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
O08675
PAR3_MOUSE
MKILILVAAGLLFLPVTVCQSGINVSDNSAKPTLTIKSFNGGPQNTFEEFPLSDIEGWTGATTTIKAECPEDSISTLHVNNATIGYLRSSLSTQVIPAIYILLFVVGVPANIVTLWKLSLRTKSISLVIFHTNLAIADLLFCVTLPFKIAYHLNGNNWVFGEVTCRITTVVFYGNMYCAILILTCMGINRYLATAHPFTYQKLPKRSFSMLMCGMVWVMVFLYMLPFVILKQEYHLVHSEITTCHDVVDACESPSSFRFYYFVSLAFFGFLIPFVIIIFCYTTLIHKLKSKDRIWLGYIKAVLLILVIFTICFAPTNIIL...
null
null
blood coagulation [GO:0007596]; G protein-coupled receptor signaling pathway [GO:0007186]; ligand-gated ion channel signaling pathway [GO:1990806]; positive regulation of insulin secretion [GO:0032024]; positive regulation of Rho protein signal transduction [GO:0035025]
apical plasma membrane [GO:0016324]; protein-containing complex [GO:0032991]
G protein-coupled receptor activity [GO:0004930]; proteinase-activated receptor activity [GO:0001648]; receptor ligand activity [GO:0048018]; thrombin-activated receptor activity [GO:0015057]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.
Mus musculus (Mouse)
O08677
KNG1_MOUSE
MKLITTLLLCSGLLLTLTQGEEAQEIDCNDEAVFQAVDFSLKQFNPGVKSGNQYMLHRVIEGTKTDGSPTFYSFKYLIKEGNCSAQSGLAWQDCDFKDAEEAATGECTATVGKRENEFFIVTQTCKIAPSKAPILKAYFPCIGCVHAISTDSPDLEPVLKHSIEHFNNNTDHSHLFTLRKVKSAHRQVVAGLNFDITYTIVQTNCSKERFPSLHGDCVALPNGDDGECRGNLFMDINNKIANFSQSCTLYSGDDLVEALPKPCPGCPRDIPVDSPELKEVLGHSIAQLNAENDHPFYYKIDTVKKATSQVVAGTKYVIEF...
null
null
blood coagulation [GO:0007596]; inflammatory response [GO:0006954]; negative regulation of blood coagulation [GO:0030195]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; vasodilation [GO:0042311]
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; perikaryon [GO:0043204]
cysteine-type endopeptidase inhibitor activity [GO:0004869]; protease binding [GO:0002020]
PF00031;
3.10.450.10;
null
PTM: Bradykinin is released from kininogen by plasma kallikrein.; PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P01042}.; PTM: [Bradykinin]: Bradykinin is inactivated by ACE, which removes the dipeptide Arg-Phe from its C-terminus. {ECO:0000250|UniProtKB:P01042}.
SUBCELLULAR LOCATION: Secreted, extracellular space.
null
null
null
null
null
FUNCTION: Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation...
Mus musculus (Mouse)
O08678
MARK1_RAT
MSARTPLPTVNERDTENHTSVDGYTETHIPPTKSSSRQNIPRCRNSITSATDEQPHIGNYRLQKTIGKGNFAKVKLARHVLTGREVAVKIIDKTQLNPTSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKCIVHRDLKAENLLLDADMNIKIADFGFSNEFTVGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRVPFYMSTDCENLLKKLLVLNPIKRGSLEQIMKDRWMNVGHEEEEL...
2.7.11.1; 2.7.11.26
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
cytoskeleton organization [GO:0007010]; establishment of mitochondrion localization [GO:0051654]; intracellular signal transduction [GO:0035556]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of epithelial to mesenchymal transition [GO:0010719]; negative regulation of gene expression [GO:00106...
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phosphatidic acid binding [GO:0070300]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase ac...
PF02149;PF00069;PF00627;
1.10.8.10;3.30.310.80;1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
PTM: Phosphorylation at Thr-613 by PRKCZ/aPKC in polarized epithelial cells inhibits the kinase activity (By similarity). Phosphorylated at Thr-215 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-215 by TAOK1 activates the kinase activity, leading to ph...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9108484}. Cytoplasm {ECO:0000250|UniProtKB:Q9P0L2}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9P0L2}. Note=Appears to localize to an intracellular network.
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:9108484}; CATALYTIC ...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase (By similarity). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates DCX, MAP2 and MAP4. Phosphorylates the microtubule-associated protein MAPT/TAU (By similarity). Involved in cell polarity by phosphorylating the microtubule-associated proteins MAP2, ...
Rattus norvegicus (Rat)
O08679
MARK2_RAT
MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMLRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPL...
2.7.11.1; 2.7.11.26
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q7KZI7};
axon development [GO:0061564]; establishment of cell polarity [GO:0030010]; establishment or maintenance of cell polarity regulating cell shape [GO:0071963]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; intracellular signal transduction [GO:0035556]; microtubule cytoskeleton organ...
actin filament [GO:0005884]; basal cortex [GO:0045180]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; microtubule bundle [GO:0097427]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]
ATP binding [GO:0005524]; lipid binding [GO:0008289]; magnesium ion binding [GO:0000287]; molecular function activator activity [GO:0140677]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau protein binding [GO:0048156]; tau-protein kinase activity [GO:0050321]
PF02149;PF00069;PF00627;
1.10.8.10;3.30.310.80;1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
PTM: Autophosphorylated. Phosphorylated at Thr-208 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Phosphorylation at Thr-208 by TAOK1 activates the kinase activity, leading to phosphorylation and detachment of MAPT/TAU from microtubules. Phosphorylation at Ser-212 by GSK3-be...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14741102}; Peripheral membrane protein {ECO:0000269|PubMed:14741102}. Lateral cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm {ECO:0000250|UniProtKB:Q7KZI7}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q7KZI7}. Note=Phosphorylati...
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:Q7KZI7}; CATALYTI...
null
null
null
null
FUNCTION: Serine/threonine-protein kinase. Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU. Plays a key role in cell polarity by phosphorylating the microtubule-associated ...
Rattus norvegicus (Rat)
O08680
EPHA3_RAT
MDCHLSILILFGCCVLSCSRELSPQPSNEVNLLDSKTIQGELGWISYPSHGWEEISGVDEHYTPIRTYQVCNVMDHSQNNWLRTNWVPRNSAQKIYVELKFTLRDCNSIPLVLGTCKETFNLYYMESDDDHGVKFLEHQFTKIDTIAADESFTQMDLGDRILKLNTEIREVGPVNKKGFYLAFQDVGACVALVSVRVYFKKCPFTVKNLAMFPDTVPMDSQSLVEVRGSCVNNSKEEDPPRMYCSTEGEWLVPIGKCTCNAGYEERGFICQACRPGFYKALDGVAKCTKCPPHSSTQEDGSMNCRCENNYFRAEKDPPSM...
2.7.10.1
null
axon guidance [GO:0007411]; cell migration [GO:0016477]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to retinoic acid [GO:0071300]; endocardial cushion development [GO:0003197]; ephrin receptor signaling pathway [GO:0048013]; fasciculation of motor neuron axon [GO:0097156]...
dendrite [GO:0030425]; early endosome [GO:0005769]; GABA-ergic synapse [GO:0098982]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; GPI-linked ephrin receptor activity [GO:0005004]; growth factor binding [GO:0019838]; transmembrane-ephrin receptor activity [GO:0005005]
PF14575;PF01404;PF07699;PF00041;PF07714;PF07647;
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
PTM: Autophosphorylates upon activation by EFNA5. Phosphorylation on Tyr-603 mediates interaction with NCK1. Dephosphorylated by PTPN1 (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P29320}; Single-pass type I membrane protein {ECO:0000255}.
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=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100...
null
null
null
null
FUNCTION: Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway down...
Rattus norvegicus (Rat)
O08686
BARX2_MOUSE
MHCHAELRLSSPGQLKAARRRYKTFMIDEILSKETCDYFEKLSLYSVCPSLVVRPKPLHSCTGSPSLRAYPLLSVITRQPTVISHLVPTGSGLTPVLTRHPVAAAEAAAAAAETPGGEALASSESETEQPTPRQKKPRRSRTIFTELQLMGLEKKFQKQKYLSTPDRLDLAQSLGLTQLQVKTWYQNRRMKWKKMVLKGGQEAPTKPKGRPKKNSIPTSEEIEAEEKMNSQAQSQELLESSERQEEPCDTQEPKACLVPLEVAEPIHQPQELSEASSEPPPLS
null
null
cartilage condensation [GO:0001502]; myotube differentiation [GO:0014902]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle cell differentiation [...
actin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
chromatin binding [GO:0003682]; 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]; RNA polymerase II transcription reg...
PF00046;
1.10.10.60;
BAR homeobox family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Transcription factor. Binds optimally to the DNA consensus sequence 5'-YYTAATGRTTTTY-3'. May control the expression of neural adhesion molecules such as L1 or Ng-CAM during embryonic development of both the central and peripherical nervous system. May be involved in controlling adhesive processes in keratiniz...
Mus musculus (Mouse)
O08689
GDF8_MOUSE
MMQKLQMYVYIYLFMLIAAGPVDLNEGSEREENVEKEGLCNACAWRQNTRYSRIEAIKIQILSKLRLETAPNISKDAIRQLLPRAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQADGKPKCCFFKFSSKIQYNKVVKAQLWIYLRPVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMSPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQ...
null
null
cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hypoxia [GO:0071456]; muscle cell cellular homeostasis [GO:0046716]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of kin...
extracellular region [GO:0005576]; extracellular space [GO:0005615]
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102]
PF00019;PF00688;
2.60.120.970;2.10.90.10;
TGF-beta family
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide...
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14671324}.
null
null
null
null
null
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000269|PubMed:14671324, ECO:0000269|PubMed:24076600, ECO:0000269|PubMed:9139826}.
Mus musculus (Mouse)
O08691
ARGI2_MOUSE
MFLRSSASRLLHGQIPCVLTRSVHSVAIVGAPFSRGQKKLGVEYGPAAIREAGLLKRLSRLGCHLKDFGDLSFTNVPQDDPYNNLVVYPRSVGLANQELAEVVSRAVSGGYSCVTMGGDHSLAIGTIIGHARHRPDLCVIWVDAHADINTPLTTVSGNIHGQPLSFLIKELQDKVPQLPGFSWIKPCLSPPNIVYIGLRDVEPPEHFILKNYDIQYFSMREIDRLGIQKVMEQTFDRLIGKRQRPIHLSFDIDAFDPKLAPATGTPVVGGLTYREGVYITEEIHNTGLLSALDLVEVNPHLATSEEEAKATARLAVDVIA...
3.5.3.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742};
adaptive immune response [GO:0002250]; arginine catabolic process to ornithine [GO:0019547]; arginine metabolic process [GO:0006525]; innate immune response [GO:0045087]; negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process [GO:1905403]; negative regulation of CD4-positive, alpha-beta T ce...
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]
arginase activity [GO:0004053]; manganese ion binding [GO:0030145]; nitric-oxide synthase binding [GO:0050998]
PF00491;
3.40.800.10;
Arginase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25009204}.
CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000250|UniProtKB:P05089};
null
PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
null
null
FUNCTION: May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to nitric oxid synthase (NOS). Arginine metabolism is a critical regulator of innate and adaptive immune respo...
Mus musculus (Mouse)
O08692
NGP_MOUSE
MAGLWKTFVLVVALAVVSCEALRQLRYEEIVDRAIEAYNQGRQGRPLFRLLSATPPSSQNPATNIPLQFRIKETECTSTQERQPKDCDFLEDGEERNCTGKFFRRRQSTSLTLTCDRDCSREDTQETSFNDKQDVSEKEKFEDVPPHIRNIYEDAKYDIIGNILKNF
null
null
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; negative regulation of angiogenesis [GO:0016525]; negative regulation of lymphang...
cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]
cysteine-type endopeptidase inhibitor activity [GO:0004869]; lipopolysaccharide binding [GO:0001530]
PF00666;
3.10.450.10;
Cathelicidin family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21518852}. Cytoplasmic granule {ECO:0000269|PubMed:8749713}. Note=Localizes in cytoplasmic granules of neutrophilic precursors (PubMed:8749713). {ECO:0000269|PubMed:21518852, ECO:0000269|PubMed:8749713}.
null
null
null
null
null
FUNCTION: Acts as an inhibitor of cathepsin B (CTSB) activity. Plays a role as a negative regulator of tumor vascular development, cell invasion and metastasis. {ECO:0000269|PubMed:21518852}.
Mus musculus (Mouse)
O08696
FOXM1_MOUSE
MRTSPRRPLILKRRRLPLPVQNAPSETSEEEAKRSPAQPEPAPAQASQEVAESSSCKFPAGIKIINHPTTPNTQVVAIPSNADIQSIITALTAKGKESGTSGPNRFILISSGGPSSHPSQPQAHSSRDSKRAEVITETLGPKPAAKGVPVPKPPGAPPRQRQESYAGGEAAGCTLDNSLTNIQWLGKMSSDGLGPCSVKQELEEKENCHLEQNRVKVEEPSGVSTSWQDSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRHLTLDQ...
null
null
cell population proliferation [GO:0008283]; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:0006978]; DNA repair [GO:0006281]; G2/M transition of mitotic cell cycle [GO:0000086]; liver development [GO:0001889]; positive regulation of DNA-templated tran...
nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]
PF00250;
1.10.10.10;
null
PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by the checkpoint kinase CHEK2 in response to DNA damage increases the FOXM1 protein stability probably stimulating the transcription of genes involved in DNA repair. Phosphorylated by CDK1 in late S and G2 phases, creating docking sites for the POLO box domains...
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
null
null
null
null
null
FUNCTION: Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis (By similarity). Plays a role in the control of cell proliferation (By similarity). Also plays a role in DNA break repair, participating in the DNA damage checkpoint response (PubMed:17101782). Promote...
Mus musculus (Mouse)
O08697
ARL2_RAT
MGLLTILKKMKQKERDVRLLMLGLDNAGKTTILKKFNGEDVDTISPTLGFNIKTLEHRGFKLNIWDVGGQKSLRSYWRNYFESTDGLIWVVDSADRQRMQDCQRELQSLLVEERLAGATLLIFANKQDLPGALSCNAIQEALELDSIRSHHWRIQGCSAVTGEDLLPGIDWLLDDISSRVFTAD
null
null
acetylcholine transport [GO:0015870]; bicellular tight junction assembly [GO:0070830]; centrosome cycle [GO:0007098]; maintenance of protein location in nucleus [GO:0051457]; negative regulation of GTPase activity [GO:0034260]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of microtub...
centrosome [GO:0005813]; cytoplasm [GO:0005737]; lateral plasma membrane [GO:0016328]; microtubule cytoskeleton [GO:0015630]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
PF00025;
3.40.50.300;
Small GTPase superfamily, Arf family
PTM: Not N-myristoylated.
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:11809823}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11809823}. Nucleus {ECO:0000269|PubMed:11809823}. Cytoplasm {ECO:0000269|PubMed:11809823}. Note=The complex formed with ARL2BP, ARL2 and SLC25A6 i...
null
null
null
null
null
FUNCTION: Small GTP-binding protein which cycles between an inactive GDP-bound and an active GTP-bound form, and the rate of cycling is regulated by guanine nucleotide exchange factors (GEF) and GTPase-activating proteins (GAP). GTP-binding protein that does not act as an allosteric activator of the cholera toxin catal...
Rattus norvegicus (Rat)
O08699
PGDH_RAT
MHVNGKVALVTGAAQGIGKAFTEALLLHGAKVALVDWNLETGVKCKAALDEQFEPQKTLFIQCDVADQKQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEQTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINISSIAGLMPVAQQPVYCASKHGIIGFTRSAAMAANLMKSGVRLNVICPGFVKTPILESIEKEENMGQYIEYTDQIKAMMKFYGILDPSAIANGLINLIEDDALNGAIMKITASKGIHFQDYDLFPSFSKAP
1.1.1.-; 1.1.1.141; 1.1.1.232
null
ductus arteriosus closure [GO:0097070]; female pregnancy [GO:0007565]; kidney development [GO:0001822]; negative regulation of cell cycle [GO:0045786]; ovulation [GO:0030728]; parturition [GO:0007567]; positive regulation of apoptotic process [GO:0043065]; positive regulation of vascular associated smooth muscle cell p...
basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]
15-hydroxyprostaglandin dehydrogenase (NAD+) activity [GO:0016404]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NAD+ binding [GO:0070403]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; prostaglandin E receptor activity [GO:0004957]
PF00106;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=NAD(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) + NADH; Xref=Rhea:RHEA:11876, ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:606564; EC=1.1.1.141; Evidence={ECO:0000305|PubMed:9099857}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:1...
null
null
null
null
FUNCTION: Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites (By similarity) (PubMed:9099857). Decreases the level...
Rattus norvegicus (Rat)
O08701
ARGI2_RAT
MFLRSSVSRLLHGQIPCALTRSVHSVAVVGAPFSRGQKKKGVEYGPAAIREAGLLKRLSMLGCHIKDFGDLSFTNVPKDDPYNNLVVYPRSVGIANQELAEVVSRAVSGGYSCVTLGGDHSLAIGTISGHARHHPDLCVIWVDAHADINTPLTTVSGNIHGQPLSFLIRELQDKVPQLPGFSWIKPCLSPPNLVYIGLRDVEPAEHFILKSFDIQYFSMRDIDRLGIQKVMEQTFDRLIGKRKRPIHLSFDIDAFDPKLAPATGTPVVGGLTYREGLYITEEIHSTGLLSALDLVEVNPHLATSEEEAKATASLAVDVIA...
3.5.3.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742};
adaptive immune response [GO:0002250]; arginine catabolic process to ornithine [GO:0019547]; arginine metabolic process [GO:0006525]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to interleukin-4 [GO:0071353]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to type...
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]
arginase activity [GO:0004053]; manganese ion binding [GO:0030145]; nitric-oxide synthase binding [GO:0050998]
PF00491;
3.40.800.10;
Arginase family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O08691, ECO:0000250|UniProtKB:P78540}.
CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000250|UniProtKB:P05089};
null
PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
null
null
FUNCTION: May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to nitric oxid synthase (NOS). Arginine metabolism is a critical regulator of innate and adaptive immune respo...
Rattus norvegicus (Rat)
O08705
NTCP_MOUSE
MEAHNVSAPFNFSLPPGFGHRATDTALSVILVVMLLLIMLSLGCTMEFSKIKAHFWKPKGVIIAIVAQYGIMPLSAFLLGKVFHLTSIEALAILICGCSPGGNLSNLFTLAMKGDMNLSIVMTTCSSFTALGMMPLLLYIYSKGIYDGDLKDKVPYKGIMLSLVMVLIPCAIGIFLKSKRPHYVPYVLKAGMIITFSLSVAVTVLSVINVGNSIMFVMTPHLLATSSLMPFTGFLMGYILSALFRLNPSCRRTISMETGFQNVQLCSTILNVTFPPEVIGPLFFFPLLYMIFQLAEGLLFIIIFRCYLKIKPQKDQTKIT...
null
null
bile acid and bile salt transport [GO:0015721]; bile acid signaling pathway [GO:0038183]; cellular response to xenobiotic stimulus [GO:0071466]; regulation of bile acid secretion [GO:0120188]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to nutrient levels [GO:0031667]; response to orga...
basolateral plasma membrane [GO:0016323]; membrane [GO:0016020]
bile acid transmembrane transporter activity [GO:0015125]; bile acid:sodium symporter activity [GO:0008508]
PF01758;
1.20.1530.20;
Bile acid:sodium symporter (BASS) (TC 2.A.28) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q14973}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q14973}.
CATALYTIC ACTIVITY: [Isoform 1]: Reaction=2 Na(+)(out) + taurocholate(out) = 2 Na(+)(in) + taurocholate(in); Xref=Rhea:RHEA:71875, ChEBI:CHEBI:29101, ChEBI:CHEBI:36257; Evidence={ECO:0000269|PubMed:10209268}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=2 Na(+)(out) + taurocholate(out) = 2 Na(+)(in) + taurocholate(in); Xr...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=86 uM for taurocholate {ECO:0000269|PubMed:10209268}; KM=104 uM for estrone 3-sulfate {ECO:0000269|PubMed:34060352}; Vmax=3004 pmol/min/mg enzyme with estrone 3-sulfate as substrate {ECO:0000269|PubMed:34060352}; Kinetic parameters: KM=14 uM for taurocholate {ECO:0...
null
null
null
FUNCTION: As a major transporter of conjugated bile salts from plasma into the hepatocyte, it plays a key role in the enterohepatic circulation of bile salts necessary for the solubilization and absorption of dietary fat and fat-soluble vitamins (PubMed:10209268). It is strictly dependent on the extracellular presence ...
Mus musculus (Mouse)
O08707
ACKR2_MOUSE
MPTVASPLPLTTVGSENSSSIYDYDYLDDMTILVCRKDEVLSFGRVFLPVVYSLIFVLGLAGNLLLLVVLLHSAPRRRTMELYLLNLAVSNLLFVVTMPFWAISVAWHWVFGSFLCKVISTLYSINFYCGIFFITCMSLDKYLEIVHAQPLHRPKAQFRNLLLIVMVWITSLAISVPEMVFVQIHQTLDGVWHCYADFGGHATIWKLYLRFQLNLLGFLLPLLAMIFFYSRIGCVLVRLRPPGQGRALRMAAALVIVFFMLWFPYNLTLFLHSLLDLHVFGNCEISHRLDYTLQVTESLAFSHCCFTPVLYAFCSHRFRR...
null
null
calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; signal transduction [GO:0007165]
actin filament [GO:0005884]; cytosol [GO:0005829]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; scavenger receptor activity [GO:0005044]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily
PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail. {ECO:0000250}.
SUBCELLULAR LOCATION: Early endosome {ECO:0000250}. Recycling endosome {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits. Once internalized, the ligand dissociates from the receptor, ...
null
null
null
null
null
FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept...
Mus musculus (Mouse)
O08709
PRDX6_MOUSE
MPGGLLLGDEAPNFEANTTIGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNGETPTEKLPFPIIDDKGRDLAILLGMLDPVEKDDNNMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTGTKPVATPVDWKKGESVMVVPTLSEEEAKQCFPKGVFTKELPSGKKYLRYTPQP
1.11.1.27; 2.3.1.23; 3.1.1.4
null
bleb assembly [GO:0032060]; cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; lipid catabolic process [GO:0016042]; response to reactive oxygen species [GO:0000302]
cytosol [GO:0005829]; lysosome [GO:0005764]; mitochondrion [GO:0005739]
1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; glutathione peroxidase activity [GO:0004602]; peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; phospholipase A2 activity [GO:0004623]
PF10417;PF00578;
3.40.30.10;
Peroxiredoxin family, Prx6 subfamily
PTM: Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress. {ECO:0000250|UniProtKB:P30041}.; PTM: Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (By similarity). The phosphorylated form e...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35244}. Lysosome {ECO:0000250|UniProtKB:O35244}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000250|UniProtKB:O35244}.
CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.27; Evidence={ECO:0000250|UniProtKB:P30041}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-s...
null
null
null
null
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (By similarity). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Has phospholipase activity (PubMed:26830860). Ca...
Mus musculus (Mouse)
O08710
THYG_MOUSE
MTALVLWVSTLLSSVCLVAANIFEYQVDAQPLRPCELQREKAFLKQAEYVPQCSEDGSFQTVQCQNDGQSCWCVDSDGREVPGSRQLGRPTVCLSFCQLHKQRILLGSYINSTDALYLPQCQDSGNYAPVQCDLQRVQCWCVDTEGMEVYGTRQQGRPTRCPRSCEIRNRRLLHGVGDRSPPQCTADGEFMPVQCKFVNTTDMMIFDLIHNYNRFPDAFVTFSSFRGRFPEVSGYCYCADSQGRELAETGLELLLDEIYDTIFAGLDQASTFTQSTMYRILQRRFLAIQLVISGRFRCPTKCEVEQFAATRFGHSYIPRC...
null
null
hormone biosynthetic process [GO:0042446]; iodide transport [GO:0015705]; regulation of myelination [GO:0031641]; response to pH [GO:0009268]; thyroid gland development [GO:0030878]; thyroid hormone generation [GO:0006590]; thyroid hormone metabolic process [GO:0042403]; transcytosis [GO:0045056]
extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]
anion binding [GO:0043168]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; signaling receptor binding [GO:0005102]
PF00135;PF07699;PF00086;
3.40.50.1820;4.10.800.10;2.10.50.10;
Type-B carboxylesterase/lipase family
PTM: Iodinated on tyrosine residues by TPO (By similarity). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-25 is coupled to donor Tyr-150 or Tyr-235, acceptor Tyr-2572 is coupled to donor Tyr-2539, acceptor Tyr-2764 in monomer 1 is coupled to donor Tyr-2764 in monomer 2 and acceptor Tyr-1310 i...
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12782676, ECO:0000269|PubMed:19276074}. Note=Secreted into the thyroid follicle lumen (PubMed:12782676). Localizes to colloid globules, a structure formed in the thyroid follicle lumen consisting of cross-linked TG arranged in concentric layers (PubMed:12782676). {ECO:...
null
null
null
null
null
FUNCTION: Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (By similarity). Following TG re-internalization ...
Mus musculus (Mouse)
O08712
TR11B_MOUSE
MNKWLCCALLVLLDIIEWTTQETLPPKYLHYDPETGHQLLCDKCAPGTYLKQHCTVRRKTLCVPCPDHSYTDSWHTSDECVYCSPVCKELQSVKQECNRTHNRVCECEEGRYLEIEFCLKHRSCPPGSGVVQAGTPERNTVCKKCPDGFFSGETSSKAPCIKHTNCSTFGLLLIQKGNATHDNVCSGNREATQKCGIDVTLCEEAFFRFAVPTKIIPNWLSVLVDSLPGTKVNAESVERIKRRHSSQEQTFQLLKLWKHQNRDQEMVKKIIQDIDLCESSVQRHLGHSNLTTEQLLALMESLPGKKISPEEIERTRKTCK...
null
null
apoptotic process [GO:0006915]; extracellular matrix organization [GO:0030198]; negative regulation of bone resorption [GO:0045779]; negative regulation of odontogenesis of dentin-containing tooth [GO:0042489]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of tumor necrosis factor-...
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; receptor complex [GO:0043235]
heparan sulfate binding [GO:1904399]
PF00531;PF00020;
1.10.533.10;2.10.50.10;
null
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Acts as a decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arteri...
Mus musculus (Mouse)
O08715
AKAP1_MOUSE
MAIQLRSLFPLALPGMLALLGWWWFFSRKKDRLSSSDKQVETLKVGPAIKDRRLSEEACPGVLSVAPTVTQPPGREEQRCVDKPSTEPLALPRTRQVRRRSESSGNLPSVADTRSQPGPCRDEIAKVELSLMGDKAKSIPLGCPLLPKDASFPYEAVERCKQESALGKTPGRGWPSPYAASGEKARETGGTEGTGDAVLGENVSEEGLLSQECVSEVEKSEFPILAPGGGEGEEVSHGPPQVAELLKKEEYIVGKLPSSFVEPVHSEPVKDEDALEPQVKGSSNTSDRDLAGELDKDETVPENDQIKQAAFQLISQVILE...
null
null
antiviral innate immune response [GO:0140374]; apoptotic process [GO:0006915]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of protein dephosphorylation [GO:0035308]; negative regulation of protein import into nucleus [GO:0042308]
endoplasmic reticulum [GO:0005783]; lipid droplet [GO:0005811]; membrane [GO:0016020]; mitochondrial crista [GO:0030061]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; postsynaptic membrane [GO:0045211]; postsynaptic specialization, intracellular component [...
beta-tubulin binding [GO:0048487]; microtubule binding [GO:0008017]; molecular adaptor activity [GO:0060090]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinase binding [GO:0019901]; protein phosphatase 2B binding [GO:0030346]; protein phosphatase binding [GO:0019903]; RNA binding [GO:0003723]
PF00013;PF00567;
2.30.30.140;2.40.50.90;3.30.1370.10;
null
null
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:24101730, ECO:0000269|PubMed:9182549}. Mitochondrion {ECO:0000269|PubMed:32072193}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:10352013}. Note=Does not contain the classic KDEL endoplasmic reticulum-targeting seque...
null
null
null
null
null
FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A (PubMed:9065479, PubMed:9182549). Anchors them to the cytoplasmic face of the mitochondrial outer membrane or allows them to reside in the endoplasmic reticulum (PubMed:9065479, PubMed:9182549). Involved in mit...
Mus musculus (Mouse)
O08719
EVL_RAT
MFAFEEFSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASNTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSTQRQVQNGPSPEEMDIQRRQVMEQQHRQESLERRISATGPILPPGHPSSAASATFSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDENQTEDPSTSPSPGSRATSQPP...
null
null
actin polymerization or depolymerization [GO:0008154]; axon guidance [GO:0007411]; cellular response to type II interferon [GO:0071346]; central nervous system development [GO:0007417]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of ruffle assembly [GO:1900028]; positive regulatio...
cytoplasm [GO:0005737]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; phagocytic vesicle [GO:0045335]; stress fiber [GO:0001725]
actin binding [GO:0003779]; profilin binding [GO:0005522]; SH3 domain binding [GO:0017124]
PF08776;PF00568;
2.30.29.30;1.20.5.1160;
Ena/VASP family
PTM: Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P70429}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:P70429}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P70429}. Note=Targeted to the leading edge of lamellipodia and the distal tip of stress fibers through interaction wit...
null
null
null
null
null
FUNCTION: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
O08721
UNC5A_RAT
MAVRPGLWPVLLGIVLAAWLRGSGAQQSATVANPVPGANPDLLPHFLVEPEDVYIVKNKPVLLVCKAVPATQIFFKCNGEWVRQVDHVIERSTDSSSGLPTMEVRINVSRQQVEKVFGLEEYWCQCVAWSSSGTTKSQKAYIRIAYLRKNFEQEPLAKEVSLEQGIVLPCRPPEGIPPAEVEWLRNEDLVDPSLDPNVYITREHSLVVRQARLADTANYTCVAKNIVARRRSTSAAVIVYVNGGWSTWTEWSVCSASCGRGWQKRSRSCTNPAPLNGGAFCEGQNVQKTACATLCPVDGSWSSWSKWSACGLDCTHWRSR...
null
null
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; netrin-activated signaling pathway [GO:0038007]; neuron projection development [GO:0031175]
membrane raft [GO:0045121]; neuron projection membrane [GO:0032589]; neuronal cell body membrane [GO:0032809]; plasma membrane [GO:0005886]
netrin receptor activity [GO:0005042]
PF00531;PF07679;PF00090;PF17217;PF00791;
2.60.220.30;1.10.533.10;2.60.40.10;2.20.100.10;
Unc-5 family
PTM: Phosphorylated on cytoplasmic tyrosine residues (By similarity). Phosphorylated by PKC in vitro. {ECO:0000250, ECO:0000269|PubMed:14672991}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is r...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12598531, ECO:0000269|PubMed:19755150, ECO:0000269|PubMed:9126742}; Single-pass type I membrane protein {ECO:0000269|PubMed:12598531, ECO:0000269|PubMed:9126742, ECO:0000305}. Membrane raft {ECO:0000269|PubMed:18582460}. Cell projection, neuron projection {ECO:000...
null
null
null
null
null
FUNCTION: Receptor for netrin required for axon guidance (PubMed:10399920, PubMed:9126742). Functions in the netrin signaling pathway and promotes neurite outgrowth in response to NTN1 (PubMed:19755150). Mediates axon repulsion of neuronal growth cones in the developing nervous system in response to netrin (PubMed:1039...
Rattus norvegicus (Rat)
O08722
UNC5B_RAT
MRARSGARGALLLALLLCWDPTPSLAGIDSGGQALPDSFPSAPAEQLPHFLLEPEDAYIVKNKPVELHCRAFPATQIYFKCNGEWVSQKGHVTQESLDEATGLRIREVQIEVSRQQVEELFGLEDYWCQCVAWSSSGTTKSRRAYIRIAYLRKNFDQEPLAKEVPLDHEVLLQCRPPEGVPVAEVEWLKNEDVIDPAQDTNFLLTIDHNLIIRQARLSDTANYTCVAKNIVAKRRSTTATVIVYVNGGWSSWAEWSPCSNRCGRGWQKRTRTCTNPAPLNGGAFCEGQACQKTACTTVCPVDGAWTEWSKWSACSTECAH...
null
null
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; negative regulation of neuron apoptotic process [GO:0043524]; positive regulation of extrinsic apoptotic signaling pa...
membrane raft [GO:0045121]; plasma membrane [GO:0005886]
netrin receptor activity [GO:0005042]
PF00531;PF07679;PF00090;PF17217;PF00791;
2.60.220.30;1.10.533.10;2.60.40.10;2.20.100.10;
Unc-5 family
PTM: Phosphorylated on cytoplasmic tyrosine residues. {ECO:0000250}.; PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage does not take place when the receptor is associated with netrin ligand. Its cleavage by caspases is required to induce apoptosis. {ECO:0000269|PubMed:11387206}.; PTM: Palmitoylat...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9126742}; Single-pass type I membrane protein {ECO:0000269|PubMed:9126742}. Membrane raft {ECO:0000269|PubMed:18582460}. Note=Associated with lipid rafts (PubMed:18582460). {ECO:0000269|PubMed:18582460}.
null
null
null
null
null
FUNCTION: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion (PubMed:10399920, PubMed:9126742). Functions ...
Rattus norvegicus (Rat)
O08725
GHSR_RAT
MWNATPSEEPEPNVTLDLDWDASPGNDSLPDELLPLFPAPLLAGVTATCVALFVVGISGNLLTMLVVSRFRELRTTTNLYLSSMAFSDLLIFLCMPLDLVRLWQYRPWNFGDLLCKLFQFVSESCTYATVLTITALSVERYFAICFPLRAKVVVTKGRVKLVILVIWAVAFCSAGPIFVLVGVEHENGTDPRDTNECRATEFAVRSGLLTVMVWVSSVFFFLPVFCLTVLYSLIGRKLWRRRGDAAVGASLRDQNHKQTVKMLAVVVFAFILCWLPFHVGRYLFSKSFEPGSLEIAQISQYCNLVSFVLFYLSAAINPIL...
null
null
actin polymerization or depolymerization [GO:0008154]; adult feeding behavior [GO:0008343]; cellular response to insulin stimulus [GO:0032869]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to thyroid hormone stimulus [GO:0...
cell surface [GO:0009986]; glutamatergic synapse [GO:0098978]; membrane raft [GO:0045121]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic membrane [GO:0097060]
G protein-coupled receptor activity [GO:0004930]; growth hormone receptor binding [GO:0005131]; growth hormone secretagogue receptor activity [GO:0001616]; growth hormone-releasing hormone receptor activity [GO:0016520]; hormone binding [GO:0042562]; peptide hormone binding [GO:0017046]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Receptor for ghrelin, coupled to G-alpha-11 proteins. Stimulates growth hormone secretion. Binds also other growth hormone releasing peptides (GHRP) (e.g. Met-enkephalin and GHRP-6) as well as non-peptide, low molecular weight secretagogues (e.g. L-692,429, MK-0677, adenosine) (By similarity). {ECO:0000250, E...
Rattus norvegicus (Rat)
O08726
GALR2_RAT
MNGSGSQGAENTSQEGGSGGWQPEAVLVPLFFALIFLVGTVGNALVLAVLLRGGQAVSTTNLFILNLGVADLCFILCCVPFQATIYTLDDWVFGSLLCKAVHFLIFLTMHASSFTLAAVSLDRYLAIRYPLHSRELRTPRNALAAIGLIWGLALLFSGPYLSYYRQSQLANLTVCHPAWSAPRRRAMDLCTFVFSYLLPVLVLSLTYARTLRYLWRTVDPVTAGSGSQRAKRKVTRMIIIVAVLFCLCWMPHHALILCVWFGRFPLTRATYALRILSHLVSYANSCVNPIVYALVSKHFRKGFRKICAGLLRPAPRRASG...
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; G protein-coupled receptor signaling pathway [GO:0007186]; galanin-activated signaling pathway [GO:0090663]; inositol phosphate metabolic proces...
cilium [GO:0005929]; plasma membrane [GO:0005886]
galanin receptor activity [GO:0004966]; neuropeptide binding [GO:0042923]; peptide hormone binding [GO:0017046]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Receptor for the hormone galanin, GALP and spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).
Rattus norvegicus (Rat)
O08727
TR11B_RAT
MNKWLCCALLVFLDIIEWTTQETFPPKYLHYDPETGRQLLCDKCAPGTYLKQHCTVRRKTLCVPCPDYSYTDSWHTSDECVYCSPVCKELQTVKQECNRTHNRVCECEEGRYLELEFCLKHRSCPPGLGVLQAGTPERNTVCKRCPDGFFSGETSSKAPCRKHTNCSSLGLLLIQKGNATHDNVCSGNREATQNCGIDVTLCEEAFFRFAVPTKIIPNWLSVLVDSLPGTKVNAESVERIKRRHSSQEQTFQLLKLWKHQNRDQEMVKKIIQDIDLCESSVQRHIGHANLTTEQLRILMESLPGKKISPDEIERTRKTCK...
null
null
apoptotic process [GO:0006915]; extracellular matrix organization [GO:0030198]; negative regulation of bone resorption [GO:0045779]; negative regulation of odontogenesis of dentin-containing tooth [GO:0042489]; negative regulation of osteoclast differentiation [GO:0045671]; negative regulation of tumor necrosis factor-...
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; receptor complex [GO:0043235]
cytokine activity [GO:0005125]; heparan sulfate binding [GO:1904399]
PF00531;PF00020;
1.10.533.10;2.10.50.10;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
null
null
null
null
null
FUNCTION: Acts as a decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arteri...
Rattus norvegicus (Rat)
O08730
GLYG_RAT
MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRTVVLASPQVSDSMRKVLETVFDEVIMVDVLDSGDSAHLTLMKRPELGITLTKLHCWSLTQYSKCVFMDADTLVLSNIDDLFEREELSAAPDPGWPDCFNSGVFVYQPSIETYNQLLHLASEQGSFDGGDQGLLNTYFSGWATTDITKHLPFVYNLSSLSIYSYLPAFKAFGKNAKVVHFLGRTKPWNYTYNPQTKSVKCESQDPIVSHPEFLNLWWDTFTTNVLPLLQHHGLVKDAGSYLMMEHVTGALSDLSFGEAPPASQPSLSSEERKERWEQGQADYMGADS...
2.4.1.186
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P13280}; Note=Divalent metal ions. Required for self-glucosylation. Manganese is the most effective. {ECO:0000250|UniProtKB:P13280};
glycogen biosynthetic process [GO:0005978]
cytoplasm [GO:0005737]
glucose binding [GO:0005536]; glycogenin glucosyltransferase activity [GO:0008466]; glycosyltransferase activity [GO:0016757]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803]; UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity [GO:0102751]
PF01501;
null
Glycosyltransferase 8 family, Glycogenin subfamily
PTM: Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195. {ECO:0000250|UniProtKB:P13280}.; PTM: Phosphorylated. {ECO:0000250|UniProtKB:P13280}.
null
CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360, Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140573; EC=2.4.1.186; Evidence={ECO:...
null
PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000250|UniProtKB:P46976}.
null
null
FUNCTION: Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. {ECO:0000250|UniProtKB:P13280, ECO:0000250|UniProtKB:...
Rattus norvegicus (Rat)
O08734
BAK_MOUSE
MASGQGPGPPKVGCDESPSPSEQQVAQDTEEVFRSYVFYLHQQEQETQGAAAPANPEMDNLPLEPNSILGQVGRQLALIGDDINRRYDTEFQNLLEQLQPTAGNAYELFTKIASSLFKSGISWGRVVALLGFGYRLALYVYQRGLTGFLGQVTCFLADIILHHYIARWIAQRGGWVAALNFRRDPILTVMVIFGVVLLGQFVVHRFFRS
null
null
animal organ regeneration [GO:0031100]; apoptotic process involved in blood vessel morphogenesis [GO:1902262]; B cell apoptotic process [GO:0001783]; B cell homeostasis [GO:0001782]; B cell negative selection [GO:0002352]; blood vessel remodeling [GO:0001974]; calcium ion transport into cytosol [GO:0060402]; cellular r...
BAK complex [GO:0097145]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; pore complex [GO:0046930]
BH domain binding [GO:0051400]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; porin activity [GO:0015288]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877];...
PF00452;
1.10.437.10;
Bcl-2 family
null
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q16611}; Single-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: In the presence of an appropriate stimulus, accelerates programmed cell death by binding to, and antagonizing the anti-apoptotic action of BCL2. {ECO:0000250}.
Mus musculus (Mouse)
O08736
CASPC_MOUSE
MAARRTHERDPIYKIKGLAKDMLDGVFDDLVEKNVLNGDELLKIGESASFILNKAENLVENFLEKTDMAGKIFAGHIANSQEQLSLQFSNDEDDGPQKICTPSSPSESKRKVEDDEMEVNAGLAHESHLMLTAPHGLQSSEVQDTLKLCPRDQFCKIKTERAKEIYPVMEKEGRTRLALIICNKKFDYLFDRDNADTDILNMQELLENLGYSVVLKENLTAQEMETELMQFAGRPEHQSSDSTFLVFMSHGILEGICGVKHRNKKPDVLHDDTIFKIFNNSNCRSLRNKPKILIMQACRGRYNGTIWVSTNKGIATADTD...
3.4.22.-
null
endoplasmic reticulum unfolded protein response [GO:0030968]; fibroblast apoptotic process [GO:0044346]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; positive regulation of apoptotic process [GO:0043065]; positive reg...
AIM2 inflammasome complex [GO:0097169]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; IPAF inflammasome complex [GO:0072557]; NLRP1 inflammasome complex [GO:0072558]; NLRP3 inflammasome complex [GO:0072559]
cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; protease binding [GO:0002020]
PF00619;PF00656;
3.40.50.1460;3.30.70.1470;1.10.533.10;
Peptidase C14A family
null
null
null
null
null
null
null
FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. {ECO:0000250}.
Mus musculus (Mouse)
O08738
CASP6_MOUSE
MTETDGFYKSREVFDPAEQYKMDHKRRGVALIFNHERFFWHLTLPERRGTNADRDNLTRRFSDLGFEVKCFNDLRAEELLLKIHEVSTSSHIDADCFICVFLSHGEGNHVYAYDAKIEIQTLTGLFKGDKCQSLVGKPKIFIIQACRGSQHDVPVVPLDMVDHQTDKLDNVTQVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLCEMLARYGSSLEFTELLTLVNRKVSQRRVDFCKDPDAIGKKQVPCFASMLTKKLHFCPKPSK
3.4.22.59
null
activation of innate immune response [GO:0002218]; acute inflammatory response to non-antigenic stimulus [GO:0002525]; axonal fasciculation [GO:0007413]; cellular response to staurosporine [GO:0072734]; epithelial cell differentiation [GO:0030855]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signalin...
axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]
PF00656;
3.40.50.1460;
Peptidase C14A family
PTM: Phosphorylated by NUAK1; phosphorylation inhibits self-activation. Phosphorylation at Ser-239 by AMP-activated protein kinase (PRKAA1 or PRKAA2) inhibits autocleavage, preventing caspase activation, thereby preventing hepatocyte apoptosis. {ECO:0000250|UniProtKB:P55212}.; PTM: Palmitoylation by ZDHHC17 blocks dime...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}.
CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000269|PubMed:22555455, ECO:0000269|PubMed:25231987};
null
null
null
null
FUNCTION: Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity (PubMed:18981099, PubMed:22555455, PubMed:23695670, PubMed:32298652). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear struc...
Mus musculus (Mouse)
O08739
AMPD3_MOUSE
MPRQFPKLNMSDLDEHVRLLAEKVFAKVLREEDSKDVMSLFTVPEDCPIGQKEAKERELQKELAEQKSVETAKRKKSFKMIRSQSLSLQMPTQQDWKGPPTASPAMSPATPLVPGATSKPGPAPYAMPEYQRVTISGDYCAGITVEDYEQAAKSLAKALMIREKYARLAYHRFPRTTAQYLAHQGESVPLEEGLPDFHPPPLPQEDPYCLDDAPPNLGYLVRMHGGVLFVYDNQTMLERQEPHSLPYPDLETYIVDMSHILALITDGPTKTYCHRRLNFLESKFSLHEMLNEMSEFKELKSNPHRDFYNVRKVDTHIHAA...
3.5.4.6
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
ADP catabolic process [GO:0046032]; ADP metabolic process [GO:0046031]; AMP catabolic process [GO:0006196]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; energy homeostasis [GO:0097009]; erythrocyte homeostasis [GO:0034101]; GTP metabolic process [GO:0046039]; IMP biosynthetic process [GO:0006...
cytosol [GO:0005829]
AMP deaminase activity [GO:0003876]; metal ion binding [GO:0046872]
PF19326;
4.10.800.20;3.20.20.140;
Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family
null
null
CATALYTIC ACTIVITY: Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; Evidence={ECO:0000269|PubMed:9133604}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778; Evidence={ECO:0000305|PubMed:...
null
PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. {ECO:0000305|PubMed:9133604}.
null
null
FUNCTION: AMP deaminase plays a critical role in energy metabolism. {ECO:0000305|PubMed:9133604}.
Mus musculus (Mouse)
O08746
MATN2_MOUSE
MEKMLVGCLLMLGQLFLVLPVDGRERPQARFPSRGRHVRMYPQTALLESSCENKRADLVFIIDSSRSVNTYDYAKVKEFILDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMTGLAIQYALNIAFSEAEGARPLRENVPRIIMIVTDGRPQDSVAEVAAKARNTGILIFAIGVGQVDLNTLKAIGSEPHKDHVFLVANFSQIESLTSVFQNKLCTVHMCSVLEHNCAHFCLNTPGSYICKCKQGYILSTDQKTCRIQDLCATEDHGCEQLCVNMLGSFVCQCYSGYTLAEDGKRCTA...
null
null
axon guidance [GO:0007411]; dendrite regeneration [GO:0031104]; extracellular matrix organization [GO:0030198]; glial cell migration [GO:0008347]; neuron migration [GO:0001764]; neuron projection development [GO:0031175]; response to axon injury [GO:0048678]
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; matrilin complex [GO:0120216]
calcium ion binding [GO:0005509]
PF07645;PF14670;PF10393;PF00092;
1.20.5.30;2.10.25.10;3.40.50.410;
null
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Involved in matrix assembly. {ECO:0000250}.
Mus musculus (Mouse)
O08747
UNC5C_MOUSE
MRKGLRATAARCGLGLGYLLQMLVLPALALLSASGTGSAAQDDEFFHELPETFPSDPPEPLPHFLIEPEEAYIVKNKPVNLYCKASPATQIYFKCNSEWVHQKDHVVDERVDETSGLIVREVSIEISRQQVEELFGPEDYWCQCVAWSSAGTTKSRKAYVRIAYLRKTFEQEPLGKEVSLEQEVLLQCRPPEGIPVAEVEWLKNEDIIDPAEDRNFYITIDHNLIIKQARLSDTANYTCVAKNIVAKRKSTTATVIVYVNGGWSTWTEWSVCNSRCGRGYQKRTRTCTNPAPLNGGAFCEGQSVQKIACTTLCPVDGRWT...
null
null
anterior/posterior axon guidance [GO:0033564]; apoptotic process [GO:0006915]; axon guidance [GO:0007411]; brain development [GO:0007420]; chemorepulsion of axon [GO:0061643]; dorsal root ganglion development [GO:1990791]; ectopic germ cell programmed cell death [GO:0035234]; netrin-activated signaling pathway [GO:0038...
axon [GO:0030424]; cell surface [GO:0009986]; dendrite [GO:0030425]; filopodium [GO:0030175]; growth cone [GO:0030426]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; synapse [GO:0045202]
netrin receptor activity [GO:0005042]; netrin receptor activity involved in chemorepulsion [GO:0005043]; protein kinase binding [GO:0019901]; tubulin binding [GO:0015631]
PF00531;PF07679;PF00090;PF17217;PF00791;
2.60.220.30;1.10.533.10;2.60.40.10;2.20.100.10;
Unc-5 family
PTM: Phosphorylated on different cytoplasmic tyrosine residues (PubMed:11533026). Phosphorylation of Tyr-568 leads to an interaction with PTPN11 phosphatase, suggesting that its activity is regulated by phosphorylation/dephosphorylation (PubMed:11533026). Tyrosine phosphorylation is netrin-dependent (PubMed:11533026, P...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22405201}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:O95185}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q761X5}. Cell projection, dendrite {ECO:0000269|PubMed:22685302}. Cell projection, axon {ECO:0000269|PubMed:22685...
null
null
null
null
null
FUNCTION: Receptor for netrin required for axon guidance (PubMed:10399920, PubMed:22685302). Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (PubMed:10399920, PubMed:22685302). NTN1/Netrin-1 binding might cause dissociation of UNC5C from polymerized TUBB3 in microtu...
Mus musculus (Mouse)
O08749
DLDH_MOUSE
MQSWSRVYRSLAKKGHFNRISHGLQGVSSVPLRTYADQPIEADVTVIGSGPGGYVAAIKSAQLGFKTVCIEKNETLGGTCLNVGCIPSKALLNNSHYYHMAHGKDFASRGIEIPEVRLNLEKMMEQKHSAVKALTGGIAHLFKQNKVVHVNGFGKITGKNQVTATKADGSTQVIDTKNILVATGSEVTPFPGITIDEDTIVSSTGALSLKKVPEKLVVIGAGVIGVELGSVWQRLGADVTAVEFLGHVGGIGIDMEISKNFQRILQRQGFKFKLNTKVTGATKKSDGKIDVSVEAASGGKAEVITCDVLLVCIGRRPFTQ...
1.8.1.4
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P09622}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P09622};
2-oxoglutarate metabolic process [GO:0006103]; acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; branched-chain amino acid catabolic process [GO:0009083]; dihydrolipoamide metabolic process [GO:0051068]; gastrulation [GO:0007369]; histone succinylation [GO:0106077]; lipoate metabolic process [GO:0009106]; mit...
acetyltransferase complex [GO:1902493]; acrosomal matrix [GO:0043159]; cilium [GO:0005929]; mitochondrial matrix [GO:0005759]; mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739]; motile cilium [GO:0031514]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; oxoglutarate dehydrogenase c...
branched-chain alpha-keto acid dehydrogenase activity [GO:0047101]; dihydrolipoyl dehydrogenase activity [GO:0004148]; flavin adenine dinucleotide binding [GO:0050660]; lipoamide binding [GO:0043544]; NAD binding [GO:0051287]; pyruvate dehydrogenase (NAD+) activity [GO:0034604]
PF07992;PF02852;
3.30.390.30;3.50.50.60;
Class-I pyridine nucleotide-disulfide oxidoreductase family
PTM: Tyrosine phosphorylated. {ECO:0000250|UniProtKB:Q811C4}.
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:36854377, ECO:0000305|PubMed:9169128}. Nucleus {ECO:0000250|UniProtKB:P09622}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q811C4}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:15888450}. Note=Mainly localizes in the mi...
CATALYTIC ACTIVITY: Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099, ChEBI:CHEBI:83100; EC=1.8.1.4; Evidence={ECO...
null
null
null
null
FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in ...
Mus musculus (Mouse)
O08750
NFIL3_MOUSE
MQLRKMQTIKKEPAPLDPTSSSDKMLLLNSALAEVAEDLASGEDLLLNEGSMGKNKSSACRRKREFIPDEKKDAMYWEKRRKNNEAAKRSREKRRLNDLVLENKLIALGEENATLKAELLSLKLKFGLISSTAYAQEIQKLSNSTAVYFQDYQTSKAAVSSFVDEHEPAMVAGSCISVIKHSPQSSLSDVSEVSSVEHTQESPAQGGCRSPENKFPVIKQEPVELESFAREAREERGTYSTSIYQSYMGSSFSTYSHSPPLLQVHGSTSNSPRTSEADEGVVGKSSDGEDEQQVPKGPIHSPVELQRVHATVVKVPEVNP...
null
null
cellular response to interleukin-4 [GO:0071353]; circadian rhythm [GO:0007623]; immune response [GO:0006955]; natural killer cell differentiation [GO:0001779]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene ex...
nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF07716;PF06529;
1.20.5.170;
BZIP family, NFIL3 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:11316793}.
null
null
null
null
null
FUNCTION: Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites (By similarity). Represses promoter activity in osteoblasts....
Mus musculus (Mouse)
O08755
HNF6_MOUSE
MNAQLTMEAIGELHGVSHEPVPAPADLLGGSPHARSSVGHRGSHLPPAHPRSMGMASLLDGGSGGSDYHHHHRAPEHSLAGPLHPTMTMACETPPGMSMPTTYTTLTPLQPLPPISTVSDKFPHHHHHHHHHHHPHHHQRLAGNVSGSFTLMRDERGLASMNNLYTPYHKDVAGMGQSLSPLSGSGLGSIHNSQQGLPHYAHPGAAMPTDKMLTPNGFEAHHPAMLGRHGEQHLTPTSAGMVPINGLPPHHPHAHLNAQGHGQLLGTAREPNPSVTGAQVSNGSNSGQMEEINTKEVAQRITTELKRYSIPQAIFAQRVL...
null
null
anatomical structure morphogenesis [GO:0009653]; B cell differentiation [GO:0030183]; cell fate commitment [GO:0045165]; cell migration [GO:0016477]; cilium assembly [GO:0060271]; endocrine pancreas development [GO:0031018]; endoderm development [GO:0007492]; enteroendocrine cell differentiation [GO:0035883]; epithelia...
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; 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]; RNA polymerase II cis-regulatory re...
PF02376;PF00046;
1.10.10.60;1.10.260.40;
CUT homeobox family
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Transcriptional activator. Binds the consensus sequence 5'-DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B and TTR. Important for liver genes transcription. Stimulates the expression of Onecut3 in the developing endoderm. {ECO:0000269|PubMed:15381696}.
Mus musculus (Mouse)
O08756
HCD2_MOUSE
MAAAVRSVKGLVAVVTGGASGPWLATAKRLVGQGATAVLLDVPDSEGESQAKKLGESCIFAPANVTSEKEIQAALTLAKEKFGRIDVAVNCAGIAVAIKTYHQKKNKIHTLEDFQRVINVNLIGTFNVIRLVAGEMGQNEPDQGGQRGVIINTASVAAFEGQVGQAAYSASKGGIDGMTLPIARDLAPTGIRVVTIAPGLFATPLLTTLPEKVRNFLASQVPFPSRLGDPAEYAHLVQTIIENPFLNGEVIRLDGAIRMQP
1.1.1.159; 1.1.1.178; 1.1.1.239; 1.1.1.35; 1.1.1.53; 1.1.1.62
null
androgen metabolic process [GO:0008209]; bile acid biosynthetic process [GO:0006699]; brexanolone metabolic process [GO:0062173]; C21-steroid hormone metabolic process [GO:0008207]; estrogen metabolic process [GO:0008210]; fatty acid beta-oxidation [GO:0006635]; fatty acid metabolic process [GO:0006631]; isoleucine cat...
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial inner membrane [GO:0005743]; mitochondrial nucleoid [GO:0042645]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739]
17-beta-hydroxysteroid dehydrogenase (NAD+) activity [GO:0044594]; 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity [GO:0047015]; 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; acetoacetyl-CoA reductase activity [GO:0018454]; amyloid-beta binding [GO:0001540]; androstan-3-alpha,17-beta-diol dehydrogenase ac...
PF00106;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99714}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q99714}.
CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000250|UniProtKB:Q99714}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:...
null
PATHWAY: Amino-acid degradation; L-isoleucine degradation. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Steroid metabolism. {ECO:0000250|UniProtKB:Q99714}.; PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000250|UniProtKB:Q9971...
null
null
FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty acid, branched-chain amino acid and steroid metabolism (By similarity). Acts as (S)-3-hydroxyacyl-CoA dehydrogenase in mitochondrial fatty acid beta-oxidation, a major degradation pathway of fatty acids. Catalyzes the third step in the beta-oxidation c...
Mus musculus (Mouse)
O08759
UBE3A_MOUSE
MATACKRSPGESQSEDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTFLRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGASNNSEIKMNKKEGKDFKDVIYLTEEKVYEIYEFCRESEDYSPLIRVIGRIFSSAEALVLSFRKVKQHTKEELKSLQEKDEDKDEDEKEKAACSAAAMEEDSEASSSRMGDSSQGDNNVQKLGPDDVTVDIDAIRRVYSSLLANEKLETAFLNALVYLSPNVECDLTYHNVYTRDPNYLNLFIIVMENSNLHSPEYLEMALPLFCKAMCKLPLEAQGKLI...
2.3.2.26
null
androgen receptor signaling pathway [GO:0030521]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; locomotory exploration behavior [GO:0035641]; modulation of chemical synaptic transmission [GO:0050804]; motor learning [GO:0061743]; negative regulation of dendritic spine morphogenesis [GO:0...
cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; proteasome complex [GO:0000502]
metal ion binding [GO:0046872]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
PF16558;PF00632;
3.30.2160.10;3.30.2410.10;3.90.1750.10;6.10.130.10;
null
PTM: Phosphorylation at Tyr-654 by ABL1 impairs E3 ligase activity. {ECO:0000250|UniProtKB:Q05086}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9182527}. Nucleus {ECO:0000269|PubMed:9182527}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:30020076};
null
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:20211139, ECO:0000269|PubMed:30020076}.
null
null
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates (PubMed:20211139, PubMed:24728990, PubMed:30020076). Several substrates have been identified including the BMAL1, ARC, LAMTOR1, RAD23A and RAD23B, MCM7 (whi...
Mus musculus (Mouse)
O08760
OGG1_MOUSE
MLFRSWLPSSMRHRTLSSSPALWASIPCPRSELRLDLVLASGQSFRWKEQSPAHWSGVLADQVWTLTQTEDQLYCTVYRGDDSQVSRPTLEELETLHKYFQLDVSLAQLYSHWASVDSHFQRVAQKFQGVRLLRQDPTECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPNLHALAGPEAETHLRKLGLGYRARYVRASAKAILEEQGGPAWLQQLRVAPYEEAHKALCTLPGVGAKVADCICLMALDKPQAVPVDVHVWQIAHRDYGWHPKTSQAKGPSPLANKELGNFFRNLWGPYAGWAQAVLFS...
3.2.2.-; 4.2.99.18
null
base-excision repair [GO:0006284]; base-excision repair, AP site formation [GO:0006285]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; negative regulation of apoptotic process [GO:0043066]; negative re...
mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
8-oxo-7,8-dihydroguanine DNA N-glycosylase activity [GO:0034039]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA N-glycosylase activity [GO:0019104]; enzyme binding [GO:0019899]; microtubule binding [GO:0008017]; oxidized b...
PF00730;PF07934;
3.30.310.40;1.10.1670.10;
Type-1 OGG1 family
null
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells. {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RH...
null
null
null
null
FUNCTION: DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.
Mus musculus (Mouse)
O08762
NETR_MOUSE
MALARCVLAVILGALSVVARADPVSRSPLHRPHPSPPRSQHAHYLPSSRRPPRTPRFPLPLRIPAAQRPQVLSTGHTPPTIPRRCGAGESWGNATNLGVPCLHWDEVPPFLERSPPASWAELRGQPHNFCRSPDGSGRPWCFYRNAQGKVDWGYCDCGQGPALPVIRLVGGNSGHEGRVELYHAGQWGTICDDQWDNADADVICRQLGLSGIAKAWHQAHFGEGSGPILLDEVRCTGNELSIEQCPKSSWGEHNCGHKEDAGVSCVPLTDGVIRLAGGKSTHEGRLEVYYKGQWGTVCDDGWTEMNTYVACRLLGFKYGK...
3.4.21.-
null
exocytosis [GO:0006887]; proteolysis [GO:0006508]; zymogen activation [GO:0031638]
axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic cleft [GO:0043083]; terminal bouton [GO:0043195]
peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]
PF00051;PF00530;PF00089;
2.40.20.10;3.10.250.10;2.40.10.10;
Peptidase S1 family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.
Mus musculus (Mouse)
O08773
RGS14_RAT
MPGKPKHLGVPNGRMVLAVSDGELTSTSGSQAQGEGRGSSLSIHSLPSGPSSPFSTDEQPVASWAQSFERLLQDPRGLAYFTEFLKKEFSAENVTFWQACERFQQIPASDTKQLAQEAHNIYHEFLSSQALSPVNIDRQAWLSEEVLAQPRPDMFRAQQLQIFNLMKFDSYARFVKSPLYQECLLAEAEGRPLREPGSSHLGSPDTARKKPKLKPGKSLPLGVEELGQLPLAEGRPLRKSFRREMPGGAVNSALRRESQGSLNSSASLDLGFLAFVSSKSESHRKSLGSGEGESESRPGKYCCVYLPDGTASLALARPGL...
null
null
cell division [GO:0051301]; chromosome segregation [GO:0007059]; learning [GO:0007612]; long-term memory [GO:0007616]; long-term synaptic potentiation [GO:0060291]; mitotic cell cycle [GO:0000278]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; nega...
centrosome [GO:0005813]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; microtubule [GO:0005874]; nuclear body [GO:0016604]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; postsynaptic density [GO:0014069]; spindle [GO:0005819...
G-protein alpha-subunit binding [GO:0001965]; GDP-dissociation inhibitor activity [GO:0005092]; GTPase activating protein binding [GO:0032794]; GTPase activator activity [GO:0005096]; microtubule binding [GO:0008017]; protein kinase binding [GO:0019901]; signaling receptor complex adaptor activity [GO:0030159]
PF02188;PF02196;PF00615;
1.10.196.10;1.10.167.10;
null
PTM: Phosphorylated by PKC. Phosphorylation is increased in presence of forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1. {ECO:0000269|PubMed:12534294}.
SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body {ECO:0000250}. Cytoplasm. Membrane. Cell membrane. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole. Cell projection, dendrite {ECO:0000250}. Cell projection, dendrit...
null
null
null
null
null
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Besides, modulates signal transduction via G protein alpha subunits by functioning as a GDP-dissociation...
Rattus norvegicus (Rat)
O08774
RGS12_RAT
MYRAGEPGKRQSGPAPPRVRSVEVARGRAGYGFTLSGQAPCVLSCVMRGSPADFVGLRAGDQILAINEINVKKASHEDVVKLIGKCSGVLRMVISEGSSHVEPSSSDEEGGLCEGKGWLRPKLDSKALGINRAERVVEEVQSGGIFNMIFESPSLCASGSEPLKLKQRSLSESAALRLDVGQDSLCTPHPSMLSKEEISKVINDDSVFTVGLDNHDDFGLDASILNVAMVVGYLGSIELPSTSSNLEHDSLQAIRGCMRRLRAEQKIHSLVTMKVMHDCVQLVTDRAGVVAEYPAEKLAFSAVCPDDRRFFGLVTMQTND...
null
null
negative regulation of G protein-coupled receptor signaling pathway [GO:0045744]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; signal transduction [GO:0007165]; termination of G protein-coupled receptor signaling pathway [GO:0038032]
apical dendrite [GO:0097440]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202]
G-protein alpha-subunit binding [GO:0001965]; GTPase activator activity [GO:0005096]; GTPase regulator activity [GO:0030695]
PF02188;PF00595;PF02196;PF00615;PF16613;PF16611;PF16612;
1.10.196.10;2.30.42.10;2.30.29.30;1.10.167.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16819986}. Cytoplasm {ECO:0000269|PubMed:16819986}. Cell projection, dendrite {ECO:0000269|PubMed:16819986}. Synapse {ECO:0000269|PubMed:16819986}.
null
null
null
null
null
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. {ECO:0000269|PubMed:11387333, ECO:0000269|PubMed:9651375}.
Rattus norvegicus (Rat)
O08775
VGFR2_RAT
MESRALLAVALWFCVETRAASVGLPGDSLHPPKLSTQKDILTILANTTLQITCRGQRDLDWLWPNTPRDSEERVLVTECGDSIFCKTLTVPRVVGNDTGAYKCFYRDTDVSSIVYVYVQDHRSPFIASVSDEHGIVYITENKNKTVVIPCRGSISNLNVSLCARYPEKRFVPDGNRISWDSEKGFTIPSYMISYAGMVFCEAKINDETYQSIMYIVLVVGYRIYDVVLSPPHEIELSAGEKLVLNCTARTELNVGLDFSWQFPSSKHQHKKIVNRDVKSLPGTVAKMFLSTLTIDSVTKSDQGEYTCTAYSGLMTKKNKT...
2.7.10.1
null
angiogenesis [GO:0001525]; blood vessel endothelial cell differentiation [GO:0060837]; branching involved in blood vessel morphogenesis [GO:0001569]; branching morphogenesis of an epithelial tube [GO:0048754]; calcium ion homeostasis [GO:0055074]; calcium-mediated signaling using intracellular calcium source [GO:003558...
anchoring junction [GO:0070161]; cell junction [GO:0030054]; cell periphery [GO:0071944]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; membrane raft ...
ATP binding [GO:0005524]; cadherin binding [GO:0045296]; coreceptor activity [GO:0015026]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; protein tyrosine kinase activity [GO:0004713]; vascular endothelial growth factor binding [GO:0038085]; vascular endotheli...
PF07679;PF00047;PF13927;PF07714;PF21339;PF17988;
2.60.40.10;1.10.510.10;
Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily
PTM: N-glycosylated. {ECO:0000250}.; PTM: Ubiquitinated. Tyrosine phosphorylation of the receptor promotes its poly-ubiquitination, leading to its degradation via the proteasome or lysosomal proteases (By similarity). {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation ...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35968}; Single-pass type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Early endosome {ECO:0000250}. Cell junction {ECO:0000250}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35968}. Note=...
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=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100...
null
null
null
null
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Pr...
Rattus norvegicus (Rat)
O08785
CLOCK_MOUSE
MVFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKETTAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSESVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEYLKSKNQLEFCCHMLRGTIDPKEPSTYEYVRFIGNFKSLTSVSTSTHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLEN...
2.3.1.48
null
cellular response to ionizing radiation [GO:0071479]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; DNA damage checkpoint signaling [GO:0000077]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of glucocorticoid receptor signaling pathway [GO:2...
chromatoid body [GO:0033391]; CLOCK-BMAL transcription complex [GO:1990513]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perichromatin fibrils [GO:0005726]; transcription regulator complex [GO:0005667]
chromatin DNA binding [GO:0031490]; 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]; E-box binding [GO:0070888]; his...
PF00010;PF00989;PF14598;
4.10.280.10;3.30.450.20;
null
PTM: Ubiquitinated, leading to its proteasomal degradation. {ECO:0000269|PubMed:16980631}.; PTM: O-glycosylated; contains O-GlcNAc. O-glycosylation by OGT prevents protein degradation by inhibiting ubiquitination. It also stabilizes the CLOCK-BMAL1 heterodimer thereby increasing CLOCK-BMAL1-mediated transcriptional act...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11779462, ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:16980631, ECO:0000269|PubMed:17310242, ECO:0000269|PubMed:18662546, ECO:0000269|PubMed:19414601}. Cytoplasm {ECO:0000269|PubMed:12897057, ECO:0000269|PubMed:16980631}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O1...
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:16678094};
null
null
null
null
FUNCTION: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a...
Mus musculus (Mouse)
O08786
CCKAR_MOUSE
MDVVDSLLMNGSNITPPCELGLENETLFCLDQPQPSKEWQSAVQILLYSFIFLLSVLGNTLVITVLIRNKRMRTVTNIFLLSLAVSDLMLCLFCMPFNLIPNLLKDFIFGSAVCKTTTYFMGTSVSVSTFNLVAISLERYGAICRPLQSRVWQTKSHALKVIAATWCLSFTIMTPYPIYSNLVPFTKNNNQTANMCRFLLPSDAMQQSWQTFLLLILFLIPGVVMVVAYGLISLELYQGIKFDASQKKSAKEKRLSSGGGGGGGSSSSRYEDSDGCYLQKSRPPRKLELQQLSTSSSGGRINRIRSSGSAANLIAKKRVI...
null
null
axonogenesis [GO:0007409]; cellular response to hormone stimulus [GO:0032870]; eating behavior [GO:0042755]; feeding behavior [GO:0007631]; forebrain development [GO:0030900]; G protein-coupled receptor signaling pathway [GO:0007186]; gastric acid secretion [GO:0001696]; insulin secretion [GO:0030073]; neuron migration...
cytosol [GO:0005829]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195]
cholecystokinin receptor activity [GO:0004951]; neuropeptide receptor activity [GO:0008188]; peptide binding [GO:0042277]; peptide hormone binding [GO:0017046]
PF00001;PF09193;
4.10.670.10;1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This recep...
Mus musculus (Mouse)
O08788
DCTN1_MOUSE
MAQSRRHMSSRTPSGSRMSTEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGADAAAKTSKLRGLKPKKAPTARKTTTRRPKPTRPASTGVAGPSSSLGPSGSASAGELSSSEPSTPAQTPLAAPIIPTPALTSPGAAPPLPSPSKEEEGLRAQVRDLEEKLETLRLKRSEDKAKLKELEKHKIQLEQVQEWKSKMQEQQADLQRRLKEARKEAKEALEAKERYMEEMADTADAIEMATLDKEMAEERAES...
null
null
cell division [GO:0051301]; centriole-centriole cohesion [GO:0010457]; cytoplasmic microtubule organization [GO:0031122]; establishment of mitotic spindle orientation [GO:0000132]; melanosome transport [GO:0032402]; microtubule anchoring at centrosome [GO:0034454]; motor behavior [GO:0061744]; neuromuscular junction de...
axon [GO:0030424]; cell cortex [GO:0005938]; cell cortex region [GO:0099738]; cell leading edge [GO:0031252]; cell tip [GO:0051286]; centriolar subdistal appendage [GO:0120103]; centriole [GO:0005814]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasmic dynein complex [GO:0005868]; cytosol [GO:0005829...
identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]
PF01302;PF12455;
2.30.30.190;
Dynactin 150 kDa subunit family
PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to its degradation by the proteasome. {ECO:0000250|UniProtKB:Q14203}.; PTM: Phosphorylation by SLK at Thr-145, Thr-146 and Thr-147 targets DCTN1 to the centrosome. It is uncertain if SLK phosphorylates all three threonines or one or two of them. PLK1-mediate...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16954346}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14203}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:2338...
null
null
null
null
null
FUNCTION: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Plays a key role in dynein-mediated retrograde transport of vesicles and organelles along microtubules by recruiting and tethering dynein to microtubules. Binds to both dyn...
Mus musculus (Mouse)
O08789
MNT_MOUSE
MSIETLLEAARFLEWQAQQQQRAREEQERLRLEREREREQEQKRASNLARLAHALPVEEPRIEAPPLPLSPPAPPPAPPPPLATPAPLTVIPIPVVTNSPQSLPPPPPLPPAAQPLPLAPRQPALVSTPGLSIKEPVTLPTRPQVPTPAPLLPDAKTTVAPTGSPKPLQPLPAPILTIAPHPGVQPQLAPQQPPPPTLGTLKLAPAEEAKSSEQKKRPGGIGTREVHNKLEKNRRAHLKECFETLKRNIPNVDDKKTSNLSVLRTALRYIQSLKRKEKEYEHEMERLAREKIATQQRLAELKHELSQWMDVLEIDRVLRQ...
null
null
cellular senescence [GO:0090398]; negative regulation of apoptotic signaling pathway [GO:2001234]; regulation of cell cycle [GO:0051726]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; 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]; identical protein binding [GO:00428...
PF00010;
4.10.280.10;
null
null
SUBCELLULAR LOCATION: Nucleus.
null
null
null
null
null
FUNCTION: Binds DNA as a heterodimer with MAX and represses transcription. Binds to the canonical E box sequence 5'-CACGTG-3' and, with higher affinity, to 5'-CACGCG-3'.
Mus musculus (Mouse)
O08790
FPRS1_MOUSE
METNYSIPLNGSDVVIYDSTISRVLWILSMVVVSITFFLGVLGNGLVIWVAGFRMPHTVTTIWYLNLALADFSFTATLPFLLVEMAMKEKWPFGWFLCKLVHIAVDVNLFGSVFLIAVIALDRCICVLHPVWAQNHRTVSLARNVVVGSWIFALILTLPLFLFLTTVRDARGDVHCRLSFVSWGNSVEERLNTAITFVTTRGIIRFIVSFSLPMSFVAICYGLITTKIHKKAFVNSSRPFRVLTGVVASFFICWFPFQLVALLGTVWLKEMQFSGSYKIIGRLVNPTSSLAFFNSCLNPILYVFMGQDFQERLIHSLSSR...
null
null
chemotaxis [GO:0006935]; complement receptor mediated signaling pathway [GO:0002430]; G protein-coupled receptor signaling pathway [GO:0007186]; inflammatory response [GO:0006954]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cytosolic calcium ion concentr...
plasma membrane [GO:0005886]
complement receptor activity [GO:0004875]; N-formyl peptide receptor activity [GO:0004982]; RAGE receptor binding [GO:0050786]; signaling receptor activity [GO:0038023]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
null
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Low affinity receptor for N-formyl-methionyl peptides. Receptor for lipoxin A4. May have an olfactory function associated with the identification of pathogens or of pathogenic states. {ECO:0000269|PubMed:19387439}.
Mus musculus (Mouse)
O08791
COE3_MOUSE
MFGIQENIPRGGTTMKEEPLGSGMNPVRSWMHTAGVVDANTAAQSGVGLARAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVEKEKEPNNEKTNNGIHYKLQLLYSNGVRTEQDLYVRLIDSMTKQAIVYEGQDKNPEMCRVLLTHEIMCSRCCDKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKNAGNPRDMRRFQVVVSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEGTAPSYLENATPCIKAISPSEGWTTGGATVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHI...
null
null
positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF16422;PF16423;PF01833;
1.10.287.4280;2.60.40.10;2.60.40.3180;
COE family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4W6}.
null
null
null
null
null
FUNCTION: Transcriptional activator (PubMed:9151732). Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3' (By similarity). {ECO:0000250|UniProtKB:Q07802, ECO:0000269|PubMed:9151732}.
Mus musculus (Mouse)
O08792
COE2_MOUSE
MFGIQDTLGRGPALKDKSLGAEMDSVRSWVRNVGVVDANVAAQSGVALSRAHFEKQPPSNLRKSNFFHFVLALYDRQGQPVEIERTAFVDFVENDKEQGNEKTNNGTHYKLQLLYSNGVRTEQDLYVRLIDSVTKQPIAYEGQNKNPEMCRVLLTHEVMCSRCCEKKSCGNRNETPSDPVIIDRFFLKFFLKCNQNCLKTAGNPRDMRRFQVVLSTTVNVDGHVLAVSDNMFVHNNSKHGRRARRLDPSEATPCIKAISPSEGWTTGGAMVIIIGDNFFDGLQVVFGTMLVWSELITPHAIRVQTPPRHIPGVVEVTLSY...
null
null
adipose tissue development [GO:0060612]; brown fat cell differentiation [GO:0050873]; cell fate determination [GO:0001709]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:00459...
nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific D...
PF16422;PF16423;PF01833;
1.10.287.4280;2.60.40.10;2.60.40.3180;
COE family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Transcription factor that, in osteoblasts, activates the decoy receptor for RANKL, TNFRSF11B, which in turn regulates osteoclast differentiation. Acts in synergy with the Wnt-responsive LEF1/CTNNB1 pathway. Recognizes variations of the palindromic sequence 5'-ATTCCCNNGGGAATT-3'. {ECO:0000269|PubMed:16326388}.
Mus musculus (Mouse)
O08795
GLU2B_MOUSE
MLLLLLLLLPLCWAVEVKRPRGVSLSNHHFYEESKPFTCLDGTATIPFDQVNDDYCDCKDGSDEPGTAACPNGSFHCTNTGYKPLYILSSRVNDGVCDCCDGTDEYNSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRAAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQERAASAFQELDDNMDGMVSLAELQTHPELDTDGDGALSEEEAQALLSGDTQTDTTSFYDRVWAAIRDKYRSEVPPTDIPVPEETEPKEEKPPVLPPTEEEEEEEEEPEE...
null
null
in utero embryonic development [GO:0001701]; liver development [GO:0001889]; N-glycan processing [GO:0006491]; negative regulation of neuron projection development [GO:0010977]
endoplasmic reticulum [GO:0005783]; glucosidase II complex [GO:0017177]; intracellular membrane-bounded organelle [GO:0043231]
calcium ion binding [GO:0005509]; protein-containing complex binding [GO:0044877]; RNA binding [GO:0003723]
PF13202;PF12999;PF13015;
1.10.238.10;4.10.400.10;2.70.130.10;
null
null
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}.
null
null
PATHWAY: Glycan metabolism; N-glycan metabolism. {ECO:0000269|PubMed:27462106}.
null
null
FUNCTION: Regulatory subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:27462106, PubMed:9148925). Required for efficient PKD1/Polycystin-1 biogenesis and trafficking to the plas...
Mus musculus (Mouse)
O08796
EF2K_MOUSE
MADEDLIFCLEGVDGGRCSRAGHNADSDTDSDDDEGYFICPITDDHMSNQNVSSKVQSYYSNLTKTECGSTGSPASSFHFKEAWKHAIEKAKHMPDPWAEFHLEDIATEHATRHRYNAVTGEWLKDEVLIKMASQPFGRGAMRECFRTKKLSNFLHAQQWKGASNYVAKRYIEPVDRSVYFEDVQLQMEAKLWGEDYNRHKPPKQVDIMQMCIIELKDRPGQPLFHLEHYIEGKYIKYNSNSGFVRDDNIRLTPQAFSHFTFERSGHQLIVVDIQGVGDLYTDPQIHTEKGTDFGDGNLGVRGMALFFYSHACNRICQSM...
2.7.11.20
null
cellular response to anoxia [GO:0071454]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular response to insulin stimulus [GO:0032869]; myosin II filament disassembly [GO:0031037]; negative regulat...
actomyosin contractile ring [GO:0005826]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; elongation factor-2 kinase activity [GO:0004686]; myosin heavy chain kinase activity [GO:0016905]; translation factor activity, RNA binding [GO:0008135]
PF02816;
3.20.200.10;1.25.40.10;
Protein kinase superfamily, Alpha-type protein kinase family
PTM: Autophosphorylated at multiple residues, Thr-347 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-397 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-77 resulting in improved protein stability, higher EE2F phosphorylated and subsequently ...
null
CATALYTIC ACTIVITY: Reaction=[translation elongation factor 2] + ATP = [translation elongation factor 2]-phosphate + ADP + H(+); Xref=Rhea:RHEA:21436, Rhea:RHEA-COMP:11268, Rhea:RHEA-COMP:11269, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.20; Evidence={ECO:0...
null
null
null
null
FUNCTION: Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation (PubMed:34815424, PubMed:9144159). Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and...
Mus musculus (Mouse)
O08807
PRDX4_MOUSE
MEARSKLLDGTTASRRWTRKLVLLLPPLLLFLLRTESLQGLESDERFRTRENECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVINGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRIEEFKSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLNHQISKDYGVYLEDSGHTLRGLFIIDDKGVLRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN
1.11.1.24
null
cell redox homeostasis [GO:0045454]; cellular response to stress [GO:0033554]; extracellular matrix organization [GO:0030198]; hydrogen peroxide catabolic process [GO:0042744]; male gonad development [GO:0008584]; negative regulation of male germ cell proliferation [GO:2000255]; protein maturation by protein folding [G...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; smooth endoplasmic reticulum [GO:0005790]
identical protein binding [GO:0042802]; molecular sequestering activity [GO:0140313]; thioredoxin peroxidase activity [GO:0008379]
PF10417;PF00578;
3.40.30.10;
Peroxiredoxin family, AhpC/Prx1 subfamily
PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond. {ECO:0000250|UniProtKB:Q13162}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13162}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}. Note=Not secreted. {ECO:0000269|PubMed:11229364}.
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000250|UniProtK...
null
null
null
null
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:11229364). Regulate...
Mus musculus (Mouse)
O08808
DIAP1_MOUSE
MEPSGGGLGPGRGTRDKKKGRSPDELPATGGDGGKHKKFLERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDISDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMNQKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELD...
null
null
actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; actin nucleation [GO:0045010]; axon midline choice point recognition [GO:0016199]; brain development [GO:0007420]; cytoskeleton organization [GO:0007010]; ephrin receptor signaling pathway [GO:0048013]; gene expression [GO:0010467...
actin filament [GO:0005884]; brush border [GO:0005903]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; neuron projection [GO:0043005]; nucleus [GO:0005634]; presynapse [GO:0098793]; ruffle membrane [GO:0032587]; spindle [GO:0005819]
actin binding [GO:0003779]; identical protein binding [GO:0042802]; profilin binding [GO:0005522]; small GTPase binding [GO:0031267]; transmembrane transporter binding [GO:0044325]
PF06346;PF06367;PF06371;PF02181;
1.20.1170.10;1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10;
Formin homology family, Diaphanous subfamily
PTM: Phosphorylation at Thr-751 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement (By similarity). {ECO:0000250|UniProtKB:O60610}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9214622}. Cell projection, ruffle membrane {ECO:0000269|PubMed:9214622}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9214622}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O60610}. Cytoplasm, cytoskeleton, spindle {ECO:...
null
null
null
null
null
FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (PubMed:10678165, PubMed:15044801, PubMed:18572016, PubMed:23558171). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (PubMed:10...
Mus musculus (Mouse)
O08811
ERCC2_MOUSE
MKLNVDGLLVYFPYDYIYPEQFSYMLELKRTLDAKGHGVLEMPSGTGKTVSLLALIVAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLSFYEQQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQQDASLPHCRFYEEFDIHGRQMPLPAGIYNLDDLKALGQRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQSNLDTLQKTVLRIKETDEQRLRDEYRRLVEGLREASVARETDAHLANPVLPDEVLQEAVP...
3.6.4.12
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
apoptotic process [GO:0006915]; bone mineralization [GO:0030282]; central nervous system myelin formation [GO:0032289]; chromosome segregation [GO:0007059]; determination of adult lifespan [GO:0008340]; DNA repair [GO:0006281]; embryonic cleavage [GO:0040016]; embryonic organ development [GO:0048568]; erythrocyte matur...
CAK-ERCC2 complex [GO:0070516]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; MMXD complex [GO:0071817]; nucleus [GO:0005634]; spindle [GO:0005819]; transcription factor TFIID complex [GO:0005669]; transcription factor TFIIH core complex [GO:0000439]; transcription factor TFIIH holo complex [GO:0005675]
4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]
PF06733;PF06777;PF13307;
3.40.50.300;
Helicase family, RAD3/XPD subfamily
PTM: ISGylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
null
null
null
null
FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH a...
Mus musculus (Mouse)
O08812
CTR3_RAT
MLWQALRRFGQKLVRRRLLELGMGETRLARCLSTLDLVALGVGSTLGAGVYVLAGEVAKEKAGPSIVICFLVAALSSVLAGLCYAEFGARVPGSGSAYLYSYVTVGELWAFTTGWNLILSYVIGTASVARAWSSAFDNLIGNHISQTLKGTILLNMPHVLAEYPDFFALALVLLLTGLLVLGANESGLVTKVFTGMNLLVLGFVIISGFIKGELRNWKLTKEDYCLTMSESNGTCSLDSMGSGGFMPFGLEGILRGAATCFYAFVGFDCIATTGEEAQNPQRSIPMGIVISLSICFLAYFGVSSALTLMMPYYKLQPESP...
null
null
basic amino acid transmembrane transport [GO:1990822]; L-arginine import across plasma membrane [GO:0097638]; L-arginine transmembrane transport [GO:1903826]; L-lysine import across plasma membrane [GO:0097639]; L-lysine transmembrane transport [GO:1903401]; L-ornithine import across plasma membrane [GO:0097640]; L-orn...
plasma membrane [GO:0005886]
basic amino acid transmembrane transporter activity [GO:0015174]; L-arginine transmembrane transporter activity [GO:0061459]; L-lysine transmembrane transporter activity [GO:0015189]; L-ornithine transmembrane transporter activity [GO:0000064]
PF13520;PF13906;
1.20.1740.10;
Amino acid-polyamine-organocation (APC) superfamily, Cationic amino acid transporter (CAT) (TC 2.A.3.3) family
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8WY07}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=L-arginine(in) = L-arginine(out); Xref=Rhea:RHEA:32143, ChEBI:CHEBI:32682; Evidence={ECO:0000269|PubMed:9079705}; CATALYTIC ACTIVITY: Reaction=L-lysine(in) = L-lysine(out); Xref=Rhea:RHEA:70935, ChEBI:CHEBI:32551; Evidence={ECO:0000269|PubMed:9079705}; CATALYTIC ACTIVITY: Reaction=L-ornithi...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=103 uM for L-arginine {ECO:0000269|PubMed:9079705}; KM=147 uM for L-lysine {ECO:0000269|PubMed:9079705}; KM=219 uM for L-ornithine {ECO:0000269|PubMed:9079705};
null
null
null
FUNCTION: Uniporter that mediates the uptake of cationic L-amino acids such as L-arginine, L-lysine and L-ornithine (PubMed:9079705). The transport is sodium ions- and pH-independent, moderately trans-stimulated and is mediated by passive diffusion (PubMed:9079705). {ECO:0000269|PubMed:9079705}.
Rattus norvegicus (Rat)
O08815
SLK_RAT
MSFFNFRKIFKLGSEKKKKQYEHVKRDLNPEEFWEIIGELGDGAFGKVYKAQNKETNVLAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTESQIQVVCKQTLEALNYLHDNKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTIQRRDSFIGTPYWMAPEVVMCETSKDRPYDYKADVWSLGITLIEMAEIEPPHHELNPMRVLLKIAKSEPPTLAQPSRWSSNFKDFLKKCLEKNVDARWTTSQLLQHPFVTVDSNKPVRELIAEAKAEVTEEVEDGKE...
2.7.11.1
null
apoptotic process [GO:0006915]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; cytoplasmic microtubule organization [GO:0031122]; phosphorylation [GO:0016310]; positive regulation of apoptotic process [GO:0043065]; regulation of apoptotic process [GO:00429...
cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
ATP binding [GO:0005524]; histone kinase activity [GO:0035173]; identical protein binding [GO:0042802]; 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:0000250}.; PTM: Autophosphorylated.
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}.
Rattus norvegicus (Rat)
O08816
WASL_RAT
MSSGQQPPRRVTNVGSLLLTPQENESLFSFLGKKCVTMSSAVVQLYAADRNCMWSKKCSGVACLVKDNPQRSYFLRIFDIKDGKLLWEQELYNNFVYNSPRGYFHTFAGDTCQVALNFANEEEAKKFRKAVTDLLGRRQRKSEKRRDAPNGPNLPMATVDIKNPEITTNRFYSSQVNNISHTKEKKKGKAKKKRLTKADIGTPSNFQHIGHVGWDPNTGFDLNNLDPELKNLFDMCGISEAQLKDRETSKVIYDFIEKTGGVEAVKNELRRQAPPPPPPSRGGPPPPPPPPHSSGPPPPPARGRGAPPPPPSRAPTAAPP...
null
null
actin cytoskeleton organization [GO:0030036]; actin filament polymerization [GO:0030041]; cell division [GO:0051301]; dendritic spine morphogenesis [GO:0060997]; membrane invagination [GO:0010324]; negative regulation of lymphocyte migration [GO:2000402]; negative regulation of membrane tubulation [GO:1903526]; plasma ...
actin cap [GO:0030478]; cell leading edge [GO:0031252]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; postsynapse [GO:0098794]
actin binding [GO:0003779]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]
PF00786;PF00568;PF02205;
3.90.810.10;2.30.29.30;
null
PTM: Phosphorylation at Ser-239, Tyr-253, Ser-480 and Ser-481 enhances actin polymerization activity. {ECO:0000250|UniProtKB:O00401}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14676198}. Nucleus {ECO:0000269|PubMed:14676198}. Cytoplasm {ECO:0000250|UniProtKB:Q91YD9}. Note=Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated (By similarity). Exported from the nucleus by an nucle...
null
null
null
null
null
FUNCTION: Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Involved in various processes, such as mitosis and cytokinesis, via its role in the regulation of actin polymerization. Together with CDC42, involved in the extension and maintenance of the formation of thin, ac...
Rattus norvegicus (Rat)
O08832
GALT4_MOUSE
MAVRWTWAGKSCLLLALLTLAYILVEFSVSTLYASPGAGGARELGPRRLPDLDTREEDLSQPLYIKPPADSHALGEWGRASKLQLNEGELKQQEELIERYAINIYLSDRISLHRHIEDKRMYECKAKKFHYRSLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRIYLKAQLETYISNLERVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNTGWLEPLLERISRDETAIVCPVIDTIDWNTFEFYMQTGEPMIGGFDWRLTFQWHSVPKHERDRRTSRIDPIRSPTMAGGLFAVSKKY...
2.4.1.41
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8N4A0};
protein O-linked glycosylation [GO:0006493]; protein O-linked glycosylation via serine [GO:0018242]; protein O-linked glycosylation via threonine [GO:0018243]
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; perinuclear region of cytoplasm [GO:0048471]
carbohydrate binding [GO:0030246]; manganese ion binding [GO:0030145]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]
PF00535;PF00652;
2.80.10.50;
Glycosyltransferase 2 family, GalNAc-T subfamily
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2...
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9153242}.
null
null
FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward EA2 peptide substrate and a much lower activity with EPO-T, Muc2, Muc1a, Muc1b. {ECO:0000269|PubM...
Mus musculus (Mouse)
O08835
SYT11_RAT
MAEITNIRPSFDVSPVAAGLIGASVLVVCVSVTVFVWTCCHQQAEKKHKTPPYKFIHMLKGISIYPETLSNKKKIIKVRRDKDGSHRESGRGNLLVNAESGLLSHDRDPRGPSPASCIDQLPIKRDYGEELRSPMTSLTPGESKPTSPSSPEEDVMLGSLTFSVDYNFPKKALVVTIQEAHGLPVMDGQTQGSDPYIKMTILPDKRHRVKTRVLRKTLDPVFDETFTFYGIPYSQLQDLVLHFLVLSFDRFSRDDVIGEVMVPLAGVDPSTGKVQLTRDIIKRNIQKCISRGELQVSLSYQPVAQRMTVVVLKARHLPKM...
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
autophagy [GO:0006914]; calcium ion regulated lysosome exocytosis [GO:1990927]; calcium ion-regulated exocytosis of neurotransmitter [GO:0048791]; cellular response to calcium ion [GO:0071277]; establishment of vesicle localization [GO:0051650]; learning [GO:0007612]; memory [GO:0007613]; negative regulation of clathri...
axon [GO:0030424]; cell body [GO:0044297]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dopaminergic synapse [GO:0098691]; early phagosome [GO:0032009]; excitatory synapse [GO:0060076]; exocytic vesicle [GO:0070382]; inhibitory synapse [GO:0...
beta-tubulin binding [GO:0048487]; clathrin binding [GO:0030276]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; phosphatidylserine binding [GO:0001786]; SNARE binding [GO:0000149]; translation initiation factor binding [GO:0031369]; ubiquitin protein ligase binding [GO:0031625]
PF00168;
2.60.40.150;
Synaptotagmin family
PTM: Ubiquitinated, at least by PRKN, and targeted to the proteasome complex for degradation (PubMed:29311685). Ubiquitination is inhibited by ATP13A2 (By similarity). {ECO:0000250|UniProtKB:Q9BT88, ECO:0000269|PubMed:29311685}.
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein {ECO:0000305}. Perikaryon {ECO:0000250|UniProtKB:Q9R0N3}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9R0N3}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R0N3}. Recycling e...
null
null
null
null
null
FUNCTION: Synaptotagmin family member involved in vesicular and membrane trafficking which does not bind Ca(2+) (PubMed:9162066). Inhibits clathrin-mediated and bulk endocytosis in neurons, functions to ensure precision in vesicle retrieval (PubMed:26589353, PubMed:29311685). Plays an important role in dopamine transmi...
Rattus norvegicus (Rat)
O08836
IGBP1_RAT
MAASEEELLLPRLPELFETSKKLLEELEVATEPTGSRTIQDKVSKGLELLEKAAGMLSQLDLFSRNEDLEEIASIDLKYLMVPALQGALTMKQVNPSKRLDHLQRAREHFIHFLTQCHCYHVAEFQLPQTKNNSAENNTARSSMAYPNLVAMASQRQAKIERYKQKKEVEHRLSALKSAVESGQADDERVREYYLLHLRRWIGISLEEIESIDQEIKILKDKDSPREESACQSSLPEKPPMKPFILTRNKAQAKVFGTGYPSLATMTVSDWYEQHQKYGALPDRGIAKPPSADFQRAAQQQEDQEQKDEENEEKALHRMR...
null
null
B cell activation [GO:0042113]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of protein dephosphorylation [GO:0035308]; negative regulation of stress-activated MAPK cascade [GO:0032873]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation o...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]
enzyme binding [GO:0019899]; mitogen-activated protein kinase kinase binding [GO:0031434]; protein domain specific binding [GO:0019904]; protein phosphatase 2A binding [GO:0051721]; protein phosphatase regulator activity [GO:0019888]; protein-containing complex binding [GO:0044877]
PF04177;
6.10.250.1140;1.25.40.540;
IGBP1/TAP42 family
PTM: Phosphorylated.; PTM: Monoubiquitination by MID1 triggers calpain-mediated cleavage and switches IGBP1 activity from protective to destructive. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
null
null
null
null
null
FUNCTION: Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits (By simil...
Rattus norvegicus (Rat)
O08837
CDC5L_RAT
MPRIMIKGGVWRNTEDEILKAAVMKYGKNQWSRIASLLHRKSAKQCKARWYEWLDPSIKKTEWSREEEEKLLHLAKLMPTQWRTIAPIIGRTAAQCLEHYEFLLDKTAQRDNEEETTDDPRKLKPGEIDPNPETKPARPDPIDMDEDELEMLSEARARLANTQGKKAKRKAREKQLEEARRLAALQKRRELRAAGIEIQKKRKKKRGVDYNAEIPFEKKPALGFYDTSEENYQALDADFRKLRQQDLDGELRSEKEGRDRKKDKQHLKRKKESDLPSAILQTSGVSEFTKKRSKLVLPAPQISDAELQEVVKVGQASEVA...
null
null
cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to interleukin-2 [GO:0071352]; cellular response to nerve growth factor stimulus [GO:1990090]; cellular response to prolactin [GO:1990646]; cellular response to wortmannin [GO:1904568]; DNA damage checkpoint signaling [GO:0000077]; D...
catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; DNA replication factor A complex [GO:0005662]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein-DNA complex [GO:0032993]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; U2-type catal...
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; leucine zipper domain binding [GO:0043522]; protein kinase binding [GO:0019901]; protein phosphatase 1 bindin...
PF11831;PF13921;
1.10.10.60;
CEF1 family
PTM: Phosphorylated on serine and threonine residues. Phosphorylation on Thr-411 and Thr-438 is required for CDC5L-mediated mRNA splicing. Has no effect on subcellular location nor on homodimerization. Phosphorylated in vitro by CDK2 (By similarity). Phosphorylation enhances interaction with PPP1R8. {ECO:0000250, ECO:0...
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:11694351, ECO:0000269|PubMed:11884640}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00625}. Cytoplasm {ECO:0000269|PubMed:11694351}. Note=May shuttle between cytoplasm and nucleus. {ECO:0000303|PubMed:11694351}.
null
null
null
null
null
FUNCTION: DNA-binding protein involved in cell cycle control. May act as a transcription activator. Plays a role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required...
Rattus norvegicus (Rat)
O08838
AMPH_RAT
MADIKTGIFAKNVQKRLNRAQEKVLQKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGDQHADKAFSIQGAPSDSGPLRIAKTPSPPEEASPLPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVPPLPKVTPTKELQQENI...
null
null
learning [GO:0007612]; positive regulation of endocytosis [GO:0045807]; synaptic vesicle endocytosis [GO:0048488]
axon terminus [GO:0043679]; cytoskeleton [GO:0005856]; extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; leading edge membrane [GO:0031256]; photoreceptor ribbon synapse [GO:0098684]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; presynaptic endocytic zone [GO:0...
phosphatase binding [GO:0019902]; phospholipid binding [GO:0005543]; protein-containing complex binding [GO:0044877]
PF03114;
1.20.1270.60;2.30.30.40;
null
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
null
null
null
null
null
FUNCTION: May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
O08839
BIN1_RAT
MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLSECLQEVYEPEWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVSLEKQHGSNTFTVKAQPSDSAPEKGNKSPSPPPDGSPAATPEIRVNHEPEPA...
null
null
endosome to lysosome transport [GO:0008333]; lipid tube assembly [GO:0060988]; muscle cell differentiation [GO:0042692]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1904878]; negative regulation of pota...
axon [GO:0030424]; axon initial segment [GO:0043194]; axon terminus [GO:0043679]; cerebellar mossy fiber [GO:0044300]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; I band [GO:0031674]; lipid tube [G...
actin filament binding [GO:0051015]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; protease binding [GO:0002020]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:...
PF03114;PF14604;
1.20.1270.60;2.30.30.40;
null
PTM: Phosphorylated by protein kinase C.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O08539}. Cytoplasm {ECO:0000250|UniProtKB:O08539}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:9182667}.
null
null
null
null
null
FUNCTION: Is a key player in the control of plasma membrane curvature, and membrane shaping and remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling. Required in muscle cells for the formation of T-tubules,...
Rattus norvegicus (Rat)
O08841
QSOX1_CAVPO
MTGCGRRSGWLPPLRLLLLPLLLGGPGVGAAQLAALYSASDPLTLLQADTVRSTVLNSPSAWAVEFFASWCGHCIAFAPTWKALAKDIKDWRPALNLAALNCADETNNAVCRDFNIAGFPSVRFFKAFSKNSTGTTLPVAGANVQMLRERLIDALESHHDTWPSACPPLEPVKPKEIDTFFARNNQEYLVLIFEQENSYLGREVTLDLSQHHDLVVRRVLSTEANVVRKFGVADFPSCYLLFRNGSVSRVPVLVESRRFYTAYLQRLSEVTREGTPTPAVPTISDQIAPTVWKFADRSKIYMADLESALHYILRVEVGRF...
1.8.3.2
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O00391}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:O00391};
extracellular matrix assembly [GO:0085029]; negative regulation of macroautophagy [GO:0016242]; protein folding [GO:0006457]
extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; intercellular bridge [GO:0045171]
FAD binding [GO:0071949]; flavin-dependent sulfhydryl oxidase activity [GO:0016971]; protein disulfide isomerase activity [GO:0003756]
PF04777;PF18371;PF18108;PF00085;
1.20.120.310;3.40.30.10;1.20.120.1960;
Quiescin-sulfhydryl oxidase (QSOX) family
PTM: N-glycosylated. O-glycosylated on Thr and Ser residues. {ECO:0000250|UniProtKB:O00391}.
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'; Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2; Evidence={ECO:0000250|UniProtKB:O00391};
null
null
null
null
FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and protein thiols to disulfides with the reduction of oxygen to hydrogen peroxide. Plays a role in disulfide bond formation in a variety of extracellular proteins. In fibroblasts, required for normal incorporation of laminin into the extracellular matri...
Cavia porcellus (Guinea pig)
O08842
GFRA2_MOUSE
MILANAFCLFFFLDETLRSLASPSSPQGSELHGWRPQVDCVRANELCAAESNCSSRYRTLRQCLAGRDRNTMLANKECQAALEVLQESPLYDCRCKRGMKKELQCLQIYWSIHLGLTEGEEFYEASPYEPVTSRLSDIFRLASIFSGTGADPVVSAKSNHCLDAAKACNLNDNCKKLRSSYISICNREISPTERCNRRKCHKALRQFFDRVPSEYTYRMLFCSCQDQACAERRRQTILPSCSYEDKEKPNCLDLRSLCRTDHLCRSRLADFHANCRASYRTITSCPADNYQACLGSYAGMIGFDMTPNYVDSNPTGIVVS...
null
null
glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; negative regulation of protein autophosphorylation [GO:0031953]; nervous system development [GO:0007399]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235]
glial cell-derived neurotrophic factor receptor activity [GO:0016167]; heparan sulfate binding [GO:1904399]
PF02351;
1.10.220.110;
GDNFR family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9182803}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:9182803}.
null
null
null
null
null
FUNCTION: Receptor for neurturin (NRTN), a growth factor that supports the survival of sympathetic neurons (PubMed:9182803). NRTN-binding leads to autophosphorylation and activation of the RET receptor (PubMed:9182803). Also able to mediate GDNF signaling through the RET tyrosine kinase receptor (By similarity). {ECO:0...
Mus musculus (Mouse)
O08848
RO60_MOUSE
MEGSANQLQPLSETQVVNSEGGCVWQVTDMNRLRRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTAKQEPLLFALAVCSQCADINTKQAAFKAVPEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAVADWYNEKGGMAVALVVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHEEYKEKALSVEAEKLLKYLEAVEKVKRTKDDLEVIHLIEEHQLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLICEKLSNEKLLKKARIH...
null
null
cellular response to interferon-alpha [GO:0035457]; cilium assembly [GO:0060271]; immune system development [GO:0002520]; regulation of gene expression [GO:0010468]; response to UV [GO:0009411]; smoothened signaling pathway [GO:0007224]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
metal ion binding [GO:0046872]; misfolded RNA binding [GO:0034336]; RNA binding [GO:0003723]; U2 snRNA binding [GO:0030620]
PF05731;
3.40.50.410;
Ro 60 kDa family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P10155}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P10155}.
null
null
null
null
null
FUNCTION: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (By similarity). May play roles in cilia formation and/or maintenance (PubMed:21289087). {ECO:0000250|UniProtKB:P10155, ECO:0000269|PubMed:21289087}.
Mus musculus (Mouse)
O08849
RGS2_MOUSE
MQSAMFLAVQHDCVPMDKSAGNGPKVEEKREKMKRTLLKDWKTRLSYFLQNSSAPGKPKTGKKSKQQTFIKPSPEEAQLWAEAFDELLASKYGLAAFRAFLKSEFCEENIEFWLACEDFKKTKSPQKLSSKARKIYTDFIEKEAPKEINIDFQTKSLIAQNIQEATSGCFTTAQKRVYSLMENNSYPRFLESEFYQDLCKKPQITTEPHAT
null
null
brown fat cell differentiation [GO:0050873]; cell cycle [GO:0007049]; G protein-coupled receptor signaling pathway [GO:0007186]; maternal process involved in female pregnancy [GO:0060135]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of cell growth involved in cardiac muscle cell ...
cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
adenylate cyclase inhibitor activity [GO:0010855]; beta-tubulin binding [GO:0048487]; G-protein alpha-subunit binding [GO:0001965]; GTPase activator activity [GO:0005096]
PF00615;
1.10.196.10;1.10.167.10;
null
PTM: Phosphorylated by protein kinase C. Phosphorylation by PRKG1 leads to activation of RGS2 activity. {ECO:0000250|UniProtKB:P41220}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41220}. Cytoplasm {ECO:0000250|UniProtKB:P41220}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P41220}.
null
null
null
null
null
FUNCTION: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (By similarity). It is involved in the negative regulation of the angiotensin-activated signaling pathway...
Mus musculus (Mouse)
O08852
PKD1_MOUSE
MPLGAPALLALALGLGLWLGALAGDPGRGCGPCPLPCFCGPAPDAACRVNCSGRWLQTLGPSLRIPADATALDLSHNLLQTLDIGLLVNLSALVELDLSNNRISTLEEGVFANLFNLSEINLSGNPFECNCGLAWLPRWAKEHQVHVVQSEATTCRGPIPLAGQPLLSIPLLDNACGEEYVACLPDNSSGAVAAVPFYFAHEGPLETEACSAFCFSAGEGLAALSEQNQCLCGAGQASNSSAACSSWCSSISLSLNSACGGPTLLQHTFPASPGATLVGPHGPLASGQPADFHITSSLPISSTRWNFGDGSPEVDMASPA...
null
null
blood vessel development [GO:0001568]; branching morphogenesis of an epithelial tube [GO:0048754]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cartilage condensation [GO:0001502]; cell-cell adhesion [GO:0098609]; cell-cell signaling by wnt [GO:0198738]; detection of mechanical ...
basolateral plasma membrane [GO:0016323]; calcium channel complex [GO:0034704]; cation channel complex [GO:0034703]; cell surface [GO:0009986]; cilium [GO:0005929]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; lateral plasma membrane [GO:0...
calcium channel activity [GO:0005262]; carbohydrate binding [GO:0030246]; monoatomic cation channel activity [GO:0005261]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; transcription regulator inhibitor activity [GO:0140416]; transmembrane transporter binding [GO:0044325]; Wnt recep...
PF00059;PF13855;PF00801;PF08016;PF01477;PF20519;PF02010;PF01822;
2.60.40.10;3.10.100.10;2.60.60.20;3.80.10.10;
Polycystin family
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P98161}.; PTM: After synthesis, undergoes autoproteolytic cleavage between Leu-3040 and Thr-3041 in the GPS region of the GAIN-B domain (PubMed:25405894). Cleavage at the GPS region occurs through a cis-autoproteolytic mechanism involving an ester-intermediate via N-O acyl re...
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P98161}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P98161}. Cell projection, cilium {ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:24939912, ECO:0000269|PubMed:25405894}. Endoplasmic reticulum {ECO:0000269|PubMed:25405894}. Golgi apparatus {ECO:00002...
null
null
null
null
null
FUNCTION: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Both PKD1 and PKD2 are required for channel activity (By similarity). Involved in renal tubulogenesis (PubMed:24939912). Involved in ...
Mus musculus (Mouse)
O08856
ELL_MOUSE
MAALKEARSYGLSCGRVSDGSRVSVFHVKLTDSALKAFESYRAHQDSVSLRPSIRFEGSQGHISIPQPDCPEEVRAFSFYLSNIGRDSPQGSFDCIQQYVSSYGDVHLDCLGSIQDKVTVCATDDSYQKARQSMAQAEEETRSRSAIVIKAGGRYMGKKVQFRKPAPGAADAVPSRKRATPINLASAIRKSSGSGASSVVQRPFRDRVLHLLALRPYRKAELLLRLQKDGLTQADKDTLDSLLQQVASVNPKDGTCTLQDCMYKSLQKDWPGYSEGDRQLLKRMLMRKLCQPQNATTDSSPPREHGRSASPSQKRPTDFI...
null
null
in utero embryonic development [GO:0001701]; positive regulation of transcription by RNA polymerase III [GO:0045945]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; snRNA transcription by RNA polymerase II [GO:0042795]; snRNA transcription by RNA polymerase III [GO:0042796]; transcri...
Cajal body [GO:0015030]; cytosol [GO:0005829]; euchromatin [GO:0000791]; histone locus body [GO:0035363]; nuclear speck [GO:0016607]; transcription elongation factor complex [GO:0008023]
cis-regulatory region sequence-specific DNA binding [GO:0000987]; phosphatase binding [GO:0019902]
PF10390;PF07303;
6.10.140.340;1.10.10.2670;
ELL/occludin family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55199}. Nucleus speckle {ECO:0000250|UniProtKB:P55199}. Nucleus, Cajal body {ECO:0000250|UniProtKB:P55199}. Note=Colocalizes with EAF2 to nuclear speckles. Colocalizes with coilin in subnuclear cajal and histone locus bodies. Translocates in the LEC complex to cajal...
null
null
null
null
null
FUNCTION: Elongation factor component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically required for stimulating the elongation step of RNA polymeras...
Mus musculus (Mouse)
O08858
SSR5_MOUSE
MEPLSLTSTPSWNASAASSSSHNWSLVDPVSPMGARAVLVPVLYLLVCTVGLGGNTLVIYVVLRYAKMKTVTNVYILNLAVADVLFMLGLPFLATQNAVSYWPFGSFLCRLVMTLDGINQFTSIFCLMVMSVDRYLAVVHPLRSARWRRPRVAKLASAAVWVFSLLMSLPLLVFADVQEGWGTCNLSWPEPVGLWGAAFITYTSVLGFFGPLLVICLCYLLIVVKVKAAGMRVGSSRRRRSERKVTRMVVVVVLVFVGCWLPFFIVNIVNLAFTLPEEPTSAGLYFFVVVLSYANSCANPLLYGFLSDNFRQSFRKALCL...
null
null
adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cellular response to glucocorticoid stimulus [GO:0071385]; glucose homeostasis [GO:0042593]; neuropeptide signaling pathway [GO:0007218]; regulation of insulin secretion [GO:0050796]
neuron projection [GO:0043005]; plasma membrane [GO:0005886]
neuropeptide binding [GO:0042923]; somatostatin receptor activity [GO:0004994]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Palmitoylated at Cys-319 by ZDHHC5, but not ZDHHC8. Palmitoylation creates an additional intracellular loop which is thought to be important for efficient coupling to G-proteins and may target the protein to lipid rafts. {ECO:0000269|PubMed:21820437}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21820437}; Multi-pass membrane protein {ECO:0000269|PubMed:21820437}.
null
null
null
null
null
FUNCTION: Receptor for somatostatin-28. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase. Increases cell growth inhibition activity of SSTR2 following heterodimerization.
Mus musculus (Mouse)
O08859
TSG6_MOUSE
MVVLLCLCVLLWEEAHGWGFKNGIFHNSIWLEQAAGVYHREARAGRYKLTYAEAKAVCEFEGGRLATYKQLEAARKIGFHVCAAGWMAKGRVGYPIVKPGPNCGFGKTGIIDYGIRLNRSERWDAYCYNPHAKECGGVFTDPKRIFKSPGFPNEYDDNQVCYWHIRLKYGQRIHLSFLDFDLEHDPGCLADYVEIYDSYDDVHGFVGRYCGDELPEDIISTGNVMTLKFLSDASVTAGGFQIKYVTVDPASKSSQAKNTSTTGNKKFLPGRFSHL
null
null
cell adhesion [GO:0007155]; fibronectin fibril organization [GO:1905590]; hyaluronan metabolic process [GO:0030212]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of inflammatory response [GO:0050728]; negative regulation of neutrophil chemotaxis [GO:0090024]; negative regulation of ost...
extracellular region [GO:0005576]; extracellular space [GO:0005615]
calcium ion binding [GO:0005509]; carboxylesterase activity [GO:0106435]; fibronectin binding [GO:0001968]; hyaluronic acid binding [GO:0005540]
PF00431;PF00193;
3.10.100.10;2.60.120.290;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P98066}.
null
null
null
null
null
FUNCTION: Major regulator of extracellular matrix organization during tissue remodeling (By similarity). Catalyzes the transfer of a heavy chain (HC) from inter-alpha-inhibitor (I-alpha-I) complex to hyaluronan. Cleaves the ester bond between the C-terminus of the HC and GalNAc residue of the chondroitin sulfate chain ...
Mus musculus (Mouse)
O08863
BIRC3_MOUSE
MVQDSAFLAKLMKSADTFELKYDFSCELYRLSTYSAFPRGVPVSERSLARAGFYYTGANDKVKCFCCGLMLDNWKQGDSPMEKHRKLYPSCNFVQTLNPANSLEASPRPSLPSTAMSTMPLSFASSENTGYFSGSYSSFPSDPVNFRANQDCPALSTSPYHFAMNTEKARLLTYETWPLSFLSPAKLAKAGFYYIGPGDRVACFACDGKLSNWERKDDAMSEHQRHFPSCPFLKDLGQSASRYTVSNLSMQTHAARIRTFSNWPSSALVHSQELASAGFYYTGHSDDVKCFCCDGGLRCWESGDDPWVEHAKWFPRCEYL...
2.3.2.27
null
apoptotic process [GO:0006915]; cellular response to tumor necrosis factor [GO:0071356]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of necroptotic process [GO:0060546]; negative regulation of phosphorylation [GO:0042326]; negative regulation of reactive ...
cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; ubiquitin protein ligase activity [GO:0061630]
PF00653;PF21290;PF00619;PF13920;
1.10.533.10;1.10.8.10;
IAP family
PTM: Auto-ubiquitinated and degraded by the proteasome in apoptotic cells. {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:18621737};
null
null
null
null
FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates bot...
Mus musculus (Mouse)
O08873
MADD_RAT
MVQKKFCPRLLDYLVIVGARHPSSDSVAQTPELLRRYPLEDHPEFPLPPDVVFFCQPEGCLSVRQRRMSLRDDTSFVFTLTDKDTGVTRYGICVNFYRSFQKRMPKEKAEGGAGPRGKEGAHAPCASEEAATESSESGSTLQPPSADSTPDVNQSPRGKRRAKAGNRSRNSTLTSLCVLSHYPFFSTFRECLYTLKRLVDCCSERLLGKKPGIPRGVQRDTMWRIFTGSLLVEEKSSALLHDLREIEAWIYRLLRSPVPVSGQKRVDIEVLPQEVQQALTFALPDPSRFTLVDFPLHLPLELLGVDACLQVLTCILLEHK...
null
null
anterograde synaptic vesicle transport [GO:0048490]; execution phase of apoptosis [GO:0097194]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of growth hormone secretion [GO:0060125]; negative regulation of pancreatic amylase secretion [GO:1902277]; positive regulation of MAPK cas...
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]
guanyl-nucleotide exchange factor activity [GO:0005085]
PF02141;PF03456;
3.30.450.200;3.40.50.11500;
MADD family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8WXG6}. Cytoplasm {ECO:0000250|UniProtKB:Q8WXG6}. Cell projection, axon {ECO:0000250|UniProtKB:Q80U28}.
null
null
null
null
null
FUNCTION: Guanyl-nucleotide exchange factor that regulates small GTPases of the Rab family (PubMed:9020086). Converts GDP-bound inactive form of RAB27A and RAB27B to the GTP-bound active forms (By similarity). Converts GDP-bound inactive form of RAB3A, RAB3C and RAB3D to the GTP-bound active forms, GTPases involved in ...
Rattus norvegicus (Rat)
O08874
PKN2_RAT
MASNPDRGEILLTELQVDSRPLPFSENVSAVQKLDFSDTIVQQKLDDVKDRIKREIRKELKIKEGAENLRKVTTDKKNLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDYTDCPRTPDTPNSDSRSSTSNNRRLMALQKQLDIELKVKQGAENMIQMYSNGPSKDRKLHGTAQQLLQDNKTKIEVIRMHILQAVLTNELAFDNAKPVISPLELRNGRIIEHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPKNHPKSSVVIEELSLVASPTLSPRQSMLSTQNQYS...
2.7.11.13
null
apical junction assembly [GO:0043297]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell projection organization [GO:0030030]; epithelial cell migration [GO:0010631]; intracellular signal transduction [GO:0035556]; positive regulation of cytokinesis [G...
apical junction complex [GO:0043296]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; lamellipodium [GO:0030027]; midbody [GO:0030496]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone deacetylase binding [GO:0042826]; kinase activity [GO:0016301]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA polymerase binding [GO:0070063]; small GTPase ...
PF02185;PF00069;PF00433;
1.10.287.160;1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily
PTM: Phosphorylated during mitosis (By similarity). Autophosphorylated. Phosphorylated. Binding to Rho and Rac promotes autophosphorylation and phosphorylation on serine and threonine residues. Phosphorylated by CDK10 (By similarity). {ECO:0000250|UniProtKB:Q16513, ECO:0000269|PubMed:9121475}.; PTM: Proteolytically cle...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16513}. Nucleus {ECO:0000250|UniProtKB:Q16513}. Membrane {ECO:0000250|UniProtKB:Q8BWW9}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q16513}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q16513}. Cleavage furrow {ECO:0000250|UniProtKB:Q16513}. Midbody ...
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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activati...
Rattus norvegicus (Rat)
O08875
DCLK1_RAT
MLELIEVNGTPGSQLSTPRSGKSPSPSPTSPGSLRKQRISQHGGSSTSLSSTKVCSSMDENDGPGEEESDEGFQIPATITERYKVGRTIGDGNFAVVKECIERSTAREYALKIIKKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDVPTELYLVMELVKGGDLFDAITSTSKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATIVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQVDFPSPYWDNVSDSAKELINMM...
2.7.11.1
null
axon extension [GO:0048675]; axonogenesis [GO:0007409]; brain development [GO:0007420]; central nervous system projection neuron axonogenesis [GO:0021952]; dendrite morphogenesis [GO:0048813]; forebrain development [GO:0030900]; negative regulation of protein localization to nucleus [GO:1900181]; neuron migration [GO:0...
axon [GO:0030424]; growth cone [GO:0030426]; postsynaptic density [GO:0014069]
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily
null
null
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: Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
O08876
KLF10_RAT
MLNFGASLQQASEGKMELISEKSKEGAHPWDKAEQSDFEAVEALMSMSCDWKSHFKKYLENRPVTPVSDTSEEDSLLPGTPDLQTVPAFCLTPPYSPSDFEPSQGSNLTAPAPPTGHFRSLSDAAKPPSIAPFKEEEKSPLAAPPLPKAQATSVIRHTADAQLCNHQSCPVKAASILNYQDNSFRRRTHINVEATRKNIPCAAVSPNRPKPEPSTAANGAEKAGTAPYDFAVPSSETVICRSSQPAPTSPVQKSVLMSSPTVSTGGVPPLPVICQMVPLPANNSLVTTVVPSSPPSQPPAVCSPVLFMGTQVPKGTVMFV...
null
null
bone mineralization [GO:0030282]; cellular response to peptide [GO:1901653]; cellular response to starvation [GO:0009267]; circadian rhythm [GO:0007623]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of transcription ...
nucleus [GO:0005634]
core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific D...
PF00096;
3.30.160.60;
Sp1 C2H2-type zinc-finger protein family
PTM: Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q13118}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20070857}.
null
null
null
null
null
FUNCTION: Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. Regulates the circadian expression of genes involved in lipogenesis, gluconeogenesis, and glycolysis in the liver. Represses the expression of PCK2, a rate-limiting step enzyme of gluconeogenesis. May play a role in the cell cycle r...
Rattus norvegicus (Rat)
O08878
GPER1_RAT
MAATTPAQDVGVEIYLGPVWPAPSNSTPLALNLSLALREDAPGNLTGDLSEHQQYVIALFLSCLYTIFLFPIGFVGNILILVVNISFREKMTIPDLYFINLAAADLILVADSLIEVFNLDEQYYDIAVLCTFMSLFLQINMYSSVFFLTWMSFDRYLALAKAMRCGLFRTKHHARLSCGLIWMASVSATLVPFTAVHLRHTEEACFCFADVREVQWLEVTLGFIVPFAIIGLCYSLIVRALIRAHRHRGLRPRRQKALRMIFAVVLVFFICWLPENVFISVHLLQWAQPGDTPCKQSFRHAYPLTGHIVNLAAFSNSCLS...
null
null
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; apoptotic chromosome condensation [GO:0030263]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to estradiol stimulus [GO:0071392]; cellular response to glucose stimulus [GO:0071333]; cellular response ...
axon [GO:0030424]; axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine head [GO:0044327]; dendritic spine membrane [GO:0032591]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endoplasmic re...
chromatin binding [GO:0003682]; estradiol binding [GO:1903924]; G protein-coupled estrogen receptor activity [GO:0038054]; nuclear estrogen receptor activity [GO:0030284]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Ubiquitinated; ubiquitination occurs at the plasma membrane and leads to proteasome-mediated degradation. {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:22919059}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:22919059}. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane; Multi-pass membrane protein. Bas...
null
null
null
null
null
FUNCTION: G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth f...
Rattus norvegicus (Rat)
O08888
PTSS2_CRIGR
MRRAERRVAGGSGSGSPLLEGRRSTESEVYDDGTNTFFWRAHTLTVLFILTCSLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRPHPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPRLGVPLPERDYGGNCLIYDADNKTDPFHNIWDKLDGFVPAHFIGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSECWWDHWIMDVLICNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFLLAELNTFYLKFVLWMPP...
2.7.8.29
null
phosphatidylserine biosynthetic process [GO:0006659]
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
L-serine-phosphatidylethanolamine phosphatidyltransferase activity [GO:0106245]
PF03034;
null
Phosphatidyl serine synthase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z1X2}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000269|PubMed:12912985}. Note=Highly enriched in the mitochondria-associated membrane (MAM). {ECO:0000250|UniProtKB:Q9Z1X2}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine; Xref=Rhea:RHEA:27606, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262, ChEBI:CHEBI:57603, ChEBI:CHEBI:64612; EC=2.7.8.29; Evidence={ECO:0000269|PubMed:12912985, ECO:0000269|PubMed:3084...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=89 uM for L-serine {ECO:0000269|PubMed:12912985}; Vmax=0.29 nmol/h/ng enzyme for L-serine {ECO:0000269|PubMed:12912985};
PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
null
null
FUNCTION: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine (PubMed:12912985, PubMed:9235902). Catalyzes the conversion of phosphatatidylethanolamine and does not act on phosphatidylcholine (PubMed:12912985, PubMed:92359...
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O08892
5HT1B_CAVPO
MGNPEASCTPPAVLGSQTGLPHANVSAPPNNCSAPSHIYQDSIALPWKVLLVVLLALITLATTLSNAFVIATVYRTRKLHTPANYLIASLAFTDLLVSILVMPISTMYTVTGRWTLGQALCDFWLSSDITCCTASIMHLCVIALDRYWAITDAVGYSAKRTPRRAAGMIALVWVFSICISLPPFFWRQAKAEEEVLDCLVNTDHVLYTVYSTGGAFYLPTLLLIALYGRIYVEARSRILKQTPNKTGKRLTRAQLITDSPGSTSSVTSINSRAPEVPCDSGSPVYVNQVKVRVSDALLEKKKLMAARERKATKTLGVILG...
null
null
adenylate cyclase-inhibiting serotonin receptor signaling pathway [GO:0007198]; behavior [GO:0007610]; bone remodeling [GO:0046849]; cellular response to alkaloid [GO:0071312]; cellular response to temperature stimulus [GO:0071502]; cellular response to xenobiotic stimulus [GO:0071466]; chemical synaptic transmission [...
dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; G protein-coupled serotonin receptor complex [GO:0098666]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; serotonergic synapse [GO:0099154]
G protein-coupled serotonin receptor activity [GO:0004993]; neurotransmitter receptor activity [GO:0030594]; serotonin binding [GO:0051378]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Phosphorylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9225276}; Multi-pass membrane protein {ECO:0000269|PubMed:9225276}.
null
null
null
null
null
FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various alkaloids and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream eff...
Cavia porcellus (Guinea pig)
O08900
IKZF3_MOUSE
MEDIQPTVELKSTEEQPLPTESPDALNDYSLPKPHEIENVDSREAPANEDEDAGEDSMKVKDEYSDRDENIMKPEPMGDAEESEMPYSYAREYSDYESIKLERHVPYDNSRPTGGKMNCDVCGLSCISFNVLMVHKRSHTGERPFQCNQCGASFTQKGNLLRHIKLHTGEKPFKCHLCNYACQRRDALTGHLRTHSVEKPYKCEFCGRSYKQRSSLEEHKERCRAFLQNPDLGDAASVEARHIKAEMGSERALVLDRLASNVAKRKSSMPQKFIGEKRHCFDANYNPGYMYEKENEMMQTRMMDQAINNAISYLGAEALR...
null
null
B cell differentiation [GO:0030183]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of apoptotic process [GO:0042981]; regulation of B cell differentiation [GO:0045577]; regulation of B cell proliferation [GO:0030888]; regulation of lymphocyte differentiation [GO:0045619]; regulation...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; protein heterodimerization activity [GO:0046982]; pro...
PF00096;
3.30.160.60;
Ikaros C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9155026}. Cytoplasm {ECO:0000269|PubMed:9155026}.
null
null
null
null
null
FUNCTION: Transcription factor that plays an important role in the regulation of lymphocyte differentiation. Binds to GGGAA. Plays an essential role in regulation of B-cell differentiation, proliferation and maturation to an effector state. Involved in regulating BCL2 expression and controlling apoptosis in T-cells in ...
Mus musculus (Mouse)
O08901
BUB1_MOUSE
MDNLENVFRMFEAHMQSYTGNDPLGEWESFIKWVEENFPDNKEYLMTLLEHLMKEFLHKKNYHNDSRFINYCLKFAEYNSDRHQFFEFLYNQGIGTKSSYIYMSWAGHLEAQGELQHASAIFQTGIHNEAEPKELLQQQYRLFQARLTGIHLPAQATTSEPLHSAQILNQVMMTNSSPEKNSACVPKSQGSECSGVASSTCDEKSNMEQRVIMISKSECSVSSSVAPKPEAQQVMYCKEKLIRGDSEFSFEELRAQKYNQRKKHEQWVSEDRNYMKRKEANAFEEQLLKQKMDELHKKLHQVVELSHKDLPASENRPDVS...
2.7.11.1
null
cell division [GO:0051301]; chromosome segregation [GO:0007059]; intrinsic apoptotic signaling pathway [GO:0097193]; meiotic sister chromatid cohesion, centromeric [GO:0051754]; mitotic spindle assembly checkpoint signaling [GO:0007094]; phosphorylation [GO:0016310]; positive regulation of intrinsic apoptotic signaling...
chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; kinetochore [GO:0000776]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]
ATP binding [GO:0005524]; histone H2A kinase activity [GO:0140995]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF08311;PF00069;
1.25.40.430;6.10.130.20;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, BUB1 subfamily
PTM: Upon spindle-assembly checkpoint activation it is hyperphosphorylated and its kinase activity toward CDC20 is stimulated. Phosphorylation at Thr-595 is required for interaction with PLK1, phosphorylation at this site probably creates a binding site for the POLO-box domain of PLK1, thus enhancing the PLK1-BUB1 inte...
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Nuclear in interphase cells. Accumulates gradually during G1 and S phase of the cell cycle, peaks at G2/M, and drops dramatically after mitosis. Localizes to the outer kinetochore. Kinetochore localization is required for normal mitotic timing and...
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 that performs 2 crucial functions during mitosis: it is essential for spindle-assembly checkpoint signaling and for correct chromosome alignment. Has a key role in the assembly of checkpoint proteins at the kinetochore, being required for the subsequent localization of CENPF, B...
Mus musculus (Mouse)
O08908
P85B_MOUSE
MAGAEGFQYRAVYPFRRERPEDLELLPGDLLVVSRVALQALGVADGGERCPHNVGWMPGFNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPLDGSSESGHILPDLAEQFSPPDPAPPILVKLVEAIEQAELDSECYSKPELPATRTDWSLSDLEQWDRTALYDAVKGFLLALPAAVVTPEAAAEAYRALREVAGPVGLVLEPPTLPLHQALTLRFLLQHLGRVARRAPSPDTAVHALASAFGPLLLRIPPSGGEGDGSEPVPDFPVLLLERLVQEHVEEQDAAPPALPPKPSKAKPAPTALANGGSPPSLQ...
null
null
cellular response to insulin stimulus [GO:0032869]; insulin receptor signaling pathway [GO:0008286]; intracellular glucose homeostasis [GO:0001678]; negative regulation of cell migration involved in sprouting angiogenesis [GO:0090051]; negative regulation of MAPK cascade [GO:0043409]; phosphatidylinositol 3-kinase/prot...
focal adhesion [GO:0005925]; nucleus [GO:0005634]; phosphatidylinositol 3-kinase complex [GO:0005942]; phosphatidylinositol 3-kinase complex, class IA [GO:0005943]
1-phosphatidylinositol-3-kinase regulator activity [GO:0046935]; phosphatidylinositol 3-kinase regulatory subunit binding [GO:0036312]; phosphotyrosine residue binding [GO:0001784]; protein heterodimerization activity [GO:0046982]; protein phosphatase binding [GO:0019903]; receptor tyrosine kinase binding [GO:0030971]
PF16454;PF00620;PF00017;
1.10.287.1490;1.10.555.10;3.30.505.10;2.30.30.40;
PI3K p85 subunit family
PTM: Phosphorylated in response to signaling from activated receptor-type protein kinases. Dephosphorylated by PTPRJ. Dephosphorylated at Tyr-649 by PTPN13. Phosphorylation of Tyr-649 impairs while its dephosphorylation promotes interaction with FBXL2 and SCF(FBXL2)-mediated polyubiquitination. {ECO:0000250|UniProtKB:O...
null
null
null
null
null
null
FUNCTION: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, a...
Mus musculus (Mouse)
O08911
MK12_MOUSE
MSSPPPARKGFYRQEVTKTAWEVRAVYQDLQPVGSGAYGAVCSAVDSRTGNKVAIKKLYRPFQSELFAKRAYRELRLLKHMRHENVIGLLDVFTPDESLDDFTDFYLVMPFMGTDLGKLMKHETLSEDRIQFLVYQMLKGLKYIHAAGVIHRDLKPGNLAVNEDCELKILDFGLARQADSEMTGYVVTRWYRAPEVILNWMRYTQTVDIWSVGCIMAEMITGKILFKGNDHLDQLKEIMKITGTPPPEFVQKLQSAEAKNYMEGLPELEKKDFASVLTNASPQAVNLLERMLVLDAEQRVTAAEALTHPYFESLRDTEDE...
2.7.11.24
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions.;
cell cycle [GO:0007049]; intracellular signal transduction [GO:0035556]; myoblast differentiation [GO:0045445]; negative regulation of cell cycle [GO:0045786]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
PTM: Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K3/MKK3 and MAP2K6/MKK6, which activates the enzyme. {ECO:0000269|PubMed:20004242}.; PTM: Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Mitochondrial when associated with SH3BP5. In skeletal muscle colocalizes with SNTA1 at the neuromuscular junction and throughout the sarcolemma. {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=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK12 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to di...
Mus musculus (Mouse)
O08912
GALT1_MOUSE
MRKFAYCKVVLATSLVWVLLDMFLLLYFSECNKCEEKQERGLPAGDVLELVQKPHEGPGEMGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSVVIVFHNEAWSTLLRTVHSVINRSPRHMIEEIVLVDDASERDFLKRPLESYVKKLKVPVHVIRMEQRSGLIRARLKGAAVSRGQVITFLDAHCECTAGWLEPLLARIKHDRRTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRDYFQEIGTYDAGMDIWGGEN...
2.4.1.41
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9153242};
protein O-linked glycosylation [GO:0006493]; protein O-linked glycosylation via serine [GO:0018242]; protein O-linked glycosylation via threonine [GO:0018243]
extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; perinuclear region of cytoplasm [GO:0048471]
carbohydrate binding [GO:0030246]; manganese ion binding [GO:0030145]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]
PF00535;PF00652;
2.80.10.50;
Glycosyltransferase 2 family, GalNAc-T subfamily
null
SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase 1]: Golgi apparatus, Golgi stack membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]: Secreted {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604, ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2...
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:10037781, ECO:0000269|PubMed:9153242}.
null
null
FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:10037781, PubMed:9153242). Has a broad spectrum of substrates such as apomucin-, MUC5AC-, MUC1- and MUC2-derived peptide...
Mus musculus (Mouse)
O08914
FAAH1_MOUSE
MVLSEVWTALSGLSGVCLACSLLSAAVVLRWTRSQTARGAVTRARQKQRAGLETMDKAVQRFRLQNPDLDSEALLALPLLQLVQKLQSGELSPEAVLFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHASTLGLSLNEGVTSESDCVVVQVLKLQGAVPFVHTNVPQSMLSYDCSNPLFGQTMNPWKPSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKSCVYGQTAVQLSVGPMARDVDSLALCMKALLCEDLFRLDSTIPPLPFREEIYR...
3.1.1.-; 3.5.1.99
null
fatty acid catabolic process [GO:0009062]; fatty acid metabolic process [GO:0006631]; monoacylglycerol catabolic process [GO:0052651]; positive regulation of vasoconstriction [GO:0045907]
endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; organelle membrane [GO:0031090]
acylglycerol lipase activity [GO:0047372]; amidase activity [GO:0004040]; fatty acid amide hydrolase activity [GO:0017064]; hydrolase activity, acting on ester bonds [GO:0016788]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; phospholipid binding [GO:0005543]
PF01425;
3.90.1300.10;
Amidase family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:32271712}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97612}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P97612}; Single-pass membrane protein {ECO:0000250|UniProtKB:P97612}. Note=Seems to be associated with the endoplasmic reticulu...
CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine; Xref=Rhea:RHEA:26136, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57603; EC=3.5.1.99; Evidence={ECO:0000269|PubMed:15533037, ECO:0000269|PubMed:32271712}; Physio...
null
null
null
null
FUNCTION: Catalyzes the hydrolysis of endogenous amidated lipids like the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides such as the taurine-conjugated fatty acids (a structural class of central nervous system (CNS) metabolites), to their corresponding fatty ...
Mus musculus (Mouse)
O08915
AIP_MOUSE
MADLIARLREDGIQKRVIQEGRGELPDFQDGTKATFHFRTLHSDNEGSVIDDSRTRGKPMELIVGKKFKLPVWETIVCTMREGEIAQFLCDIKHVVLYPLVAKSLRNIAEGKDPLEGQRHCCGIAQMHEHSSLGHADLDALQQNPQPLIFHIEMLKVESPGTYQQDPWAMTDEEKAKAVPVIHQEGNRLYREGQVKEAAAKYYDAIACLKNLQMKEQPGSPDWIQLDLQITPLLLNYCQCKLVAQEYYEVLDHCSSILNKYDDNVKAYFKRGKAHAAVWNAQEAQADFAKVLELDPALAPVVSRELRALETRIRQKDEED...
null
null
protein maturation by protein folding [GO:0022417]; protein targeting to mitochondrion [GO:0006626]; regulation of protein kinase A signaling [GO:0010738]; xenobiotic metabolic process [GO:0006805]
aryl hydrocarbon receptor complex [GO:0034751]; cytosol [GO:0005829]; membrane [GO:0016020]; plasma membrane [GO:0005886]
aryl hydrocarbon receptor binding [GO:0017162]; GAF domain binding [GO:0036004]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; transcription coregulator activity [GO:0003712]; unfolded protein binding [GO:0051082]
PF00254;
3.10.50.40;1.25.40.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm.
null
null
null
null
null
FUNCTION: May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.
Mus musculus (Mouse)
O08917
FLOT1_MOUSE
MFFTCGPNEAMVVSGFCRSPPVMVAGGRVFVLPCIQQIQRISLNTLTLNVKSEKVYTRHGVPISVTGIAQVKIQGQNKEMLAAACQMFLGKTEAEIAHIALETLEGHQRAIMAHMTVEEIYKDRQKFSEQVFKVASSDLVNMGISVVSYTLKDIHDDQDYLHSLGKARTAQVQKDARIGEAEAKRDAGIREAKAKQEKVSAQCLSEIEMAKAQRDYELKKATYDIEVNTRRAQADLAYQLQVAKTKQQIEEQRVQVQVVERAQQVAVQEQEIARREKELEARVRKPAEAERYRLERLAEAEKAQLIMQAEAEAESVRMRG...
null
null
axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cellular response to exogenous dsRNA [GO:0071360]; dsRNA transport [GO:0033227]; endocytosis [GO:0006897]; extracellular matrix disassembly [GO:0022617]; plasma membrane raft assembly [GO:0044854]; positive regulation of canonical NF-kappaB signal transduction [GO:...
adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; caveola [GO:0005901]; cell-cell contact zone [GO:0044291]; centriolar satellite [GO:0034451]; COP9 signalosome [GO:0008180]; cortical actin cytoskeleton [GO:0030864]; cytoplasmic vesicle [GO:0031410]; dopaminergic synapse [GO:0098691]; early endo...
ionotropic glutamate receptor binding [GO:0035255]; protease binding [GO:0002020]
PF01145;PF15975;
3.30.479.30;
Band 7/mec-2 family, Flotillin subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75955}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75955}. Endosome {ECO:0000250|UniProtKB:O75955}. Membrane, caveola {ECO:0000269|PubMed:9153235}; Peripheral membrane protein {ECO:0000269|PubMed:9153235}. Melanosome {ECO:0000250|UniProtKB:O75955}. Me...
null
null
null
null
null
FUNCTION: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Mus musculus (Mouse)
O08919
NUMBL_MOUSE
MSRSAAASGGPRRPDQHLSPAPCGASGPPETFRTESDGAGTMNKLRQSLRRRKPAYVPEASRPHQWQADEDAVRKGTCSFPVRYLGHVEVEESRGMHVCEDAVKKLKAMGRKSVKSVLWVSADGLRVVDDKTKDLLVDQTIEKVSFCAPDRNLDKAFSYICRDGTTRRWICHCFLALKDSGERLSHAVGCAFAACLERKQRREKECGVTAAFDASRTSFAREGSFRLSGGGRPAEREAGDKKKAEAAAAPAVAPGPAQPGHVSPTPATTSPGEKGEAGTPVAAGTTAAAIPRRHAPLEQLVRQGSFRGFPALSQKNSPFK...
null
null
adherens junction organization [GO:0034332]; axonogenesis [GO:0007409]; cytokine-mediated signaling pathway [GO:0019221]; forebrain development [GO:0030900]; lateral ventricle development [GO:0021670]; nervous system development [GO:0007399]; neuroblast division in subventricular zone [GO:0021849]; neuroblast prolifera...
cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]
null
PF06311;PF00640;
2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9169836}. Note=Symmetrically distributed throughout the cytoplasm in non dividing neuroblasts of the CNS.
null
null
null
null
null
FUNCTION: Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells befor...
Mus musculus (Mouse)
O08934
UNC4_MOUSE
MMDGRLLEHPHAQFGGSLGGVVGFPYPLGHHHVYELAGHQLQSAAAAAAAASVPFSIDGLLSGSCAAAAASVVNPTPLLPAACGVAGESQPFKLADSGDPDKESPGCKRRRTRTNFTGWQLEELEKAFNESHYPDVFMREALALRLDLVESRVQVWFQNRRAKWRKKENTKKGPGRPAHNSHPTTCSGEPMDPEEIARKELEKMEKKKRKHEKKLLKSQSRHLHSPGGLSLHSAPSSDSDSGGGGLSPEPPEPPPPTAAAKGPGAHGSGIAGSAPVPPGEPPAPGTCDPAFYPSQRSGAGSQPRLGRPADKDTVPCGPGA...
null
null
cartilage condensation [GO:0001502]; common myeloid progenitor cell proliferation [GO:0035726]; dorsal spinal cord development [GO:0021516]; olfactory bulb interneuron differentiation [GO:0021889]; pattern specification process [GO:0007389]; regulation of cell differentiation [GO:0045595]; regulation of gene expression...
nucleus [GO:0005634]
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific double-stranded DNA binding [GO:1990837]
PF00046;
1.10.10.60;
Paired homeobox family, Unc-4 subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: Transcription factor involved in somitogenesis and neurogenesis. Required for the maintenance and differentiation of particular elements of the axial skeleton. May act upstream of PAX9. Plays a role in controlling the development of connections of hypothalamic neurons to pituitary elements, allowing central n...
Mus musculus (Mouse)
O08949
TF2AA_RAT
MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLIQHMNASSITSAAATAATLALPAGVTPVQQILTNSGQLLQVVRAANGAQYIFQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPTPAQAQIPAAGQQQPQAQPAQQQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDD...
null
null
positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; transcription factor TFIIA complex [GO:0005672]; transcription factor TFIID complex [GO:0005669]; transcription preinitiation complex [GO:0097550]
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; RNA polymerase II core promoter sequence-specific DNA binding [GO:0000979]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; RNA polymerase II general transcription initiation factor binding [GO:0001091]; RNA pol...
PF03153;
1.10.287.100;2.30.18.10;
TFIIA subunit 1 family
PTM: The alpha and beta subunits are postranslationally produced from the precursor formby TASP1. The cleavage promotes proteasomal degradation (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
O08954
SNAI2_RAT
MPRSFLVKKHFNASKKPNYSELDTHTVIISPYLCESYPMPVIPKPEILTSGAYSPITVWTSAVPFHSPLPSGLSPLTGYSSSLGRVSPLPSSDTSSKDHSGSESPISDEEERLQPKLSDPHAIEAEKFQCNLCNKTYSTFSGLAKHKQLHCDAQARKSFSCKYCDKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH
null
null
cartilage morphogenesis [GO:0060536]; cell migration involved in endocardial cushion formation [GO:0003273]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to ionizing radiation [GO:0071479]; chromatin organizati...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific...
PF00096;
3.30.160.60;
Snail C2H2-type zinc-finger protein family
PTM: GSK3B-mediated phosphorylation results in cytoplasmic localization and degradation. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43623}. Cytoplasm {ECO:0000250}. Note=Observed in discrete foci in interphase nuclei. These nuclear foci do not overlap with the nucleoli, the SP100 and the HP1 heterochromatin or the coiled body, suggesting SNAI2 is associated with active transcription or active sp...
null
null
null
null
null
FUNCTION: Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial ...
Rattus norvegicus (Rat)
O08961
ZN423_RAT
MSRRKQAKPRSVKVEEGEASDFSLAWDSSVAAAGGLEGESECDRKSSRALEDRNSVTSQEERNEDDEDVEDESIYTCDHCQQDFESLADLTDHRAHRCPGDGDDDPQLSWVASSPSSKDVASPTQMIGDGCDLGLGEEEGGTGLPYPCQFCDKSFIRLSYLKRHEQIHSDKLPFKCTFCSRLFKHKRSRDRHIKLHTGDKKYHCHECEAAFSRRDHLKIHLKTHSSSKPFKCSVCKRGFSSTSSLQSHMQAHKKNKEHLAKSEKEAKKDDFMCDYCEDTFSQTEELEKHVLTLHPQLSEKADLQCIHCPEVFVDESTLLA...
null
null
brown fat cell differentiation [GO:0050873]; cerebellar granule cell precursor proliferation [GO:0021930]; cilium assembly [GO:0060271]; negative regulation of cold-induced thermogenesis [GO:0120163]; negative regulation of DNA-templated transcription [GO:0045892]; Notch signaling pathway [GO:0007219]; positive regulat...
chromosome [GO:0005694]; nucleus [GO:0005634]
chromatin insulator sequence binding [GO:0043035]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein-containing complex binding [GO:0044877]; sequence-specific DNA binding [GO:0043565]
PF00096;PF13912;
3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Transcription factor that can both act as an activator or a repressor depending on the context. Plays a central role in BMP signaling and olfactory neurogenesis. Associates with SMADs in response to BMP2 leading to activate transcription of BMP target genes. Acts as a transcriptional repressor via its interac...
Rattus norvegicus (Rat)
O08962
KCNH2_RAT
MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPSTSWLASGRAKTFRLKLPALLALTARESPMRTGSTGSPGAPGAVVVDVDLTPAAPSSESLALDEVSAMDNHVAGLGPAEERRALVGPASASPVASIPGPHPSPRAQSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGALPLPPRHASTGAMHPLRSGLLNS...
null
null
cardiac muscle contraction [GO:0060048]; cellular response to xenobiotic stimulus [GO:0071466]; membrane depolarization during action potential [GO:0086010]; membrane repolarization [GO:0086009]; membrane repolarization during action potential [GO:0086011]; membrane repolarization during cardiac muscle cell action pote...
cell surface [GO:0009986]; cytoplasm [GO:0005737]; inward rectifier potassium channel complex [GO:1902937]; nuclear envelope [GO:0005635]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
C3HC4-type RING finger domain binding [GO:0055131]; delayed rectifier potassium channel activity [GO:0005251]; identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242]; monoatomic ion channel activity [GO:0005216]; potassium channel activity [GO:0005267]; protein homodimerization...
PF00027;PF00520;PF13426;
1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20;
Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.1/KCNH2 sub-subfamily
PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (By similarity). {ECO:0000250|UniProtKB:Q12809}.
Rattus norvegicus (Rat)
O08966
S22A1_MOUSE
MPTVDDVLEHVGEFGWFQKQAFLLLCLISASLAPIYVGIVFLGFTPDHHCRSPGVAELSQRCGWSPAEELNYTVPGLGSAGEASFLSQCMKYEVDWNQSTLDCVDPLSSLAANRSHLPLSPCEHGWVYDTPGSSIVTEFNLVCGDAWKVDLFQSCVNLGFFLGSLVVGYIADRFGRKLCLLVTTLVTSLSGVLTAVAPDYTSMLLFRLLQGMVSKGSWVSGYTLITEFVGSGYRRTTAILYQVAFTVGLVGLAGVAYAIPDWRWLQLAVSLPTFLFLLYYWFVPESPRWLLSQKRTTQAVRIMEQIAQKNRKVPPADLKM...
null
null
(R)-carnitine transmembrane transport [GO:1902270]; acetylcholine transport [GO:0015870]; acyl carnitine transmembrane transport [GO:1902616]; cellular detoxification [GO:1990748]; dopamine transport [GO:0015872]; epinephrine transport [GO:0048241]; establishment or maintenance of transmembrane electrochemical gradient...
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]; presynapse [GO:0098793]
(R)-carnitine transmembrane transporter activity [GO:1901235]; acetylcholine transmembrane transporter activity [GO:0005277]; dopamine:sodium symporter activity [GO:0005330]; identical protein binding [GO:0042802]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter act...
PF00083;
1.20.1250.20;
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q63089}.
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:28942964}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:23680637}; Multi-pass membrane protein {ECO:0000305}. Lateral cell membrane {ECO:0000250|UniProtKB:O15245}; Multi-pass membrane protein {ECO:0000305}. Basal ...
CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000250|UniProtKB:Q63089}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:35469921}; CATALYTIC ACTIV...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=242 uM for adrenaline {ECO:0000269|PubMed:35469921}; KM=1286 uM for choline {ECO:0000269|PubMed:35469921}; KM=285 uM for dopamine {ECO:0000269|PubMed:35469921}; KM=497 uM for histamine {ECO:0000269|PubMed:35469921}; KM=1470 uM for O-isobutanoyl-(R)-carnitine {ECO:0...
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5 for TEA transport (PubMed:10216142). Optimum pH is 8.4 for MPP(+) transport (PubMed:12176030). {ECO:0000269|PubMed:10216142, ECO:0000269|PubMed:12176030};
null
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:10216142, PubMed:11463829, PubMed:12176030, PubMed:23458604, PubMed:24961373). Functions as a pH- and Na(+)-independent, bidirectio...
Mus musculus (Mouse)
O08967
CYH3_MOUSE
MDEGGGGEGGSVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVED...
null
null
establishment of epithelial cell polarity [GO:0090162]; Golgi vesicle transport [GO:0048193]; positive regulation of cell adhesion [GO:0045785]; regulation of ARF protein signal transduction [GO:0032012]
adherens junction [GO:0005912]; bicellular tight junction [GO:0005923]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; ruffle [GO:0001726]
guanyl-nucleotide exchange factor activity [GO:0005085]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:0005547]
PF00169;PF01369;
1.10.220.20;1.10.1000.11;2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18042453}; Peripheral membrane protein {ECO:0000269|PubMed:18042453}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Note=Translocates from the cytosol ...
null
null
null
null
null
FUNCTION: Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP (PubMed:18042453). Plays a role in the epithelial polarization (PubMed:20080746). {ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:20080746}.
Mus musculus (Mouse)
O08969
PHLA2_MOUSE
MASKIVMSSKTVKTSDEILCEGELEKRSDSLFQVWKKKRCVLTADRLRLFSGKTSPAKELFFHSILKVDCVEHTSKYVYFTIVTNYYKEIDFRCTVESCWNAAITMALIDFQNRRALQDFPRYRYQRSESEMPSEPGEQSALGP
null
null
animal organ morphogenesis [GO:0009887]; placenta development [GO:0001890]; positive regulation of apoptotic process [GO:0043065]; regulation of cell migration [GO:0030334]; regulation of embryonic development [GO:0045995]; regulation of gene expression [GO:0010468]; regulation of glycogen metabolic process [GO:0070873...
cytoplasm [GO:0005737]; membrane [GO:0016020]
phosphatidylinositol phosphate binding [GO:1901981]
null
2.30.29.30;
PHLDA2 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12374806}. Membrane {ECO:0000269|PubMed:12374806}; Peripheral membrane protein {ECO:0000269|PubMed:12374806}.
null
null
null
null
null
FUNCTION: Plays a role in regulating placenta growth. May act via its PH domain that competes with other PH domain-containing proteins, thereby preventing their binding to membrane lipids. {ECO:0000269|PubMed:12032310}.
Mus musculus (Mouse)
O08983
HPS1_MOUSE
MKCVLVATEGAEVLFYWTDEEFAESLRLKLQQSEDEEEELPVLEDQLSTLLAPVIISSMTMLEKLSDTYTCFSTENDNHLYVLHLFGEYLFVAINGDHSESEGDLRRKLCVLKYLFEVHFGLVTVDGQLIRKELRPPDLEERARVWKHFQRLLGTYSYLRDREQSFAVEAVERLIHPQLCEQSIETLERHVVQAINASPERGGEEVLHAFLLVHCKLLAFYSGHGASTLRPADLLALILLVQDLQPSPGTTEEEEEEEDSDSPQRRPKSSQNIPVQQARSQSTSVPTRSSRETDTDSISLPEEYFTPAPSPGDQSSGSLV...
null
null
blood coagulation [GO:0007596]; cell morphogenesis [GO:0000902]; eye pigmentation [GO:0048069]; gene expression [GO:0010467]; inflammatory response [GO:0006954]; intracellular transport [GO:0046907]; intracellular zinc ion homeostasis [GO:0006882]; lipid homeostasis [GO:0055088]; lipid metabolic process [GO:0006629]; l...
BLOC-3 complex [GO:0031085]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]
guanyl-nucleotide exchange factor activity [GO:0005085]
PF19036;PF19037;PF19038;
null
null
null
null
null
null
null
null
null
FUNCTION: Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and m...
Mus musculus (Mouse)
O08984
LBR_RAT
MPGRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKESDIKPLKSFKQRKSGSTSSSPSRRRSSRSRSRSRSRSPGRAPKGSRRSVSASYQADAKEKEMRREILQVKLTPLVLKPFANSVSVYNGEPEHMEKSATPPKNKQERVILSTEDSYIATQYSLRPRREEVKPKHRVRGTNLVTRGPVPLGTFQVTTPQRRDLEFGGVPGALLIMLGLPACVFLLLLQCAQKDPGLLQFPPPLPALRELWEARVCGVYLLWFFLQALFSLLPVGKVVEGTPLVDGRRLKYRLNGLYAFILTSAAVGTAVFW...
1.3.1.70
null
cholesterol biosynthetic process [GO:0006695]; ergosterol biosynthetic process [GO:0006696]; neutrophil differentiation [GO:0030223]
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleus [GO:0005634]
chromo shadow domain binding [GO:0070087]; delta14-sterol reductase activity [GO:0050613]; DNA binding [GO:0003677]; NADPH binding [GO:0070402]; nuclear localization sequence binding [GO:0008139]; protein-folding chaperone binding [GO:0051087]
PF01222;PF09465;
1.20.120.1630;2.30.30.140;
ERG4/ERG24 family
PTM: Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin (By similarity). It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures (By similarity). Phosphorylation of LB...
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:Q14739}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q14739}. Cytoplasm {ECO:0000250|UniProtKB:Q14739}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14739}. Note=Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q1473...
CATALYTIC ACTIVITY: Reaction=5alpha-cholest-8,14-dien-3beta-ol + H(+) + NADPH = 5alpha-cholest-8-en-3beta-ol + NADP(+); Xref=Rhea:RHEA:46456, ChEBI:CHEBI:15378, ChEBI:CHEBI:16608, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:86131; Evidence={ECO:0000250|UniProtKB:Q14739}; CATALYTIC ACTIVITY: Reaction=4,4-dimethyl-...
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PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
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FUNCTION: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (By similarity). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Medi...
Rattus norvegicus (Rat)
O08992
SDCB1_MOUSE
MSLYPSLEDLKVDKVIQAQTAYSANPASQAFVLVDASAALPPDGNLYPKLYPELSQYMGLSLNEAEICESMPMVSGAPAQGQLVARPSSVNYMVAPVTGNDAGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTVTMHKDSSGHVGFIFKSGKITSIVKDSSAARNGLLTDHHICEINGQNVIGLKDAQIADILSTAGTVVTITIMPTFIFEHIIKRMAPSIMKSLMDHTIPEV
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negative regulation of receptor internalization [GO:0002091]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell growth [GO:0030307]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulatio...
adherens junction [GO:0005912]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; interleukin-5 receptor complex [GO:0005895]; melanosome [GO:0042470]; membrane raft [GO:0045121]; nuclear...
cell adhesion molecule binding [GO:0050839]; ephrin receptor binding [GO:0046875]; frizzled binding [GO:0005109]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; interleukin-5 receptor binding [GO:0005137]; ionotropic glutamate receptor binding [GO:0035255]; neurexin family protein binding [...
PF00595;
2.30.42.10;
null
PTM: Phosphorylated on tyrosine residues. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250|UniProtKB:O00560}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O00560}. Cell membrane {ECO:0000250|UniProtKB:O00560}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00560}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00560}; Pe...
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FUNCTION: Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis. Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cel...
Mus musculus (Mouse)
O08999
LTBP2_MOUSE
MRAPTTARCSGCIQRVRWRGFLPLVLAVLMGTSHAQRDSIGRYEPASRDANRLWHPVGSHPAAAAAKVYSLFREPDAPVPGLSPSEWNQPAQGNPGWLAEAEARRPPRTQQLRRVQPPVQTRRSHPRGQQQIAARAAPSVARLETPQRPAAARRGRLTGRNVCGGQCCPGWTTSNSTNHCIKPVCQPPCQNRGSCSRPQVCICRSGFRGARCEEVIPEEEFDPQNARPVPRRSVERAPGPHRSSEARGSLVTRIQPLVPPPSPPPSRRLSQPWPLQQHSGPSRTVRRYPATGANGQLMSNALPSGLELRDSSPQAAHVNH...
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Golgi to vacuole transport [GO:0006896]; protein targeting to vacuole [GO:0006623]; supramolecular fiber organization [GO:0097435]
collagen-containing extracellular matrix [GO:0062023]; endosome [GO:0005768]; extracellular region [GO:0005576]; Golgi transport complex [GO:0017119]; membrane [GO:0016020]; trans-Golgi network [GO:0005802]
calcium ion binding [GO:0005509]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; microfibril binding [GO:0050436]
PF00008;PF07645;PF12661;PF00683;
2.10.25.10;3.90.290.10;
LTBP family
PTM: N-Glycosylated. {ECO:0000250|UniProtKB:Q14767}.; PTM: Contains hydroxylated asparagine residues. {ECO:0000250|UniProtKB:Q14766}.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q14767}.
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FUNCTION: May play an integral structural role in elastic-fiber architectural organization and/or assembly. {ECO:0000250|UniProtKB:Q14767}.
Mus musculus (Mouse)