIRLHPAKDREGTKINLAVANTGILVFQGFTKINAFNWAKVRKLSFKRKRFLIKLRPDVNSSYQDTLEFLMAGRDFCKSFWKICVEHHAFFRLFE...
null
null
dendrite morphogenesis [GO:0048813]; enzyme-linked receptor protein signaling pathway [GO:0007167]; positive regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904395]; postsynaptic actin cytoskeleton organization [GO:0098974]; Rac protein signal transduction [GO:0016601]; regulation of presynaps...
cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; extrinsic component of postsynaptic membrane [GO:0098890]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978]
cytoskeletal protein binding [GO:0008092]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267]
PF08736;PF09380;PF00373;PF09379;PF00169;PF00621;
1.20.80.10;1.20.900.10;2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23209303}; Peripheral membrane protein {ECO:0000269|PubMed:23209303}; Cytoplasmic side {ECO:0000269|PubMed:23209303}. Synapse {ECO:0000250}. Synapse, synaptosome {ECO:0000269|PubMed:23209303}. Cytoplasm, cytosol {ECO:0000269|PubMed:23209303}. Cell projection, filo...
null
null
null
null
null
FUNCTION: May play a role in semaphorin signaling (By similarity). Functions as a guanine nucleotide exchange factor for RAC1. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses. {ECO:0000250, ECO...
Rattus norvegicus (Rat)
F1LZW6
S2513_RAT
MAAAKVALTKRADPAELKAIFLKYASIEKNGEFFMSPHDFVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTFEDVRQVFGQTTIHQHIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEIQLEHAKQAFVQRDNAKTGKVTAIDFRDIMVTIRPHVLTPFVEECLVAAAGGTRSHQVSFSYFNGFNSLLNNMELIRKIYSTLAGSRKDVEVTKEEFALAAQKFGQVTPMEVDILFQLADLYEPRGRMTLADIERIAPLEEGMLPFNLAEAQRQQKASGDAAR...
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aspartate transmembrane transport [GO:0015810]; ATP biosynthetic process [GO:0006754]; cellular respiration [GO:0045333]; gluconeogenesis [GO:0006094]; L-glutamate transmembrane transport [GO:0015813]; malate-aspartate shuttle [GO:0043490]; response to calcium ion [GO:0051592]
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
3-sulfino-L-alanine: proton, glutamate antiporter activity [GO:0000514]; acidic amino acid transmembrane transporter activity [GO:0015172]; aspartate:glutamate, proton antiporter activity [GO:0000515]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; L-aspartate transmembrane transporter activi...
PF00153;
1.10.238.10;1.50.40.10;
Mitochondrial carrier (TC 2.A.29) family
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SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:4436323, ECO:0000305|PubMed:486467}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-aspartate(in) + L-glutamate(out) = H(+)(in) + L-aspartate(out) + L-glutamate(in); Xref=Rhea:RHEA:70783, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:4436323}; CATALYTIC ACTIVITY: Reaction=3-sulfino-L-alanine(out) + H(+)(in) + L-glutamat...
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FUNCTION: Mitochondrial electrogenic aspartate/glutamate antiporter that favors efflux of aspartate and entry of glutamate and proton within the mitochondria as part of the malate-aspartate shuttle (PubMed:4436323). Also mediates the uptake of L-cysteinesulfinate by mitochondria in exchange of L-glutamate and proton. C...
Rattus norvegicus (Rat)