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
O54880
RPH3L_RAT
MADTIFSSGNDQWVCPNDRQLALRAKLQTGWSVHTYQTEKQRRTQCLSPGEVEVILQVIQRAERLDILEQQRIGRLVERLETMQKNVMGNGVSQCLLCGEMLGFLGSSSVFCKDCRKKVCTKCGIEASPGQKRPLWLCKICSEQREVWKRSGAWFYKGLPKYILPLKTPGRADDPHFRPLPVEPTEPQPQSAEVSRVYTWARGRVVSSDSDSDSDLSSSSLEDRPMPSGIKGTKYDKPRGDSGGSMESPRMGPARPPSHLSGSQSSLGSETGAGATDPQGGTLPRPEPRVSGKRHTWATTHY
null
null
exocytosis [GO:0006887]; G protein-coupled receptor signaling pathway [GO:0007186]; glucose homeostasis [GO:0042593]; intracellular protein transport [GO:0006886]; negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; positive regulation of insulin secretion [GO:0032024]; positive regulation...
presynapse [GO:0098793]; secretory granule [GO:0030141]; synapse [GO:0045202]; transport vesicle membrane [GO:0030658]
LIM domain binding [GO:0030274]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267]
PF02318;
3.30.40.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle, secretory vesicle membrane. Note=Recruited to the exocytic secretory vesicles by RAB27A.
null
null
null
null
null
FUNCTION: Rab GTPase effector involved in the late steps of regulated exocytosis, both in endocrine and exocrine cells. Regulates the exocytosis of dense-core vesicles in neuroendocrine cells through interaction with RAB27A. Acts as a potential RAB3B effector protein in epithelial cells. {ECO:0000269|PubMed:11134008, E...
Rattus norvegicus (Rat)
O54885
TYOBP_MOUSE
MGALEPSWCLLFLPVLLTVGGLSPVQAQSDTFPRCDCSSVSPGVLAGIVLGDLVLTLLIALAVYSLGRLVSRGQGTAEGTRKQHIAETESPYQELQGQRPEVYSDLNTQRQYYR
null
null
actin cytoskeleton organization [GO:0030036]; apoptotic cell clearance [GO:0043277]; forebrain development [GO:0030900]; integrin-mediated signaling pathway [GO:0007229]; macrophage activation involved in immune response [GO:0002281]; microglial cell activation involved in immune response [GO:0002282]; negative regulat...
cell surface [GO:0009986]; plasma membrane [GO:0005886]
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
null
1.10.287.770;
TYROBP family
PTM: Tyrosine phosphorylated (PubMed:11754004, PubMed:12426565, PubMed:15728241, PubMed:17086186, PubMed:18691974, PubMed:9490415, PubMed:9852069). Following ligand binding by associated receptors, tyrosine phosphorylated in the ITAM domain which leads to activation of additional tyrosine kinases and subsequent cell ac...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9647200}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (PubMed:15471863, PubMed:9647200). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligan...
Mus musculus (Mouse)
O54888
RPA2_RAT
MDVDSRWRNLPSGPSLKHLTDPSYAVPPEQQKAALQDLTRAHVDSFNYAVLEGLSHAVQAIPPFEFAFKDERISLTIVDAAISPPAVPKGTICKELNIYPAECRGRRSTYRGKLTADISWAVNGVPKGIIKQFLGXVPIMVKSKLCNLYNLPPQVLIEHHEEAEEMGGYFIINGIEKVIRMLIMPRRNFPIAMIRPKWKSRGLGYTQFGVSIHCVREEHSAVNMNLHYVENGTVMLNFIYRKELFFLPLGFALKALVSFSDYQIFQELIKGKEEDSFFKNSVSQMLRIVMEEGCHTQKQVLDYLGERFRVKLSLPDWYPN...
2.7.7.6
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P08518, ECO:0000250|UniProtKB:P30876}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P08518, ECO:0000250|U...
embryo implantation [GO:0007566]; neural crest formation [GO:0014029]; nucleologenesis [GO:0017126]; rRNA transcription [GO:0009303]
chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]
DNA binding [GO:0003677]; DNA/RNA hybrid binding [GO:0071667]; metal ion binding [GO:0046872]; ribonucleoside binding [GO:0032549]; RNA polymerase I activity [GO:0001054]
PF04563;PF04561;PF04565;PF00562;PF04560;
2.40.50.150;3.90.1070.20;3.90.1100.10;2.40.270.10;3.90.1800.10;3.90.1110.10;
RNA polymerase beta chain family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9H9Y6}. Chromosome {ECO:0000250|UniProtKB:P70700}.
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:Q9H9Y6, ECO:0000269|PubMed:9422795}; PhysiologicalDirec...
null
null
null
null
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (By similarity...
Rattus norvegicus (Rat)
O54889
RPA1_RAT
MLASKHTPWRRLQGISFGMYSAEELKKLSVKSITNPRYVDSLGNPSADGLYDLALGPADSKEVCSTCVQDFNNCSGHLGHIDLPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAAIHLLVCQLKVLDVGALQAVYELERILSRFLEETSDPSAFEIQEELEEYTSKILQNNLLGSQGAHVKNVCESRSKLVAHFWKTHMAAKRCPHCKTGRSVVRKEHNSKLTITYPAMVHKKSGQKDAELPEGAPAAPGIDEAQMGKRGYLTPSSAQEHLFAIWKNEGFFLNYLFSGLDDIGPESSFNPSMFFLDFIVVPPSRYRPIN...
2.7.7.6
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O95602}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:O95602};
negative regulation of protein localization to nucleolus [GO:1904750]; rRNA transcription [GO:0009303]
chromosome [GO:0005694]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA/RNA hybrid binding [GO:0071667]; RNA polymerase I activity [GO:0001054]; zinc ion binding [GO:0008270]
PF04997;PF00623;PF04983;PF05000;PF04998;
1.10.132.30;1.10.357.120;2.40.40.20;3.30.70.2850;6.10.250.2940;3.30.1490.180;4.10.860.120;1.10.274.100;
RNA polymerase beta' chain family
PTM: Phosphorylated. {ECO:0000269|PubMed:9422795}.
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O95602}. Chromosome {ECO:0000250|UniProtKB:O35134}.
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:O95602}; PhysiologicalDirection=left-to-right; Xref=Rhe...
null
null
null
null
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (By similarity...
Rattus norvegicus (Rat)
O54890
ITB3_MOUSE
MRAQWPGQLWAALLALGALAGVVVGESNICTTRGVNSCQQCLAVSPVCAWCSDETLSQGSPRCNLKENLLKDNCAPESIEFPVSEAQILEARPLSSKGSGSSAQITQVSPQRIALRLRPDDSKIFSLQVRQVEDYPVDIYYLMDLSFSMKDDLSSIQTLGTKLASQMRKLTSNLRIGFGAFVDKPVSPYMYISPPQAIKNPCYNMKNACLPMFGYKHVLTLTDQVSRFNEEVKKQSVSRNRDAPEGGFDAIMQATVCDEKIGWRNDASHLLVFTTDAKTHIALDGRLAGIVLPNDGHCHIGTDNHYSASTTMDYPSLGLM...
null
null
apolipoprotein A-I-mediated signaling pathway [GO:0038027]; apoptotic cell clearance [GO:0043277]; blood coagulation, fibrin clot formation [GO:0072378]; cell adhesion mediated by integrin [GO:0033627]; cell projection morphogenesis [GO:0048858]; cell-matrix adhesion [GO:0007160]; cell-substrate junction assembly [GO:0...
alpha9-beta1 integrin-ADAM8 complex [GO:0071133]; alphav-beta3 integrin-HMGB1 complex [GO:0035868]; alphav-beta3 integrin-IGF-1-IGF1R complex [GO:0035867]; alphav-beta3 integrin-PKCalpha complex [GO:0035866]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; external side ...
C-X3-C chemokine binding [GO:0019960]; enzyme binding [GO:0019899]; extracellular matrix binding [GO:0050840]; fibrinogen binding [GO:0070051]; fibroblast growth factor binding [GO:0017134]; fibronectin binding [GO:0001968]; identical protein binding [GO:0042802]; insulin-like growth factor I binding [GO:0031994]; inte...
PF07974;PF18372;PF08725;PF07965;PF00362;PF17205;
4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410;
Integrin beta chain family
PTM: Phosphorylated on tyrosine residues in response to thrombin-induced platelet aggregation. Probably involved in outside-in signaling. {ECO:0000250|UniProtKB:P05106}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05106}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05106}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:P05106}. Cell junction, focal adhesion {ECO:0000269|PubMed:29038237}. Postsynaptic cell membrane {ECO:0000269|PubMed:1854...
null
null
null
null
null
FUNCTION: Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIB/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, ...
Mus musculus (Mouse)
O54898
CAC1G_RAT
MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCSLDYETYNSSSNTTCVNWNQYY...
null
null
action potential [GO:0001508]; artery smooth muscle contraction [GO:0014824]; AV node cell action potential [GO:0086016]; AV node cell to bundle of His cell signaling [GO:0086027]; calcium ion import [GO:0070509]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport into cytosol [GO:0060402]; cardiac...
cell body [GO:0044297]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated calcium channel complex [GO:0005891]; voltage-gated sodium channel compl...
low voltage-gated calcium channel activity [GO:0008332]; scaffold protein binding [GO:0097110]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated calcium channel activity involved in AV node cell action potential [GO:0086056]; voltage-gated calcium channel activity involved SA node cell action potentia...
PF00520;
1.10.287.70;1.20.120.350;
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1G subfamily
PTM: In response to raising of intracellular calcium, the T-type channels are activated by CaM-kinase II.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O43497}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:O43497}.
null
null
null
null
null
FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha...
Rattus norvegicus (Rat)
O54901
OX2G_MOUSE
MGSLVFRRPFCHLSTYSLIWGMAAVALSTAQVEVVTQDERKALHTTASLRCSLKTSQEPLIVTWQKKKAVSPENMVTYSKTHGVVIQPAYKDRINVTELGLWNSSITFWNTTLEDEGCYMCLFNTFGSQKVSGTACLTLYVQPIVHLHYNYFEDHLNITCSATARPAPAISWKGTGTGIENSTESHFHSNGTTSVTSILRVKDPKTQVGKEVICQVLYLGNVIDYKQSLDKGFWFSVPLLLSIVSLVILLVLISILLYWKRHRNQERGESSQGMQRMK
null
null
cell-cell adhesion [GO:0098609]; heterotypic cell-cell adhesion [GO:0034113]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of macrophage activation [GO:0043031]; negative regulation of macrophage migration [GO:190552...
axon [GO:0030424]; cell surface [GO:0009986]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
cell-cell adhesion mediator activity [GO:0098632]; protein binding involved in heterotypic cell-cell adhesion [GO:0086080]
PF00047;
2.60.40.10;
null
null
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O54902
NRAM2_RAT
MVLDPEEKIPDDGASGDHGDSASLGAINPAYSNSSLPHSTGDSEEPFTTYFDEKIPIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWVLLLATIVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRIILWLMVELAIIGSDMQEVIGSAIAINLLSAGRVPLYGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLRGMFVPSCSGCHTPQVEQAVGIVGAVIMPHNMYLHSALVKSRQVNRANKQEVREANKYFFIESCIALFVSFIINVFVVSVFAE...
null
null
cadmium ion transmembrane transport [GO:0070574]; cellular response to hypoxia [GO:0071456]; cellular response to iron ion [GO:0071281]; cellular response to tumor necrosis factor [GO:0071356]; cobalt ion transport [GO:0006824]; copper ion import across plasma membrane [GO:0098705]; copper ion transport [GO:0006825]; d...
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basal part of cell [GO:0045178]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endos...
cadmium ion binding [GO:0046870]; cadmium ion transmembrane transporter activity [GO:0015086]; cobalt ion binding [GO:0050897]; cobalt ion transmembrane transporter activity [GO:0015087]; copper ion binding [GO:0005507]; copper ion transmembrane transporter activity [GO:0005375]; ferrous iron transmembrane transporter ...
PF01566;
null
NRAMP family
PTM: Ubiquitinated by WWP2. {ECO:0000250|UniProtKB:P49282}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P49281}.
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P49282}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:P49281}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:P49282}; Multi-pass membran...
CATALYTIC ACTIVITY: [Isoform 2]: Reaction=Fe(2+)(in) + H(+)(in) = Fe(2+)(out) + H(+)(out); Xref=Rhea:RHEA:29579, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:16091957, ECO:0000269|PubMed:29317744, ECO:0000269|PubMed:9242408}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29580; Evidence={EC...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.9 uM for Fe(2+) {ECO:0000269|PubMed:16091957}; KM=1.4 uM for H(+) {ECO:0000269|PubMed:16091957}; KM=1.3 uM for Fe(2+) {ECO:0000269|PubMed:29317744};
null
null
null
FUNCTION: Proton-coupled metal ion symporter operating with a proton to metal ion stoichiometry of 1:1 (PubMed:16091957, PubMed:9242408). Selectively transports various divalent metal cations, in decreasing affinity: Cd(2+) > Fe(2+) > Co(2+), Mn(2+) >> Zn(2+), Ni(2+), VO(2+) (By similarity) (PubMed:16091957, PubMed:293...
Rattus norvegicus (Rat)
O54904
B3GT1_MOUSE
MASKVSCLYVLTVVCWASALWYLSITRPTSSYTGSKPFSHLTVARKNFTFGNIRTRPINPHSFEFLINEPNKCEKNIPFLVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSKAKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGGPIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVAELIYKTSLHTRLLHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQISPEEMHRIWNDMSS...
2.4.1.86
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9417047};
galactosylceramide biosynthetic process [GO:0006682]; lipid glycosylation [GO:0030259]; oligosaccharide biosynthetic process [GO:0009312]; protein O-linked glycosylation [GO:0006493]
Golgi membrane [GO:0000139]
glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity [GO:0047275]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]
PF01762;
3.90.550.50;
Glycosyltransferase 31 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133506; EC=2.4.1.86; Evidence={...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 mM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9417047}; KM=11.8 mM for GlcNAc-beta-pNP {ECO:0000269|PubMed:9417047};
PATHWAY: Protein modification; protein glycosylation.
null
null
FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-alpha-D-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. {ECO:0000269|PubMed:9417047}.
Mus musculus (Mouse)
O54905
B3GT2_MOUSE
MLQWRRRHCCFAKMTWSPKRSLLRTPLTGVLSLVFLFAMFLFFNHHDWLPGRPGFKENPVTYTFRGFRSTKSETNHSSLRTIWKEVAPQTLRPHTASNSSNTELSPQGVTGLQNTLSANGSIYNEKGTGHPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNETLAPGIQIIRVFLLGISIKLNGYLQHAIQEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHTPYVMKTDSDMFVNTEYLIHKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFS...
2.4.1.86
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9417047};
galactosylceramide biosynthetic process [GO:0006682]; oligosaccharide biosynthetic process [GO:0009312]; protein O-linked glycosylation [GO:0006493]
Golgi membrane [GO:0000139]
glucosaminylgalactosylglucosylceramide beta-galactosyltransferase activity [GO:0047275]; UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase activity [GO:0008499]
PF19341;PF01762;
3.90.550.50;
Glycosyltransferase 31 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:53432, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133506; EC=2.4.1.86; Evidence={...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 mM for UDP-alpha-D-galactose {ECO:0000269|PubMed:9417047}; KM=38.3 mM for GlcNAc-beta-pNP {ECO:0000269|PubMed:9417047};
PATHWAY: Protein modification; protein glycosylation.
null
null
FUNCTION: Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of gly...
Mus musculus (Mouse)
O54907
TNF12_MOUSE
MAARRSQRRRGRRGEPGTALLAPLVLSLGLALACLGLLLVVVSLGSWATLSAQEPSQEELTAEDRREPPELNPQTEESQDVVPFLEQLVRPRRSAPKGRKARPRRAIAAHYEVHPRPGQDGAQAGVDGTVSGWEETKINSSSPLRYDRQIGEFTVIRAGLYYLYCQVHFDEGKAVYLKLDLLVNGVLALRCLEEFSATAASSPGPQLRLCQVSGLLPLRPGSSLRIRTLPWAHLKAAPFLTYFGLFQVH
null
null
angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; extrinsic apoptotic signaling pathway [GO:0097191]; immune response [GO:0006955]; positive regulation of extrinsic apoptotic signaling pathway [GO:2001238]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; positive regulation of protein...
extracellular region [GO:0005576]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
cytokine activity [GO:0005125]; receptor ligand activity [GO:0048018]; tumor necrosis factor receptor binding [GO:0005164]
PF00229;
2.60.120.40;
Tumor necrosis factor family
PTM: The soluble form is produced from the membrane form by proteolytic processing. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 12, secreted form]: Secreted {ECO:0000250}.
null
null
null
null
null
FUNCTION: Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O54908
DKK1_MOUSE
MMVVCAAAAVRFLAVFTMMALCSLPLLGASATLNSVLINSNAIKNLPPPLGGAGGQPGSAVSVAPGVLYEGGNKYQTLDNYQPYPCAEDEECGSDEYCSSPSRGAAGVGGVQICLACRKRRKRCMRHAMCCPGNYCKNGICMPSDHSHFPRGEIEESIIENLGNDHNAAAGDGYPRRTTLTSKIYHTKGQEGSVCLRSSDCAAGLCCARHFWSKICKPVLKEGQVCTKHKRKGSHGLEIFQRCYCGEGLACRIQKDHHQASNSSRLHTCQRH
null
null
canonical Wnt signaling pathway [GO:0060070]; cell morphogenesis [GO:0000902]; embryonic limb morphogenesis [GO:0030326]; endoderm development [GO:0007492]; endoderm formation [GO:0001706]; face morphogenesis [GO:0060325]; forebrain development [GO:0030900]; hair follicle development [GO:0001942]; head morphogenesis [G...
extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
co-receptor binding [GO:0039706]; low-density lipoprotein particle receptor binding [GO:0050750]; receptor antagonist activity [GO:0048019]
PF04706;PF21481;PF21479;
2.10.80.10;
Dickkopf family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6 (PubMed:18524778). Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic act...
Mus musculus (Mouse)
O54909
RDH16_MOUSE
MWLYLVALVGLWTLLRFFRVRQVVSHLQDKYVFITGCDSGFGTLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVTATQWVKEHVGNRGLWGLVNNAGISTPSGPNEWMKKQDFAHVLDVNLLGMIEVTLSMLPLVRKARGRVVNVSSVMGRVSLFGGGYCISKYGVEAFSDSLRRELSYFGVKVAIIEPGFFLTGVTSSARLCSNTQMLWDQTSSEIREIYGEKYLASYLKRLNKLDKRCNKDLSGVTDCMEHALTACHPRTRYSAGWDAKLFYLPLSYLPTFLVDALLYWTSLKPEKAL
1.1.1.105; 1.1.1.209; 1.1.1.315; 1.1.1.53
null
9-cis-retinoic acid biosynthetic process [GO:0042904]; positive regulation of retinoic acid biosynthetic process [GO:1900054]; retinoic acid metabolic process [GO:0042573]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572]; steroid metabolic process [GO:0008202]
endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; organelle membrane [GO:0031090]
11-cis-retinol dehydrogenase [GO:0106429]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; androsterone dehydrogenase activity [GO:0047023]; identical protein binding [GO:0042802]; NAD-retinol dehydrogenase activity [GO:0004745]
PF00106;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family
PTM: Not glycosylated. {ECO:0000269|PubMed:15355969}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11279029, ECO:0000269|PubMed:15355969, ECO:0000269|PubMed:16223484}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000269|PubMed:9407098}.
CATALYTIC ACTIVITY: Reaction=all-trans-retinol--[retinol-binding protein] + NAD(+) = all-trans-retinal--[retinol-binding protein] + H(+) + NADH; Xref=Rhea:RHEA:48488, Rhea:RHEA-COMP:14428, Rhea:RHEA-COMP:14430, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 uM for 3alpha-hydroxy-5alpha-androstan-17-one (androsterone) {ECO:0000269|PubMed:9407098};
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:O75452}.
null
null
FUNCTION: Oxidoreductase with a preference for NAD. Oxidizes all-trans-retinol, 9-cis-retinol, 11-cis-retinol and 13-cis-retinol to the corresponding aldehydes. Has higher activity towards CRBP-bound retinol than with free retinol. Oxidizes 3-alpha-hydroxysteroids. Oxidizes androstanediol and androsterone to dihydrotes...
Mus musculus (Mouse)
O54912
KCNK3_RAT
MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPEMIERQRLELRQLELRARYNLSEGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVRYLLHRAKRGLGMRHAEVSMANMVLIGFVSCISTLCIGAAAFSYYERWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTHNGQAGGLGGLSCLSGSLGDGVRPRDPVTCAAAAGGMGVGVGVGGSGFRNVYAEM...
null
null
cellular response to hypoxia [GO:0071456]; cellular response to zinc ion [GO:0071294]; cochlea development [GO:0090102]; monoatomic ion transmembrane transport [GO:0034220]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; potassium ion transmembrane transport [GO:0071805]; potassium ion transpo...
plasma membrane [GO:0005886]
monoatomic ion channel activity [GO:0005216]; open rectifier potassium channel activity [GO:0005252]; outward rectifier potassium channel activity [GO:0015271]; potassium ion leak channel activity [GO:0022841]; S100 protein binding [GO:0044548]
PF07885;
1.10.287.70;
Two pore domain potassium channel (TC 1.A.1.8) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14649}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14649}.
null
null
null
null
null
FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward....
Rattus norvegicus (Rat)
O54915
NR1I2_MOUSE
MRPEESWSRVGLVQCEEADSALEEPINVEEEDGGLQICRVCGDKANGYHFNVMTCEGCKGFFRRAMKRNVRLRCPFRKGTCEITRKTRRQCQACRLRKCLESGMKKEMIMSDAAVEQRRALIKRKKREKIEAPPPGGQGLTEEQQALIQELMDAQMQTFDTTFSHFKDFRLPAVFHSGCELPEFLQASLLEDPATWSQIMKDRVPMKISLQLRGEDGSIWNYQPPSKSDGKEIIPLLPHLADVSTYMFKGVINFAKVISYFRDLPIEDQISLLKGATFEMCILRFNTMFDTETGTWECGRLAYCFEDPNGGFQKLLLDPL...
null
null
cell differentiation [GO:0030154]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of transcr...
intermediate filament cytoskeleton [GO:0045111]; nuclear body [GO:0016604]; transcription regulator complex [GO:0005667]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; nuclear receptor activity [GO:0004879]; nuclear receptor binding [GO:0016922]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
PF00104;PF00105;
3.30.50.10;1.10.565.10;
Nuclear hormone receptor family, NR1 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
null
null
null
null
null
FUNCTION: Nuclear receptor that binds and is activated by a variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, endogenous compounds and drugs. Response to specific ligands is...
Mus musculus (Mouse)
O54916
REPS1_MOUSE
MEGLTLSDAEQKYYSDLFSYCDIESTKKVVVNGRVLELFRAAQLPNDVVLQIMELCGATRLGYFGRSQFYIALKLVAVAQSGFPLRVESINTVKDLPLPRFVASKNEQESRLAASYSSDSENQGSYSGVIPPPPGRGQVKKGPGSHDAVQPRPSAEQQEPVSPVVSPQQSPPTSPHTWRKHSRHPSGGNSERPLTGPGPFWSPFGDAQAGSSAGDAVWSGQSPPPPQDNWVSFADTPPTSALLTMHPASVQDQTTVRTVASAATANEIRRQSSSYEDPWKITDEQRQYYVNQFKTIQPDLNGFIPGSAAKEFFTKSKLPI...
null
null
clathrin-dependent synaptic vesicle endocytosis [GO:0150007]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]
clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular vesicle [GO:0097708]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
calcium ion binding [GO:0005509]; molecular adaptor activity [GO:0060090]; SH3 domain binding [GO:0017124]
PF12763;
1.10.238.10;
null
PTM: EGF stimulates phosphorylation on Tyr-residues.
SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}. Note=Colocalize with ITSN1 at the plasma membrane in structures that are most probably clathrin-coated pits. {ECO:0000250}.
null
null
null
null
null
FUNCTION: May coordinate the cellular actions of activated EGF receptors and Ral-GTPases.
Mus musculus (Mouse)
O54917
E2F6_MOUSE
MSQQRTARRQPSLLVDPAQETVRRRCRDPINVENLLPSKIRINLEENVQYVSMRKALKVKRPRFDVSLVYLTRKFMDLVRSAPGGILDLNKVATKLGVRKRRVYDITNVLDGIELVEKKSKNHIRWIGSDLNNFGAAPQQKKLQAELSDLSAMEDALDELIKDCAQQLLELTDDKENERLAYVTYQDIHGIQAFHEQIVIAVKAPEETRLDVPAPREDSITVHIRSTKGPIDVYLCEVEQNHSNGKTNDGIGASPSKSSHPQCPEKEDEPPQ
null
null
cell cycle [GO:0007049]; regulation of transcription by RNA polymerase II [GO:0006357]
DNA replication factor A complex [GO:0005662]; MLL1 complex [GO:0071339]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
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, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-r...
PF16421;PF02319;
6.10.250.540;1.10.10.10;
E2F/DP family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75461}.
null
null
null
null
null
FUNCTION: Inhibitor of E2F-dependent transcription (PubMed:9403682). Binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' (PubMed:18667754, PubMed:9403682). Has a preference for the 5'-TTTCCCGC-3' E2F recognition site (PubMed:9403682). E2F6 lacks the transcriptional activation and...
Mus musculus (Mouse)
O54918
B2L11_MOUSE
MAKQPSDVSSECDREGGQLQPAERPPQLRPGAPTSLQTEPQGNPDGEGDRCPHGSPQGPLAPPASPGPFATRSPLFIFVRRSSLLSRSSSGYFSFDTDRSPAPMSCDKSTQTPSPPCQAFNHYLSAMASIRQSQEEPEDLRPEIRIAQELRRIGDEFNETYTRRVFANDYREAEDHPQMVILQLLRFIFRLVWRRH
null
null
apoptotic process involved in embryonic digit morphogenesis [GO:1902263]; B cell homeostasis [GO:0001782]; cell-matrix adhesion [GO:0007160]; developmental pigmentation [GO:0048066]; ear development [GO:0043583]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; in utero embryonic development [GO...
Bcl-2 family protein complex [GO:0097136]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; mitochondrion [GO:0005739]
microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]
PF08945;PF06773;
null
Bcl-2 family
PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with TRIM2 and ubiquitination, followed by proteasomal degradation (PubMed:21478148). Deubiquitination catalyzed by USP27X stabilizes the protein (PubMed:27013495). {ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:27013495}.; PTM: Ubiquitination by TRIM2 f...
SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9430630}; Peripheral membrane protein {ECO:0000269|PubMed:9430630}. Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic membranes.
null
null
null
null
null
FUNCTION: Induces apoptosis and anoikis. The isoforms vary in cytotoxicity with isoform BimS being the most potent and isoform BimEL being the least potent. {ECO:0000269|PubMed:9430630}.
Mus musculus (Mouse)
O54924
EXOC8_RAT
MSDSGASRLRRQLESGGFEARLYVKQLSQQSDGDRDLQEHRQRVQALAEETAQNLKRNVYQNYRQFIETAREISYLESEMYQLSHLLTEQKSSLESIPLALLPAAAAGASTGEDTAGAGPRERGAAQAGFLPGPAGVPREGPGTGEEGKQRTLTTLLEKVEGCRDLLETPGQYLVYNGDLVEYEADHMAQLQRVHGFLMNDCLLVATWLPQRRGMYRYNALYPLDRLAVVNVKDNPPMKDMFKLLMFPESRIFQAENAKIKREWLEVLEETKRALSDKRRREQEEAAALRAPPPVTSKGSNPFEDEAEEELATPEAEEEK...
null
null
endosome organization [GO:0007032]; exocytosis [GO:0006887]; extracellular matrix disassembly [GO:0022617]; Golgi to plasma membrane transport [GO:0006893]; protein localization [GO:0008104]; protein transport [GO:0015031]
cell leading edge [GO:0031252]; exocyst [GO:0000145]; growth cone [GO:0030426]; late endosome [GO:0005770]; perinuclear region of cytoplasm [GO:0048471]
phosphatidylinositol binding [GO:0035091]; small GTPase binding [GO:0031267]
PF16528;PF08700;
1.20.58.1220;1.20.58.1210;2.30.29.30;
EXO84 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12954101}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12954101}. Cell projection, growth cone {ECO:0000269|PubMed:12954101}. Cell projection {ECO:0000269|PubMed:21658605}. Note=Binds lipids with phosphatidylinositol 3,4,5-trisphosphate groups (By similarity). P...
null
null
null
null
null
FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Rattus norvegicus (Rat)
O54926
SIVA_MOUSE
MPKRSCPFADAAPLQLKVHVGLKELSHGVFAERYSREVFERTKQLLFQGARAYRDHISSEDCSVNHLQESLKSGVVGAPQPARGQMLIGPDGRLTRCQAQASEGGLPRTAPIACSSCMRSVDGKAVCSQCERALCGQCVYTCWGCGALACVLCGLADYADDGEKTLCTSCAMFEA
null
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Isoform 1 binds 3 zinc ions. Isoform 2 binds 2 zinc ions. {ECO:0000250};
extrinsic apoptotic signaling pathway [GO:0097191]
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]
CD27 receptor binding [GO:0005175]; metal ion binding [GO:0046872]; tumor necrosis factor receptor binding [GO:0005164]; virus receptor activity [GO:0001618]
PF05458;
null
null
PTM: Phosphorylated by ABL2/ARG in response to oxidative stress. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. Note=In the nucleus, accumulates in dot-like structures. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis (By similarity). {ECO:0000250, ECO:0000269|PubMed:9177220}.
Mus musculus (Mouse)
O54928
SOCS5_MOUSE
MDKVGKMWNNLKYRCQNLFSHEGGSRNENVEMNPNRCPSVKEKSISLGEAAPQQESSPLRENVALQLGLSPSKTFSRRNQNCAAEIPQVVEISIEKDSDSGATPGTRLARRDSYSRHAPWGGKKKHSCSTKTQSSLDTEKKFGRTRSGLQRRERRYGVSSMQDMDSVSSRAVGSRSLRQRLQDTVGLCFPMRTYSKQSKPLFSNKRKIHLSELMLEKCPFPAGSDLAQKWHLIKQHTAPVSPHSTFFDTFDPSLVSTEDEEDRLRERRRLSIEEGVDPPPNAQIHTFEATAQVNPLYKLGPKLAPGMTEISGDGSAIPQT...
null
null
cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cytokine-mediated signaling pathway [GO:0019221]; epidermal growth factor receptor signaling pathway [GO:0007173]; intracellular signal transduction [GO:0035556]; negative regulation of endothelial cell activation [GO:1904988]; negative regula...
cytoplasm [GO:0005737]; phosphatidylinositol 3-kinase complex [GO:0005942]
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; epidermal growth factor receptor binding [GO:0005154]; kinase inhibitor activity [GO:0019210]; receptor tyrosine kinase binding [GO:0030971]
PF00017;PF12610;PF07525;
3.30.505.10;
null
PTM: Phosphorylated. Phosphorylation is induced by EGF (By similarity). {ECO:0000250}.
null
null
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal d...
Mus musculus (Mouse)
O54931
AKAP2_MOUSE
MAEAELHKERLQAIAEKRKRQTEIEGKRRQLDEQVLLLQHSKSKVLREKWLLQGVPAGTAEEEEARRRQSEEDEFKVKQLEDNIQRLEQEIQALESEESQISAKEQIILEKLKETEKSFKDLQKSFSTADGASGWSTVLLQGDELTADPIGTNADMAIQKPPQLSEDANQLRSKQDNCGDSRLEPAASSLSPDHKNMEIGVSVAECKSVPGVTSTPHSKDHSSPFYSPSHNGLLADHHESLDNDVAREIQYLDEVLEANCCDSSVDGTYNGISSPEPGAAILVSSLGSPAHSVTEAEPTEKASGRQVPPHIELSRSPSDR...
null
null
actin filament organization [GO:0007015]; protein localization [GO:0008104]; regulation of cell shape [GO:0008360]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]
apical plasma membrane [GO:0016324]; protein-containing complex [GO:0032991]; side of membrane [GO:0098552]
protein domain specific binding [GO:0019904]; protein kinase A binding [GO:0051018]; protein-containing complex binding [GO:0044877]
PF03285;
null
null
null
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:9497389}; Lipid-anchor, GPI-like-anchor {ECO:0000269|PubMed:9497389}; Cytoplasmic side {ECO:0000269|PubMed:9497389}. Note=Accumulates near the inner, apical surface of highly polarized epithelium in tubules of nephrons. {ECO:0000269|PubMed:9497389}.
null
null
null
null
null
FUNCTION: Binds to regulatory subunit (RII) of protein kinase A (PubMed:9497389). May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP (PubMed:9497389). Binds tp and modula...
Mus musculus (Mouse)
O54937
PDK4_RAT
MKAARFVMRSASSLGNAGLVPREVELFSRYSPSPLSMKQLLDFGSENACERTSFSFLRQELPVRLANILKEIDILPEHLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQKVLSDFVDTLVKVRNRHHNVVPTMAQGILEYKDNCTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDSKTGNPSHIGSIDPNCDVVAVVEDAFECAKMLCDQYYLTSPELKLTQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRPFLTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMD...
2.7.11.2
null
acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; cellular response to fatty acid [GO:0071398]; cellular response to starvation [GO:0009267]; glucose homeostasis [GO:0042593]; insulin receptor signaling pathway [GO:0008286]; negative regulation of anoikis [GO:2000811]; phosphorylation [GO:0016310]; reactive o...
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; pyruvate dehydrogenase (acetyl-transferring) kinase activity [GO:0004740]
PF10436;PF02518;
1.20.140.20;3.30.565.10;
PDK/BCKDK protein kinase family
null
SUBCELLULAR LOCATION: Mitochondrion matrix.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit]; Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:45621...
null
null
null
null
FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates ...
Rattus norvegicus (Rat)
O54939
DHB3_RAT
MEQFLLSVGLLVCLVCLVKCVRFSRYLFLSFCKALPGSFLRSMGQWAVITGAGDGIGKAYSFELARHGLNVVLISRTLEKLQVISEEIERTTGSRVKVVQADFTREDIYDHIEEQLKGLEIGVLVNNVGMLPNLLPSHFLSTSGESQSVIHCNITSVVKMTQLVLKHMESRRRGLILNISSGVGVRPWPLYSLYSASKAFVCTFSKALNVEYRDKGIIIQVLTPYSVSTPMTKYLNTSRVTKTADEFVKESLKYVTIGAETCGCLAHEILAIILNLIPSRIFYSSTTQRFLLKQFSDYLKSNISNR
1.1.1.62; 1.1.1.64
null
biphenyl metabolic process [GO:0018879]; cellular response to antibiotic [GO:0071236]; cellular response to gonadotropin stimulus [GO:0071371]; cellular response to hormone stimulus [GO:0032870]; hippocampus development [GO:0021766]; insecticide metabolic process [GO:0017143]; Leydig cell differentiation [GO:0033327]; ...
endoplasmic reticulum [GO:0005783]
17-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0072582]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; testosterone 17-beta-dehydrogenase (NADP+) activity [GO:0047045]; testosterone dehydrogenase (NAD+) activity [GO:0047035]
PF00106;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family, 17-beta-HSD 3 subfamily
null
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P37058}.
CATALYTIC ACTIVITY: Reaction=a 17beta-hydroxy steroid + NADP(+) = a 17-oxo steroid + H(+) + NADPH; Xref=Rhea:RHEA:69284, ChEBI:CHEBI:15378, ChEBI:CHEBI:19168, ChEBI:CHEBI:35343, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000250|UniProtKB:P37058}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69286; Evi...
null
PATHWAY: Hormone biosynthesis; testosterone biosynthesis. {ECO:0000250|UniProtKB:P37058}.; PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:P37058}.
null
null
FUNCTION: Catalyzes the conversion of 17-oxosteroids to 17beta-hydroxysteroids. Favors the reduction of androstenedione to testosterone. Testosterone is the key androgen driving male development and function (By similarity). Uses NADPH while the two other EDH17B enzymes use NADH. Androgens such as epiandrosterone, dehy...
Rattus norvegicus (Rat)
O54940
BNIP2_MOUSE
MEGVELKEEWQDEDFPIPLPEDDSIEADTLDGTDPDRQPGSLEVNGNKVRKKLMAPDISLTLDPGEDSLWSDDLDEAGEVDLEGLDTPSENSDEFEWEDDLPKPKTTEVIRKGSITEYTATEEKGDGRRWRMFRIGEQDHRVDMKAIEPYKKVISHGGYYGDGLNAIVVFAVCFMPESGQPNYRYLMDNLFKYVIGTLELLVAENYMIIYLNGATTRRKMPSLGWLRRCYQQIDRRLRKNLKSLIIVHPSWFIRTLLAVTRPFISSKFSQKIRYVFNLAELAELVPMEYVGIPECIKQYEEEKFKKRQKRVDQELNGKQE...
null
null
apoptotic process [GO:0006915]; blastocyst development [GO:0001824]; centrosome cycle [GO:0007098]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of small GTPase mediated signal transduction [GO:0051057]; striated muscle cell differenti...
centriole [GO:0005814]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]; spindle pole centrosome [GO:0031616]
null
PF12496;PF13716;
3.40.525.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Localizes to the nuclear envelope region and to other cytoplasmic structures. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Implicated in the suppression of cell death. Interacts with the BCL-2 and adenovirus E1B 19 kDa proteins (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O54941
SMCE1_MOUSE
MSKRPSYAPPPTPAPATQMPSTPGFVGYNPYSHLAYNNYRLGGNPGTNSRVTASSGITIPKPPKPPDKPLMPYMRYSRKVWDQVKASNPDLKLWEIGKIIGGMWRDLTDEEKQEYLNEYEAEKIEYNESMKAYHNSPAYLAYINAKSRAEAALEEESRQRQSRMEKGEPYMSIQPAEDPDDYDDGFSMKHTATARFQRNHRLISEILSESVVPDVRSVVTTARMQVLKRQVQSLMVHQRKLEAELLQIEERHQEKKRKFLESTDSFNNELKRLCGLKVEVDMEKIAAEIAQAEEQARKRQEEREKEAAEQAERSQSSMAP...
null
null
chromatin remodeling [GO:0006338]; negative regulation of DNA-templated transcription [GO:0045892]; neurogenesis [GO:0022008]; nucleosome disassembly [GO:0006337]; positive regulation of cell differentiation [GO:0045597]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of myoblast di...
bBAF complex [GO:0140092]; brahma complex [GO:0035060]; chromatin [GO:0000785]; kinetochore [GO:0000776]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514]
N-acetyltransferase activity [GO:0008080]; nuclear receptor binding [GO:0016922]; nucleosomal DNA binding [GO:0031492]; RNA binding [GO:0003723]
PF00505;
1.10.30.10;
null
PTM: Ubiquitinated by TRIP12, leading to its degradation by the proteasome. Ubiquitination is prevented upon interaction between TRIP12 and SMARCC1 (By similarity). {ECO:0000250|UniProtKB:Q969G3}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
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)
O54942
CLD5_MOUSE
MGSAALEILGLVLCLVGWVGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYESVLALSAEVQAARALTVGAVLLALVALFVTLTGAQCTTCVAPGPVKARVALTGGALYAVCGLLALVPLCWFANIVVREFYDPTVPVSQKYELGAALYIGWAASALLMCGGGLVCCGAWVCTGRPEFSFPVKYSAPRRPTANGDYDKKNYV
null
null
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; establishment of blood-retinal barrier [GO:1990963]; maintenance of blood-brain barrier [GO:0035633]; myelination...
apicolateral plasma membrane [GO:0016327]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; lateral plasma membrane [GO:0016328]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; Schmidt-Lanterman incisure [GO:0043220]; tight junction ...
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]
PF00822;
1.20.140.150;
Claudin family
null
SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:9892664}. Cell membrane {ECO:0000269|PubMed:9892664}; Multi-pass membrane protein {ECO:0000269|PubMed:9892664}.
null
null
null
null
null
FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}.
Mus musculus (Mouse)
O54943
PER2_MOUSE
MNGYVDFSPSPTSPTKEPGAPQPTQAVLQEDVDMSSGSSGNENCSTGRDSQGSDCDDNGKELRMLVESSNTHPSPDDAFRLMMTEAEHNPSTSGCSSEQSAKADAHKELIRTLKELKVHLPADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSESQPCSVDVPSYSMEQVEGITSEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAKFVEFLAPHDVSVFHSYTTPYKLPPWSVCSGLDSFTQECMEEKSFFCRVSVGKHHENEIRYQPFRMTPYLVKVQEQQGAESQLCCLLLAERVHSGYE...
null
null
chromatin remodeling [GO:0006338]; circadian regulation of gene expression [GO:0032922]; circadian regulation of translation [GO:0097167]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; fatty acid metabolic process [GO:0006631]; gluconeogenesis [GO:0006094]; glycogen biosynth...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
DNA-binding transcription factor binding [GO:0140297]; histone deacetylase binding [GO:0042826]; histone methyltransferase binding [GO:1990226]; identical protein binding [GO:0042802]; kinase binding [GO:0019900]; nuclear receptor binding [GO:0016922]; pre-mRNA binding [GO:0036002]; RNA polymerase binding [GO:0070063];...
PF08447;PF21353;PF12114;
3.30.450.20;
null
PTM: Acetylated (PubMed:18662546, PubMed:30782483). Deacetylated by SIRT1, resulting in decreased protein stability (PubMed:18662546). Deacetylated by SIRT6, preventing its degradation by the proteasome, resulting in increased protein stability (PubMed:30782483). {ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:3078248...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:22208286}. Cytoplasm {ECO:0000269|PubMed:11889036, ECO:0000269|PubMed:22208286}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22274616}. Note=Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator pr...
null
null
null
null
null
FUNCTION: Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a...
Mus musculus (Mouse)
O54946
DNJB6_MOUSE
MVDYYEVLGVQRHASPEDIKKAYRKQALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGGIHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFDDFFGNRRGPRGNRSRGAGSFFSTFSGFPSFGSGFPAFDTGFTPFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKIVNGKKITTKRIVENGQERVEVEEDGQLKSLTINGVADENALAEECQRRGQPTPALAPGPAPAPVRVPSQARPLAPTPAPTPAPTPAPAPAQTPAPSVSTRPQKPPRPAPTAKLGSKSNWEDD...
null
null
actin cytoskeleton organization [GO:0030036]; chaperone-mediated protein folding [GO:0061077]; chorio-allantoic fusion [GO:0060710]; chorion development [GO:0060717]; extracellular matrix organization [GO:0030198]; intermediate filament organization [GO:0045109]; negative regulation of DNA-templated transcription [GO:0...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; Z disc [GO:0030018]
ATPase activator activity [GO:0001671]; DNA binding [GO:0003677]; Hsp70 protein binding [GO:0030544]; protein folding chaperone [GO:0044183]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
PF00226;
1.10.287.110;
null
null
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O75190}. Nucleus {ECO:0000250|UniProtKB:O75190}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:O75190}.
null
null
null
null
null
FUNCTION: Has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70 (PubMed:18373498). Plays an indispensable role in the organization of KRT8/KRT18 filaments. Acts as an endogenous molecular chaperone for neuronal proteins including...
Mus musculus (Mouse)
O54947
HAVR1_RAT
MVQLQVFISGLLLLLPGSVDSYEVVKGVVGHPVTIPCTYSTRGGITTTCWGRGQCPYSSCQNILIWTNGYQVTYRSSGRYNIKGRISEGDVSLTIENSVDSDSGLYCCRVEIPGWFNDQKMTFSLEVKPEIPTSPPTRPTTTRPTTTRPTTISTRSTHVPTSTRVSTSTPTPEQTQTHKPEITTFYAHETTAEVTETPSYTPADWNGTVTSSEEAWNNHTVRIPLRKPQRNPTKGFYVGMSVAALLLLLLASTVVVTRYIIIRKKMGSLSFVAFHVSKSRALQNAAIVHPRAEDNIYIIEDRSRGAE
null
null
phagocytosis, engulfment [GO:0006911]; positive regulation of mast cell activation [GO:0033005]; response to lipopolysaccharide [GO:0032496]; response to mycotoxin [GO:0010046]; response to nutrient [GO:0007584]; response to testosterone [GO:0033574]; response to wounding [GO:0009611]; response to xenobiotic stimulus [...
apical plasma membrane [GO:0016324]; brush border [GO:0005903]; cell surface [GO:0009986]; extracellular space [GO:0005615]; motile cilium [GO:0031514]; phagocytic vesicle [GO:0045335]
phosphatidylserine binding [GO:0001786]; virus receptor activity [GO:0001618]
PF07686;
2.60.40.10;
Immunoglobulin superfamily, TIM family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q96D42}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q96D42}.
null
null
null
null
null
FUNCTION: Phosphatidylserine receptor that plays an important functional role in regulatory B-cells homeostasis including generation, expansion and suppressor functions (By similarity). As P-selectin/SELPLG ligand, plays a specialized role in activated but not naive T-cell trafficking during inflammatory responses. Con...
Rattus norvegicus (Rat)
O54949
NLK_MOUSE
MSLCGTRANAKMMAAYNGGTSAAAAGHHHHHHHHLPHLPPPHLHHHHHPQHHLHPGSAAAVHPVQQHTSSAAAAAAAAAAAAAMLNPGQQQPYFPSPAPGQAPGPAAAAPAQVQAAAAATVKAHHHQHSHHPQQQLDIEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIDYFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEELDESRHMTQEVVTQYYRAPEILMGSRHYSN...
2.7.11.24
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
cellular response to osmotic stress [GO:0071470]; intracellular signal transduction [GO:0035556]; negative regulation of TORC1 signaling [GO:1904262]; negative regulation of Wnt signaling pathway [GO:0030178]; peptidyl-threonine phosphorylation [GO:0018107]; protein phosphorylation [GO:0006468]; protein stabilization [...
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; SH2 domain binding [GO:0042169]...
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
PTM: Phosphorylated on Thr-298. Intermolecular autophosphorylation on Thr-298 activates the enzyme. {ECO:0000269|PubMed:21118996}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21118996, ECO:0000269|PubMed:9448268}. Cytoplasm {ECO:0000269|PubMed:21118996}. Note=Predominantly nuclear. A smaller fraction is cytoplasmic. {ECO:0000269|PubMed:21118996}.
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=2.7.11.24; Evidence={ECO:0000269|PubMed:15004007, ECO:00002...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase that regulates a number of transcription factors with key roles in cell fate determination (PubMed:10391247, PubMed:11745377, PubMed:12482967, PubMed:12556497, PubMed:14720327, PubMed:15004007, PubMed:17785444, PubMed:18765672, PubMed:20874444, PubMed:21118996, PubMed:9448268)....
Mus musculus (Mouse)
O54950
AAKG1_MOUSE
MESVAAESSPALENEHFQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLQELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQA...
null
null
cellular response to nutrient levels [GO:0031669]; fatty acid biosynthetic process [GO:0006633]; import into nucleus [GO:0051170]; positive regulation of gene expression [GO:0010628]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleotide-activated protein kinase complex [GO:0031588]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
ADP binding [GO:0043531]; AMP binding [GO:0016208]; AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887]; protein-containing complex binding [GO:0044877]
PF00571;
3.10.580.10;
5'-AMP-activated protein kinase gamma subunit family
PTM: Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. {ECO:0000269|PubMed:21460634}.; PTM: Glycosylated; O-GlcNAcylated by OGT, promoting the AMP-activated protein kinase (AMPK) activity. {ECO:0000250|Un...
null
null
null
null
null
null
FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits prote...
Mus musculus (Mouse)
O54951
SEM6B_MOUSE
MWTPRVPPPRPALSFFLLLLLGVTYGLFPEEPPPLSVAPRDYLSHYPVFVGSGPGRLTAAEGAEDLNIQRVLRVNRTLFIGDRDNLYQVELEPSTSTELRYQRKLTWRSNPSDIDVCRMKGKQEGECRNFVKVLLLRDESTLFVCGSNAFNPICANYSMDTLQLLGDSISGMARCPYDPKHANVALFSDGMLFTATVTDFLAIDAVIYRSLGDRPTLRTVKHDSKWFKEPYFVHAVEWGSHVYFFFREIAMEFNYLEKVVVSRVARVCKNDVGGSPRVLEKQWTSFLKARLNCSVPGDSHFYFNVLQAVTGVVSLGGRPV...
null
null
axon guidance [GO:0007411]; central nervous system development [GO:0007417]; hippocampus development [GO:0021766]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; neural crest cell migration [GO:0001755]; positive regulation of cell migration [GO:0030335];...
plasma membrane [GO:0005886]
chemorepellent activity [GO:0045499]; semaphorin receptor binding [GO:0030215]
PF01437;PF01403;
3.30.1680.10;2.130.10.10;
Semaphorin family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:20484647}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Functions as a cell surface repellent for mossy fibers of developing neurons in the hippocampus where it plays a role in axon guidance (PubMed:20484647). May function through the PLXNA4 receptor expressed by mossy cell axons (PubMed:20484647). {ECO:0000269|PubMed:20484647}.
Mus musculus (Mouse)
O54952
BRCA1_RAT
MDLSAVRIQEVQNVLHAMQKILECPICLELIKEPVSTQCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVEELLKIIDAFELDTGMQCANGFSFSKKKNSSSELLNEDASIIQSVGYRNRVKKLQQIESGSATLKDSLSVQLSNLGIVRSMKKNRQTQPQNKSVYIALESDSSEERVNAPDGCSVRDQELFQIAPGGAGDEGKLNSAKKAACDFSEGIRNIEHHQCSDKDLNPTENHATERHPEKCPRISVANVHVEPCGTDARASSLQRGTRSLLFTEDRLDAEKAEFCDRSKQSGAAVSQQSRWA...
2.3.2.27
null
cellular response to indole-3-methanol [GO:0071681]; cellular response to ionizing radiation [GO:0071479]; cellular response to tumor necrosis factor [GO:0071356]; centrosome cycle [GO:0007098]; chordate embryonic development [GO:0043009]; chromosome segregation [GO:0007059]; DNA damage response [GO:0006974]; double-st...
BRCA1-A complex [GO:0070531]; BRCA1-B complex [GO:0070532]; BRCA1-BARD1 complex [GO:0031436]; BRCA1-C complex [GO:0070533]; chromosome [GO:0005694]; condensed chromosome [GO:0000793]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; DNA repair complex [GO:1990391]; intracellular non-membrane-bounded o...
chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; DNA-binding transcription activator activity [GO:0001216]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; p53 binding [GO:0002039]; RNA binding [GO:0003723]; RNA polymerase binding [GO:0070063]; transcription cis-regulatory region b...
PF00533;PF12820;PF00097;
3.40.50.10190;3.30.40.10;
null
PTM: Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR. Phosphorylation at Ser-975 by CHEK2 regulates mitotic spindle assembly. Phosphorylation by AURKA regulates centrosomal microtubule nucleation. {ECO:0000250|UniProtKB:P38398}.; PTM: Autoubiquitinated,...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P38398}. Chromosome {ECO:0000250|UniProtKB:P48754}. Cytoplasm {ECO:0000250|UniProtKB:P38398}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. Translocated to the cytoplasm durin...
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:P38398};
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The BRCA1-BARD1 hete...
Rattus norvegicus (Rat)
O54957
LAT_MOUSE
MEADALSPVGLGLLLLPFLVTLLAALCVRCRELPVSYDSTSTESLYPRSILIKPPQITVPRTPAVSYPLVTSFPPLRQPDLLPIPRSPQPLGGSHRMPSSQQNSDDANSVASYENQEPACKNVDADEDEDDYPNGYLVVLPDSSPAAVPVVSSAPVPSNPDLGDSAFSVESCEDYVNVPESEESAEASLDGSREYVNVSPEQQPVTRAELASVNSQEVEDEGEEEGVDGEEAPDYENLQELN
null
null
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; cellular defense response [GO:0006968]; gene expression [GO:0010467]; homeostasis of number of cells [GO:0048872]; immune response [GO:0006955]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; intracell...
cell-cell junction [GO:0005911]; COP9 signalosome [GO:0008180]; Golgi apparatus [GO:0005794]; immunological synapse [GO:0001772]; plasma membrane [GO:0005886]
protein kinase binding [GO:0019901]; signaling receptor complex adaptor activity [GO:0030159]
PF15234;
null
null
PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ. Phosphorylat...
SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane protein. Note=Present in lipid rafts.
null
null
null
null
null
FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-med...
Mus musculus (Mouse)
O54960
CAPON_RAT
MPSKTKYNLVDDGHDLRIPLHNEDAFQHGISFEAKYVGSLDVPRPNSRVEIVAAMRRIRYEFKAKNIKKKKVSIMVSVDGVKVILKKKKKKKEWTWDESKMLVMQDPIYRIFYVSHDSQDLKIFSYIARDGASNIFRCNVFKSKKKSQAMRIVRTVGQAFEVCHKLSLQHTQQNADGQEDGESERNSDGSGDPGRQLTGAERVSTATAEETDIDAVEVPLPGNDILEFSRGVTDLDAIGKDGGSHIDTTVSPHPQEPMLAASPRMLLPSSSSSKPPGLGTGTPLSTHHQMQLLQQLLQQQQQQTQVAVAQVHLLKDQLAA...
null
null
neuron projection regeneration [GO:0031102]; neurotransmitter secretion [GO:0007269]; positive regulation of peptidyl-cysteine S-nitrosylation [GO:2000170]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1902514]; r...
anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; podosome [GO:0002102]; postsynapse [GO:0098794]; presynapse [GO:0098793]; sarcoplasmic reticulum membrane [GO:0033017]; Z disc [GO...
mitogen-activated protein kinase kinase binding [GO:0031434]; nitric-oxide synthase binding [GO:0050998]; PDZ domain binding [GO:0030165]; protease binding [GO:0002020]; signaling adaptor activity [GO:0035591]
PF00640;
2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000269|PubMed:33523862}. Cell projection, podosome {ECO:0000269|PubMed:33523862}.
null
null
null
null
null
FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ...
Rattus norvegicus (Rat)
O54962
BAF_MOUSE
MTTSQKHRDFVAEPMGEKPVGSLAGIGDVLSKRLEERGFDKAYVVLGQFLVLKKDEDLFREWLKDTCGANAKQSRDCFGCLREWCDAFL
null
null
chromatin organization [GO:0006325]; chromosome organization [GO:0051276]; DNA integration [GO:0015074]; establishment of integrated proviral latency [GO:0075713]; mitotic nuclear membrane reassembly [GO:0007084]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; negative regulation of innate immune res...
chromatin [GO:0000785]; condensed chromosome [GO:0000793]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
PF02961;
1.10.150.40;
BAF family
PTM: Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins. Non phosphorylated BAF seems to enhance binding between EMD and LMNA. Dephosphorylated by protein pho...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75531}. Chromosome {ECO:0000250|UniProtKB:O75531}. Nucleus envelope {ECO:0000250|UniProtKB:O75531}. Cytoplasm {ECO:0000250|UniProtKB:O75531}. Note=Significantly enriched at the nuclear inner membrane, diffusely throughout the nucleus during interphase and concentrat...
null
null
null
null
null
FUNCTION: Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (By similarity). Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (By...
Mus musculus (Mouse)
O54963
REST_RAT
MATQVMGQSSGGGSLFNNSGNMGMALPNDMYDLHDLSKAELAAPQLIMLANVALTGEVNGSCCDYLVGEERQMAELMPVGDNHFSDSEGEGLEESAELKGDPSGLDNMELRSLELSVVEPQPVFEASAAPEVYSSNKDPAPEAPVAEDKCKNLKAKPFRCKPCQYEAESEEQFVHHIRVHSAKKFFVEESAEKQAKARESGASPSEEGEFSKGPIRCDRCGYNTNRYDHYTAHLKHHLRAGDNERVYKCIICTYTTVSEYHWRKHLRNHFPRKVYTCSKCNYFSTEKNNYVQHVRTHTGERPYKCELCPYSSSQKTHLTR...
null
null
auditory receptor cell stereocilium organization [GO:0060088]; cardiac muscle cell myoblast differentiation [GO:0060379]; cellular response to electrical stimulus [GO:0071257]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to xenobiotic stimulus [GO:0071466]; chromatin remodeling [GO:0006...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription repressor complex [GO:0017053]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]...
PF00096;
3.30.160.60;
null
PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q8VIG1}.; PTM: Phosphorylated; phosphorylation is required for ubiquitination. {ECO:0000250|UniProtKB:Q13127}.; PTM: Ubiquitinated; ubiquitination is mediated by BTRC and leads to proteasomal degradation in G2 phase (By similarity). Ubiquitination increases during neuronal di...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10490617, ECO:0000269|PubMed:12657670, ECO:0000269|PubMed:22371606, ECO:0000269|PubMed:22960932}. Cytoplasm {ECO:0000250|UniProtKB:Q13127}. Note=Colocalizes with ZFP90 in the nucleus (By similarity). In response to hypoxia, there is a more pronounced increase in levels ...
null
null
null
null
null
FUNCTION: Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells (By similarity). Restricts the expression of neuronal genes by associating with two distinct corepressors, SIN3A and RCOR1, which in turn recruit histone deacetylase...
Rattus norvegicus (Rat)
O54965
RNF13_MOUSE
MLLSIGMLMLSATQVYTILTVQLFAFLNLLPVEADILAYNFENASQTFEDLPARFGYRLPAEGLKGFLINSKPENACEPIVPPPLKDNSSGTFIVLIRRLDCNFDIKVLNAQRAGYKAAIVHNVDSDDLISMGSNDIDTLKKIDIPSVFIGESSANSLKDEFTYEKGGHIILVPELSLPLEYYLIPFLIIVGICLILIVIFMITKFVQDRHRNRRNRLRKDQLKKLPVHKFKKGDEYDVCAICLEEYEDGDKLRILPCSHAYHCKCVDPWLTKTKKTCPVCKQKVVPSQGDSDSDTDSSQEENQVSEHTPLLPPSASART...
2.3.2.27
null
organelle localization [GO:0051640]; positive regulation of JNK cascade [GO:0046330]; protein autoubiquitination [GO:0051865]; ubiquitin-dependent protein catabolic process [GO:0006511]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; nuclear inner membrane [GO:0005637]; nucleoplasm [GO:0005654]
JUN kinase binding [GO:0008432]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
PF02225;PF13639;
3.50.30.30;3.30.40.10;
null
PTM: Autoubiquitinated. {ECO:0000269|PubMed:19292867}.; PTM: N-glycosylated and also modified with chondroitin sulfate. {ECO:0000269|PubMed:19292867}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43567}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:19292867}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:19292867}; Single-pass type I membrane pr...
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:19292867};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:19292867}.
null
null
FUNCTION: E3 ubiquitin-protein ligase that regulates cell proliferation (PubMed:19292867). Involved in apoptosis regulation (By similarity). Mediates ER stress-induced activation of JNK signaling pathway and apoptosis by promoting ERN1 activation and splicing of XBP1 mRNA (By similarity). Also involved in protein traff...
Mus musculus (Mouse)
O54967
ACK1_MOUSE
MQPEEGTGWLLELLSEVQLQQYFLRLRDDLNITRLSHFEYVKNEDLEKIGMGRPGQRRLWEAVKRRKAMCKRKSWMSKVFSGKRLEAEFPSQHSQSTFRKPSPTPGSLPGEGTLQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPAGKTVSVAVKCLKPDVLSQPEAMDDFIREVNAMHSLDHRNLIRLYGVVLTLPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQVAEGMAYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAWCAPESLKTRTFSHASDTWMFGVTL...
2.7.10.2; 2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
endocytosis [GO:0006897]; negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059]; phosphorylation [GO:0016310]; regulation of keratinocyte differentiation [GO:0045616]; signal transduction [GO:0007165]; spermatid development [GO:0007286]
adherens junction [GO:0005912]; axon [GO:0030424]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; growth cone [GO:0030426]; neuronal cell body [GO:0043025]; nuc...
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activ...
PF09027;PF11555;PF07714;PF14604;
4.10.680.10;1.10.8.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family
PTM: Autophosphorylation regulates kinase activity. Phosphorylation on Tyr-533 is required for interaction with SRC and is observed during association with clathrin-coated pits (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated by NEDD4 and NEDD4L. Degradation can be induced by EGF and is lysosome-dependent. {ECO:...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16777958, ECO:0000269|PubMed:20333297}. Nucleus {ECO:0000269|PubMed:20333297}. Endosome {ECO:0000269|PubMed:17182860}. Cell junction, adherens junction {ECO:0000269|PubMed:18477472}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side {ECO:...
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 tyrosine-protein and serine/threonine-protein kinase that is implicated in cell spreading and migration, cell survival, cell growth and proliferation. Transduces extracellular signals to cytosolic and nuclear effectors. Phosphorylates AKT1, AR, MCF2, WASL and WWOX. Implicated in trafficking and c...
Mus musculus (Mouse)
O54968
NF2L2_RAT
MMDLELPPPGLQSQQDMDLIDILWRQDIDLGVSREVFDFSQRQKDYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQTDTSGSVSYSQVAHIPKQDALYFEDCMQLLAETFPFVDDHEVSSPTFQSLALDIPSHVESSVFTTPDQAQSLDSSLETAMTDLSSIQQDMEQVWQELFSIPELQCLNTENKQQAETTTVPSPEATLTEMDSNYHFYSSIPSLEKEVDSCSPHFLHGFEDSFSSILSTDDASQLNSLDSNPTLNTDFGDEFYSAFLAEPSGGGSMPSSAAISQSLSELLGGPIEGCDL...
null
null
aflatoxin catabolic process [GO:0046223]; cell redox homeostasis [GO:0045454]; cellular response to angiotensin [GO:1904385]; cellular response to copper ion [GO:0071280]; cellular response to fluid shear stress [GO:0071498]; cellular response to glucose starvation [GO:0042149]; cellular response to hydrogen peroxide [...
centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-DNA complex [GO:0032993]; RNA polymerase II transcription regulator complex [GO:0090575]
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; molecular condensate scaffold activity [GO:0140693]; protein domain...
PF03131;
1.10.880.10;
BZIP family, CNC subfamily
PTM: Ubiquitinated in the cytoplasm by the BCR(KEAP1) E3 ubiquitin ligase complex leading to its degradation. In response to oxidative stress, electrophile metabolites, such as sulforaphane, modify KEAP1, leading to inhibit activity of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and activity. In ...
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q60795}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:16314513}. Note=Cytosolic under unstressed conditions: ubiquitinated and degraded by the BCR(KEAP1) E3 ubiquitin ligase complex. Translocates into the nucleus upon induction by elec...
null
null
null
null
null
FUNCTION: Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles (PubMed:1631...
Rattus norvegicus (Rat)
O54972
MTG16_MOUSE
MSQASTTTLESGALLSGPRGLQYGSPAHRKEKAAAMPDSPAEVKTQPRSTPPSMPPPPPTSSQGATRPPSFTPHTHGEDGPATSLPHGRFHGCLKWSMVCLLMNGSSHSPTAIHGAPSTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHAKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQTPAQYLAQHEQLLLDASATSPVDSSELLLEVNENGKRRTPDRTKENGSDRDPLHPDHLSKRSCTLSPAQRCSPSNGLPHPTPPPPPHYR...
null
null
DNA-templated transcription [GO:0006351]; granulocyte differentiation [GO:0030851]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of glycolytic process [GO:0045820]; negative regulation of transcription by RNA poly...
Golgi membrane [GO:0000139]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]
PF08788;PF07531;PF01753;
6.10.140.2220;6.10.250.230;1.20.120.1110;
CBFA2T family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10022820}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10022820}. Golgi apparatus membrane {ECO:0000250}.
null
null
null
null
null
FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes. Can repress the expression of MMP7 in a ZBTB33-dependent manner. Reduces the protein levels and stability of ...
Mus musculus (Mouse)
O54975
XPP1_RAT
MAPKVTSELLRQLRQAMRNSECVAEPIQAYIIPSGDAHQSEYIAPCDCRRAFVSGFDGSAGTAIITEEHAAMWTDGRYFLQAAKQMDNNWTLMKMGLKDTPTQEDWLVSVLPEGSRVGVDPLIIPTDYWKKMAKVLRSAGHHLVPVKENLVDKIWTDRPERPCKPLLTLGLDYTGISWKEKVADLRLKMAERSIVWFVVTALDEIAWLFNLRGSDVEHNPVFFSYAIIGLERIMLFIDGDRIDAPGVKQHLLLDLGLEAEYKIQVLPYKSILSELKTLCADLSPREKVWVSDKASYAVSEAIPKDHRCCMPYTPICIAKA...
3.4.11.9
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NQW7}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:Q9NQW7};
bradykinin catabolic process [GO:0010815]; negative regulation of programmed cell death [GO:0043069]; proteolysis [GO:0006508]
cytoplasm [GO:0005737]; cytosol [GO:0005829]
aminopeptidase activity [GO:0004177]; manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; protein homodimerization activity [GO:0042803]
PF01321;PF16189;PF00557;PF16188;
3.90.230.10;3.40.350.10;
Peptidase M24B family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10095056}.
CATALYTIC ACTIVITY: Reaction=Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.; EC=3.4.11.9; Evidence={ECO:0000269|PubMed:10095056};
null
null
null
null
FUNCTION: Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (PubMed:10095056). Contributes to the degradation of bradykinin (By similarity). {ECO:0000250|UniProtKB:Q9NQW7, ECO:0000269|PubMed:10095056}.
Rattus norvegicus (Rat)
O54980
SNG2_RAT
MESGAYGAANAGGSFDLRRYVSQPQVVTRLVSMVLALIVFSCIFGEGYINLHSSDQLHCVFNRNEDACRYGSAIGVLAFLASAFFLVVDAFFSQISNATDRKYLVIGDLLFSALWTFLWFVGFCFLTNQWAATKPDDVLVGADSARAAITFSFFSIFSWGVLASLAYQRYKAGVDAFIQNYVDPTPDPTTAYASYPSASVENYQQPPFTQNVETTEGYQPPPVY
null
null
protein targeting [GO:0006605]; regulated exocytosis [GO:0045055]; synaptic vesicle membrane organization [GO:0048499]
membrane [GO:0016020]; neuromuscular junction [GO:0031594]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
null
PF01284;
null
Synaptogyrin family
PTM: May be tyrosine phosphorylated by Src. {ECO:0000269|PubMed:9446595}.
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:26071524}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12928441, ECO:0000269|PubMed:9446595}; Multi-pass membrane protein {ECO:0000255}...
null
null
null
null
null
FUNCTION: May play a role in regulated exocytosis (PubMed:10383386). In neuronal cells, modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in the formation and/or the maturation of this vesicles (PubMed:12928441, PubMed:15590695). May also play a role in GLUT4...
Rattus norvegicus (Rat)
O54982
KCNU1_MOUSE
MSQTLLDSLNQKELTETSCTIEIQAAFILSSLATFFGGLIILFLFRIALKSSRSWKYVKGPRGLLELFSSRRIEANPLRKLYFHGVFRQRIEMLLSAQTVVGQVLVILVFVLSIGSLVIYFINSMDPVRRCSSYEDKIVHGDLSFNAFFSFYFGLRFWAAEDKIKFWLEMNSIVDIFTIPPTFISYYLKSNWLGLRFLRALRLLELPKILQILQVIKTSNSVKLSKLLSIVISTWFTAAGFLHLVENSGDPWLNGRNSQTMSYFESIYLVTATMSTVGFGDVVAKTSLGRIFIVFFTLGSLILFANYIPEMVELFSTRKK...
null
null
establishment of localization in cell [GO:0051649]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein stabilization [GO:0050821]; reproductive process [GO:0022414]
membrane [GO:0016020]; monoatomic ion channel complex [GO:0034702]; postsynaptic membrane [GO:0045211]
potassium channel activity [GO:0005267]
PF03493;PF00520;PF21014;
1.10.287.70;3.40.50.720;
Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa5.1/KCNU1 sub-subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22084117}; Multi-pass membrane protein {ECO:0000269|PubMed:22084117}.
null
null
null
null
null
FUNCTION: Testis-specific potassium channel activated by both intracellular pH and membrane voltage that mediates export of K(+). Represents the primary spermatozoan K(+) current. In contrast to KCNMA1/SLO1, it is not activated by Ca(2+) or Mg(2+). Critical for fertility. May play an important role in sperm osmoregulat...
Mus musculus (Mouse)
O54983
CRYM_MOUSE
MKRAPAFLSAEEVQDHLRSSSLLIPPLEAALANFSKGPDGGVMQPVRTVVPVAKHRGFLGVMPAYSAAEDALTTKLVTFYEGHSNTAVPSHQASVLLFDPSNGSLLAVMDGNVITAKRTAAVSAIATKLLKPPGSDVLCILGAGVQAYSHYEIFTEQFSFKEVRMWNRTRENAEKFASTVQGDVRVCSSVQEAVTGADVIITVTMATEPILFGEWVKPGAHINAVGASRPDWRELDDELMRQAVLYVDSREAALKESGDVLLSGADIFAELGEVISGAKPAHCEKTTVFKSLGMAVEDLVAAKLVYDSWSSGK
1.5.1.25
null
mitochondrial transport [GO:0006839]; negative regulation of transcription by RNA polymerase II [GO:0000122]; sensory perception of sound [GO:0007605]; thyroid hormone metabolic process [GO:0042403]; thyroid hormone transport [GO:0070327]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
hormone binding [GO:0042562]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]; thiomorpholine-carboxylate dehydrogenase activity [GO:0047127]; thyroid hormone binding [GO:0070324]; transcription corepressor activity [GO:0003714]
PF02423;
3.40.50.720;3.30.1780.10;
Ornithine cyclodeaminase/mu-crystallin family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=(3R)-1,4-thiomorpholine-3-carboxylate + NAD(+) = 3,4-dehydrothiomorpholine-3-carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:12504, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58517, ChEBI:CHEBI:176873; EC=1.5.1.25; CATALYTIC ACTIVITY: Reaction=(3R)-1,4-thiomorpholine-3...
null
null
null
null
FUNCTION: Specifically catalyzes the reduction of imine bonds in brain substrates that may include cystathionine ketimine (CysK) and lanthionine ketimine (LK). Binds thyroid hormone which is a strong reversible inhibitor. Presumably involved in the regulation of the free intracellular concentration of triiodothyronine ...
Mus musculus (Mouse)
O54988
SLK_MOUSE
MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWEIIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSKWSSNFKDFLRKCLEKNVDARWTTSQLLQHPFVTVDSNKPVRELIAEAKAEVTEEVEDGKE...
2.7.11.1
null
apoptotic process [GO:0006915]; cellular response to type II interferon [GO:0071346]; cytoplasmic microtubule organization [GO:0031122]; positive regulation of apoptotic process [GO:0043065]; protein autophosphorylation [GO:0046777]; regulation of apoptotic process [GO:0042981]; regulation of cell migration [GO:0030334...
cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
ATP binding [GO:0005524]; histone kinase activity [GO:0035173]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF12474;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Proteolytically cleaved by caspase-3. {ECO:0000269|PubMed:10611247}.; PTM: Autophosphorylated. {ECO:0000269|PubMed:9808774}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10611247, ECO:0000269|PubMed:9808774}.
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: Mediates apoptosis and actin stress fiber dissolution. {ECO:0000269|PubMed:10611247}.
Mus musculus (Mouse)
O54990
PROM1_MOUSE
MALVFSALLLLGLCGKISSEGQPAFHNTPGAMNYELPTTKYETQDTFNAGIVGPLYKMVHIFLSVVQPNDFPLDLIKKLIQNKKFDISVDSKEPEIIVLALKIALYEIGVLICAILGLLFIILMPLVGCFFCMCRCCNKCGGEMHQRQKQNAPCRRKCLGLSLLVICLLMSLGIIYGFVANQQTRTRIKGTQKLAKSNFRDFQTLLTETPKQIDYVVEQYTNTKNKAFSDLDGIGSVLGGRIKDQLKPKVTPVLEEIKAMATAIKQTKDALQNMSSSLKSLQDAATQLNTNLSSVRNSIENSLSSSDCTSDPASKICDSI...
null
null
camera-type eye photoreceptor cell differentiation [GO:0060219]; photoreceptor cell maintenance [GO:0045494]; retina layer formation [GO:0010842]
apical plasma membrane [GO:0016324]; brush border [GO:0005903]; cell projection [GO:0042995]; cell surface [GO:0009986]; cilium [GO:0005929]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular space [GO:0005615]; microvillus [GO:0005902]; microvillus mem...
cholesterol binding [GO:0015485]
PF05478;
null
Prominin family
PTM: Acetylation at Lys-226, Lys-258 and Lys-265 by NAT8 and NAT8B may control PROM1 protein expression and its function in cell apoptosis.
SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane protein. Cell projection, microvillus membrane; Multi-pass membrane protein. Cell projection, cilium, photoreceptor outer segment. Endoplasmic reticulum {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Found in extrac...
null
null
null
null
null
FUNCTION: May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenes...
Mus musculus (Mouse)
O54991
CNTP1_MOUSE
MMSLRLFSILLATVVSGAWGWGYYGCNEELVGPLYARSLGASSYYGLFTTARFARLHGISGWSPRIGDPNPWLQIDLMKKHRIRAVATQGAFNSWDWVTRYMLLYGDRVDSWTPFYQKGHNATFFGNVNDSAVVRHDLHYHFTARYIRIVPLAWNPRGKIGLRLGIYGCPYTSSILYFDGDDAISYRFQRGASQSLWDVFAFSFKTEEKDGLLLHTEGSQGDYVTLELQGAHLLLHMSLGSSPIQPRPGHTTVSLGGVLNDLSWHYVRVDRYGRDANFTLDGYAHHFVLNGDFERLNLENEIFIGGLVGAARKNLAYRHN...
null
null
axonogenesis [GO:0007409]; cell adhesion [GO:0007155]; central nervous system myelination [GO:0022010]; cytoskeleton organization [GO:0007010]; mitochondrion organization [GO:0007005]; myelination [GO:0042552]; myelination in peripheral nervous system [GO:0022011]; neuromuscular junction development, skeletal muscle fi...
axon [GO:0030424]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; myelin sheath [GO:0043209]; paranodal junction [GO:0033010]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; presynaptic active zone [GO:0048786]; septate junction [GO:0005918]
SH3 domain binding [GO:0017124]
PF00754;PF02210;
2.60.120.1000;2.60.120.200;2.60.120.260;2.10.25.10;
Neurexin family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, paranodal septate junction {ECO:0000269|PubMed:25378149}.
null
null
null
null
null
FUNCTION: Required, with CNTNAP2, for radial and longitudinal organization of myelinated axons (PubMed:25378149). Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the paranodal region of the axo-glial junction. In ass...
Mus musculus (Mouse)
O54992
MAPK5_MOUSE
MSEDSDMEKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALQHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRKKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLM...
2.7.11.1
null
negative regulation of TOR signaling [GO:0032007]; positive regulation of dendritic spine development [GO:0060999]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; protein autophosphorylation [GO:0046777]; Ras protein signal transduction [GO...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; septin cytoskeleton [GO:0032156]
ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; mitogen-activated protein kinase binding [GO:0051019]; p53 binding [GO:0002039]; protein kinase activity [GO:0004672]; protein se...
PF00069;
4.10.1170.10;1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
PTM: Phosphorylated on Thr-182 ERK3/MAPK6 or ERK4/MAPK4; which is the regulatory phosphorylation site and is located on the T-loop/loop 12, leading to activation. Phosphorylation at Thr-182 by p38-alpha/MAPK14, p38-beta/MAPK11 is subject to debate. Phosphorylated at Ser-115 by PKA/PRKACA, leading to localization to the...
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 als...
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20640477}; CATALYTIC...
null
null
null
null
FUNCTION: Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcr...
Mus musculus (Mouse)
O54998
FKBP7_MOUSE
MNLLFRLAVFLSLWCCSDAQGQTKEESTEEVKIEVLHRPENCSKTSRKGDLLNAHYDGYLAKDGSKFYCSRTQDEGHPKWFVLGVGHVIKGLDIAMMDMCPGEKRKVIIPPSFAYGKEGYAEGKIPPNATLMFEIELYAVTKGPRSIETFKQIDTDNDRQLSKAEIELYLQKDFEKDANPRDKSYQKAVLEDIFKKNDHNGDGFISPKEYNVHQHDEL
5.2.1.8
null
null
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]
calcium ion binding [GO:0005509]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]
PF13499;PF00254;
3.10.50.40;1.10.238.10;
null
PTM: Glycosylated. {ECO:0000269|PubMed:9806833}.
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:9806833}.
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
null
null
null
null
FUNCTION: PPIases accelerate the folding of proteins during protein synthesis.
Mus musculus (Mouse)
O55000
PP1RA_RAT
MGSGPIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKEEGKSRTTLPERPLTEVKAETRAEEAPEKKKEKPKSLRTTAPSHAKFRSTGLELDTPSLVPVKKNSSTVVVSDKYNLKPIPLKRQSATAAPGDAAPPAEKKYKPLNTTPNTTKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPS...
null
null
negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of mitotic DNA damage checkpoint [GO:1904290]; positive regulation of telomere maintenance [GO:0032206]
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; nuclear body [GO:0016604]; PTW/PP1 phosphatase complex [GO:0072357]
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase inhibitor activity [GO:0004864]; RNA binding [GO:0003723]
PF08711;PF00642;
1.20.930.10;
null
PTM: Phosphorylated on Thr-398 by PKA within the region necessary for interaction with PPP1CA. {ECO:0000269|PubMed:12574161}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}. Note=Found in discrete nucleoplasmic bodies and within nucleoli. Associates with chromatin during interphase, excluded from condensed chromosomes during early mitosis and is reloaded onto chromosomes at the late telophase (By similarity). {ECO:000025...
null
null
null
null
null
FUNCTION: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. M...
Rattus norvegicus (Rat)
O55003
BNIP3_MOUSE
MSQSGEENLQGSWVELHFSNGNGSSVPASVSIYNGDMEKILLDAQHESGRSSSKSSHCDSPPRSQTPQDTNRAEIDSHSFGEKNSTLSEEDYIERRREVESILKKNSDWIWDWSSRPENIPPKEFLFKHPKRTATLSMRNTSVMKKGGIFSADFLKVFLPSLLLSHLLAIGLGIYIGRRLTTSTSTF
null
null
apoptotic process [GO:0006915]; autophagic cell death [GO:0048102]; brown fat cell differentiation [GO:0050873]; cardiac muscle cell apoptotic process [GO:0010659]; cellular response to cobalt ion [GO:0071279]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular resp...
cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]
GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]
PF06553;
6.10.250.1020;
NIP3 family
null
SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=Coexpression with the EIB 19-kDa protein results in a shift in NIP3 localization pattern to the nuclear envelope. Colocalizes with ACAA2 in the mitochondria. Colocalizes with SPATA18 at the ...
null
null
null
null
null
FUNCTION: Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2 (By similarity). Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial d...
Mus musculus (Mouse)
O55005
ROBO1_RAT
MKWKHLPLLVMISLLTLSKKHLLLAQLIPDPEDLERGNDNGTPAPTSDNDDNSLGYTGSRLRQEDFPPRIVEHPSDLIVSKGEPATLNCKAEGRPTPTIEWYKGGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRKSRPDEGVYICVARNYLGEAVSHNASLEVAILRDDFRQNPSDVMVAVGEPAVMECQPPRGHPEPTISWKKDGSPLDDKDERITIRGGKLMITYTRKSDAGKYVCVGTNMVGERESKVADVTVLERPSFVKRPSNLAVTVDDSAEFKCEARGDPVPTFGWRKDDGELPKSRYEIRDDHTLKIRKV...
null
null
aorta development [GO:0035904]; aortic valve morphogenesis [GO:0003180]; axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to hypoxia [GO:0071456]; chemorepulsion involved in postnatal olfactory bulb interneu...
axolemma [GO:0030673]; axon [GO:0030424]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]
axon guidance receptor activity [GO:0008046]; identical protein binding [GO:0042802]; LRR domain binding [GO:0030275]
PF00041;PF07679;PF13927;
2.60.40.10;
Immunoglobulin superfamily, ROBO family
PTM: Ubiquitinated. May be deubiquitinated by USP33. {ECO:0000250|UniProtKB:O89026}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28859078}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9Y6N7}. Cell projection, axon {ECO:0000250|UniProtKB:O89026}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:28859078}; Single-pass membrane protein {ECO:0000...
null
null
null
null
null
FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development. Interaction with the intracellular domain of FLRT3 med...
Rattus norvegicus (Rat)
O55012
PICAL_RAT
MSGQSLTDRITAAQHSVTGSAVSKTVCKATTHEIMGPKKKHLDYLIQCTNEMNVNIPQLADSLFERTTNSSWVVVFKSLITTHHLMVYGNERFIQYLASRNTLFNLSNFLDKSGLQGYDMSTFIRRYSRYLNEKAVSYRQVAFDFTKVKRGADGVMRTMNTEKLLKTVPIIQNQMDALLDFNVNSNELTNGVINAAFMLLFKDAIRLFAAYNEGIINLLEKYFDMKKNQCKEGLDIYKKFLTRMTRISEFLKVAEQVGIDRGDIPDLSQAPSSLLDALEQHLASLEGKKIKDSTAASRATTLSNAVSSLASTGLSLTKVD...
null
null
amyloid-beta clearance by transcytosis [GO:0150093]; axonogenesis [GO:0007409]; clathrin coat assembly [GO:0048268]; clathrin-dependent endocytosis [GO:0072583]; dendrite morphogenesis [GO:0048813]; endocytosis [GO:0006897]; endosomal transport [GO:0016197]; hemopoiesis [GO:0030097]; intracellular iron ion homeostasis ...
cell surface [GO:0009986]; clathrin coat of coated pit [GO:0030132]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; early endosome [GO:0005769]; endosome [GO:0005768]; endosome to plasma membrane transport vesicle [GO:0070381]; extrinsic component of presynaptic endocytic zone membrane [GO:0098...
1-phosphatidylinositol binding [GO:0005545]; clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; identical protein binding [GO:0042802]; low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; SH3 domain binding [GO:0017124]; smal...
PF07651;
1.25.40.90;1.20.58.150;
PICALM/SNAP91 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13492}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q13492}. Golgi apparatus {ECO:0000250|UniProtKB:Q13492}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q13492}. Nucleus {ECO:0000250|UniProtKB:Q13492}. Note=Colocalized with cla...
null
null
null
null
null
FUNCTION: Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane lea...
Rattus norvegicus (Rat)
O55013
TPPC3_MOUSE
MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDRMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSALIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE
null
null
COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; vesicle coating [GO:0006901]; vesicle tethering [GO:0099022]
cis-Golgi network membrane [GO:0033106]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]; TRAPP complex [GO:0030008]; TRAPPII protein complex [GO:1990071]; TRAPPIII protein complex [GO:1990072]
null
PF04051;
3.30.1380.20;
TRAPP small subunits family, BET3 subfamily
null
SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
null
null
null
null
null
FUNCTION: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Mus musculus (Mouse)
O55017
CAC1B_MOUSE
MVRFGDELGGRYGGTGGGERARGGGAGGAGGPGQGGLPPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDTEPVGDFPCGKDPPARQCDGDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDIL...
null
null
calcium ion import [GO:0070509]; calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; chemical synaptic transmission [GO:0007268]; establishment of localization in cell [GO:0051649]; locomotory behavior [GO:0007626]; neurotransmitt...
axon terminus [GO:0043679]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; presynaptic active zone [GO:0048786]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685]; voltage-gated calciu...
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; high voltage-gated calcium channel activity [GO:0008331]; protein phosphatase 2A binding [GO:0051721]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels [G...
PF08763;PF16905;PF00520;
1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350;
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1B subfamily
PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK. {ECO:0000250}.
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q00975}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q00975}.
null
null
null
null
null
FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. This alpha-1B sub...
Mus musculus (Mouse)
O55022
PGRC1_MOUSE
MAAEDVVATGADPSELEGGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPGASGDNDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTPAQQETLSDWDSQFTFKYHHVGKLLKEGEEPTVYSDDEEPKDETARKNE
null
null
associative learning [GO:0008306]; heme biosynthetic process [GO:0006783]; memory [GO:0007613]; modification of synaptic structure [GO:0099563]; negative regulation of synapse organization [GO:1905809]; positive regulation of lipoprotein transport [GO:0140077]; positive regulation of protein localization to plasma memb...
cell body [GO:0044297]; endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; synapse [GO:004...
heme binding [GO:0020037]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; steroid binding [GO:0005496]
PF00173;
3.10.120.10;
Cytochrome b5 family, MAPR subfamily
PTM: O-glycosylated; contains chondroitin sulfate attached to Ser-54. Ser-54 is in the cytoplasmic domain but the glycosylated form was detected in urine, suggesting that the membrane-bound form is cleaved, allowing for production of a secreted form which is glycosylated. {ECO:0000250|UniProtKB:O00264}.
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00264}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:27599036}; Single-pass membrane protein {ECO:00...
null
null
null
null
null
FUNCTION: Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (PubMed:28005395). Intracellular heme chaperone. Regulates ...
Mus musculus (Mouse)
O55023
IMPA1_MOUSE
MADPWQECMDYAVILARQAGEMIREALKNEMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTESPTWFIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRKPETLRIVLSNMEKLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVTEAGGVLMDVTGGPFDLMSRRIIAANSITLAKRIAKEIEIIPLQRDDES
3.1.3.25; 3.1.3.94
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000303|PubMed:23027737};
inositol biosynthetic process [GO:0006021]; inositol metabolic process [GO:0006020]; phosphatidylinositol biosynthetic process [GO:0006661]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; signal transduction [GO:0007165]
axon [GO:0030424]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]
inositol monophosphate 1-phosphatase activity [GO:0008934]; inositol monophosphate 3-phosphatase activity [GO:0052832]; inositol monophosphate 4-phosphatase activity [GO:0052833]; inositol monophosphate phosphatase activity [GO:0052834]; lithium ion binding [GO:0031403]; magnesium ion binding [GO:0000287]; manganese io...
PF00459;
3.40.190.80;3.30.540.10;
Inositol monophosphatase superfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
CATALYTIC ACTIVITY: Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate; Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268, ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25; Evidence={ECO:0000250|UniProtKB:P29218}; CATALYTIC ACTIVITY: Reaction=alpha-D-galactose 1-phosphate + H2O = D-galactose +...
null
PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
null
null
FUNCTION: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol monophosphates, myo-inositol 1,3-diphosphate, myo-inosi...
Mus musculus (Mouse)
O55026
ENTP2_MOUSE
MAGKLVSLVPPLLLAAVGLAGLLLLCVPTQDVREPPALKYGIVLDAGSSHTSMFVYKWPADKENDTGIVGQHSSCDVRGGGISSYANDPSRAGQSLVECLEQALRDVPKDRYASTPLYLGATAGMRLLNLTSPEATAKVLEAVTQTLTRYPFDFRGARILSGQDEGVFGWVTANYLLENFIKYGWVGRWIRPRKGTLGAMDLGGASTQITFETTSPSEDPDNEVHLRLYGQHYRVYTHSFLCYGRDQVLQRLLASALQIHRFHPCWPKGYSTQVLLREVYQSPCTMGQRPQTFNSSATVSLSGTSNAALCRDLVSGLFNI...
3.6.1.-
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
cellular response to interleukin-6 [GO:0071354]; G protein-coupled receptor signaling pathway [GO:0007186]; nucleoside diphosphate catabolic process [GO:0009134]; platelet activation [GO:0030168]; purine ribonucleoside diphosphate catabolic process [GO:0009181]
basement membrane [GO:0005604]; cell body [GO:0044297]; cell projection membrane [GO:0031253]; cell surface [GO:0009986]; plasma membrane [GO:0005886]
ADP phosphatase activity [GO:0043262]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; GDP phosphatase activity [GO:0004382]; identical protein binding [GO:0042802]; nucleoside diphosphate phosphatase activity [GO:0017110]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase a...
PF01150;
3.30.420.40;3.30.420.150;
GDA1/CD39 NTPase family
null
SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O55028
BCKD_MOUSE
MILTSVLGSGPRSWSSLWPLLGSSLSLRARSTSATDTHHVELARERSKTVTSFYNQSAIDVAAEKPSVRLTPTMMLYSGRSQDGSHLLKSGRYLQQELPVRIAHRIKGFRSLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIQDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDIDLIIRISDRGGGI...
2.7.11.1; 2.7.11.4
null
branched-chain amino acid catabolic process [GO:0009083]; isoleucine catabolic process [GO:0006550]; leucine catabolic process [GO:0006552]; lipid biosynthetic process [GO:0008610]; phosphorylation [GO:0016310]; regulation of glucose metabolic process [GO:0010906]; spermatogenesis [GO:0007283]; valine catabolic process...
mitochondrial oxoglutarate dehydrogenase complex [GO:0009353]; mitochondrion [GO:0005739]
[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity [GO:0047323]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine phospha...
PF10436;PF02518;
1.20.140.20;3.30.565.10;
PDK/BCKDK protein kinase family
PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O14874}.
SUBCELLULAR LOCATION: Mitochondrion matrix. Mitochondrion {ECO:0000250|UniProtKB:O14874}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[3-methyl-2-oxobutanoate dehydrogenase] = ADP + H(+) + O-phospho-L-seryl-[3-methyl-2-oxobutanoate dehydrogenase]; Xref=Rhea:RHEA:17301, Rhea:RHEA-COMP:13695, Rhea:RHEA-COMP:13696, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; E...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with PPM1K, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial...
Mus musculus (Mouse)
O55029
COPB2_MOUSE
MPLRLDIKRKLTARSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTLEGHAQNVSCASFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHS...
null
null
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
COPI vesicle coat [GO:0030126]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
protein kinase C binding [GO:0005080]; structural molecule activity [GO:0005198]
PF04053;PF00400;
1.25.40.470;2.130.10.10;
WD repeat COPB2 family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17360540}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:000...
null
null
null
null
null
FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra...
Mus musculus (Mouse)
O55033
NCK2_MOUSE
MTEEVIVIAKWDYTAQQDQELDIRKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKNSLKKGSLVKNLKDTLGLGKTRRKPSARDASPTPSTDAEYPANGSGADRIYDLNIPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSFNGQIGWFPSNYVLEEADEAAAEAPSFLSLRRGTALSNGQGARVLHVVQTLYPFSSVTEEELSFEKGETMEVIEKPENDPEWWKCKNARGQVGLVPKNYVVVLSDGPALHPAHTPQISYTGPSASGRFAGREWYYGNVTRHQAECALNERGVEGDFLIRDSESSPSDF...
null
null
actin filament organization [GO:0007015]; cell migration [GO:0016477]; dendritic spine development [GO:0060996]; ephrin receptor signaling pathway [GO:0048013]; immunological synapse formation [GO:0001771]; lamellipodium assembly [GO:0030032]; negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosp...
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; postsynaptic density [GO:0014069]; synapse [GO:0045202]; vesicle membrane [GO:0012506]
phosphotyrosine residue binding [GO:0001784]; protein-containing complex binding [GO:0044877]; receptor tyrosine kinase binding [GO:0030971]; scaffold protein binding [GO:0097110]; signaling adaptor activity [GO:0035591]
PF00017;PF00018;PF14604;
3.30.505.10;2.30.30.40;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
null
null
null
null
null
FUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling (By sim...
Mus musculus (Mouse)
O55034
SPAG4_RAT
MRRNPRPGSAASSHNHTPNFYSENSNSSHSATSGDSNGRRSAGPELGEPDGRMARGSSCGEPALSSGVPGGDTWAGSSRPKLAPRSHNGQTACGAATVRGGASEPSGSPAVLEEQLNLLPILDLRQEMPPPPVSKSFLSLFFQVLSVFLSLVADGLVCVYREICSIRFLFTAVSLLSIFLAALWWGLLYLIPPLENEPKEMLTLSQYHHRVHSQGQQLQQLQAELSKLHKEVTSVRAAHSERVAKLVFQRLNEDFVRKPDYALSSVGASIDLEKTSSDYEDRNTAYFWNRLSFWNYARPPSVILEPDVFPGNCWAFEGEQ...
null
null
cell differentiation [GO:0030154]; spermatogenesis [GO:0007283]
cytoplasm [GO:0005737]; meiotic nuclear membrane microtubule tethering complex [GO:0034993]; microtubule [GO:0005874]; motile cilium [GO:0031514]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]
identical protein binding [GO:0042802]; protein-membrane adaptor activity [GO:0043495]
PF07738;
2.60.120.260;
null
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10373309}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:10373309}. Nucleus envelope {ECO:0000250|UniProtKB:Q9JJF2}. Nucleus inner membrane {ECO:0000250|UniProtKB:Q9JJF2}...
null
null
null
null
null
FUNCTION: Involved in spermatogenesis. Required for sperm head formation but not required to establish and maintain general polarity of the sperm head. Required for anchoring and organization of the manchette. Required for targeting of SUN3 and probably SYNE1 through a probable SUN1:SYNE3 LINC complex to the nuclear en...
Rattus norvegicus (Rat)
O55035
PPIG_RAT
MGIKVQRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILSCGELVPKSKVKKEEKKRHKSSSSSSSSDSDSSSDSQSSSDSSDSESASEEKSRKRKKKHRKNSRKHKKEKKKRKKSKKSPSSESEADNVDAQPQSTVRPEEIPPIPENRFLMRKSPPKADDKERKNRERERERECNPPNSQPASYQR...
5.2.1.8
null
protein folding [GO:0006457]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]
PF00160;
2.40.100.10;
null
null
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:9525923}. Nucleus speckle {ECO:0000269|PubMed:9525923}. Note=Colocalizes with splicing factors at nuclear speckles. {ECO:0000269|PubMed:9525923}.
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000269|PubMed:9525923};
null
null
null
null
FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing. {ECO:0000269|PubMed:9525923}.
Rattus norvegicus (Rat)
O55036
TERF1_CRIGR
MAEDVSSTAPSPRGCADGRDADPTEEQMAQTQRNDQDQFECQELLECQVQVGAPDEEEEEEEDSGLVAEAEAVAAGWMLHFLCLSLCRAFRDGRSEDFRRTRNSAEAIIHGLSSLTACQLRTIYICQFLTRIAAGKTLDAQFENDERITPLESALMIWGSIEKEHDKLHEEIQNLIKIPAIAVCMENGNFKEAEEVFERIFGDPNSHMPFKSKLLMIISQKDTFHSFFQHFSYYHMMEKIKSYVNYVLSEKSSTFLMKAAAKVVESKRTRTITSQDKPSGNDVEMETEANLDTRKSVSDKQSAVTESSEGTVSLLRSHKN...
null
null
cell cycle [GO:0007049]; cell division [GO:0051301]; negative regulation of DNA replication [GO:0008156]; negative regulation of telomeric D-loop disassembly [GO:1905839]; telomere maintenance via telomerase [GO:0007004]
cytoplasm [GO:0005737]; nuclear telomere cap complex [GO:0000783]; nucleus [GO:0005634]; spindle [GO:0005819]
ankyrin repeat binding [GO:0071532]; DNA binding, bending [GO:0008301]; double-stranded telomeric DNA binding [GO:0003691]; G-rich strand telomeric DNA binding [GO:0098505]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; telomerase activity [GO:0003720]
PF00249;PF08558;
1.10.10.60;1.25.40.210;
null
PTM: Phosphorylated preferentially on Ser-219 in an ATM-dependent manner in response to ionizing DNA damage. {ECO:0000250}.; PTM: ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to bind to telomeric DNA. {ECO:0000250}.; PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the proteasome. Ubiquitina...
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}. Chromosome, telomere {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Colocalizes with telomeric DNA in interphase and prophase cells. Telomeric localization decreases in metaphase, anaphase and telophase. Associates with the mitot...
null
null
null
null
null
FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and negatively regulates telomere length. Involved in the regulation of the mitotic spindle. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-st...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O55038
CXL13_MOUSE
MRLSTATLLLLLASCLSPGHGILEAHYTNLKCRCSGVISTVVGLNIIDRIQVTPPGNGCPKTEVVIWTKMKKVICVNPRAKWLQRLLRHVQSKSLSSTPQAPVSKRRAA
null
null
activation of GTPase activity [GO:0090630]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; B cell chemotaxis [GO:0035754]; B cell chemotaxis across high endothelial venule [GO:0035769]; cell-cell signaling [GO:0007267]; cellular response to lipopolysaccharide [GO:0071222]; chemoki...
extracellular region [GO:0005576]; extracellular space [GO:0005615]
CCR10 chemokine receptor binding [GO:0031735]; chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; CXCR5 chemokine receptor binding [GO:0031724]; fibroblast growth factor binding [GO:0017134]; heparin binding [GO:0008201]; receptor ligand activit...
PF00048;
2.40.50.40;
Intercrine alpha (chemokine CxC) family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Strongly chemotactic for B-lymphocytes, weakly for spleen monocytes and macrophages but no chemotactic activity for granulocytes. Binds to BLR1/CXCR5. May play a role in directing the migration of B-lymphocytes to follicles in secondary lymphoid organs.
Mus musculus (Mouse)
O55042
SYUA_MOUSE
MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA
null
null
adult locomotory behavior [GO:0008344]; behavioral response to cocaine [GO:0048148]; cellular response to copper ion [GO:0071280]; cellular response to oxidative stress [GO:0034599]; chemical synaptic transmission [GO:0007268]; dopamine biosynthetic process [GO:0042416]; dopamine metabolic process [GO:0042417]; excitat...
actin cytoskeleton [GO:0015629]; axon terminus [GO:0043679]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular space [GO:0005615]; growth cone [GO:0030426]; inclusion body [GO:0016234]; mitochondrial inner membrane...
actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; arachidonic acid binding [GO:0050544]; beta-tubulin binding [GO:0048487]; calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; cuprous ion binding [GO:1903136]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:...
PF01387;
1.10.287.700;
Synuclein family
PTM: Phosphorylated, predominantly on serine residues. Phosphorylated on Tyr-125 upon osmotic stress. {ECO:0000250|UniProtKB:P37840}.; PTM: Ubiquitinated. The predominant conjugate is the diubiquitinated form. {ECO:0000250|UniProtKB:P37377}.; PTM: Acetylation at Met-1 seems to be important for proper folding and native...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31034892}. Membrane {ECO:0000250|UniProtKB:P37840}. Nucleus {ECO:0000250|UniProtKB:P37840}. Synapse {ECO:0000250|UniProtKB:P37840}. Secreted {ECO:0000250|UniProtKB:P37840}. Cell projection, axon {ECO:0000269|PubMed:17296554}. Note=Membrane-bound in dopaminergic neuron...
null
null
null
null
null
FUNCTION: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (By similarity). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (By s...
Mus musculus (Mouse)
O55043
ARHG7_RAT
MTDNANSQLVVRAKFNFQQTNEDELSFSKGDVIHVTRVEEGGWWEGTHNGRTGWFPSNYVREIKPSEKPVSPKSGTLKSPPKGFDTTAINKSYYNVVLQNILETEHEYSKELQSVLSTYLWPLQTSEKLSSANTSYLMGNLEEISSFQQVLVQSLEECTKSPEAQQRVGGCFLSLMPQMRTLYLAYCANHPSAVSVLTEHSEDLGEFMETKGASSPGILVLTTGLSKPFMRLDKYPTLLKELERHMEDYHPDRQDIQKSMTAFKNLSAQCQEVRKRKELELQILTEPIRSWEGDDIKTLGSVTYMSQVTIQCAGSEEKNE...
null
null
astrocyte cell migration [GO:0043615]; Golgi organization [GO:0007030]; hematopoietic progenitor cell differentiation [GO:0002244]; lamellipodium assembly [GO:0030032]; negative regulation of microtubule nucleation [GO:1905833]; positive regulation of apoptotic process [GO:0043065]; positive regulation of growth hormon...
cell cortex [GO:0005938]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; GABA-ergic synapse [GO:0098982]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; mitotic spindle pole [GO:0097431]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma ...
gamma-tubulin binding [GO:0043015]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein kinase binding [GO:0019901]
PF16523;PF00169;PF00621;PF16614;PF07653;
1.20.900.10;1.20.5.390;2.30.29.30;2.30.30.40;
null
PTM: Phosphorylated on Ser-516 by CaMK1; enhancement of GEF activity and downstream activation of RAC1. Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1 (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Note=Detected at cell adhesions. A small proportion is detected at focal adhesions.
null
null
null
null
null
FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and can induce membrane ruffling. Functions in cell migration, attachment and cell spreading. Promotes targeting of RAC1 to focal adhesions. May function as a positive regulator of apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade...
Rattus norvegicus (Rat)
O55044
G6PD_CRIGR
MAEQVALSRTQVCGILREELYQGDAFHQADTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPEDTFIVGYARSRLTVDDIRKQSEPFFKATPEERPKLEEFFARNSYVAGQYDDPASYKHLNSHMNALHQGMQANRLFYLALPPTVYEAVTKNIQETCMSQTGWNRIIVEKPFGRDLQSSNQLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTDSDDVRDEKVKVLKCISEVETSNVVLGQYVGNPNGEGEATN...
1.1.1.49
null
cellular response to oxidative stress [GO:0034599]; cholesterol biosynthetic process [GO:0006695]; erythrocyte maturation [GO:0043249]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glutathione metabolic process [GO:0006749]; NADP metabolic process [GO:0006739]; negative re...
centriolar satellite [GO:0034451]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]
glucose binding [GO:0005536]; glucose-6-phosphate dehydrogenase activity [GO:0004345]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]
PF02781;PF00479;
3.40.50.720;
Glucose-6-phosphate dehydrogenase family
PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity (By similarity). {ECO:0000250|UniProtKB:P11413}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11413}. Membrane {ECO:0000250|UniProtKB:P11413}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11413}.
CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; PhysiologicalDirection=left-to-right; ...
null
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000250|UniProtKB:P11413}.
null
null
FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty a...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O55047
TLK2_MOUSE
MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYDTSQGKGTPRGHKISDYFERRAEQPLYGLDGSAAKEASEEQSALPTLMSVMLAKPRLDTEQLAPRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQ...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q86UE8};
cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; chromosome segregation [GO:0007059]; DNA damage response [GO:0006974]; intracellular signal transduction [GO:0035556]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; peptidyl-serine phosphorylation [G...
intermediate filament [GO:0005882]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family
PTM: Phosphorylated at Ser-696, probably by CHEK1. {ECO:0000250}.; PTM: Autophosphorylated; phosphorylation promotes the assembly of higher order oligomers and enzymatic activity. {ECO:0000250|UniProtKB:Q86UE8}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10455159}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q86UE8}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10455159}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10455159}. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of ...
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:Q86UE8}; CATALYTI...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation (By similarity). Phosphorylates the chromatin assembly factors ASF1A and ASF1B (By similarity). Phosphorylation of ASF1A prevents its proteasome-me...
Mus musculus (Mouse)
O55055
TRDMT_MOUSE
MEPLRVLELYSGIGGMHHALRESHIPAHVVAAIDVNTVANEVYKHNFPHTHLLSKTIEGISLEDFDKLSFNMILMSPPCQPFTRIGLQGDMTDPRTTSFLYILDILPRLQKLPKYILLENVKGFEVSSTRGLLIQTIEACGFQYQEFLLSPSSLGIPNSRLRYFLIAKLQSEPFPFQAPGQILMEFPKIVTVEPQKYAVVEESQPRVQRTGPRICAESSSTQSSGKDTILFKLETVEERDRKHQQDSDLSVQMLKDFLEDGDTDEYLLPPKLLLRYALLLDIVKPTSRRSMCFTKGYGSYIEGTGSVLQAAEDAQIENIY...
2.1.1.204
null
response to amphetamine [GO:0001975]; tRNA methylation [GO:0030488]; tRNA stabilization [GO:0036416]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
RNA binding [GO:0003723]; tRNA (cytidine-5-)-methyltransferase activity [GO:0016428]; tRNA methyltransferase activity [GO:0008175]
PF00145;
3.90.120.10;3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, C5-methyltransferase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14717}.
CATALYTIC ACTIVITY: Reaction=cytidine(38) in tRNA + S-adenosyl-L-methionine = 5-methylcytidine(38) in tRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42956, Rhea:RHEA-COMP:10299, Rhea:RHEA-COMP:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.204; Ev...
null
null
null
null
FUNCTION: Specifically methylates cytosine 38 in the anticodon loop of tRNA(Asp) (PubMed:21183079, PubMed:22885326, PubMed:26271101). Has higher activity on tRNA(Asp) modified with queuosine at position 34 (By similarity). {ECO:0000250|UniProtKB:O14717, ECO:0000269|PubMed:21183079, ECO:0000269|PubMed:22885326, ECO:0000...
Mus musculus (Mouse)
O55058
FBLN4_CRIGR
MLPFASCLPGSLLLWALLLLLLGAASPQDSEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVINDLHGEGPPPPVPPAQHPNPCPPGYEPDEQESCVDVDECAQALHDCRPSQDCHNLPGSYQCTCPDGYRKVGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECSYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYV...
null
null
aorta development [GO:0035904]; aorta smooth muscle tissue morphogenesis [GO:0060414]; elastic fiber assembly [GO:0048251]; negative regulation of vascular associated smooth muscle cell proliferation [GO:1904706]; positive regulation of aortic smooth muscle cell differentiation [GO:1904831]; positive regulation of coll...
basement membrane [GO:0005604]; elastic fiber [GO:0071953]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; microfibril [GO:0001527]
calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; protein homodimerization activity [GO:0042803]
PF12662;PF07645;PF12661;
2.10.25.10;
Fibulin family
PTM: N-glycosylated; contains mostly complex-type glycans. Not O-glycosylated. {ECO:0000250|UniProtKB:O95967}.; PTM: Cleaved by ELANE; produces a 50-55 kDa fragment. Cleaved by MMP2 and MMP9; produces several fragments. {ECO:0000250|UniProtKB:O95967}.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9WVJ9}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q9WVJ9}. Note=Localizes on the microfibrils surrounding ELN cores. {ECO:0000250|UniProtKB:Q9WVJ9}.
null
null
null
null
null
FUNCTION: Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall i...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O55070
DNSL3_MOUSE
MSLHPASPRLASLLLFILALHDTLALRLCSFNVRSFGASKKENHEAMDIIVKIIKRCDLILLMEIKDSSNNICPMLMEKLNGNSRRSTTYNYVISSRLGRNTYKEQYAFVYKEKLVSVKTKYHYHDYQDGDTDVFSREPFVVWFHSPFTAVKDFVIVPLHTTPETSVKEIDELVDVYTDVRSQWKTENFIFMGDFNAGCSYVPKKAWQNIRLRTDPKFVWLIGDQEDTTVKKSTSCAYDRIVLCGQEIVNSVVPRSSGVFDFQKAYDLSEEEALDVSDHFPVEFKLQSSRAFTNNRKSVSLKKRKKGNRS
3.1.21.-
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q13609}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q13609};
apoptotic DNA fragmentation [GO:0006309]; DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; programmed cell death involved in cell development [GO:0010623]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:007094...
endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; nucleus [GO:0005634]
deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]; DNA endonuclease activity [GO:0004520]; endonuclease activity [GO:0004519]
PF03372;
3.60.10.10;
DNase I family
PTM: Poly-ADP-ribosylated by PARP1. ADP-ribosylation negatively regulates enzymatic activity during apoptosis. {ECO:0000250|UniProtKB:Q13609}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13609, ECO:0000269|PubMed:12050166}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13609}. Secreted {ECO:0000269|PubMed:12095301, ECO:0000269|PubMed:15796714, ECO:0000269|PubMed:27293190}. Note=Contradictory reports exist about the subcellular localization under nor...
null
null
null
null
null
FUNCTION: Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (By similarity). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA (PubMed:12095301, PubMed:15796714, PubMed:19154352). Acts in internucleos...
Mus musculus (Mouse)
O55074
AKA7A_MOUSE
MGQLCCFPFARDEGKICEKDRREPEDAELVRLSKRLVENAVLKAVQQYLEETQNKKQPGEGNSTKAEEGDRNGDGSDNNRK
null
null
modulation of chemical synaptic transmission [GO:0050804]; protein localization [GO:0008104]; regulation of protein kinase A signaling [GO:0010738]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178]
apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; exocytic vesicle [GO:0070382]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; lateral plasma membrane [GO:0016328]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; sarcoplasmic reticulum [GO:0016529]; T-tubule [GO:0030315]
AMP binding [GO:0016208]; protein domain specific binding [GO:0019904]; protein kinase A binding [GO:0051018]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]
PF10470;
null
null
null
SUBCELLULAR LOCATION: Lateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000269|PubMed:9545239}.
null
null
null
null
null
FUNCTION: Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by i...
Mus musculus (Mouse)
O55075
CADH2_CRIGR
TKPLDRELIARFHLRAHAVDINGNRVENPIDIVINVIDMNDNRPEFLHQVWNGSVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRILSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVEVIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIHTDPNSNDGLVTVVKPIDFETNRMFV
null
null
adherens junction organization [GO:0034332]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [...
adherens junction [GO:0005912]; apical part of cell [GO:0045177]; catenin complex [GO:0016342]; cell junction [GO:0030054]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; lamellipodium [GO:0030027]; neuron projection [GO:0043005]; plasma membrane [GO:0005886];...
cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]
PF00028;
2.60.40.60;
null
PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound C-terminal fragment 1 (CTF1), which is further cleaved by gamma-secretase into a 35 kDa. Cleavage in neural stem cells by MMP24 affects CDH2-mediated anchorage of neural stem ce...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction {ECO:0000250|UniProtKB:P19022}. Cell surface {ECO:0000250|UniProtKB:P15116}. Cell junction, desmosome {ECO:0000250|UniProtKB:P151...
null
null
null
null
null
FUNCTION: Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O55076
CDK2_CRIGR
MENFQKVEKIGEGTYGVVYKAKNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASAVTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINAEGSIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
2.7.11.22
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P24941}; Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:P24941};
cell division [GO:0051301]; DNA repair [GO:0006281]; G1/S transition of mitotic cell cycle [GO:0000082]; meiotic cell cycle [GO:0051321]; protein phosphorylation [GO:0006468]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of gene expression [GO:0010468]; response to organic substance [GO:...
Cajal body [GO:0015030]; centrosome [GO:0005813]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; endosome [GO:0005768]; midbody [GO:0030496]
ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein kinase activity [GO:0097472]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
PTM: Phosphorylated at Thr-160 by CDK7 in a CAK complex. Phosphorylation at Thr-160 promotes kinase activity, whereas phosphorylation at Tyr-15 by WEE1 reduces slightly kinase activity. Phosphorylated on Thr-14 and Tyr-15 during S and G2 phases before being dephosphorylated by CDC25A. {ECO:0000250|UniProtKB:P24941}.; P...
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Nucleus, Cajal body {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Note=Localized at the centrosomes in late G2 phase after separation of the centrosomes but before the start of prophase. Nuclear-cyt...
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=2.7.11.22; Evidence={ECO:0000269|PubMed:11506705}; CATALYTI...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis (PubMed:11506705). Phosphorylates CABLES1, CTNNB1, CDK2AP2, ERCC6, NBN, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at t...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O55082
PTN20_MOUSE
MSSPRKVRGKTGRDNDEEEGNSGNLNLRNSLPSSSQKMTPTKPIFGNKMNSENVKPSHHLSFSDKYELVYPEPLESDTDETVWDVSDRSLRNRWNSMDSETAGPSKTVSPVLSGSSRLSKDTETSVSEKELTQLAQIRPLIFNSSARSAMRDCLNTLQKKEELDIIREFLELEQMTLPDDFNSGNTLQNRDKNRYRDILPYDSTRVPLGKNKDYINASYIRIVNHEEEYFYIATQGPLPETIEDFWQMVLENNCNVIAMITREIECGVIKCYSYWPISLKEPLEFEHFSVFLETFHVTQYFTVRVFQIVKKSTGKSQCVK...
3.1.3.48
null
dephosphorylation [GO:0016311]
centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; microtubule [GO:0005874]; nucleus [GO:0005634]
phosphoprotein phosphatase activity [GO:0004721]
PF00102;
3.90.190.10;
Protein-tyrosine phosphatase family, Non-receptor class subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with the microtubule-organizing center and intracellular membrane compartments. {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, ECO:0000269|PubMe...
null
null
null
null
FUNCTION: Tyrosine-protein phosphatase targeted to sites of actin polymerization in response of varied extracellular stimuli. Has tyrosine phosphatase activity towards various tyrosyl phosphorylated substrates.
Mus musculus (Mouse)
O55087
MEF2B_MOUSE
MGRKKIQISRILDQRNRQVTFTKRKFGLMKKAYELSVLCDCDIALIIFNSAQRLFQYASSDMDRVLLKYTEYSEPHESRTNADILQTLKRRGVGLDGPELDMEEGPEGPGEKLLRTLGGDRGSASPRPRIYPVAPAMSVSELSYRVPPATPGCDPGGLGEVPSVHSRPAYFRPPGLGHPIFSPSHLASKTPPPLYLATDGRRPDLPPGLVGARGGLGTSRSLYSGLQSPGAPGPALGSFAFLPSGSTDCSPGDAAQGPLQPSPWPPTRDAVDPARPVARSLCKEGPPSRGASPPTPPVSIKSERLSPVTGTSGDFPRSFP...
null
null
cell differentiation [GO:0030154]; heart development [GO:0007507]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]
nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; histone deacetylase binding [GO:0042826]; protein dimerization activity [GO:0046983]; RNA pol...
PF00319;
3.40.1810.10;
MEF2 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
null
null
null
null
null
FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Activates transcription via this element. May be involved in muscle-specific and/or growth factor-related transcription. {ECO:0000269|PubMed:8668199, ECO:0000269|PubMed:9443808...
Mus musculus (Mouse)
O55091
IMPCT_MOUSE
MAEEEVGNSQRQSEEIEAMAAIYGEEWCVIDENAKIFCIRVTDFMDDPKWTLCLQVMLPSEYPGTAPPSYQLNAPWLKGQERADLSNSLEEIYVHNMGESILYQWVEKIRDALIQKSQITEPDPDVKKKTEEVEVESEEDPILEHPPENPVKTLDLKISEETQPETEELPPVAHGVPITDRRSTFQAHVAPVVCPEQVKLVLAKLYENKKIASATHNIYAYRIFCEDKQTFLQDCEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNFTNTPDESTKNLGKKKVKKDKKKNDH
null
null
cellular response to amino acid starvation [GO:0034198]; GCN2-mediated signaling [GO:0140469]; intracellular signal transduction [GO:0035556]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron projection extension [GO:1990138]; po...
cytoplasm [GO:0005737]; cytosol [GO:0005829]
actin binding [GO:0003779]; protein sequestering activity [GO:0140311]; ribosome binding [GO:0043022]
PF05773;PF01205;
3.30.230.30;3.10.110.10;
IMPACT family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23447528}.
null
null
null
null
null
FUNCTION: Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated...
Mus musculus (Mouse)
O55092
SLK_CAVPO
MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWETIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLKKCLEKNVDARWTTSQLLQHPFVTIDSNKPIRELIAEAKAEVTEEVEDGKE...
2.7.11.1
null
apoptotic process [GO:0006915]; protein autophosphorylation [GO:0046777]; regulation of cell migration [GO:0030334]; regulation of focal adhesion assembly [GO:0051893]
cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF12474;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Proteolytically cleaved by caspase-3. {ECO:0000250}.; PTM: Autophosphorylated. {ECO:0000269|PubMed:9143322}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Mediates apoptosis and actin stress fiber dissolution. {ECO:0000250}.
Cavia porcellus (Guinea pig)
O55096
DPP3_RAT
MADTQYILPNDIGVSSLDCREAFRLLSPTERLYAHHLSRAAWYGGLAVLLQTSPEAPYIYALLSRLFRAQDPDQLRQHALAEGLTEEEYQAFLVYAAGVYSNMGNYKSFGDTKFVPNLPKEKLERVILGSKAAQQHPEEVRSLWQTCGELMFSLEPRLRHLGLGKEGVTTYFSGDCAMEDAKLAQDFLDSQNLSAYNTRLFKVVGQEGKYHYEVRLASVLNTEPALDSELTSKLKSYEFQGNHFQVTRGDYAPILQKVVEHLEKAKAYAANSHQEQMLAQYVESFTQGSIEAHKRGSRFWIQDKGPIVESYIGFIESYRD...
3.4.14.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10387075}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:10387075};
protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
cytoplasm [GO:0005737]; cytosol [GO:0005829]
aminopeptidase activity [GO:0004177]; dipeptidyl-peptidase activity [GO:0008239]; metalloexopeptidase activity [GO:0008235]; zinc ion binding [GO:0008270]
PF03571;
3.30.540.30;
Peptidase M49 family
null
SUBCELLULAR LOCATION: Cytoplasm.
CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.; EC=3.4.14.4;
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0.;
null
FUNCTION: Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin (By similarity). Also cleaves Arg-Arg-beta-naphthylamide. {ECO:0000250|UniProtKB:Q9NY33}.
Rattus norvegicus (Rat)
O55098
STK10_MOUSE
MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNDVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYYDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHGKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVLCETMKDAPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLQHPFVSRVTSNKALRELVAEAKAEVMEEIED...
2.7.11.1
null
cell cycle [GO:0007049]; lymphocyte aggregation [GO:0071593]; protein autophosphorylation [GO:0046777]; regulation of lymphocyte migration [GO:2000401]
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;PF12474;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylates following homodimerization, leading to activation of the protein. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator b...
Mus musculus (Mouse)
O55099
AURKB_RAT
MAQKENVYPWPYGSKTSQSGLNTLPQRVLRKEPAVTPAQALMNRSNSQSTAVPGQKLTENKGATALQGSQSRQPFTIDNFEIGRPLGKGKFGNVYLAREKKSRFIVALKILFKSQIEKEGVEHQLRREIEIQAHLKHPNILQLYNYFYDQQRIYLILEYAPRGELYKELQKSGTFDEQRTATIMEELSDALMYCHKKKVIHRDIKPENLLLGLQGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEMVDLWCIGVLCYELMVGNPPFESPSHSETYRRIVKVDLKFPSSMPLGAKDLISKLLKHNPSQRLP...
2.7.11.1
null
abscission [GO:0009838]; cell cycle G2/M phase transition [GO:0044839]; cellular response to UV [GO:0034644]; cleavage furrow formation [GO:0036089]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic spindle midzone assembly [GO:0051256]; mitotic spindle organization [GO:0007052]; negative regulation of B ...
chromocenter [GO:0010369]; chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindl...
ATP binding [GO:0005524]; histone H3S28 kinase activity [GO:0044022]; kinase binding [GO:0019900]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
PTM: The phosphorylation of Thr-235 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-235 phosphorylation is indispensable for the AURKB kinase activity. {ECO:0000250|UniProtKB:Q96GD4}.; PTM: Acetylated at Lys-218 by KAT5 at kinetochores, increasing AURKB activity and promoting...
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GD4}. Chromosome {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q96GD4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96GD4}. Midbody {ECO:0000250|UniPro...
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:Q96GD4}; CATALYTI...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (By similarity). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced micr...
Rattus norvegicus (Rat)
O55100
SNG1_MOUSE
MEGGAYGAGKAGGAFDPYTLVRQPHTILRVVSWVFSIVVFGSIVNEGYLNNPEEEEEFCIYNRNPNACSYGVTVGVLAFLTCLLYLALDVYFPQISSVKDRKKAVLSDIGVSAFWAFFWFVGFCFLANQWQVSKPKDNPLNEGTDAARAAIAFSFFSIFTWAGQAVLAFQRYQIGADSALFSQDYMDPSQDSSMPYAPYVEPSAGSDPAGMGGTYQHPANAFDAEPQGYQSQGY
null
null
cellular response to leukemia inhibitory factor [GO:1990830]; protein targeting [GO:0006605]; regulated exocytosis [GO:0045055]; regulation of long-term neuronal synaptic plasticity [GO:0048169]; regulation of short-term neuronal synaptic plasticity [GO:0048172]; synaptic vesicle membrane organization [GO:0048499]
melanosome [GO:0042470]; neuromuscular junction [GO:0031594]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
null
PF01284;
null
Synaptogyrin family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62876}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62876}. Melanosome {ECO:0000250|UniProtKB:O43759}.
null
null
null
null
null
FUNCTION: May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity (PubMed:...
Mus musculus (Mouse)
O55102
BL1S1_MOUSE
MLSRLLKEHQAKQNERKELQEKRRREAIAAATCLTEALVDHLNVGVAQAYMNQRKLDHEVKTLQVQAAQFAKQTGQWIGMVENFNQALKEIGDVENWARSIELDMRTIATALEYVYKGQLQSAPS
null
null
aerobic respiration [GO:0009060]; anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; endosomal transport [GO:0016197]; lysosome localization [GO:0032418]; melanosome organization [GO:0032438]; neuron projection development [GO:0031175]; organelle transport along microtubule ...
axon cytoplasm [GO:1904115]; BLOC-1 complex [GO:0031083]; BORC complex [GO:0099078]; cytoplasmic side of lysosomal membrane [GO:0098574]; cytosol [GO:0005829]; early endosome [GO:0005769]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
null
PF06320;
null
BLOC1S1 family
null
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:22309213}. Mitochondrion matrix {ECO:0000269|PubMed:22309213}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78537}. Lysosome membrane {ECO:0000250|UniProtKB:P78537}.
null
null
null
null
null
FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for...
Mus musculus (Mouse)
O55103
PRAX_MOUSE
MEARSRSAEELRRAELVEIIVETEAQTGVSGFNVAGGGKEGIFVRELREDSPAAKSLSLQEGDQLLSARVFFENFKYEDALRLLQCAEPYKVSFCLKRTVPTGDLALRPGTVSGYEMKGPRAKVAKLNIQSLAPVKKKKMVTGALGTPADLAPVDVEFSFPKFSRLRRGLKAEAVKGPVPAAPARRRLQLPRLRVREVAEEAQVARMAAAAPPPRKAKAEAEAATGAGFTAPQIELVGPRLPSAEVGVPQVSVPKGTPSTEAASGFALHLPTLGLGAPAAPAVEPPATGIQVPQVELPTLPSLPTLPTLPCLDTQEGAAV...
null
null
peripheral nervous system myelin formation [GO:0032290]; peripheral nervous system myelin maintenance [GO:0032287]; regulation of RNA splicing [GO:0043484]; sensory perception of pain [GO:0019233]; transmission of nerve impulse [GO:0019226]
anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
null
PF00595;
2.30.42.10;
Periaxin family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21745462}. Cell junction {ECO:0000269|PubMed:21745462}. Note=Colocalizes with ACTB at tricellular junctions between eye lens fiber cells. {ECO:0000269|PubMed:21745462}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:9488714}; Peripheral memb...
null
null
null
null
null
FUNCTION: Scaffolding protein that functions as part of a dystroglycan complex in Schwann cells, and as part of EZR and AHNAK-containing complexes in eye lens fiber cells (PubMed:11430802, PubMed:21745462, PubMed:22764250). Required for the maintenance of the peripheral myelin sheath that is essential for normal transm...
Mus musculus (Mouse)
O55111
DSG2_MOUSE
MARSPGDRCALLLLVQLLAVVCLDFGNGLHLEVFSPRNEGKPFPKHTHLVRQKRAWITAPVALREGEDLSRKNPIAKIHSDLAEEKGIKITYKYTGKGITEPPFGIFVFDRNTGELNITSILDREETPYFLLTGYALDSRGNNLEKPLELRIKVLDINDNEPVFTQEVFVGSIEELSAAHTLVMKITATDADDPETLNAKVSYRIVSQEPANSHMFYLNKDTGEIYTTSFTLDREEHSSYSLTVEARDGNGQITDKPVQQAQVQIRILDVNDNIPVVENKMYEGTVEENQVNVEVMRIKVTDADEVGSDNWLANFTFASG...
null
null
bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell-cell adhesion [GO:0098609]; desmosome organization [GO:0002934]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; maternal process involved in female pregnancy [GO:0060135]; Purkinje myocyte devel...
apical plasma membrane [GO:0016324]; desmosome [GO:0030057]; intercalated disc [GO:0014704]; intracellular membrane-bounded organelle [GO:0043231]; lateral plasma membrane [GO:0016328]
calcium ion binding [GO:0005509]; cell adhesion molecule binding [GO:0050839]
PF00028;
2.60.40.60;4.10.900.10;
null
PTM: Palmitoylated by ZDHHC5 at the plasma membrane. {ECO:0000250|UniProtKB:Q14126}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14126}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q14126}. Cell junction, desmosome {ECO:0000250|UniProtKB:Q14126}.
null
null
null
null
null
FUNCTION: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion.
Mus musculus (Mouse)
O55112
AFF2_MOUSE
MDLFDFFRDWDLEQQCHYEQDRSALKKREWERRNQEVQQEEDLFSSGFDLFGEPYKVAEYTNKGDALANRVQNTLGSYDEMKDLLSNHSSQNHLVGIPKNSAPQTPISKSEASFYPEQKNRMIPSHQETTHSSTPMPPPSVVILNSTLIHSNRKSKSEWPRDSHNTSPAQASQTSSQPNKMQTSTQDPPQTRLEDFFVYPAEQPQIGTVEKSNPSSKEENNPNSGGEDTFKEIFQSNSPEESEFTVQAPGSPLVASSLLAPSSGLSVPTFPPGLYCKTSMGQQKPTAYVRPMDGQDQATDISPTLKPSIEFENSFGNLSF...
null
null
learning or memory [GO:0007611]; mRNA processing [GO:0006397]; negative regulation of gene expression [GO:0010629]; nuclear speck organization [GO:0035063]; regulation of gene expression [GO:0010468]; regulation of RNA splicing [GO:0043484]; RNA splicing [GO:0008380]
nuclear speck [GO:0016607]; nucleus [GO:0005634]
G-quadruplex RNA binding [GO:0002151]
PF05110;PF18875;PF18876;
6.10.250.2670;
AF4 family
null
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19136466}. Note=When splicing or transcription are inhibited, accumulates in large, rounded speckles and in the nucleolus. {ECO:0000250}.
null
null
null
null
null
FUNCTION: RNA-binding protein. Might be involved in alternative splicing regulation through an interaction with G-quartet RNA structure. {ECO:0000269|PubMed:19136466}.
Mus musculus (Mouse)
O55123
MMP10_MOUSE
MEPLAILALLSLPICSAYPLHGAVTQGHPSMDLAQQYLEKYYNFKKNEKQIFKRKDSSPVVKKIQEMQKFLGLEMTGKLDSNTMELMHKPRCGVPDVGGFSTFPGSPKWRKSHITYRIVNYTPDLPRQSVDSAIEKALKVWEEVTPLTFSRISEGEADIMISFAVGEHGDFYPFDGPGQSLAHAYPPGPGFYGDVHFDDDEKWTLAPSGTNLFLVAAHELGHSLGLFHSDKKESLMYPVYRFSTSPANFHLSQDDIEGIQSLYGAGPSSDATVVPVLSVSPRPETPDKCDPALSFDSVSTLRGEVLFFKDRYFWRRSHWN...
3.4.24.22
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; regulation of cell migration [GO:0030334]
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
PF00045;PF00413;PF01471;
3.40.390.10;2.110.10.10;
Peptidase M10A family
null
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=Similar to stromelysin 1, but action on collagen types III, IV and V is weak.; EC=3.4.24.22;
null
null
null
null
FUNCTION: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
Mus musculus (Mouse)
O55127
CP26A_MOUSE
MGLPALLASALCTFVLPLLLFLAALKLWDLYCVSSRDRSCALPLPPGTMGFPFFGETLQMVLQRRKFLQMKRRKYGFIYKTHLFGRPTVRVMGADNVRRILLGEHRLVSVHWPASVRTILGAGCLSNLHDSSHKQRKKVIMQAFSREALQCYVLVIAEEVSSCLEQWLSCGERGLLVYPEVKRLMFRIAMRILLGCEPGPAGGGEDEQQLVEAFEEMTRNLFSLPIDVPFSGLYRGVKARNLIHARIEENIRAKIRRLQATEPDGGCKDALQLLIEHSWERGERLDMQALKQSSTELLFGGHETTASAATSLITYLGLYP...
1.14.13.-
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
anterior/posterior pattern specification [GO:0009952]; cellular response to retinoic acid [GO:0071300]; central nervous system development [GO:0007417]; neural crest cell development [GO:0014032]; retinoic acid catabolic process [GO:0034653]; retinoic acid metabolic process [GO:0042573]; retinoic acid receptor signalin...
endoplasmic reticulum membrane [GO:0005789]
all-trans retinoic acid 18-hydroxylase activity [GO:0062183]; all-trans retinoic acid 4-hydrolase activity [GO:0062182]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, N...
PF00067;
1.10.630.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein. Microsome membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein.
CATALYTIC ACTIVITY: Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein reductase] = all-trans-(4S)-hydroxyretinoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51492, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:...
null
null
null
null
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:15911617, PubMed:9250660, PubMed:9442090). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-d...
Mus musculus (Mouse)
O55128
SAP18_MOUSE
MAVESRVTQEEIKKEPEKPIDREKTCPLLLRVFTTNNGRHHRMDEFSRGNVPSSELQIYTWMDATLKELTSLVKEVYPEARKKGTHFNFAIVFMDLKRPGYRVKEIGSTMSGRKGTDDSMTLQSQKFQIGDYLDIAITPPNRAPPSSGRMRPY
null
null
mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of apoptotic process [GO:0043065]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of DNA-templated tra...
ASAP complex [GO:0061574]; cytoplasm [GO:0005737]; histone deacetylase complex [GO:0000118]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
transcription corepressor activity [GO:0003714]
PF06487;
3.10.20.550;
SAP18 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00422}. Cytoplasm {ECO:0000250|UniProtKB:O00422}. Nucleus speckle {ECO:0000250|UniProtKB:O00422}. Note=Shuttles between the nucleus and the cytoplasm (By similarity). Colocalizes with ACIN1 and SRSF2 in nuclear speckles (By similarity). {ECO:0000250|UniProtKB:O00422...
null
null
null
null
null
FUNCTION: Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) ...
Mus musculus (Mouse)
O55131
SEPT7_MOUSE
MSVSARSAAAEERSVNCGTMAQPKNLEGYVGFANLPNQVYRKSVKRGFEFTLMVVGESGLGKSTLINSLFLTDLYSPEYPGPSHRIKKTVQVEQSKVLIKEGGVQLLLTIVDTPGFGDAVDNSNCWQPVIDYIDSKFEDYLNAESRVNRRQMPDNRVQCCLYFIAPSGHGLKPLDIEFMKRLHEKVNIIPLIAKADTLTPEECQQFKKQIMKEIQEHKIKIYEFPETDDEEENKLVKKIKDRLPLAVVGSNTIIEVNGKRVRGRQYPWGVAEVENGEHCDFTILRNMLIRTHMQDLKDVTNNVHYENYRSRKLAAVTYNG...
null
null
cilium assembly [GO:0060271]; collateral sprouting [GO:0048668]; cortical cytoskeleton organization [GO:0030865]; cytoskeleton-dependent cytokinesis [GO:0061640]; dendritic spine morphogenesis [GO:0060997]; glucose import [GO:0046323]; mitotic cytokinesis [GO:0000281]; postsynapse organization [GO:0099173]; pseudopodiu...
axon terminus [GO:0043679]; axoneme [GO:0005930]; cell cortex [GO:0005938]; cell division site [GO:0032153]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; kinetochore [GO:0000776]; membrane [GO:0016020]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; motile cili...
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; molecular adaptor activity [GO:0060090]; structural constituent of postsynapse [GO:0099186]
PF00735;
3.40.50.300;
TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily, Septin GTPase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17546647}. Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000250|U...
null
null
null
null
null
FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements. Forms a filamentou...
Mus musculus (Mouse)
O55134
PCD12_MOUSE
MMLLLPFLLGLLGPGSYLFISGDCQEVATVMVKFQVTEEVPSGTVIGKLSQELRVEERRGKAGDAFQILQLPQALPVQMNSEDGLLSTSSRLDREKLCRQEDPCLVSFDVLATGASALIHVEIQVLDINDHQPQFPKDEQELEISESASLHTRIPLDRALDQDTGPNSLYSYSLSPSEHFALDVIVGPDETKHAELVVVKELDRELHSYFDLVLTAYDNGNPPKSGISVVKVNVLDSNDNSPVFAESSLALEIPEDTVPGTLLINLTATDPDQGPNGEVEFFFGKHVSPEVMNTFGIDAKTGQIILRQALDYEKNPAYEV...
null
null
calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell adhesion [GO:0007155]; glycogen metabolic process [GO:0005977]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; labyrinthine layer development [GO:0060711]
cell-cell junction [GO:0005911]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]
PF00028;PF08266;
2.60.40.60;
null
PTM: N-glycosylated. {ECO:0000269|PubMed:15541725}.; PTM: [Protocadherin-12]: Cleaved by ADAM10 close to the transmembrane domain to release the Protocadherin-12, secreted form in the serum. Cleavage results in reduced cellular adhesion in a cell migration assay. {ECO:0000250|UniProtKB:Q9NPG4}.
SUBCELLULAR LOCATION: [Protocadherin-12]: Cell membrane {ECO:0000250|UniProtKB:Q9NPG4}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000269|PubMed:9651350}.; SUBCELLULAR LOCATION: [Protocadherin-12, secreted form]: Secreted {ECO:0000250|UniProtKB:Q9NPG4}. Note=The secreted form is produced fol...
null
null
null
null
null
FUNCTION: Cellular adhesion molecule that may play an important role in cell-cell interactions at interendothelial junctions (PubMed:9651350). Acts as a regulator of cell migration, probably via increasing cell-cell adhesion (By similarity). Promotes homotypic calcium-dependent aggregation and adhesion and clusters at ...
Mus musculus (Mouse)
O55135
IF6_MOUSE
MAVRASFENNCEVGCFAKLTNAYCLVAIGGSENFYSVFEGELSDAIPVVHASIAGCRIIGRMCVGNRHGLLVPNNTTDQELQHIRNSLPDSVQIRRVEERLSALGNVTTCNDYVALVHPDLDRETEEILADVLKVEVFRQTVADQVLVGSYCVFSNQGGLVHPKTSIEDQDELSSLLQVPLVAGTVNRGSEVIAAGMVVNDWCAFCGLDTTSTELSVVESVFKLNEAKPSTIATSMRDSLIDSLT
null
null
assembly of large subunit precursor of preribosome [GO:1902626]; cytosolic ribosome assembly [GO:0042256]; maturation of 5.8S rRNA [GO:0000460]; maturation of LSU-rRNA [GO:0000470]; miRNA-mediated gene silencing by inhibition of translation [GO:0035278]; miRNA-mediated post-transcriptional gene silencing [GO:0035195]; ...
cytosol [GO:0005829]; intermediate filament [GO:0005882]; lamin filament [GO:0005638]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; preribosome, large subunit precursor [GO:0030687]; synapse [GO:0045202]
ribosomal large subunit binding [GO:0043023]; ribosome binding [GO:0043022]; translation initiation factor activity [GO:0003743]
PF01912;
null
EIF-6 family
PTM: Phosphorylation at Ser-174 and Ser-175 by CSNK1D/CK1 promotes nuclear export. {ECO:0000250|UniProtKB:P56537}.; PTM: Ufmylated by UFL1. {ECO:0000269|PubMed:28575669}.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Shuttles between cytoplasm and nucleus/nucleolus.
null
null
null
null
null
FUNCTION: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunit...
Mus musculus (Mouse)
O55137
ACOT1_MOUSE
MEATLNLEPSGRSCWDEPLSIAVRGLAPEQPVTLRSVLRDEKGALFRAHARYRADSHGELDLARTPALGGSFSGLEPMGLLWAMEPDRPFWRLVKRDVQTPFVVELEVLDGHEPDGGQRLAHAVHERHFLAPGVRRVPVREGRVRATLFLPPEPGPFPGIIDLFGVGGGLLEYRASLLAGKGFAVMALAYYNYDDLPKNMETMHMEYFEEAVNYLRSHPEVKGPGIGLLGISKGGELGLAMASFLKGITAAVVINGSVAAVGNTISYKDETIPPVTILRNQVKMTKDGLKDVVDALQSPLVDKKSFIPVERSDTTFLFLV...
3.1.2.-; 3.1.2.2
null
acyl-CoA metabolic process [GO:0006637]; fatty acid metabolic process [GO:0006631]; long-chain fatty acid metabolic process [GO:0001676]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
carboxylic ester hydrolase activity [GO:0052689]; fatty acyl-CoA hydrolase activity [GO:0047617]
PF08840;PF04775;
2.60.40.2240;3.40.50.1820;
C/M/P thioester hydrolase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O88267}.
CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000269|PubMed:11694534}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.6 uM for C16:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=15.2 uM for C10:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=2.6 uM for C12:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=3.5 uM for C14:0-acyl-CoA {ECO:0000269|PubMed:11694534}; KM=0.5 uM for C20:0-acyl-Co...
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:11694534}.
null
null
FUNCTION: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. More active towards saturated and unsaturated long chain fatty acyl-CoAs (C12-C20). {ECO:0000269|PubMed:11694534}.
Mus musculus (Mouse)
O55142
RL35A_MOUSE
MSGRLWCKAIFAGYKRGLRNQREHTALLKIEGVYARDETEFYLGKRCAYVYKAKNNTVTPGGKPNKTRVIWGKVTRAHGNSGMVRAKFRSNLPAKAIGHRIRVMLYPSRI
null
null
cytoplasmic translation [GO:0002181]; ribosomal large subunit biogenesis [GO:0042273]; translation at postsynapse [GO:0140242]; translation at presynapse [GO:0140236]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; mitochondrion [GO:0005739]; postsynapse [GO:0098794]; presynapse [GO:0098793]; ribosome [GO:0005840]; synapse [GO:0045202]
structural constituent of ribosome [GO:0003735]
PF01247;
2.40.10.190;
Eukaryotic ribosomal protein eL33 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}.
null
null
null
null
null
FUNCTION: Component of the large ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). Required for the proliferation and viability of hematopoietic cells (By similarity). {ECO:0000250|UniProtKB:P18077, ECO:0000269...
Mus musculus (Mouse)
O55143
AT2A2_MOUSE
MENAHTKTVEEVLGHFGVNESTGLSLEQVKKLKERWGSNELPAEEGKTLLELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILVANAIVGVWQERNAENAIEALKEYEPEMGKVYRQDRKSVQRIKAKDIVPGDIVEIAVGDKVPADIRLTSIKSTTLRVDQSILTGESVSVIKHTDPVPDPRAVNQDKKNMLFSGTNIAAGKAMGVVVATGVNTEIGKIRDEMVATEQERTPLQQKLDEFGEQLSKVISLICIAVWIINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLA...
7.2.2.10
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P11607};
autophagosome assembly [GO:0000045]; autophagosome membrane docking [GO:0016240]; calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; calcium ion transport from cytosol to endoplasmic reticulum [GO:1903515]; cardiac muscle hy...
apical ectoplasmic specialization [GO:0061831]; endoplasmic reticulum [GO:0005783]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane bounded cell projection [GO:0120025]; protein-containing complex [GO:0032991];...
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; enzyme binding [GO:0019899]; lncRNA binding [GO:0106222]; lutropin-choriogonadotropic hormone receptor binding [GO:0031775]; P-type calcium transporter activity [GO:0005388]; P-type calcium transporter activity involved in...
PF13246;PF00689;PF00690;PF00122;PF00702;
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily
PTM: Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity. {ECO:0000250|UniProtKB:P16615}.; PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia, leading to its inactivation. {ECO:0000269|PubMed:32116663}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23395171, ECO:0000269|PubMed:32973183}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:22355118}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with FLVCR2 at the mitochondrial-ER conta...
CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000269|PubMed:28890335}; PhysiologicalDirection=left-to-right; ...
null
null
null
null
FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome ...
Mus musculus (Mouse)
O55144
TLX3_MOUSE
MEAPASAQTPHPHEPISFGIDQILNSPDQDSAPAPRGPDGASYLGGPPGGRPGAAYPSLPASFAGLGAPFEDAGSYSVNLSLAPAGVIRVPAHRPLPGAVPPPLPSALPAMPSVPTVSSLGGLNFPWMESSRRFVKDRFTAAAALTPFTVTRRIGHPYQNRTPPKRKKPRTSFSRVQICELEKRFHRQKYLASAERAALAKSLKMTDAQVKTWFQNRRTKWRRQTAEEREAERQQASRLMLQLQHDAFQKSLNDSIQPDPLCLHNSSLFALQNLQPWEEDSSKVPAVTSLV
null
null
animal organ development [GO:0048513]; central nervous system development [GO:0007417]; GABAergic neuron differentiation [GO:0097154]; negative regulation of neuron differentiation [GO:0045665]; neuron differentiation [GO:0030182]; neuron fate specification [GO:0048665]; neuron migration [GO:0001764]; regulation of res...
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00046;
1.10.10.60;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
null
Mus musculus (Mouse)
O55145
X3CL1_RAT
MAPSQLAWLLRLAAFFHLCTLLAGQHLGMTKCNITCHKMTSPIPVTLLIHYQLNQESCGKRAIILETRQHRHFCADPKEKWVQDAMKHLDHQTAALTRNGGKFEKRVDNVTPRITSATRGLSPTALAKPESATVEDLTLEPTAISQEARRPMGTSQEPPAAVTGSSPSTSKAQDAGLAAKPQSTGISEVAAVSTTIWPSSAVYQSGSSLWAEEKATESPPTIALSTQASTTSSPKQNVGSEGQPPWVQEQDSTPEKSPGPEETNPVHTDIFQDRGPGSTVHPSVAPTSSEKTPSPELVASGSQAPKVEEPIHATADPQKL...
null
null
angiogenesis involved in wound healing [GO:0060055]; autocrine signaling [GO:0035425]; cell adhesion [GO:0007155]; cell chemotaxis [GO:0060326]; cell-cell adhesion [GO:0098609]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interfe...
cell body [GO:0044297]; cell projection [GO:0042995]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsy...
CCR chemokine receptor binding [GO:0048020]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; CX3C chemokine receptor binding [GO:0031737]; CXCR1 chemokine receptor binding [GO:0045237]; integrin binding [GO:0005178]
PF00048;
2.40.50.40;
Intercrine delta family
PTM: A soluble short form may be released by proteolytic cleavage from the long membrane-anchored form. {ECO:0000250|UniProtKB:P78423}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P78423}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed fractalkine]: Secreted {ECO:0000250|UniProtKB:P78423}.
null
null
null
null
null
FUNCTION: Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1. The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis. Regulates leukocyte adhesion and migration processes at the en...
Rattus norvegicus (Rat)