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 |
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O88728 | IFM5_MOUSE | MDTSYPREDPRAPSSRKADAAAHTALSMGTPGPTPRDHMLWSVFSTMYLNLCCLGFLALVHSVKARDQKMAGNLEAARQYGSKAKCYNILAAMWTLVPPLLLLGLVVTGALHLSKLAKDSAAFFSTKFDEEDYN | null | null | bone mineralization [GO:0030282]; bone morphogenesis [GO:0060349]; in utero embryonic development [GO:0001701]; regulation of bone mineralization [GO:0030500] | cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886] | null | PF04505; | null | CD225/Dispanin family | PTM: Palmitoylated. {ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24715519}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:24715519}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:18442316}. | null | null | null | null | null | FUNCTION: Required for normal bone mineralization. {ECO:0000269|PubMed:18442316, ECO:0000269|PubMed:20838829, ECO:0000269|PubMed:24058703, ECO:0000269|PubMed:24715519}. | Mus musculus (Mouse) |
O88735 | MAP7_MOUSE | MAEQGAGGDGHRGGDGATHSDPASDGYKVQEKRTAPSRPTSTVSGQTSNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAARETVWLEREERARQHYERHLEARKKKLEDQRLKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPRQKSNRWSWGSPLHGSSSIHSGDPDRRSVSTMNLSKHVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVSRLLTPTHSFLARSKSTAALSGDTASCSPIIMPFKAAHSRNPVDRPKLFVTPPEGSARRRTIHGLASHKREREREHVPFHVSPGARRTLSPSNL... | null | null | cell morphogenesis [GO:0000902]; cell population proliferation [GO:0008283]; fertilization [GO:0009566]; germ cell development [GO:0007281]; glycosphingolipid metabolic process [GO:0006687]; homeostasis of number of cells [GO:0048872]; Leydig cell differentiation [GO:0033327]; microtubule bundle formation [GO:0001578];... | axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | signaling receptor binding [GO:0005102] | PF05672; | null | MAP7 family | PTM: The association with microtubules is regulated by phosphorylation during the cell cycle. During interphase only phosphorylated on serine. Phosphorylated on threonine in mitosis (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:14517216}. Basolateral cell membrane {ECO:0000269|PubMed:14517216}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14517216}. Note=Colocalized on microtubules. An intracellular redistribution is triggered during induction of keratinocyte terminal diff... | null | null | null | null | null | FUNCTION: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in ... | Mus musculus (Mouse) |
O88736 | DHB7_MOUSE | MRKVVLITGASSGIGLALCGRLLAEDDDLHLCLACRNLSKARAVRDTLLASHPSAEVSIVQMDVSSLQSVVRGAEEVKQKFQRLDYLYLNAGILPNPQFNLKAFFCGIFSRNVIHMFTTAEGILTQNDSVTADGLQEVFETNLFGHFILIRELEPLLCHADNPSQLIWTSSRNAKKANFSLEDIQHSKGPEPYSSSKYATDLLNVALNRNFNQKGLYSSVMCPGVVMTNMTYGILPPFIWTLLLPIMWLLRFFVNALTVTPYNGAEALVWLFHQKPESLNPLTKYASATSGFGTNYVTGQKMDIDEDTAEKFYEVLLELE... | 1.1.1.210; 1.1.1.270; 1.1.1.62 | null | androgen metabolic process [GO:0008209]; brain development [GO:0007420]; cell differentiation [GO:0030154]; cholesterol biosynthetic process [GO:0006695]; embryonic organ development [GO:0048568]; embryonic skeletal system development [GO:0048706]; estrogen biosynthetic process [GO:0006703]; nervous system development ... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | 3-keto sterol reductase activity [GO:0000253]; 5alpha-androstane-3beta,17beta-diol dehydrogenase activity [GO:0047024]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; prolactin receptor binding [GO:0005148] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family, ERG27 subfamily | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q62904}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12829805}; Single-pass membrane protein {ECO:0000255}. Note=Colocalizes with HMGCR in a wide range of tissues during embryonic development. {ECO:0000269|PubMed:12829805}. | CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62; Evidence={ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:9658408}; PhysiologicalDirection=right-to-left; Xr... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.28 uM for estrone {ECO:0000269|PubMed:9658408}; KM=12.87 uM for 17beta-estradiol {ECO:0000269|PubMed:9658408}; KM=1.19 uM for estrone {ECO:0000269|PubMed:12732193}; Vmax=556 pmol/min/mg enzyme with estrone as substrate {ECO:0000269|PubMed:9658408}; Vmax=616 pmol/... | PATHWAY: Steroid biosynthesis; estrogen biosynthesis. {ECO:0000269|PubMed:12732193, ECO:0000269|PubMed:9658408}.; PATHWAY: Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 5/6. {ECO:0000269|PubMed:12829805}. | null | null | FUNCTION: Bifunctional enzyme involved in steroid-hormone metabolism and cholesterol biosynthesis (PubMed:12732193, PubMed:12829805, PubMed:20659585, PubMed:9658408). Catalyzes the NADP(H)-dependent reduction of estrogens and androgens and regulates the biological potency of these steroids. Converts estrone (E1)to a mo... | Mus musculus (Mouse) |
O88737 | BSN_MOUSE | MGNEASLEGGAGEGPLPPGGSGLGPGPGAGKPPSALAGGGQLPVAGAARAAGPPTPGLGPVPGPGPGPGPGSVPRRLDPKEPLGSQRTTSPTPKQASATAPGRESPRETRAQGPSGQEAESPRRTLQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQIAPLPSSTLCPICKTSDLTSTPSQPNFNTCTQCHNKVCNQCGFNPNPHLTQVKEWLCLNCQMQRALGMDMTTAPRSKSQQQLHSPALSPAHSPAKQPLGKPEQERSPRGPGATQSGPRQAEAARATSVPGPTQATAPPEVGRVSPQPPLSTKPSTAEPRPPAG... | null | null | axo-dendritic transport [GO:0008088]; modulation of chemical synaptic transmission [GO:0050804]; presynapse to nucleus signaling pathway [GO:0099526]; presynaptic active zone assembly [GO:1904071]; protein localization to synapse [GO:0035418]; regulation of synaptic vesicle cycle [GO:0098693]; retrograde axonal transpo... | axon [GO:0030424]; axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cell surface [GO:0009986]; cochlear hair cell ribbon synapse [GO:0098683]; cytoskeleton of presynaptic active zone [GO:0048788]; cytosol [GO:0005829]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; extrinsic component of membrane [GO:001... | dynein light chain binding [GO:0045503]; enzyme inhibitor activity [GO:0004857]; metal ion binding [GO:0046872]; structural constituent of presynaptic active zone [GO:0098882]; transcription corepressor binding [GO:0001222] | PF05715; | 3.30.40.10; | null | PTM: Myristoylated. The N-terminal myristoylation is not sufficient for presynaptic localization (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88778}. Presynaptic active zone {ECO:0000269|PubMed:12628168, ECO:0000269|PubMed:12628169}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O88778}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:12628169}; Peripheral membrane... | null | null | null | null | null | FUNCTION: Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released (PubMed:12628168, PubMed:12628169, PubMed:19812333). After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transpo... | Mus musculus (Mouse) |
O88738 | BIRC6_MOUSE | MVTGCGAAPPGTVTERLPSVIVLSAGRKMAAAAAEASGPSCSSAAAAAGAGAAGVSEWLVLRDGCMRCDADGLHSLSYHPALNAILAVTSRGTIKVIDGTSGATLQASALSAKPGGQVKCQYISAVDKVIFVDDYAVGCRKDLNGILLLDTALQTPVSKQDDVVQLELPVTEAQQLLSACIEKIDVSSTEGYDLFITQLKDGLKNTSHETAANHKVAKWATVTFHLPHHVLKSIASAIVNELKKINQNVAALPVASSVMDRLSYLLPSARPELGVGPGRSVDRALMYSEANRRETFTSWPHVGYRWAQPDPMAQAGFYHQ... | 2.3.2.27 | null | apoptotic process [GO:0006915]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; labyrinthine layer development [GO:0060711]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; placenta develop... | centrosome [GO:0005813]; endosome [GO:0005768]; Flemming body [GO:0090543]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle pole [GO:0000922]; trans-Golgi network [GO:0005802] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; ubiquitin conjugating enzyme activity [GO:0061631] | PF00653;PF12356;PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: Ubiquitinated. Ubiquitination is mediated by the RNF41 E3 ligase and leads to proteasomal degradation, impairing inhibition of apoptosis. Deubiquitinated by USP8/UBPY (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9NR09}. Endosome {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9NR09}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9NR09}. Midbody, M... | 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:15300255}; | null | null | null | null | FUNCTION: Anti-apoptotic protein which can regulate cell death by controlling caspases and by acting as an E3 ubiquitin-protein ligase. Has an unusual ubiquitin conjugation system in that it could combine in a single polypeptide, ubiquitin conjugating (E2) with ubiquitin ligase (E3) activity, forming a chimeric E2/E3 u... | Mus musculus (Mouse) |
O88741 | GDAP1_MOUSE | MARRQDEARAGVPLRVEGPPDKEVHLILYHWTHSFSSQKVRLVIAEKALKCEEHDVSLPLSEHNEPWFMRLNSAGEVPVLVHGENIICEATQIIDYLEQTFLDERTPRLMPDEGSMYYPRVQHYRELLDSLPMDAYTHGCILHPELTVDSMIPAYATTRIRSQIGNTESELKKLAEENPDLQEAYIAKQKRLKSKLLDHDNVKYLKKILDELEKVLDQVETELQRRNEETPEEGNQPWLCGESFTLADVSLAVTLHRLKFLGFARRNWGHGKRPNLETYYERVLKRKTFNKVLGHVNNILISAVLPTAFRVAKKRAPKVL... | null | null | cellular response to vitamin D [GO:0071305]; mitochondrial fission [GO:0000266]; mitochondrial fusion [GO:0008053]; protein targeting to mitochondrion [GO:0006626]; response to retinoic acid [GO:0032526] | cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741] | null | PF13410;PF13417; | 1.20.1050.10;3.40.30.10; | GST superfamily | PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30. {ECO:0000250|UniProtKB:Q8TB36}. | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8TB36}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TB36}. Cytoplasm {ECO:0000269|PubMed:16172208}. | null | null | null | null | null | FUNCTION: Regulates the mitochondrial network by promoting mitochondrial fission. {ECO:0000250, ECO:0000269|PubMed:16172208}. | Mus musculus (Mouse) |
O88746 | TOM1_MOUSE | MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDAFRAVKKRIMGNKNFHEVMLALTVLETCVKNCGHRFHVLVANQDFVENVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVAVYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETPSRQNSVSSNTSQRGDLSQHATPLPTPAVLPGDSPITPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQVEPADLELLQELNRTCRAMQQRILELIPRISNEQLTEELLMINDNLNNVFLRHERFERFRTGQTAKASSEAELAT... | null | null | autophagosome-lysosome fusion [GO:0061909]; endosomal transport [GO:0016197]; positive regulation of autophagosome maturation [GO:1901098]; protein transport [GO:0015031]; regulation of endosome organization [GO:1904978]; signal transduction [GO:0007165]; substrate localization to autophagosome [GO:0061753] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; endosome membrane [GO:0010008]; membrane [GO:0016020] | clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; myosin VI binding [GO:0070853]; phosphatidylinositol-5-phosphate binding [GO:0010314]; polyubiquitin modification-dependent protein binding [GO:0031593]; ubiquitin binding [GO:0043130] | PF03127;PF00790; | 1.20.58.160;1.25.40.90; | TOM1 family | PTM: Monoubiquitinated. {ECO:0000250|UniProtKB:O60784}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25588840}. Endosome membrane {ECO:0000269|PubMed:25588840}; Peripheral membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000250|UniProtKB:O60784}; Peripheral membrane protein {ECO:0000305}. Note=Localized to endo/exosomal vesicles (PubMed:25588840). Enrich... | null | null | null | null | null | FUNCTION: Adapter protein that plays a role in the intracellular membrane trafficking of ubiquitinated proteins, thereby participating in autophagy, ubiquitination-dependent signaling and receptor recycling pathways (By similarity). Acts as a MYO6/Myosin VI adapter protein that targets MYO6 to endocytic structures (By ... | Mus musculus (Mouse) |
O88751 | CABP1_RAT | MSSHIAKSESKTSLLKAAAASGGSRAPRHSSARDPGLRGRRLPGPCPDSPATCGDPSSRRPLCRPVPRDEGARGSRRGLPQAHCRPRETLPPARGRDGEERGLAPALSLRGSLRSRGRGDPAPAGTPEADPFLHQLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR | null | null | modification of postsynaptic actin cytoskeleton [GO:0098885]; negative regulation of cell communication by electrical coupling [GO:0010651]; negative regulation of protein import into nucleus [GO:0042308]; postsynapse to nucleus signaling pathway [GO:0099527]; regulation of postsynapse to nucleus signaling pathway [GO:... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic density [GO:001406... | calcium channel regulator activity [GO:0005246]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; nuclear localization sequence binding [GO:0008139]; protein domain specific binding [GO:0019904]; transmembrane transporter binding [GO:0044325]; typ... | PF13499; | 1.10.238.10; | null | PTM: Phosphorylated. The phosphorylation regulates the activity (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15095872}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15095872}. Note=Occurs in both the cytoplasmic and cytoskeletal compartment of cell somata and dendrites. | null | null | null | null | null | FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs). Inhibits agonist-induced intracellular calcium signaling (By similarity). Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels (PubMed:11865310). Causes ca... | Rattus norvegicus (Rat) |
O88763 | PK3C3_RAT | MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKPFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGRAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFR... | 2.7.1.137 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8NEB9}; | autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; autophagy [GO:0006914]; cell cycle [GO:0007049]; cell division [GO:0051301]; cellular response to glucose starvation [GO:0042149]; cellular response to starvation [GO:0009267]; early endosome to late endosome transport [GO:0045022]; endocytosis... | autolysosome [GO:0044754]; autophagosome [GO:0005776]; axoneme [GO:0005930]; cytoplasm [GO:0005737]; endosome [GO:0005768]; late endosome [GO:0005770]; membrane [GO:0016020]; midbody [GO:0030496]; peroxisome [GO:0005777]; phagocytic vesicle [GO:0045335]; phagophore assembly site [GO:0000407]; phosphatidylinositol 3-kin... | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; ATP binding [GO:0005524]; kinase activity [GO:0016301]; phosphatidylinositol kinase activity [GO:0052742]; protein kinase activity [GO:0004672] | PF00454;PF00792;PF00613; | 2.60.40.150;1.10.1070.11;1.25.40.70; | PI3/PI4-kinase family | PTM: Ubiquitinated via 'Lys-29'- and 'Lys-48'-linked ubiquitination by UBE3C, promoting its degradation. Deubiquitination by ZRANB1/TRABID promotes its stabilization, leading to autophagosome maturation. {ECO:0000250|UniProtKB:Q8NEB9}. | SUBCELLULAR LOCATION: Midbody {ECO:0000250|UniProtKB:Q8NEB9}. Late endosome {ECO:0000250|UniProtKB:Q8NEB9}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q8NEB9}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216; EC=2.7.1.137; Evidence={ECO:0000250... | null | null | null | null | FUNCTION: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis.... | Rattus norvegicus (Rat) |
O88764 | DAPK3_RAT | MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERF... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:9840928}; | apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; cellular response to type II interferon [GO:0071346]; chromatin organization [GO:0006325]; intracellular signal transduction [GO:0035556]; negative regulation of translation [GO:0017148]; neuron differentiation [GO:0030182]; positive regulation o... | actin filament [GO:0005884]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; membrane raft [GO:0045121]; microtubule organizing center [GO:0005815]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; identical protein binding [GO:0042802]; kinase activity [GO:0016301]; leucine zipper domain binding [GO:0043522]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase ... | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily | PTM: Ubiquitinated. Ubiquitination mediated by the UBE2D3 E3 ligase does not lead to proteasomal degradation, but influences promyelocytic leukemia protein nuclear bodies (PML-NBs) formation in the nucleus (By similarity). {ECO:0000250|UniProtKB:O54784}.; PTM: The phosphorylation status is critical for kinase activity,... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10602474, ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9840928}. Nucleus, PML body {ECO:0000269|PubMed:10602474}. Cytoplasm {ECO:0000303|PubMed:10602480}. Cytoplasm, cytoskeleton, microtubule organizing center... | 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:10602480, ECO:000026... | null | null | null | null | FUNCTION: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involve... | Rattus norvegicus (Rat) |
O88766 | MMP8_RAT | MLHLKTLPFLFFFHTQLATALPVPPEHLEEKNMKTAENYLRKFYHLPSNQFRSARNATMIAEKLKEMQRFFGLPETGKPDAATIEIMEKPRCGVPDSGDFLLTPGSPKWTHTNLTYRIINHTPQMSKAEVKTEIEKAFKIWSVPSTLTFTETLEGEADINIAFVSRDHGDNSPFDGPNGILAHAFQPGRGIGGDAHFDSEETWTQDSKNYNLFLVAAHEFGHSLGLSHSTDPGALMYPNYAYREPSTYSLPQDDINGIQTIYGPSDNPVQPTGPSTPTACDPHLRFDAATTLRGEIYFFKDKYFWRRHPQLRTVDLNFIS... | 3.4.24.34 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; | cellular response to lipopolysaccharide [GO:0071222]; collagen catabolic process [GO:0030574]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; ossification [GO:0001503]; positive regulation of microglial cell activation [GO:1903980]; positive regulation of neuroinflammatory... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; tumor necrosis factor binding [GO:0043120]; zinc ion binding [GO:0008270] | PF00045;PF00413;PF01471; | 3.40.390.10;2.110.10.10; | Peptidase M10A family | null | SUBCELLULAR LOCATION: Cytoplasmic granule. Secreted, extracellular space, extracellular matrix {ECO:0000250}. Note=Stored in intracellular granules. | CATALYTIC ACTIVITY: Reaction=Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.; EC=3.4.24.34; | null | null | null | null | FUNCTION: Can degrade fibrillar type I, II, and III collagens. | Rattus norvegicus (Rat) |
O88767 | PARK7_RAT | MASKRALVILAKGAEEMETVIPVDIMRRAGIKVTVAGLAGKDPVQCSRDVVICPDTSLEEAKTQGPYDVVVLPGGNLGAQNLSESALVKEILKEQENRKGLIAAICAGPTALLAHEVGFGCKVTSHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALSGKDMANQVKAPLVLKD | 3.1.2.-; 3.5.1.-; 3.5.1.124 | COFACTOR: Note=Deglycase activity does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate. {ECO:0000250|UniProtKB:Q99497}; | adult locomotory behavior [GO:0008344]; autophagy [GO:0006914]; cellular detoxification of aldehyde [GO:0110095]; cellular detoxification of methylglyoxal [GO:0140041]; cellular response to glyoxal [GO:0036471]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; cellular res... | axon [GO:0030424]; cell body [GO:0044297]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; membrane raft [GO:0045121]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:000573... | copper ion binding [GO:0005507]; cupric ion binding [GO:1903135]; cuprous ion binding [GO:1903136]; cytokine binding [GO:0019955]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; glyoxalase (glycolic acid-forming) activity [GO:1990422]; identical protein binding [GO:0042802]; kinase ... | PF01965; | 3.40.50.880; | Peptidase C56 family | PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity. {ECO:0000250|UniProtKB:Q99497}.; PTM: Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress. {ECO:0000250|UniProtKB:Q99497}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99LX0}; Lipid-anchor {ECO:0000250|UniProtKB:Q99LX0}. Cytoplasm {ECO:0000269|PubMed:10022524}. Membrane raft {ECO:0000269|PubMed:23847046}. Nucleus {ECO:0000269|PubMed:10022524}. Mitochondrion {ECO:0000269|PubMed:31536960}. Endoplasmic reticulum {ECO:0000269|Pu... | CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] = H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965, ChEBI:CHEBI:131708; EC=3.5.1.124; Evidence={ECO:00... | null | null | null | null | FUNCTION: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired prote... | Rattus norvegicus (Rat) |
O88775 | EMB_RAT | MRSHTGLRALVAPGCSLLLLYLLAATRPDRAVGDPADSAFTSLPVREEMMAKYANLSLETYNISLTEQTRVSEQNITLERPSHLELECTFTATEDVMSMNVTWKKDDALLETTDGFNTTKMGDTLYSQYRFTVFNSKQMGKYSCFLGEELRGTFNIRVPKVHGKNKPLITYVGDSTVLKCECQNCLPLNWTWYMSNGTAQVPIDVHVNDKFDINGSYANETKLKVKHLLEEDGGSYWCRAAFPLGESEEHIKLVVLSFMVPLKPFLAIIAEVILLVAIILLCEVYTQKKKNDPDDGKEFEQIEQLKSDDSNGIENNVPRY... | null | null | axon guidance [GO:0007411]; cell adhesion [GO:0007155]; dendrite self-avoidance [GO:0070593]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; plasma membrane lactate transport [GO:0035879] | axon [GO:0030424]; plasma membrane [GO:0005886]; synapse [GO:0045202] | cell-cell adhesion mediator activity [GO:0098632] | PF07679; | 2.60.40.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:9169423}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20695846, ECO:0000269|PubMed:9169423}; Single-pass type I membrane protein {ECO:0000305|PubMed:19473976, ECO:0000305|PubMed:9169423}. Synapse {ECO:0000250|UniProtKB:P21995}. Note=Localizes to the neuromuscular junctions. {ECO:0000250|UniProtKB:P21995}. | null | null | null | null | null | FUNCTION: Plays a role in the outgrowth of motoneurons and in the formation of neuromuscular junctions. Following muscle denervation, promotes nerve terminal sprouting and the formation of additional acetylcholine receptor clusters at synaptic sites without affecting terminal Schwann cell number or morphology. Delays t... | Rattus norvegicus (Rat) |
O88777 | PSN2_RAT | MLTFMASDSEEEVCDERTSLMSAESPTSRSCQDSRPGPEDGENTAQWRSQENEDDCEEDPDHYACSGVPGRPSGLEEELTLKYGAKHVIMLFVPVTLCMIVVVATIKSVRFYTEKNGQLIYTPFTEDTPSVGQRLLNSVLNTLIMISVIVVMTIFLVVLYKYRCYKFIHGWLIMSSLMLLFLFTYIYLGEVFKTYNVAMDYPTLFLAVWNFGAVGMVCIHWKGPLVLQQAYLIVISALMALVFIKYLPEWSAWVILGAISVYDLVAVLCPKGPLRMLVETAQERNEPIFPALIYSSAMVWTVGMAKLDPSSQGALQLPYD... | 3.4.23.- | null | amyloid precursor protein catabolic process [GO:0042987]; amyloid-beta formation [GO:0034205]; amyloid-beta metabolic process [GO:0050435]; apoptotic signaling pathway [GO:0097190]; brain morphogenesis [GO:0048854]; calcium ion transport [GO:0006816]; cardiac muscle contraction [GO:0060048]; cell fate specification [GO... | apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; ciliary rootlet [GO:0035253]; cytosol [GO:0005829]; dendritic shaft [GO:0043198]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum mem... | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175] | PF01080; | 1.10.472.100; | Peptidase A22A family | PTM: Phosphorylated on serine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. Ma... | Rattus norvegicus (Rat) |
O88778 | BSN_RAT | MGNEASLEGGAGEGPLPPGGSGLGPGPGAGKPPSALAGGGQLPVAGAARAAGPPTPGLGLVPGPGPGPGPGSVSRRLDPKEPLGSQRATSPTPKQASATAPGRESPRETRAQGLSGQEAEGPRRTLQVDSRTQRSGRSPSVSPDRGSTPTSPYSVPQIAPLPSSTLCPICKTSDLTSTSSQPNFNTCTQCHNKVCNQCGFNPNPHLTQVKEWLCLNCQMQRALGMDMTTAPRSKSQQQLHSPALSPAHSPAKQPLGKPEQERSRSPGATQSGPRQAEAARATSVPGPTQATAPPEVGRVSPQPPLSTKPSTAEPRPPAGE... | null | null | axo-dendritic transport [GO:0008088]; cytoskeleton organization [GO:0007010]; maintenance of presynaptic active zone structure [GO:0048790]; modulation of chemical synaptic transmission [GO:0050804]; presynapse to nucleus signaling pathway [GO:0099526]; presynaptic active zone assembly [GO:1904071]; protein localizatio... | axon [GO:0030424]; axon cytoplasm [GO:1904115]; cell cortex [GO:0005938]; cell surface [GO:0009986]; cochlear hair cell ribbon synapse [GO:0098683]; cytoskeleton of presynaptic active zone [GO:0048788]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:00... | dynein light chain binding [GO:0045503]; enzyme inhibitor activity [GO:0004857]; metal ion binding [GO:0046872]; structural constituent of presynaptic active zone [GO:0098882]; transcription corepressor binding [GO:0001222] | PF05715; | 3.30.40.10; | null | PTM: Myristoylated. The N-terminal myristoylation is not sufficient for presynaptic localization. {ECO:0000269|PubMed:12812759}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10564375}. Presynaptic active zone {ECO:0000269|PubMed:10564375, ECO:0000269|PubMed:12812759, ECO:0000269|PubMed:26212709}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10564375}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:262... | null | null | null | null | null | FUNCTION: Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released (PubMed:22875941). After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transp... | Rattus norvegicus (Rat) |
O88780 | KLK8_RAT | MGRPPPCAIQTWILLFLLMGAWAGLTRAQGSKILEGQECKPHSQPWQTALFQGERLVCGGVLVGDRWVLTAAHCKKDKYSVRLGDHSLQKRDEPEQEIQVARSIQHPCFNSSNPEDHSHDIMLIRLQNSANLGDKVKPIELANLCPKVGQKCIISGWGTVTSPQENFPNTLNCAEVKIYSQNKCERAYPGKITEGMVCAGSSNGADTCQGDSGGPLVCNGVLQGITTWGSDPCGKPEKPGVYTKICRYTNWIKKTMGKRD | 3.4.21.118 | null | keratinocyte proliferation [GO:0043616]; memory [GO:0007613]; neuron projection morphogenesis [GO:0048812]; proteolysis [GO:0006508]; regulation of synapse organization [GO:0050807]; response to wounding [GO:0009611]; synapse organization [GO:0050808] | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; secretory granule [GO:0030141]; serine protease inhibitor complex [GO:0097180] | peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shows a cytoplasmic distribution in the keratinocytes. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys.; EC=3.4.21.118; | null | null | null | null | FUNCTION: Serine protease which is capable of degrading a number of proteins such as casein, fibrinogen, kininogen, fibronectin and collagen type IV. Also cleaves L1CAM in response to increased neural activity. Induces neurite outgrowth and fasciculation of cultured hippocampal neurons. Plays a role in the formation an... | Rattus norvegicus (Rat) |
O88783 | FA5_MOUSE | MLLVCPCFFLLVVLGTRWAGWGSHQAEAAQLRQFYVAAQGILWNYHPEPTDPSLNSIPSFKKIVYREYEQYFKKEKPRSSNSGLLGPTLYAEVGDVIKVHFRNKADKPLSIHPQGIKYSKFSEGASYADHTFPAERKDDAVAPGEEYTYEWIVSEDSGPTPDDPPCLTHIYYSYENLTQDFNSGLIGPLLICKKGTLTEDGTQKMFDKQHVLLFAVFDESKSRSQSPSLMYTINGFVNKTMPDITVCAHDHVSWHLIGMSSGPELFSIHFNGQVLEQNQHKVSTVTLVSATSTTANMTMSPEGRWIVSSLIPKHYQAGMQ... | null | null | blood circulation [GO:0008015]; blood coagulation [GO:0007596]; response to vitamin K [GO:0032571] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule [GO:0031091] | copper ion binding [GO:0005507]; signaling receptor activity [GO:0038023] | PF07732;PF00754; | 2.60.40.420;2.60.120.260; | Multicopper oxidase family | PTM: Thrombin activates factor V proteolytically to the active cofactor, factor Va (formation of a heavy chain at the N-terminus and a light chain at the C-terminus). {ECO:0000250}.; PTM: Sulfation is required for efficient thrombin cleavage and activation and for full procoagulant activity. {ECO:0000250}.; PTM: Activa... | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin. | Mus musculus (Mouse) |
O88786 | I13R2_MOUSE | MAFVHIRCLCFILLCTITGYSLEIKVNPPQDFEILDPGLLGYLYLQWKPPVVIEKFKGCTLEYELKYRNVDSDSWKTIITRNLIYKDGFDLNKGIEGKIRTHLSEHCTNGSEVQSPWIEASYGISDEGSLETKIQDMKCIYYNWQYLVCSWKPGKTVYSDTNYTMFFWYEGLDHALQCADYLQHDEKNVGCKLSNLDSSDYKDFFICVNGSSKLEPIRSSYTVFQLQNIVKPLPPEFLHISVENSIDIRMKWSTPGGPIPPRCYTYEIVIREDDISWESATDKNDMKLKRRANESEDLCFFVRCKVNIYCADDGIWSEWS... | null | null | cytokine-mediated signaling pathway [GO:0019221]; immunoglobulin mediated immune response [GO:0016064]; negative regulation of immunoglobulin production [GO:0002638]; negative regulation of mast cell degranulation [GO:0043305] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; receptor complex [GO:0043235] | cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896] | PF09240; | 2.60.40.10; | Type I cytokine receptor family, Type 5 subfamily | null | SUBCELLULAR LOCATION: [Isoform 1]: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted. | null | null | null | null | null | FUNCTION: Binds as a monomer with high affinity to interleukin-13 (IL13). {ECO:0000269|PubMed:9725226}. | Mus musculus (Mouse) |
O88792 | JAM1_MOUSE | MGTEGKAGRKLLFLFTSMILGSLVQGKGSVYTAQSDVQVPENESIKLTCTYSGFSSPRVEWKFVQGSTTALVCYNSQITAPYADRVTFSSSGITFSSVTRKDNGEYTCMVSEEGGQNYGEVSIHLTVLVPPSKPTISVPSSVTIGNRAVLTCSEHDGSPPSEYSWFKDGISMLTADAKKTRAFMNSSFTIDPKSGDLIFDPVTAFDSGEYYCQAQNGYGTAMRSEAAHMDAVELNVGGIVAAVLVTLILLGLLIFGVWFAYSRGYFERTKKGTAPGKKVIYSQPSTRSEGEFKQTSSFLV | null | null | actomyosin structure organization [GO:0031032]; cell adhesion [GO:0007155]; cellular response to mechanical stimulus [GO:0071260]; epithelial cell differentiation [GO:0030855]; establishment of endothelial intestinal barrier [GO:0090557]; intestinal absorption [GO:0050892]; leukocyte cell-cell adhesion [GO:0007159]; me... | bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; slit diaphragm [GO:0036057] | integrin binding [GO:0005178]; PDZ domain binding [GO:0030165]; protein homodimerization activity [GO:0042803] | PF13927;PF07686; | 2.60.40.10; | Immunoglobulin superfamily | null | SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:11036763}. Cell membrane {ECO:0000269|PubMed:11036763}; Single-pass type I membrane protein {ECO:0000269|PubMed:11036763}. Note=Localized at tight junctions of both epithelial and endothelial cells. | null | null | null | null | null | FUNCTION: Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3 (PubMed:11447115). The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (PubMed:11447115). Plays ... | Mus musculus (Mouse) |
O88797 | DAB2_RAT | MSNEVETSTTNGQPDQQAAPKAPSKKEKKKGSEKTDEYLLARFKGDGVKYKAKLIGIDDVPDARGDKMSQDSMMKLKGMAAAGRSQGQHKQRIWVNISLSGIKIIDEKTGVIEHEHPVNKISFIARDVTDNRAFGYVCGGEGQHQFFAIKTGQQAEPLVVDLKDLFQVIYNVKKKEEEKKKVEEANKAEENGSEALMTLDDQANKLKLGVDQMDLFGDMSTPPDLNNPTESRDILLVDLNSEIDTNQNSLRENPFLTNGVTSCSLPRPKPQASFLPESAFSANLNFFPTPNPDPFRDDPFAQPDQSAPSSFHSLTSADQK... | null | null | cell morphogenesis [GO:0000902]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to transforming growth factor beta stimulus [GO:0071560]; clathrin coat assembly [GO:0048268]; extrinsic apoptotic signaling pathway [GO:0097191]; hematopoietic stem cell proliferation [GO:0071425]; in... | apical plasma membrane [GO:0016324]; clathrin coat of coated pit [GO:0030132]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; clathrin-coated vesicle membrane [GO:0030665]; cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear ... | AP-2 adaptor complex binding [GO:0035612]; cargo receptor activity [GO:0038024]; clathrin adaptor activity [GO:0035615]; clathrin binding [GO:0030276]; integrin binding [GO:0005178]; low-density lipoprotein particle receptor binding [GO:0050750]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-4,5-bisph... | PF21792;PF00640; | 2.30.29.30; | null | PTM: Phosphorylated. Phosphorylation during mitosis is leading to membrane displacement. There is some ambiguity for the mitotic phosphosite Ser-326/328. {ECO:0000269|PubMed:21097498}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane, clathrin-coated pit. Note=Colocalizes with large insert-containing isoforms of MYO6 at clathrin-coated pits/vesicles. During mitosis is progressively displaced from the membrane and translocated to the cytopl... | null | null | null | null | null | FUNCTION: Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY... | Rattus norvegicus (Rat) |
O88799 | ZAN_MOUSE | MALPVWTLMLLVGAAWGQEQVPAWRPNSPDLGPMVHTSREDSILSKCDFEDNSRPFCDWSQMSADDGDWIRTTGPSLTGTSGPPGGYPNGEGYYLHMDPKTFPQGGVARLRSPDIWEQGPLCVHFAFHMFGLSWGAQLRLLLLRGRKHLRPYVLWKHVNTQSPSWMPTTVTVPADHDIPSWLMFEGMRGNTAYLDISLDGLSIQRGTCNQVCMSQMCTFDTLNDLCGWSWVPTATGAKWTQKKGPTGKQGVGPAEDFSNPGNGYYMLLDSTNARPGQKAVLLSPLSHSRGCMTLSFHYIMHGQGHEEGLFVYATFLGNIR... | null | null | binding of sperm to zona pellucida [GO:0007339]; cell adhesion [GO:0007155]; regulation of binding of sperm to zona pellucida [GO:2000359] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | extracellular matrix binding [GO:0050840] | PF00629;PF01826;PF12714;PF00094; | 2.60.120.200;2.10.70.10;2.10.25.10; | null | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=Exclusively on the apical region of the sperm head. | null | null | null | null | null | FUNCTION: Binds in a species-specific manner to the zona pellucida of the egg. May be involved in gamete recognition and/or signaling. | Mus musculus (Mouse) |
O88801 | HOME2_RAT | MGEQPIFTTRAHVFQIDPSTKKNWVPASKQAVTVSYFYDVTRNSYRIISVDGAKVIINSTITPNMTFTKTSQKFGQWADSRANTVFGLGFSSEQQLTKFAEKFQEVREAARLARDKSQEKIETSSNHSQESGCETPSSTQASSVNGTDDEKASHASPADTHLKSENDKLKIALTQSAANVKKWEIELQTLRESNARLTTALQESAASVEQWKRQFSICRDENDRLRSKIEELEEQCGEINREKEKNTQLKRRIEELESEVREKEMELKDLRKQSEIIPQLMSECEYVSEKLEAAERDNQNLEDKVRSLKTDIEESKYRQR... | null | null | behavioral response to cocaine [GO:0048148]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; G protein-coupled glutamate receptor signaling pathway [GO:0007216]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of interleukin-2 production [GO:003270... | apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; intracellular organelle [GO:0043229]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; stereocilium tip [GO:0032426] | actin binding [GO:0003779]; G protein-coupled glutamate receptor binding [GO:0035256]; glutamate receptor binding [GO:0035254]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877]; synaptic receptor adaptor activity [GO:0030160] | PF00568; | 1.20.5.1700;2.30.29.30; | Homer family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17584991}. Cell membrane {ECO:0000269|PubMed:17584991}. Postsynaptic density. Synapse. Cell projection, stereocilium {ECO:0000250|UniProtKB:Q9QWW1}. Note=Postsynaptic density of neuronal cells. The stabilization and clustering of the metabotropic glutamate receptors a... | null | null | null | null | null | FUNCTION: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM... | Rattus norvegicus (Rat) |
O88807 | PADI4_RAT | MAQGAVIHVAPEEPTHAVCVVGTATPLDIRGSAPRGSTSFSITASPEVVVDVIHGPPSKKSTTGASKWPLDPKLEVTLQMKAASSRIDDQKVRISYYGPKTSSTQALLYLTGVELSLSADVTRTGKAKPAPAGKDQSTWTWGPDGHGAILLVNCDKEDPKSSGMDFEDDKVLDNKDLQDMSPMTLSTKTPKDFFDKYQLVLQVPKAKMNKVRVFRATRGKLPSRYKVVLGPQQFSHRLELLGGQHSTDFYVEGLAFPDADFKGLIPLTISLLDKSNPELPEALVFQDTVMFRVAPWIMTPNTQPPQEVYVCRFSDNEDFL... | 3.5.3.15 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q9UM07}; Note=Binds 5 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9UM07}; | chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; innate immune response [GO:0045087]; nucleosome assembly [GO:0006334]; post-translational protein modification [GO:0043687]; stem cell population maintenance [GO:0019827] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | calcium ion binding [GO:0005509]; histone arginine deiminase activity [GO:0140794]; histone H3R17 arginine deiminase activity [GO:0140797]; histone H3R2 arginine deiminase activity [GO:0140795]; histone H3R26 arginine deiminase activity [GO:0140798]; histone H3R8 arginine deiminase activity [GO:0140796]; identical prot... | PF03068;PF08527;PF08526; | 2.60.40.1700;2.60.40.1860; | Protein arginine deiminase family | PTM: Autocitrullination at Arg-372 and Arg-374 inactivates the enzyme. {ECO:0000250|UniProtKB:Q9UM07}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UM07}. Nucleus {ECO:0000250|UniProtKB:Q9UM07}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q9UM07}. Note=Cytoplasmic granules of eosinophils and neutrophils. {ECO:0000250|UniProtKB:Q9UM07}. | CATALYTIC ACTIVITY: Reaction=H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+); Xref=Rhea:RHEA:18089, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:10588, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29965, ChEBI:CHEBI:83397; EC=3.5.3.15; Evidence={ECO:0000250|UniProtKB:Q9UM07}; | null | null | null | null | FUNCTION: Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance. Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8... | Rattus norvegicus (Rat) |
O88808 | TUB_RAT | MTSKPHSDWIPYSVLDDEGSNLRQQKLDRQRALLEQKQKKKRQEPLMVQANADGRPRSRRARQSEEQAPLVESYLSSSGSTSYQVQEADSLASVQPGATRPPAPASAKKTKGAAASGGQGGAPRKEKKGKHKGTSGPATLAEDKSEAQGPVQILTVGQSDHAKDAGETAAGGGAQPSGQDLRATMQRKGISSSMSFDEEEDEDENSSSSSQLNSNTRPSSATSRKSTREAASAPSPAAPEPPVDIEVQDLEEFALRPAPQGITIKCRITRDKKGMDRGMYPTYFLHLDREDGKKVFLLAGRKRKKSKTSNYLISVDPTDL... | null | null | intraciliary transport [GO:0042073]; phagocytosis, recognition [GO:0006910]; photoreceptor cell maintenance [GO:0045494]; positive regulation of phagocytosis [GO:0050766]; protein localization to cilium [GO:0061512]; protein localization to photoreceptor outer segment [GO:1903546]; receptor localization to non-motile c... | cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | G protein-coupled receptor binding [GO:0001664]; intraciliary transport particle A binding [GO:0120160]; protein-containing complex binding [GO:0044877] | PF01167;PF16322; | null | TUB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19695251}. Nucleus {ECO:0000250}. Secreted {ECO:0000269|PubMed:19695251}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Binds phospholipid and is anchored to the plasma membrane through binding phosphatidy... | null | null | null | null | null | FUNCTION: Functions in signal transduction from heterotrimeric G protein-coupled receptors. Binds to membranes containing phosphatidylinositol 4,5-bisphosphate. Can bind DNA (in vitro). May contribute to the regulation of transcription in the nucleus. Could be involved in the hypothalamic regulation of body weight (By ... | Rattus norvegicus (Rat) |
O88809 | DCX_MOUSE | MELDFGHFDERDKASRNMRGSRMNGLPSPTHSAHCSFYRTRTLQALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINLPQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNVKTSANMKAPQSLASSNSAQARENKDFVRPKLVTIIRSGVKPRKAVRVLLNKKTAHSFEQVLTDITEAIKLETGVVKKLYTLDGKQVTCLHDFFGDDDVFIACGPEKFRYAQDDFSLDENECRVMKGNPSAAAGPKASPTPQKTSAKSPGPMRRSKSPADSGNDQDANGTS... | null | null | axon extension [GO:0048675]; axoneme assembly [GO:0035082]; brain development [GO:0007420]; central nervous system projection neuron axonogenesis [GO:0021952]; dendrite morphogenesis [GO:0048813]; hippocampus development [GO:0021766]; intracellular signal transduction [GO:0035556]; layer formation in cerebral cortex [G... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; growth cone [GO:0030426]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025] | microtubule binding [GO:0008017] | PF03607; | 3.10.20.230; | null | PTM: Phosphorylation by MARK1, MARK2 and PKA regulates its ability to bind microtubules (By similarity). Phosphorylation at Ser-265 and Ser-297 seems to occur only in neonatal brain, the levels falling precipitously by postnatal day 21 (PubMed:15099191, PubMed:22807455). {ECO:0000250|UniProtKB:Q9ESI7, ECO:0000269|PubMe... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q9ESI7}. Note=Localizes at neurite tips. {ECO:0000250|UniProtKB:Q9ESI7}. | null | null | null | null | null | FUNCTION: Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for... | Mus musculus (Mouse) |
O88811 | STAM2_MOUSE | MPLFTANPFEQDVEKATNEYNTTEDWSLIMDICDRVGSTPSGAKDCLKAIMKRVNHKVPHVALQALTLLGACVANCGKIFHLEVCSRDFATEVRSVIKNKAHPKVCEKLKSLMVEWSEEFQKDPQFSLISATIKSMKEEGVTFPSAGSQTVAAAAKNGTSLNKNKEDEDIAKAIELSLQEQKQQYTETKALYPPAESQLNNKAARRVRALYDFEAVEDNELTFKHGELITVLDDSDANWWQGENHRGTGLFPSNFVTTDLSTEVETATVDKLNVIDDDVEEIKKSEPEPVYIDEGKMDRALQILQSIDPKESKPDSQDLL... | null | null | protein transport [GO:0015031]; signal transduction [GO:0007165] | cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endocytic vesicle [GO:0030139]; nucleoplasm [GO:0005654] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130] | PF00018;PF02809;PF00790; | 1.20.5.1940;1.25.40.90;2.30.30.40; | STAM family | PTM: Phosphorylated in response to IL-2, GM-CSF, EGF and PDGF. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10651905, ECO:0000269|PubMed:12551915}. Early endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. | null | null | null | null | null | FUNCTION: Involved in intracellular signal transduction mediated by cytokines and growth factors. Upon IL-2 and GM-CSL stimulation, it plays a role in signaling leading to DNA synthesis and MYC induction. May also play a role in T-cell development. Involved in down-regulation of receptor tyrosine kinase via multivesicu... | Mus musculus (Mouse) |
O88813 | ACSL5_RAT | MLFIFNFLFSPLPTPALICLLTFGTAIFLWLINRPQPVLPLIDLDNQSVGIEGGARRGAFQKNNDLILYYFSDAKTLYEVFQRGLAVSDNGPCLGYRKPNQPYKWISYKQVSDRAEYLGSCLLHKGYKPSQDQFIGIFAQNRPEWVISELACYTYSMVAVPLYDTLGAEAIIYVINRADISVVICDTPQKATMLIENVEKDLTPGLKTVILMDPFDDDLMKRGEKCGIEMLSLHDAENLGKENFKKPMPPNPEDLSVICFTSGTTGDPKGAMLTHQNIVSNMAAFLKFLEPIFQPTPEDVTISYLPLAHMFERLVQGVIF... | 6.2.1.15; 6.2.1.3 | null | cellular response to insulin stimulus [GO:0032869]; fatty acid metabolic process [GO:0006631]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; positive regulation of long-chain fatty acid import across plasma membrane [GO:0010747]; positive regulation o... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; oleoyl-CoA ligase activity [GO:0090434] | PF00501; | 3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16263710}. Endoplasmic reticulum {ECO:0000269|PubMed:16263710}. Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Cell... | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDi... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=666 uM for ATP {ECO:0000269|PubMed:15683247}; KM=2.4 uM for CoA {ECO:0000269|PubMed:15683247}; KM=8.6 uM for palmitate {ECO:0000269|PubMed:15683247}; KM=6.5 uM for palmitate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=4.4 uM for stearate (when ex... | null | null | null | FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:28209804). ACSL5 may sensitize epithelial cells to apoptosis specifically triggered by the death ligand TRAIL at the villus tip of the crypt-villu... | Rattus norvegicus (Rat) |
O88816 | SNAT_MOUSE | MLNINSLKPEALHLPLGTSEFLGCQRRHTLPASEFRCLTPEDATSAFEIEREAFISVSGTCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLTQESLTLHRPGGRTAHLHVLAVHRTFRQQGKGSVLLWRYLHHLGSQPAVRRAVLMCEDALVPFYEKFGFQAVGPCAITVGSLTFTELQCSLRCHAFLRRNSGC | 2.3.1.87 | null | cellular response to cAMP [GO:0071320]; circadian rhythm [GO:0007623]; melatonin biosynthetic process [GO:0030187]; N-terminal protein amino acid acetylation [GO:0006474]; photoperiodism [GO:0009648]; response to calcium ion [GO:0051592]; response to copper ion [GO:0046688]; response to corticosterone [GO:0051412]; res... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471] | 14-3-3 protein binding [GO:0071889]; aralkylamine N-acetyltransferase activity [GO:0004059]; arylamine N-acetyltransferase activity [GO:0004060] | PF00583; | 3.40.630.30; | Acetyltransferase family, AANAT subfamily | PTM: cAMP-dependent phosphorylation on both N-terminal Thr-29 and C-terminal Ser-203 regulates AANAT activity by promoting interaction with 14-3-3 proteins. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16613}. | CATALYTIC ACTIVITY: Reaction=a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine + CoA + H(+); Xref=Rhea:RHEA:20497, ChEBI:CHEBI:15378, ChEBI:CHEBI:55469, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:77827; EC=2.3.1.87; Evidence={ECO:0000250|UniProtKB:Q29495}; | null | PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. | null | null | FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin. {ECO:0000250|UniProtKB:Q29495}. | Mus musculus (Mouse) |
O88819 | FUT9_MOUSE | MTSTSKGILRPFLIVCIILGCFMACLLIYIKPTNSWVFSPMESASSVLKMKNFFSTKTDYFNETTILVWVWPFGQTFDLTSCQAMFNIQGCHLTTDRSLYNKSHAVLIHHRDISWDLTNLPQQARPPFQKWIWMNLESPTHTPQKSGIEHLFNLTLTYRRDSDIQVPYGFLTVSTNPFVFEVPSKEKLVCWVVSNWNPEHARVKYYNELSKSIEIHTYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKLYNAFLAGSVPVVLGPSRENYENYIPADSFIHVEDFNSPSELAKYLKEVDKNNKLYLSYFNWRK... | 2.4.1.152 | null | fucosylation [GO:0036065]; glycosphingolipid biosynthetic process [GO:0006688]; Lewis x epitope biosynthetic process [GO:0106402]; N-glycan fucosylation [GO:0036071]; nervous system development [GO:0007399]; neuron differentiation [GO:0030182]; neuronal stem cell division [GO:0036445]; oligosaccharide biosynthetic proc... | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588] | 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity [GO:0017083]; alpha-(1->3)-fucosyltransferase activity [GO:0046920]; protein homodimerization activity [GO:0042803] | PF17039;PF00852; | 3.40.50.11660; | Glycosyltransferase 10 family | PTM: N-glycosylated with complex-type N-glycans. {ECO:0000250|UniProtKB:Q9Y231}. | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y231}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6P4F1}. Golgi apparatus membrane {ECO:0000269|PubMed:12626397}. | CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:13350... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:22645129}.; PATHWAY: Glycolipid biosynthesis. {ECO:0000269|PubMed:12626397, ECO:0000269|PubMed:16973732}. | null | null | FUNCTION: Catalyzes alpha(1->3) linkage of fucosyl moiety transferred from GDP-beta-L-fucose to N-acetyl glucosamine (GlcNAc) within type 2 lactosamine (LacNAc, beta-D-Gal-(1->4)-beta-D-GlcNAc-) glycan attached to glycolipids and N- or O-linked glycoproteins. Fucosylates distal type 2 LacNAc and its fucosylated (H-type... | Mus musculus (Mouse) |
O88824 | JTB_MOUSE | MLAGAGRRGLPRAGHLCWLLCAFTLKLCEAEAPVREEKLSVSTSTSPCWLAEEFVVTEECTPCSNFQIKTTPECGSTGYVEKITCSSSKRNEFKSCRSALLEQHLFWKFEGVVVAVALVFACLVIVRQRQLDRKALEKVRKQIESI | null | null | apoptotic mitochondrial changes [GO:0008637]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; positive regulation of protein kinase activity [GO:0045860]; regulation of cell population proliferation [GO:0042127] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; membrane [GO:0016020]; midbody [GO:0030496]; mitochondrion [GO:0005739]; spindle [GO:0005819] | protein kinase binding [GO:0019901] | PF05439; | 3.30.720.220; | JTB family | PTM: Undergoes N-terminal proteolytic processing, removing a peptide of about 1 kDa from the N-terminus of the protein. {ECO:0000269|PubMed:17369841}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:17369841}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Detected at the ce... | null | null | null | null | null | FUNCTION: Required for normal cytokinesis during mitosis. Plays a role in the regulation of cell proliferation. May be a component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome align... | Mus musculus (Mouse) |
O88828 | RPAB2_RAT | MSDNEDNFDGDDFDDVEEDEGLDDLENAEEEGQENVEILPSGERPQANQKRITTPYMTKYERARVLGTRALQIAMCAPVMVELEGETDPLLIAMKELKARKIPIIIRRYLPDGSYEDWGVDELIISD | null | null | transcription by RNA polymerase I [GO:0006360]; transcription by RNA polymerase II [GO:0006366]; transcription by RNA polymerase III [GO:0006383]; tRNA transcription by RNA polymerase III [GO:0042797] | fibrillar center [GO:0001650]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736]; RNA polymerase II, core complex [GO:0005665]; RNA polymerase III complex [GO:0005666] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; RNA polymerase I activity [GO:0001054]; RNA polymerase II activity [GO:0001055]; RNA polymerase III activity [GO:0001056] | PF01192; | 3.90.940.10; | Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61218}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P61218}. | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II, and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA... | Rattus norvegicus (Rat) |
O88829 | SIAT9_MOUSE | MHTEAVGGAARRPQKLRSQAAAPACRAMPSEFTSAKLRSDCSRTSLQWYTRTQHKMRRPSLLIKDICKCTLVAFGVWLLYILILNYTAEECDMKRMHYVDPDRIKRAQSYAQEVLQKECRPRYAKTAMALLFEDRYSINLEPFVQKVPTASEAELKYDPPFGFRKFSSKVQSLLDMLPEHDFPEHLRAKACKRCVVVGNGGILHGLELGHALNQFDVVIRLNSAPVEGYSEHVGNKTTIRMTYPEGAPLSDVEYYANDLFVTVLFKSVDFKWLQAMVKNESLPFWVRLFFWKQVAEKVPLQPKHFRILNPVIIKETAFDI... | 2.4.3.9 | null | lipid metabolic process [GO:0006629]; protein glycosylation [GO:0006486] | Golgi membrane [GO:0000139] | lactosylceramide alpha-2,3-sialyltransferase activity [GO:0047291] | PF00777; | 3.90.1480.20; | Glycosyltransferase 29 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = a ganglioside GM3 (d18:1(4E)) + CMP + H(+); Xref=Rhea:RHEA:18417, ChEBI:CHEBI:15378, ChEBI:CHEBI:17950, ChEBI:CHEBI:57812, ChEBI:CHEBI:60065, ChEBI:CHEBI:60377; EC=2.4.3.9; Evidence={ECO:0000269|PubMed:1... | null | null | null | null | FUNCTION: (Microbial infection) Gangliosides GD1b and GT1b (derived from GM3) may serve as receptors for some C.botulinum neurotoxins (minimally types BoNT/A, B, C) (PubMed:16115873). {ECO:0000305|PubMed:16115873}.; FUNCTION: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-redu... | Mus musculus (Mouse) |
O88831 | KKCC2_RAT | MSSCVSSQPTSDRAAPQDELGSGGVSRESQKPCEALRGLSSLSIHLGMESFIVVTECEPGRGVDLSLARDQPLEADGQELPLDASEPESRSLLSGGKMSLQERSQGGPASSSSLDMNGRCICPSLSYSPASSPQSSPRMPRRPTVESHHVSITGLQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVG... | 2.7.11.17 | null | CAMKK-AMPK signaling cascade [GO:0061762]; positive regulation of protein phosphorylation [GO:0001934]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468] | cytosol [GO:0005829]; neuron projection [GO:0043005]; nucleoplasm [GO:0005654] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein kinase activator activity [GO:0030295]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activ... | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Phosphorylated by PKA (By similarity). Each isoform may show a different pattern of phosphorylation (By similarity). Autophosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96RR4}. Cytoplasm {ECO:0000250|UniProtKB:Q96RR4}. Cell projection, neuron projection {ECO:0000250|UniProtKB:Q96RR4}. Note=Predominantly nuclear in unstimulated cells, relocalizes into cytoplasm and neurites after forskolin induction. {ECO:0000250|UniProtKB:Q96RR4}. | 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=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1 and CAMK4. Phosphorylates CAMK1D (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). Efficiently phosph... | Rattus norvegicus (Rat) |
O88833 | CP4AA_MOUSE | MSVSALSPTRFADSLSGFLQVASVLGLLLLLVKAVQFYLHRQWLLKAFQQFPSPPFHWFFGHEKFKGDQELQEIVSCIENFPSAFPRWFWGSKAYLTVYDPDYMKVILGRSDPKANGAYRLLAPWIGYGLLLLNGQPWFQHRRMLTPAFHYDILKPYVKNMADSIRLMLDKWERLADQDSSIEIFQHISLMTLDTVMKCAFSHKGSVQVDGNYRTYLQAIGDLNNLFHSRVRNIFHQNDTIYKLSSNGRLAKQACQLAHDHTDGVIKLRKDQLQDEGELEKIKKKRRLDFLDILLFARMENGDSMSDKDLRAEVDTFMFE... | 1.14.14.80 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P08516}; | arachidonic acid metabolic process [GO:0019369]; fatty acid metabolic process [GO:0006631]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651] | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid monooxygenase activity [GO:0008391]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; long-chain fatty acid omega-hydroxylase activity [GO:0102033]; monooxygenase activity [GO:0004497] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08516}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:P08516}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for dodecanoate {ECO:0000269|PubMed:17112342}; Vmax=55 nmol/min/nmol enzyme toward dodecanoate {ECO:0000269|PubMed:17112342}; | null | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long-chain fatty acids (By similarity). Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver (By similarity) (PubMed:17112342). In kid... | Mus musculus (Mouse) |
O88838 | SPSB2_MOUSE | MGQTALARGSSSTPTSQALYSDFSPPEGLEELLSAPPPDLVAQRHHGWNPKDCSENIDVKEGGLCFERRPVAQSTDGVRGKRGYSRGLHAWEISWPLEQRGTHAVVGVATALAPLQADHYAALLGSNSESWGWDIGRGKLYHQSKGLEAPQYPAGPQGEQLVVPERLLVVLDMEEGTLGYSIGGTYLGPAFRGLKGRTLYPSVSAVWGQCQVRIRYMGERRVEEPQSLLHLSRLCVRHALGDTRLGQISTLPLPPAMKRYLLYK | null | null | intracellular signal transduction [GO:0035556]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytosol [GO:0005829]; SCF ubiquitin ligase complex [GO:0019005] | ubiquitin ligase-substrate adaptor activity [GO:1990756] | PF07525;PF00622; | 2.60.120.920;1.10.750.20; | SPSB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99619}. Note=Exhibits a diffuse cytosolic localization. {ECO:0000250|UniProtKB:Q99619}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20603330). Negatively regulates nitric oxide (NO) production and limits cellular toxici... | Mus musculus (Mouse) |
O88839 | ADA15_MOUSE | MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTLSGSMESRVVQDSPPMSLADVLQTGLPEALRISLELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLSPERGYTLELGPGDLQRPVISRIQDHLLLGHTCAPSWHASVPTRAGPDLLLEQHHAHRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQ... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; Note=Binds 1 zinc ion per subunit. {ECO:0000305}; | angiogenesis [GO:0001525]; cardiac epithelial to mesenchymal transition [GO:0060317]; cell adhesion [GO:0007155]; cellular response to phorbol 13-acetate 12-myristate [GO:1904628]; collagen catabolic process [GO:0030574]; immune response to tumor cell [GO:0002418]; innate immune response [GO:0045087]; integrin-mediated... | acrosomal vesicle [GO:0001669]; adherens junction [GO:0005912]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; motile cilium [GO:0031514] | integrin binding [GO:0005178]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; SH3 domain binding [GO:0017124] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10;2.60.120.260; | null | PTM: The precursor is cleaved by a furin endopeptidase. An additional membrane proximal site of cleavage affects a small percentage of the proteins and results in disulfide-linked fragments. The prodomain is apparently cleaved in several positions that are N-terminal of the furin cleavage site. {ECO:0000269|PubMed:9748... | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:18390692}; Single-pass type I membrane protein {ECO:0000269|PubMed:18390692}. Cell junction, adherens junction {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:18390692}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubM... | null | null | null | null | null | FUNCTION: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. ... | Mus musculus (Mouse) |
O88844 | IDHC_MOUSE | MSRKIQGGSVVEMQGDEMTRIIWELIKEKLILPYVELDLHSYDLGIENRDATNDQVTKDAAEAIKKYNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVTGWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPKDGTQKVTYMVHDFEEGGGVAMGMYNQDKSIEDFAHSSFQMALSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKKYKSQFEAQKICYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLICPDGKTVEAEAAHGTVTRHYRMYQ... | 1.1.1.42 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:29923039}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:29923039}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000305|PubMed:29923039}; | 2-oxoglutarate metabolic process [GO:0006103]; female gonad development [GO:0008585]; glutathione metabolic process [GO:0006749]; glyoxylate cycle [GO:0006097]; isocitrate metabolic process [GO:0006102]; NADP metabolic process [GO:0006739]; regulation of phospholipid biosynthetic process [GO:0071071]; regulation of pho... | cytosol [GO:0005829]; mitochondrion [GO:0005739]; peroxisome [GO:0005777] | isocitrate dehydrogenase (NADP+) activity [GO:0004450]; magnesium ion binding [GO:0000287]; NAD binding [GO:0051287]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803] | PF00180; | 3.40.718.10; | Isocitrate and isopropylmalate dehydrogenases family | PTM: Acetylation at Lys-374 dramatically reduces catalytic activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12031902}. | CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; Evidence={ECO:0000269|PubMed:12031902, ECO:0000269|PubMed:29923039}; PhysiologicalDirection=left-to-... | null | null | null | null | FUNCTION: Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase (PubMed:12031902, PubMed:29923039). Plays a critical role in the generation of NADPH, an important cofactor... | Mus musculus (Mouse) |
O88845 | AKA10_MOUSE | MRGAGPSPRHSPRALRPDPGPAMSFFRRKVKGKEQEKTLDVKSTKASVAVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLRDTVVLPYFLQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKRHETPASSVTEALDRRLGDSSSAPLLVTQSEGTDLSSRTQNPQNHLLLSQEGHSARSLHREVARTGSHQIPTDSQDSSSRLAVGSRNSCSSPLRELSEKLMKSIEQDAVNTFTKYISPDAAKPIPITEAM... | null | null | protein localization [GO:0008104] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | protein kinase A binding [GO:0051018] | PF00615; | 1.10.167.10; | null | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11248059}. Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but also membrane associated and cytoplasmic. | null | null | null | null | null | FUNCTION: Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is... | Mus musculus (Mouse) |
O88846 | RNF4_RAT | MSTRNPQRKRRGGAVNSRQTQKRTRETTSTPEISLEAEPIELVETVGDEIVDLTCESLEPVVVDLTHNDSVVIVEERRRPRRNGRRLRQDHADSCVVSSDDEELSKDKDVYVTTHTPRSTKDEGTTGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI | 2.3.2.27 | null | cellular response to arsenic-containing substance [GO:0071243]; cellular response to cytokine stimulus [GO:0071345]; cellular response to gamma radiation [GO:0071480]; cellular response to hydroxyurea [GO:0072711]; cellular response to testosterone stimulus [GO:0071394]; male gonad development [GO:0008584]; negative re... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605] | DNA binding [GO:0003677]; identical protein binding [GO:0042802]; nuclear androgen receptor binding [GO:0050681]; nuclear estrogen receptor binding [GO:0030331]; nucleosome binding [GO:0031491]; SUMO polymer binding [GO:0032184]; TBP-class protein binding [GO:0017025]; ubiquitin conjugating enzyme binding [GO:0031624];... | PF13639; | 3.30.40.10; | null | PTM: Sumoylated; conjugated by one or two SUMO1 moieties. {ECO:0000269|PubMed:15707587}.; PTM: Autoubiquitinated. {ECO:0000269|PubMed:14987998}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P78317}. Nucleus {ECO:0000269|PubMed:11319220, ECO:0000269|PubMed:9710597}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20943951}. Nucleus, PML body {ECO:0000269|PubMed:20943951}. | 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:18408734}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:18408734}. | null | null | FUNCTION: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation (PubMed:14987998, PubMed:15707587, PubMed:184087... | Rattus norvegicus (Rat) |
O88848 | ARL6_MOUSE | MGLLDRLSGLLGLKKKEVHVLCLGLDNSGKTTIINKLKPSNAQSQDIVPTIGFSIEKFKSSSLSFTVFDMSGQGRYRNLWEHYYKDGQAIIFVIDSSDKLRMVVAKEELDTLLNHPDIKHRRIPILFFANKMDLRDSVTSVKVSQLLCLESIKDKPWHICASDAIKGEGLQEGVDWLQDQIQAVKT | null | null | brain development [GO:0007420]; cilium assembly [GO:0060271]; fat cell differentiation [GO:0045444]; intracellular protein transport [GO:0006886]; protein localization to cilium [GO:0061512]; protein localization to non-motile cilium [GO:0097499]; protein polymerization [GO:0051258]; protein targeting to membrane [GO:0... | axonemal microtubule [GO:0005879]; axoneme [GO:0005930]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; membrane coat [GO:0030117] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; phospholipid binding [GO:0005543] | PF00025; | 3.40.50.300; | Small GTPase superfamily, Arf family | null | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. Note=Appears in a pattern of punctae flanking the microtubule ... | null | null | null | null | null | FUNCTION: Involved in membrane protein trafficking at the base of the ciliary organelle (By similarity). Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia (By similarity). Together with BBS1, is n... | Mus musculus (Mouse) |
O88850 | HIPK3_RAT | MASQVLVYPPYVYQTQSSAFCSVKKLKVEPSGCVFQERACPQIHVNGRHFGNPLPSTKGSAFQTKIPFSKPRGHSFSLQAGAIVVKDTAGATKVIAAQAQQAGVEAPRAVVWRNRLHFLGGPQRCGLKRKSEELDNHSGAMQIVDELSILPAMLQTNMGNPVTVVTATTGSKQNCTSGEGDYQLVQHEVLCSVKNTYEVLDFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTENADEYNFVRAYECFQHRNHTCLVFEMLEQNLYDFLKQNKFSPLPLKVIRPVLQQVATALKKLKSLGLIH... | 2.7.11.1 | null | apoptotic process [GO:0006915]; mRNA transcription [GO:0009299]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, HIPK subfamily | PTM: Autophosphorylated. Autophosphorylation is not required for catalytic activity.; PTM: May be sumoylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9725910}. | 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: Seems to negatively regulate apoptosis by promoting FADD phosphorylation. Enhances androgen receptor-mediated transcription. May act as a transcriptional corepressor for NK homeodomain transcription factors. {ECO:0000269|PubMed:9725910}. | Rattus norvegicus (Rat) |
O88856 | TPST2_MOUSE | MRLSVRKVLLAAGCALALVLAVQLGQQVLECRAVLGGTRNPRRMRPEQEELVMLGADHVEYRYGKAMPLIFVGGVPRSGTTLMRAMLDAHPEVRCGEETRIIPRVLAMRQAWTKSGREKLRLDEAGVTDEVLDAAMQAFILEVIAKHGEPARVLCNKDPFTLKSSVYLARLFPNSKFLLMVRDGRASVHSMITRKVTIAGFDLSSYRDCLTKWNKAIEVMYAQCMEVGRDKCLPVYYEQLVLHPRRSLKRILDFLGIAWSDTVLHHEDLIGKPGGVSLSKIERSTDQVIKPVNLEALSKWTGHIPRDVVRDMAQIAPMLA... | 2.8.2.20 | null | fusion of sperm to egg plasma membrane involved in single fertilization [GO:0007342]; peptidyl-tyrosine sulfation [GO:0006478]; prevention of polyspermy [GO:0060468] | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | protein-tyrosine sulfotransferase activity [GO:0008476] | PF13469; | 3.40.50.300; | Protein sulfotransferase family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:O60704}. | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O60704}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O60704}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + L-tyrosyl-[protein] = adenosine 3',5'-bisphosphate + H(+) + O-sulfo-L-tyrosine-[protein]; Xref=Rhea:RHEA:16801, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:11688, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:65286; EC=2.8.2.20... | null | null | null | null | FUNCTION: Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate. {ECO:0000269|PubMed:9733778}. | Mus musculus (Mouse) |
O88867 | KMO_RAT | MASSDTEGKRVVVIGGGLVGALNACFLAKRNFQVDVYEAREDIRVANFMRGRSINLALSYRGRQALKAVGLEDQIVSKGVPMKARMIHSLSGKKSAIPYGNKSQYILSISREKLNKDLLTAVESYPNAKVHFGHKLSKCCPEEGILTMLGPNKVPRDITCDLIVGCDGAYSTVRAHLMKKPRFDYSQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRNAFMMIALPNMDKSFTCTLFMSFEEFEKLPTHSDVLDFFQKNFPDAIPLMGEQALMRDFFLLPAQPMISVKCSPFHLKSRCVLMGDAAHAIVPFFGQGMNAG... | 1.14.13.9 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O15229, ECO:0000255|HAMAP-Rule:MF_03018}; | 'de novo' NAD biosynthetic process from tryptophan [GO:0034354]; anthranilate metabolic process [GO:0043420]; cellular response to interleukin-1 [GO:0071347]; cellular response to lipopolysaccharide [GO:0071222]; kynurenic acid biosynthetic process [GO:0034276]; kynurenine metabolic process [GO:0070189]; L-kynurenine m... | extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741] | FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; kynurenine 3-monooxygenase activity [GO:0004502]; NAD(P)H oxidase H2O2-forming activity [GO:0016174] | PF01494; | 3.50.50.60; | Aromatic-ring hydroxylase family, KMO subfamily | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:1332540}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:1332540}. | CATALYTIC ACTIVITY: Reaction=H(+) + L-kynurenine + NADPH + O2 = 3-hydroxy-L-kynurenine + H2O + NADP(+); Xref=Rhea:RHEA:20545, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:57959, ChEBI:CHEBI:58125, ChEBI:CHEBI:58349; EC=1.14.13.9; Evidence={ECO:0000255|HAMAP-Rule:MF_03018, ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=258 uM for L-kynurenine {ECO:0000269|PubMed:26752518}; KM=11.3 uM for NADPH {ECO:0000269|PubMed:1332540}; KM=316 uM for NADH {ECO:0000269|PubMed:1332540}; | PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 1/3. {ECO:0000255|HAMAP-Rule:MF_03018}. | null | null | FUNCTION: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain developme... | Rattus norvegicus (Rat) |
O88869 | RASF9_RAT | MAPFGRNLLKTRHKNRSPTKDMDPEEKEIVVWVCQEEKIVCGLTKRTTSIDVIQALLEEHEATFGEKRFLLGKASDYCIVEKWRGSERALPPLTRILKLWKAWGDEQPNMQFVLVKTDAFLPVPLWRTAETKLVQNNEKPWELSPANYMKTLPPDKQKRIVRKTFRKLAKIRQDTGSHDRDNMECLVHLIISQDHTIHQQVQRMKELDMEIEKCEAKIHLDRIGNDGADYVQEAYLMPRSSEEEQKLDFQSEDNQTLEDLNDGEGVSQLEEQLQYYRALIDKLSAEIEREVKGAGTDGSEDMEGAAACELENSDLESVKC... | null | null | endosomal transport [GO:0016197]; intracellular transport [GO:0046907]; protein targeting [GO:0006605]; signal transduction [GO:0007165] | cytosol [GO:0005829]; endosome [GO:0005768]; recycling endosome [GO:0055037]; trans-Golgi network transport vesicle membrane [GO:0012510] | enzyme binding [GO:0019899]; protein domain specific binding [GO:0019904] | null | null | null | null | SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:9837933}. Note=Accumulates on perinuclear endosomes. | null | null | null | null | null | FUNCTION: May play a role in regulating vesicuar trafficking in cells. {ECO:0000269|PubMed:9837933}. | Rattus norvegicus (Rat) |
O88870 | BEST1_MOUSE | MTITYTNKVANARLGSFSSLLLCWRGSIYKLLYGEFLVFIFLYYSIRGLYRMVLSSDQQLLFEKLALYCDSYIQLIPISFVLGFYVTLVVSRWWSQYENLPWPDRLMIQVSSFVEGKDEEGRLLRRTLIRYAILGQVLILRSISTSVYKRFPTLHHLVLAGFMTHGEHKQLQKLGLPHNTFWVPWVWFANLSMKAYLGGRIRDTVLLQSLMNEVCTLRTQCGQLYAYDWISIPLVYTQVVTVAVYSFFLACLIGRQFLNPNKDYPGHEMDLVVPVFTILQFLFYMGWLKVAEQLINPFGEDDDDFETNWIIDRNLQVSLL... | null | null | chloride transport [GO:0006821]; detection of light stimulus involved in visual perception [GO:0050908]; gamma-aminobutyric acid secretion, neurotransmission [GO:0061534]; glutamate secretion [GO:0014047]; protein complex oligomerization [GO:0051259]; regulation of calcium ion transport [GO:0051924]; regulation of syna... | basolateral plasma membrane [GO:0016323]; chloride channel complex [GO:0034707]; membrane microdomain [GO:0098857]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | bicarbonate channel activity [GO:0160133]; chloride channel activity [GO:0005254]; identical protein binding [GO:0042802]; intracellular calcium activated chloride channel activity [GO:0005229]; ligand-gated channel activity [GO:0022834] | PF01062; | null | Anion channel-forming bestrophin (TC 1.A.46) family, Calcium-sensitive chloride channel subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23021213, ECO:0000269|PubMed:29121962}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76090}. Basolateral cell membrane {ECO:0000250|UniProtKB:O76090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76090}. Note=Localized at the surface membrane of micr... | CATALYTIC ACTIVITY: Reaction=4-aminobutanoate(in) = 4-aminobutanoate(out); Xref=Rhea:RHEA:35035, ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:20929730}; CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:23021213, ECO:0000269|PubMed:... | null | null | null | null | FUNCTION: Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (By similarity). Allows the movement of chloride and hydrogencarbonate (By similarity). Found in a partially open conformation leading to significantly smaller chloride movement (By similarity)... | Mus musculus (Mouse) |
O88871 | GABR2_RAT | MASPPSSGQPRPPPPPPPPARLLLPLLLSLLLWLAPGAWGWTRGAPRPPPSSPPLSIMGLMPLTKEVAKGSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHFRWRRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFSNDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAFEESMFGSKYQWIIPGWYEPAWWEQVHVEANSSRCLRRSLLAAMEGYIGVDFEP... | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; gamma-aminobutyric acid signaling pathway [GO:0007214]; neuron-glial cell signaling [GO:0150099]; synaptic transmission, GABAergic [GO:0051932] | cytoplasm [GO:0005737]; dendrite [GO:0030425]; G protein-coupled GABA receptor complex [GO:1902712]; G protein-coupled receptor heterodimeric complex [GO:0038039]; GABA receptor complex [GO:1902710]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; perikaryon [GO:0043... | G protein-coupled GABA receptor activity [GO:0004965]; protein heterodimerization activity [GO:0046982] | PF00003;PF01094;PF18455; | 3.40.50.2300; | G-protein coupled receptor 3 family, GABA-B receptor subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9872315, ECO:0000269|PubMed:9872317, ECO:0000305|PubMed:10457184}; Multi-pass membrane protein {ECO:0000269|PubMed:9872317}. Postsynaptic cell membrane {ECO:0000269|PubMed:9872317}; Multi-pass membrane protein {ECO:0000269|PubMed:9872317}. Perikaryon {ECO:0000269|... | null | null | null | null | null | FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:9872315, PubMed:9872317, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:10658574, PubMed:9872317). Ligand bin... | Rattus norvegicus (Rat) |
O88873 | GMEB2_RAT | MATPDVSVHMEEVVVVTTPDTAVDGSGVEEVKTVLVTTNLAPHGGDLTEDNMETENAAAAACAFTASSQLKEAVLVKMAEEGENLEAEIVYPITCGDSRANLIWRKFVCPGINVKCVQYDEHVISPKEFVHLAGKSTLKDWKRAIRMNGIMLRKIMDSGELDFYQHDKVCSNTCRSTKIDLSGARVSLSSPTSTEYIPLTPAAADVNGSPATITIETCEDPGDWTTTIGDDTFAFWRGLKDAGLLDEVIQEFQQELEETMKGLQQRVQDPPLQLRDAVLLNNIVQNFGMLDLVKKVLASHKCQMDRSREQYARDLAALEQ... | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | cytoplasm [GO:0005737]; 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]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:000... | PF01342; | 3.10.390.10; | null | null | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=May be also cytoplasmic. | null | null | null | null | null | FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory elements (GME) present in the TAT (tyrosine aminotransferase) promoter and increases sensitivity to low concentrations of glucocorticoids. Binds also to the transferrin receptor promoter (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
O88874 | CCNK_MOUSE | MKENKENSSPSVTSANLDHTKPCWYWDKKDLAHTPSQLEGLDPATEARYRREGARFIFDVGTRLGLHYDTLATGIIYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFGQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLKYAKQLKGDKNKIQKLVQMAWTFVNDSLCTTLSLQWEPEIIAVAVMYLAGRLCKFEIQEWTSKPMYRRWWEQFVQDVPVDVLEDICHQILDLYSQGKQQMPHHTPHQLQQPPSLQPTPQVPQGPQSQPSQGSEAAQPPQKDSQQSAQQQQQQAQQ... | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; DNA damage response [GO:0006974]; in utero embryonic development [GO:0001701]; negative regulation of stem cell differentiation [GO:2000737]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of transcription elongation ... | cyclin K-CDK12 complex [GO:0002944]; cyclin K-CDK13 complex [GO:0002945]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; nucleus [GO:0005634] | cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein kinase binding [GO:0019901]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353] | PF00134;PF21797; | 1.10.472.10; | Cyclin family, Cyclin C subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:22012619}. | null | null | null | null | null | FUNCTION: Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A). {ECO:0000269|PubMed:22012619}. | Mus musculus (Mouse) |
O88875 | BY55_MOUSE | MQRILMAPGQSCCALAILLAIVNFQHGGCIHVTSSASQKGGRLDLTCTLWHKKDEAEGLILFWCKDNPWNCSPETNLEQLRVKRDPETDGITEKSSQLVFTIEQATPSDSGTYQCCARSQKPEIYIHGHFLSVLVTGNHTEIRQRQRSHPDFSHINGTLSSGFLQVKAWGMLVTSLVALQALYTL | null | null | adaptive immune response [GO:0002250]; defense response to Gram-negative bacterium [GO:0050829]; innate immune response [GO:0045087]; mucosal immune response [GO:0002385]; negative regulation of adaptive immune memory response [GO:1905675]; negative regulation of angiogenesis [GO:0016525]; negative regulation of CD4-po... | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | activating MHC class I receptor activity [GO:0032397]; kinase binding [GO:0019900]; MHC class I protein complex binding [GO:0023024]; MHC class Ib receptor activity [GO:0032394]; signaling receptor binding [GO:0005102] | PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: [CD160 antigen]: Cell membrane {ECO:0000269|PubMed:22801499, ECO:0000269|PubMed:25711213}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O95971}.; SUBCELLULAR LOCATION: [CD160 antigen, soluble form]: Secreted {ECO:0000250|UniProtKB:O95971, ECO:0000305|PubMed:16177084}. Note=Released from the cel... | null | null | null | null | null | FUNCTION: [CD160 antigen]: Receptor on immune cells capable to deliver stimulatory or inhibitory signals that regulate cell activation and differentiation. Exists as a GPI-anchored and as a transmembrane form, each likely initiating distinct signaling pathways via phosphoinositol 3-kinase in activated NK cells and via ... | Mus musculus (Mouse) |
O88876 | DHRS3_MOUSE | MVWKWLGALVVFPLQMIYLVTKAAVGMVLPPKLRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAALEEIHRFSGTYTCMNTFKGRT | 1.1.1.300 | null | bone morphogenesis [GO:0060349]; cardiac septum morphogenesis [GO:0060411]; negative regulation of retinoic acid receptor signaling pathway [GO:0048387]; outflow tract morphogenesis [GO:0003151]; regulation of ossification [GO:0030278]; regulation of retinoic acid receptor signaling pathway [GO:0048385]; retinoid metab... | lipid droplet [GO:0005811]; membrane [GO:0016020] | NAD-retinol dehydrogenase activity [GO:0004745]; NADP-retinol dehydrogenase activity [GO:0052650] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH; Xref=Rhea:RHEA:25033, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17898, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.300; Evidence={ECO:0000250|UniProtKB:O75911}; | null | null | null | null | FUNCTION: Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH. {ECO:0000250|UniProtKB:O75911}. | Mus musculus (Mouse) |
O88878 | ZFAN5_MOUSE | MAQETNQTPGPMLCSTGCGFYGNPRTNGMCSVCYKEHLQRQQNSGRMSPMGTASGSNSPTSDSASVQRADAGLNNCEGAAGSTSEKSRNVPVAALPVTQQMTEMSISREDKITTPKTEVSEPVVTQPSPSVSQPSSSQSEEKAPELPKPKKNRCFMCRKKVGLTGFDCRCGNLFCGLHRYSDKHNCPYDYKAEAAAKIRKENPVVVAEKIQRI | null | null | face development [GO:0060324]; fibroblast migration [GO:0010761]; in utero embryonic development [GO:0001701]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; respiratory system process [GO:0003016]; skeletal system morphogenesis [GO:0048705]; smooth muscle tissue development [GO:0048745]; vascu... | cytoplasm [GO:0005737] | DNA binding [GO:0003677]; zinc ion binding [GO:0008270] | PF01754;PF01428; | 1.20.5.4770;4.10.1110.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Involved in protein degradation via the ubiquitin-proteasome system. May act by anchoring ubiquitinated proteins to the proteasome. Plays a role in ubiquitin-mediated protein degradation during muscle atrophy. Plays a role in the regulation of NF-kappa-B activation and apoptosis. Inhibits NF-kappa-B activatio... | Mus musculus (Mouse) |
O88879 | APAF_MOUSE | MDAKARNCLLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAALLQSGLPLVSSSSGKDTDGGITSFVRTVLCEGGVPQRPVIFVTRKKLVHAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAEAVRDHSLLEGCFSGGVHWVSIGKQDKSGLLMKLQNLCMRLDQEESFSQRLPLNIEEAKDRLRVLMLRKHPRSLLILDDVWDPWVLKAFDNQCQILLTTRDKSVTDSVMGPKHVVPVESGLGREKGLEILSLFVNMKKEDLPAEAHSIIKECKGS... | null | null | brain development [GO:0007420]; cardiac muscle cell apoptotic process [GO:0010659]; cell differentiation [GO:0030154]; cellular response to transforming growth factor beta stimulus [GO:0071560]; forebrain development [GO:0030900]; intrinsic apoptotic signaling pathway [GO:0097193]; intrinsic apoptotic signaling pathway... | apoptosome [GO:0043293]; cytosol [GO:0005829]; nucleus [GO:0005634] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; heat shock protein binding [GO:0031072]; identical protein binding [GO:0042802] | PF21296;PF17908;PF00619;PF00931;PF00400; | 1.25.40.370;1.10.533.10;1.10.8.430;3.40.50.300;1.10.10.10;2.130.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
O88881 | BEGIN_RAT | MWTGGRRPGRLRRAASAADMEKLSALQEQKGELRKRLSYTTHKLEKLETEFDSTRHYLEIELRRAQEELDKVTEKLRRIQSNYMALQRINQELEDKLYRMGQHYEEEKRAMSHEIVALNSHLLEAKVTIDKLSEDNELYRKDCNLAAQLLQCSQTYGRVHKVSELPSDFQQRVSLHMEKHGCSLPSPLCHPSYADSVPTCVIAKVLEKPDPGSLSSRMSDASARDLAYRDGVENPGPRPPYKGDIYCSDTALYCPDERDHDRRPSVDTPVTDVGFLRAQNSTDSLAEEEEAEAAAFPEAYRREAFQGYAASLPTSSSYSS... | null | null | evoked excitatory postsynaptic potential [GO:0098817] | cytosol [GO:0005829]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; postsynapse [GO:0098794]; presynapse [GO:0098793]; synapse [GO:0045202] | null | null | null | null | null | SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein. | null | null | null | null | null | FUNCTION: May sustain the structure of the postsynaptic density (PSD). | Rattus norvegicus (Rat) |
O88884 | AKAP1_RAT | MAIQFRSLFPLALPGMLALLGWWWFFSRKKDRLSSNGKQVGTLKVGPAIEDRLPTEEACPGVLSVTPSVTQPPGKEEQRSMDRPLSDPPALPRTRQVRRRSESSGNLPSIVDTRLQAGQCSDENSKVVLSLMGDEAKSIPLGRPLFPKDLSFPYEAVEGCKQESALGRTPGRGWLSQCAASGENARETGGAEGTGDAVLGESVLEEGLLPQECVSEVEKSEFPILAPGGGGGEKVRSGPPQVDELLKKEEYIVGKLPSSFVGPVHSELVKDEGALVPQVKGSQDRSLARELDKDKTLPEKDQIEQTAFQIISQVILEATE... | null | null | antiviral innate immune response [GO:0140374]; apoptotic process [GO:0006915]; cellular response to cAMP [GO:0071320]; cellular response to peptide hormone stimulus [GO:0071375]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of protein dephosphorylation [GO:0035308]; negative regul... | 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 [GO:0099091] | 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;PF10522;PF00567; | 2.30.30.140;2.40.50.90;3.30.1370.10; | null | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:O08715}. Mitochondrion {ECO:0000250|UniProtKB:O08715}. | null | null | null | null | null | FUNCTION: Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane (By similarity). Involved in mitochondrial-mediated antiviral innate immunity (By similarity). Promotes translocation of NDUFS1 into mitochondria to regulate mitochondria... | Rattus norvegicus (Rat) |
O88890 | SH21A_MOUSE | MDAVTVYHGKISRETGEKLLLATGLDGSYLLRDSESVPGVYCLCVLYQGYIYTYRVSQTETGSWSAETAPGVHKRFFRKVKNLISAFQKPDQGIVTPLQYPVEKSSGRGPQAPTGRRDSDICLNAP | null | null | adaptive immune response [GO:0002250]; cell-cell signaling [GO:0007267]; cellular defense response [GO:0006968]; humoral immune response [GO:0006959]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of natural killer cell... | cytoplasm [GO:0005737] | null | PF00017; | 3.30.505.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as SLAMF1, CD244, LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling seems to cooperate with SH2D1B/EAT-2. Initially it has been proposed that association with SLAMF1 prevents SLAMF1 binding to inhibitory... | Mus musculus (Mouse) |
O88895 | HDAC3_MOUSE | MAKTVAYFYDPDVGNFHYGAGHPMKPHRLALTHSLVLHYGLYKKMIVFKPYQASQHDMCRFHSEDYIDFLQRVSPTNMQGFTKSLNAFNVGDDCPVFPGLFEFCSRYTGASLQGATQLNNKICDIAINWAGGLHHAKKFEASGFCYVNDIVIGILELLKYHPRVLYIDIDIHHGDGVQEAFYLTDRVMTVSFHKYGNYFFPGTGDMYEVGAESGRYYCLNVPLRDGIDDQSYKHLFQPVISQVVDFYQPTCIVLQCGADSLGCDRLGCFNLSIRGHGECVEYVKSFNIPLLVLGGGGYTVRNVARCWTYETSLLVEEAIS... | 3.5.1.-; 3.5.1.98 | null | cellular response to fluid shear stress [GO:0071498]; chromatin organization [GO:0006325]; circadian regulation of gene expression [GO:0032922]; cornified envelope assembly [GO:1903575]; DNA repair-dependent chromatin remodeling [GO:0140861]; epidermis development [GO:0008544]; establishment of mitotic spindle orientat... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; histone deacetylase complex [GO:0000118]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Rpd3L-Expanded complex [GO:0070210]; transcription repressor complex [... | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cyclin binding [GO:0030332]; deacetylase activity [GO:0019213]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; GTPase binding [GO:0051020]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:004... | PF00850; | 3.40.800.20; | Histone deacetylase family, HD type 1 subfamily | PTM: Sumoylated in vitro. {ECO:0000269|PubMed:19204783}.; PTM: Deubiquitinated on 'Lys-63'-linked ubiquitin chains by USP38; leading to a decreased level of histone acetylation. {ECO:0000250|UniProtKB:O15379}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26776516}. Cytoplasm {ECO:0000269|PubMed:26776516}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O15379}. Note=Colocalizes with XBP1 and AKT1 in the cytoplasm. Predominantly expressed in the nucleus in the presence of CCAR2 (By similarity). {ECO:0000250|UniProtKB:O15379}. | CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98; Evidence={ECO:0000305|PubMed:23911289, ECO:0000305|PubMed:30279482}; P... | null | null | null | null | FUNCTION: Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates (PubMed:23911289, PubMed:30279482). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transc... | Mus musculus (Mouse) |
O88898 | P63_MOUSE | MNFETSRCATLQYCPDPYIQRFIETPAHFSWKESYYRSAMSQSTQTSEFLSPEVFQHIWDFLEQPICSVQPIELNFVDEPSENGATNKIEISMDCIRMQDSDLSDPMWPQYTNLGLLNSMDQQIQNGSSSTSPYNTDHAQNSVTAPSPYAQPSSTFDALSPSPAIPSNTDYPGPHSFDVSFQQSSTAKSATWTYSTELKKLYCQIAKTCPIQIKVMTPPPQGAVIRAMPVYKKAEHVTEVVKRCPNHELSREFNEGQIAPPSHLIRVEGNSHAQYVEDPITGRQSVLVPYEPPQVGTEFTTVLYNFMCNSSCVGGMNRRP... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | anatomical structure formation involved in morphogenesis [GO:0048646]; animal organ morphogenesis [GO:0009887]; apoptotic process [GO:0006915]; cellular senescence [GO:0090398]; chromatin remodeling [GO:0006338]; cloacal septation [GO:0060197]; cranial skeletal system development [GO:1904888]; determination of adult li... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | chromatin binding [GO:0003682]; damaged DNA binding [GO:0003684]; 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]; d... | PF00870;PF07710;PF07647; | 2.60.40.720;4.10.170.10;1.10.150.50; | P53 family | PTM: May be sumoylated. {ECO:0000250}.; PTM: Ubiquitinated. Polyubiquitination involves WWP1 and leads to proteasomal degradation of this protein. {ECO:0000269|PubMed:18806757}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14729569}. | null | null | null | null | null | FUNCTION: Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. May be required in conjunction with TP73/p73 for initiation of p53/TP53 depend... | Mus musculus (Mouse) |
O88900 | GRB14_RAT | MTTSLQDGQSAAGRAGAQDSPLAVQVCRVAQGKGDAQDPAQVPGLHALSPASDATRRGAMDRRKAKDLEVQETPSIPNPFPELCCSPLTSVLSAGLFPRSNSRKKQVIKVYSEDETSRALEVPSDVTARDVCQLLILKNHYVDDNSWTLFEHLSHTGVERTVEDHELLTEVLSHWVMEEDNKLYLRKNYAKYEFFKNPMYFFPEHMVSFATEMNGDRSLTQIPQVFLSSNTYPEIHGFLHAKEQGKKSWKKAYFFLRRSGLYFSTKGTSKEPRHLQFFSEFSTSNVYMSLAGKKKHGAPTPYGFCFKPTKAGGPRDLKML... | null | null | cellular response to insulin stimulus [GO:0032869]; insulin receptor signaling pathway [GO:0008286]; intracellular signal transduction [GO:0035556]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904145] | cytoplasm [GO:0005737]; endosome [GO:0005768]; endosome membrane [GO:0010008]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | molecular adaptor activity [GO:0060090]; phosphoprotein binding [GO:0051219]; protein-macromolecule adaptor activity [GO:0030674]; receptor tyrosine kinase binding [GO:0030971] | PF08947;PF00169;PF00788;PF00017; | 2.30.29.30;3.30.505.10; | GRB7/10/14 family | PTM: Phosphorylated on serine residues. Phosphorylated on tyrosine residues by TEK/TIE2 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14449}. Endosome membrane {ECO:0000250|UniProtKB:Q14449}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14449}. Note=Upon insulin stimulation, translocates to the plasma membrane. {ECO:0000250|UniProtKB:Q14449}. | null | null | null | null | null | FUNCTION: Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation ... | Rattus norvegicus (Rat) |
O88902 | PTN23_RAT | LNVNLMLGQAQECLLEKSMLDNRKSFLVARISAQVVDYYKEACRALENPDTASLLGRIQKDWKKLVQMKIYYFAAVAHLHMGKQAEEQQKFGERVAYFQSALDKLNEAIKLAKGQPDTVQDALRFAMDVIGGKYNSAKKDNDFIYHEAVPALDTLQPVKGAPLVKPLPVNPTDPAVTGPDIFAKLVPMAAHEASSLYSEEKAKLLREMLAKIEDKNEVLDQFMDSMQLDPDTVDNLDAYNHIPPQLMEKCAALSVRPDTVKNLVQSMQVLSGVFTDVEASLKDIRDLLEEDELQEQKLQETLGQAGAGPGPSVTKAELGE... | 3.1.3.48 | null | cilium assembly [GO:0060271]; dephosphorylation [GO:0016311]; early endosome to late endosome transport [GO:0045022]; endocytic recycling [GO:0032456]; negative regulation of epithelial cell migration [GO:0010633]; positive regulation of adherens junction organization [GO:1903393]; positive regulation of early endosome... | ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endosome [GO:0005768]; nucleus [GO:0005634] | protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725] | PF13949;PF03097;PF00102; | 1.20.120.560;1.20.140.50;1.25.40.280;3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000269|PubMed:9694860}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes. May act as a negative regulator of Ras-mediated mitogenic activity. Plays a ro... | Rattus norvegicus (Rat) |
O88904 | HIPK1_MOUSE | MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQASSSHQVANFNLPAYDQGLLLPAPAVEHIVVTAADSSGSAATATFQSSQTLTHRSNVSLLEPYQKCGLKRKSEEVESNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPEN... | 2.7.11.1 | null | adherens junction assembly [GO:0034333]; anterior/posterior pattern specification [GO:0009952]; cell population proliferation [GO:0008283]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; endothelial cell apoptotic process [GO:0072577]; extrinsic apo... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; PML body [GO:0016605] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]; transcription corepressor activity [GO:0003714] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, HIPK subfamily | PTM: Phosphorylated and activated by JNK1 (By similarity). Autophosphorylated. {ECO:0000250}.; PTM: Sumoylated. When conjugated it is directed to nuclear speckles. SENP1-mediated desumoylation is mediated by TNF in response to stress stimuli, triggering transient translocation from nucleus to cytoplasm. {ECO:0000269|Pu... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:18219322, ECO:0000269|PubMed:20579985}. Cytoplasm {ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:18219322, ECO:0000269|PubMed:20579985}. Nucleus speckle {ECO:0000269|PubMed:12529400}. Note=Predominantly nuclear. Translocates from nucleus t... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplas... | Mus musculus (Mouse) |
O88907 | PIAS1_MOUSE | MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIMTPADLSIPNVHSSPMPPTLSPSTIPQLTYDGHPASSPLLPVSLLGPKHELELPHLTSALHPVHPDIKLQKLPFYDLLDELIKPTSLASDNSQRFRETCFAFALTPQQVQQISSSMDISGTKCDFTVQVQLRFCLSETSCPQEDHFPPNLCVKVNTKPCSLPGYLPPTKNGVEPKRPSRPINITSLVRLSTTVPNTIVVSWTAEIGRTYSMAVYLVKQLSSTVLLQRLRAKGIRNPDHSRALIKEKLTADP... | 2.3.2.27 | null | fat cell differentiation [GO:0045444]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of apoptotic process [GO:0043066]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of proteasomal ub... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; nuclear periphery [GO:0034399]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605] | DNA-binding transcription factor binding [GO:0140297]; protein domain specific binding [GO:0019904]; SUMO ligase activity [GO:0061665]; SUMO transferase activity [GO:0019789]; transcription cis-regulatory region binding [GO:0000976]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [G... | PF14324;PF02891; | 2.60.120.780;1.10.720.30;3.30.40.10; | PIAS family | PTM: Sumoylated. {ECO:0000250|UniProtKB:O75925}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16600910}. Nucleus speckle {ECO:0000250|UniProtKB:O75925}. Nucleus, PML body {ECO:0000269|PubMed:12077349, ECO:0000269|PubMed:22406621}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O75925}. Note=Interaction with CSRP2 may induce a partial redistribution along the cyt... | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | PATHWAY: Protein modification; protein sumoylation. | null | null | FUNCTION: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor (PubMed:24061474). Catalyzes sumoylation of various proteins, such as CEBPB, MRE11, MTA1, PTK2 and PML (PubMed:24061474). Plays a crucial role as a t... | Mus musculus (Mouse) |
O88908 | SOAT2_MOUSE | MQPKVPQLRRREGLGEEQEKGARGGEGNARTHGTPDLVQWTRHMEAVKTQFLEQAQRELAELLDRALWEAMQAYPKQDRPLPSAAPDSTSKTQELHPGKRKVFITRKSLIDELMEVQHFRTIYHMFIAGLCVLIISTLAIDFIDEGRLMLEFDLLLFSFGQLPLALMTWVPMFLSTLLVPYQTLWLWARPRAGGAWMLGASLGCVLLAAHAVVLCVLPVHVSVRHELPPASRCVLVFEQVRLLMKSYSFLRETVPGIFCVRGGKGISPPSFSSYLYFLFCPTLIYRETYPRTPSIRWNYVAKNFAQVLGCLLYACFILGR... | 2.3.1.26 | null | cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol storage [GO:0010878]; very-low-density lipoprotein particle assembly [GO:0034379] | brush border [GO:0005903]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772] | PF03062; | null | Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily | PTM: Polyubiquitinated by AMFR/gp78 at Cys-280, leading to its degradation when the lipid levels are low. Association with AMFR/gp78 is mediated via interaction with INSIG1. High concentration of cholesterol and fatty acid results in Cys-280 oxidation, preventing ubiquitination at the same site, resulting in protein st... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11071899}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA; Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26; Evidence={ECO:0000250|UniProtKB:O75908}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817; Evidence={ECO:00... | null | null | null | null | FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates. May provide... | Mus musculus (Mouse) |
O88909 | S22A8_MOUSE | MTFSEILDRVGSMGPFQYLHVTLLALPILGIANHNLLQIFTATTPDHHCRPPPNASLEPWVLPLGPNGKPEKCLRFVHLPNASLPNDTQGATEPCLDGWIYNSTRDTIVTEWDLVCGSNKLKEMAQSVFMAGILVGGPVFGELSDRFGRKPILTWSYLLLAASGSSAAFSPSLTVYMIFRFLCGCSISGISLSTIILNVEWVPTSTRAISSTTIGYCYTIGQFILPGLAYAVPQWRWLQLSVSAAFFIFSLLSWWVPESIRWLVLSGKFSKALKTLQRVATFNGKKEEGEKLTVEELKFNLQKDITSAKVKYGLSDLFRV... | null | null | glutathione transport [GO:0034635]; monoatomic ion transport [GO:0006811]; prostaglandin transport [GO:0015732]; quaternary ammonium group transport [GO:0015697]; response to toxic substance [GO:0009636] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323] | antiporter activity [GO:0015297]; organic anion transmembrane transporter activity [GO:0008514]; prostaglandin transmembrane transporter activity [GO:0015132]; protein kinase C binding [GO:0005080]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; solute:inorganic anion antiporter activity [GO... | PF00083; | 1.20.1250.20; | Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family | null | SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:15944205, ECO:0000269|PubMed:17220594, ECO:0000269|PubMed:23389457}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the basolateral side of all renal epithelia except the glomerulus (PubMed:15944205). Localizes on the brush border membran... | CATALYTIC ACTIVITY: Reaction=estrone 3-sulfate(out) + glutarate(in) = estrone 3-sulfate(in) + glutarate(out); Xref=Rhea:RHEA:72151, ChEBI:CHEBI:30921, ChEBI:CHEBI:60050; Evidence={ECO:0000269|PubMed:17220594, ECO:0000305|PubMed:12011098, ECO:0000305|PubMed:15075193, ECO:0000305|PubMed:21325432}; CATALYTIC ACTIVITY: Rea... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=61.9 nM for L-carnitine {ECO:0000269|PubMed:15100168}; KM=4.01 uM for 6-mercaptopurine {ECO:0000269|PubMed:15100168}; KM=53.9 nM for 5-fluorouracil {ECO:0000269|PubMed:15100168}; KM=1.48 uM for prostaglandin E(2) {ECO:0000269|PubMed:17220594}; | null | null | null | FUNCTION: Functions as an organic anion/dicarboxylate exchanger that couples organic anion uptake indirectly to the sodium gradient (By similarity). Transports organic anions such as estrone 3-sulfate (E1S) and urate in exchange for dicarboxylates such as glutarate or ketoglutarate (2-oxoglutarate) (PubMed:17220594). P... | Mus musculus (Mouse) |
O88910 | MPP3_MOUSE | MPVLSEDSGLHETLALLTSQLRPDSNHREEMGFLRDVFSEKSLSYLMKIHEKLRYYERQSPTPVLHSAMALAEDVMEELQAASVHSDERELLQLLSTPHLRAVLMVHDTVAQKNFDPVLPPLPDNIDEDFEEESVKIVRLVKNKEPLGATIRRDEHSGAVVVARIMRGGAADRSGLVHVGDELREVNGIAVLHKRPDEISQILAQSQGSITLKIIPATQEEDRFKDSKVFMRALFHYDPREDRAIPCQEAGLPFQRRQVLEVVSQDDPTWWQAKRVGDTNLRAGLIPSKQFQERRLSYRRTTGTLPSPQNFKKPPYDQPC... | null | null | null | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cell-cell junction [GO:0005911]; plasma membrane [GO:0005886] | PDZ domain binding [GO:0030165] | PF00625;PF02828;PF00595;PF07653; | 2.30.42.10;1.10.287.650;3.40.50.300;2.30.30.40; | MAGUK family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:23658188, ECO:0000269|PubMed:23893895}. Cell membrane {ECO:0000250|UniProtKB:Q13368}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q13368}. Note=Localized in apical villi of Mueller glia cells (PubMed:23893895). Localized at the apical membrane i... | null | null | null | null | null | FUNCTION: Participates in cell spreading through the phosphoinositide-3-kinase (PI3K) pathway by connecting CADM1 to DLG1 and the regulatory subunit of phosphoinositide-3-kinase (PI3K) (By similarity). Stabilizes HTR2C at the plasma membrane and prevents its desensitization (PubMed:16914526). May participates in the ma... | Mus musculus (Mouse) |
O88917 | AGRL1_RAT | MARLAAALWSLCVTTVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFM... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell surface receptor signaling pathway [GO:0007166]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; positive reg... | axon [GO:0030424]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synapse [GO:0045202] | carbohydrate binding [GO:0030246]; cell adhesion molecule binding [GO:0050839]; G protein-coupled receptor activity [GO:0004930]; latrotoxin receptor activity [GO:0016524]; toxic substance binding [GO:0015643] | PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191; | 1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10; | G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily | PTM: Autoproteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. This proteolytic processing takes place early in the biosynthetic pathway, either in the endoplasmic reticulum or in the early compartment of the Golgi apparatus. {ECO:0000269|PubMed:9208860}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21724987, ECO:0000269|PubMed:22333914}; Multi-pass membrane protein {ECO:0000269|PubMed:21724987, ECO:0000269|PubMed:22333914}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane. Cell projection, axon. Cell projection, growth cone. Synapse. Presynaptic cell membra... | null | null | null | null | null | FUNCTION: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. {ECO:0000269|PubMed:9208860, ECO:0000269|PubMe... | Rattus norvegicus (Rat) |
O88923 | AGRL2_RAT | MVSSGCRMRSLWFIMIISFSPNTEGFSRAALPFGLVRRELSCEGYSIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAFKIMTQRCNNRTQCVVVTGSDVFPDPCPGTYKYLEVQYECVPYMEQKVFVCPGTLKAIVDSPSIYEAEQKAGAWCKDPLQAADKIYFMPWTPYRTDTLIEYASLEDFQNSRQTTTYKLPNRVDGTGFVVYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINYANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEQNNGMIVISQLNPYTLRFEATWETTYDKRAASNAFM... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; positive regulation of synapse assembly [GO:0051965]; response to bacterium [GO:0009617]; synapse organization [GO:0050808] | glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211] | carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930]; PDZ domain binding [GO:0030165] | PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191; | 1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10; | G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily | PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:O88917}. | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Calcium-independent receptor of low affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. {ECO:0000269|PubMed:10026162}. | Rattus norvegicus (Rat) |
O88935 | SYN1_MOUSE | MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPSAASPGATPGSATASAERASTAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAAARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIG... | null | null | neuron development [GO:0048666]; neurotransmitter secretion [GO:0007269]; regulation of short-term neuronal synaptic plasticity [GO:0048172]; regulation of synaptic vesicle cycle [GO:0098693]; regulation of synaptic vesicle exocytosis [GO:2000300]; synapse organization [GO:0050808]; synaptic vesicle clustering [GO:0097... | axon [GO:0030424]; cell body [GO:0044297]; clathrin-sculpted glutamate transport vesicle membrane [GO:0060203]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; extrinsic component of synaptic vesicle membrane [GO:0098850]; Golgi apparatus [GO:0005794]; myelin sheath [GO:0043209]; postsynaptic density [GO:0014069]; pr... | actin binding [GO:0003779]; ATP binding [GO:0005524]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901] | PF02078;PF02750;PF10581; | 3.40.50.20;3.30.1490.20;3.30.470.20; | Synapsin family | PTM: Substrate of different protein kinases. Phosphorylation, including phosphorylation at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, regulates its rate of dispersion, and controls the kinetics of vesicle pool turnover. {ECO:0000250|UniProtKB:P09951}. | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:11571277}. Golgi apparatus {ECO:0000269|PubMed:11571277}. Presynapse {ECO:0000250|UniProtKB:P09951}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P09951}. Note=Dissociates from synaptic vesicles and redistributes into the axon during a... | null | null | null | null | null | FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (By similarity). Also involved in the regulation of axon outgrowth and synaptogenesis (Pub... | Mus musculus (Mouse) |
O88939 | ZBT7A_MOUSE | MAGGVDGPIGIPFPDHSSDILSGLNEQRTQGLLCDVVILVEGREFPTHRSVLAACSQYFKKLFTSGAVVDQQNVYEIDFVSAEALTALMDFAYTATLTVSTANVGDILSAARLLEIPAVSHVCADLLERQILAADDVGDASQPDGAGPTDQRNLLRAKEYLEFFRSNPMNSLPPTAFPWSGFGAPDDDLDATKEAVAAAVAAVAAGDCNGLDFYGPGPPADRPPAGDGDEGDSTPGLWPERDEDAPPGGLFPPPTAPPATTQNGHYGRAGAGTGEEEAAALSEAAPEPGDSPGFLSGAAEGEDGDAADVDGLAASTLLQQ... | null | null | B cell differentiation [GO:0030183]; cartilage development [GO:0051216]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA-templated transcription [GO:0006351]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; erythrocyte maturation [GO:0043249]; fat cell differ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | 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]; histone acetyltransferase binding [GO:0035035]; metal ion binding [... | PF00651;PF00096; | 3.30.160.60; | null | PTM: Sumoylated. Undergoes sumoylation with SUMO1 that may regulate its transcriptional activity. {ECO:0000250|UniProtKB:O95365}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15662416, ECO:0000269|PubMed:9927193}. Note=Recruited to double-strand break sites of damaged DNA. {ECO:0000269|PubMed:26446488}. | null | null | null | null | null | FUNCTION: Transcription factor that represses the transcription of a wide range of genes involved in cell proliferation and differentiation (PubMed:15337766, PubMed:15662416, PubMed:17495164, PubMed:26816381, PubMed:29813070). Directly and specifically binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and repre... | Mus musculus (Mouse) |
O88940 | MUSC_MOUSE | MSTGSVSDPEDSEMRGLQRVYPAPASKRPPLLRMERGYGSPSDISSAEEEDGEEEPGSLGAAGGCKRKRLRGADAGGAGGRAGGAGKKPLPPKGSAAECKQSQRNAANARERARMRVLSKAFSRLKTSLPWVPPDTKLSKLDTLRLASSYIAHLRQLLQEDRYEDSYVHPVNLTWPFVVSGRPDSDSKDVSAANRLCGTSA | null | null | branchiomeric skeletal muscle development [GO:0014707]; cellular response to leukemia inhibitory factor [GO:1990830]; diaphragm development [GO:0060539]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]; roof of mouth development [GO:0... | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II tra... | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription repressor that blocks myogenesis and activation of E-box dependent muscle genes. | Mus musculus (Mouse) |
O88942 | NFAC1_MOUSE | MPNTSFPVPSKFPLGPPAAVCGSGETLRPAPPSGGTMKAAEEEHYSYVSPSVTSTLPLPTAHSALPAACHDLQTSTPGISAVPSANHPPSYGGAVDSGPSGYFLSSGNTRPNGAPTLESPRIEITSYLGLHHGSGQFFHDVEVEDVLPSCKRSPSTATLHLPSLEAYRDPSCLSPASSLSSRSCNSEASSYESNYSYPYASPQTSPWQSPCVSPKTTDPEEGFPRSLGACHLLGSPRHSPSTSPRASITEESWLGARGSRPTSPCNKRKYSLNGRQPSCSPHHSPTPSPHGSPRVSVTEDTWLGNTTQYTSSAIVAAINA... | null | null | aortic valve development [GO:0003176]; aortic valve morphogenesis [GO:0003180]; B-1a B cell differentiation [GO:0002337]; branching involved in lymph vessel morphogenesis [GO:0060854]; calcineurin-NFAT signaling cascade [GO:0033173]; calcium ion transport [GO:0006816]; cellular response to calcium ion [GO:0071277]; end... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasm [GO:0016528]; 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, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor ... | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | PTM: Phosphorylated by NFATC-kinase and GSK3B; phosphorylation induces NFATC1 nuclear exit and dephosphorylation by calcineurin promotes nuclear import. Phosphorylation by PKA and DYRK2 negatively modulates nuclear accumulation, and promotes subsequent phosphorylation by GSK3B or casein kinase 1 (By similarity). {ECO:0... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19626032, ECO:0000269|PubMed:24970700, ECO:0000269|PubMed:28341745, ECO:0000269|PubMed:32741026}. Nucleus {ECO:0000269|PubMed:19626032, ECO:0000269|PubMed:21514407, ECO:0000269|PubMed:23990468, ECO:0000269|PubMed:24039232, ECO:0000269|PubMed:26644563, ECO:0000269|PubM... | null | null | null | null | null | FUNCTION: Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription (PubMed:9388475). Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and progra... | Mus musculus (Mouse) |
O88943 | KCNQ2_RAT | MVQKSRNGGVYPGTSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSVLSKPRTGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKV... | null | null | action potential [GO:0001508]; action potential initiation [GO:0099610]; apoptosome assembly [GO:0097314]; brain development [GO:0007420]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; cognition [GO:0050890]; dentate gyrus development [GO:0021542]; determination o... | axon initial segment [GO:0043194]; cell surface [GO:0009986]; mitochondrion [GO:0005739]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:0008076] | ankyrin binding [GO:0030506]; calmodulin binding [GO:0005516]; potassium channel activity [GO:0005267]; voltage-gated monoatomic ion channel activity [GO:0005244]; voltage-gated potassium channel activity [GO:0005249] | PF00520;PF16642;PF03520;PF11956; | 1.10.287.70;6.10.140.1910; | Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.2/KCNQ2 sub-subfamily | PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region. {ECO:0000250|UniProtKB:O43526}.; PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is in... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11038262, ECO:0000269|PubMed:11230508}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the respo... | Rattus norvegicus (Rat) |
O88944 | KCNQ3_RAT | MGLKARRAAGAAGGGGGEGGGGGGGAANPAGGDSAVAGDEERKVGLAPGDVEQVTLALGTGADKDGTLLLEGGGREEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEMDAQGEEMKEEFETYADALWWGLITLATIGY... | null | null | action potential initiation [GO:0099610]; apoptosome assembly [GO:0097314]; cellular response to ammonium ion [GO:0071242]; cellular response to calcium ion [GO:0071277]; cellular response to xenobiotic stimulus [GO:0071466]; endocytosis [GO:0006897]; establishment of localization in cell [GO:0051649]; excitatory chemi... | axon initial segment [GO:0043194]; cell surface [GO:0009986]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; node of Ranvier [GO:0033268]; plasma membrane [GO:0005886]; somatodendritic compartment [GO:0036477]; synapse [GO:0045202]; voltage-gated potassium channel complex [GO:000807... | calmodulin binding [GO:0005516]; potassium channel activity [GO:0005267]; protein kinase binding [GO:0019901]; transmembrane transporter binding [GO:0044325]; ubiquitin protein ligase binding [GO:0031625]; voltage-gated monoatomic ion channel activity [GO:0005244]; voltage-gated potassium channel activity [GO:0005249] | PF00520;PF03520;PF11956; | 1.10.287.70;6.10.140.1910; | Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.3/KCNQ3 sub-subfamily | PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation. Degradation induced by NEDD4L is inhibited by USP36. {ECO:0000250|UniProtKB:O43525}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9836639}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as ... | Rattus norvegicus (Rat) |
O88947 | FA10_MOUSE | MGSPVQLSLLCVVLASLLLPGKGVFINRERANNVLARTRRANSFFEEFKKGNLERECMEEICSYEEVREIFEDDEKTKEYWTKYKDGDQCESSPCQNQGACRDGIGGYTCTCSEGFEGKNCELFVRKLCRLDNGDCDQFCREEQNSVVCSCASGYFLGNDGKSCISTAPFPCGKITTGRRKRSVALNTSDSELDLEDALLDEDFLSPTENPIELLNLNETQPERSSDDLVRIVGGRECKDGECPWQALLINEDNEGFCGGTILNEFYILTAAHCLHQARRFKVRVGDRNTEKEEGNEMVHEVDVVIKHNKFQRDTYDYDI... | 3.4.21.6 | null | blood coagulation [GO:0007596]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508] | extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (By similarity). The activation peptide is cleaved by factor IXa (in the intrinsic pathw... | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6; | null | null | null | null | FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. | Mus musculus (Mouse) |
O88951 | LIN7B_MOUSE | MAALVEPLGLERDVSRAVELLERLQRSGELPPQKLQALQRVLQSRFCSAIREVYEQLYDTLDITGSAEVRAHATAKATVAAFTASEGHAHPRVVELPKTDEGLGFNIMGGKEQNSPIYISRVIPGGVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTPRVLEEMEARFEKMRSARRRQQHHSYTSLESRG | null | null | exocytosis [GO:0006887]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; neurotransmitter secretion [GO:0007269]; protein localization to basolateral plasma membrane [GO:1903361]; protein transport [GO:0015031] | basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; MPP7-DLG1-LIN7 complex [GO:0097025]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; synapse [GO:0045202]; transport vesicle membrane [GO:0030658] | L27 domain binding [GO:0097016]; PDZ domain binding [GO:0030165]; protein kinase binding [GO:0019901] | PF02828;PF00595; | 2.30.42.10;1.10.287.650; | Lin-7 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Basolateral cell membrane {ECO:0000269|PubMed:15494546}; Peripheral membrane protein {ECO:0000269|PubMed:15494546}. Cell junction {ECO:0000269|PubMed:15494546}. Postsynaptic density membrane {EC... | null | null | null | null | null | FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed o... | Mus musculus (Mouse) |
O88952 | LIN7C_MOUSE | MAALGEPVRLERDICRAIELLEKLQRSGEVPPQKLQALQRVLQSEFCNAVREVYEHVYETVDISSSPEVRANATAKATVAAFAASEGHSHPRVVELPKTEEGLGFNIMGGKEQNSPIYISRIIPGGIADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGKVKLVVRYTPKVLEEMESRFEKMRSAKRRQQT | null | null | exocytosis [GO:0006887]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; morphogenesis of an epithelial sheet [GO:0002011]; neurotransmitter secretion [GO:0007269]; protein localization to basolateral plasma membrane [GO:1903361]; protein transport [GO:0015031] | basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; glutamatergic synapse [GO:0098978]; MPP7-DLG1-LIN7 complex [GO:0097025]; postsynaptic density membrane [GO:0098839]; presynapse [GO:0098793]; synapse [GO:0045202]; transport vesicle membrane [GO:0030658] | cytoskeletal protein binding [GO:0008092]; L27 domain binding [GO:0097016]; PDZ domain binding [GO:0030165] | PF02828;PF00595; | 2.30.42.10;1.10.287.650; | Lin-7 family | null | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Basolateral cell membrane; Peripheral membrane protein. Cell junction. Postsynaptic density membrane; Peripheral membrane protein. Cell junction, tight junction. Note=Mainly basolateral in renal epithelial cells. | null | null | null | null | null | FUNCTION: Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed o... | Mus musculus (Mouse) |
O88956 | PLPP1_CAVPO | MFDKARLPYVALDVLCVVLAGLPFAILTSRHTPFQRGIFCNDESIKYPYKEDTIPYALLGGIMIPFSIVVMIIGETLSVYCNLLHSNSFIRNNYIATIYKSIGTFLFGAAASQSLTDIAKYSIGRLRPHFLSVCDPDWSKVNCSDGYIEYYVCRGNAEKVKEGRLSFYSGHSSFSMYCMVFVALYLQARMKGDWARLLRPTLQFGLVAASIYVGLSRISDYKHHWSDVLTGLIQGAIVAILVAVYVSDFFKARNSPFQERKEEDSHTTLHETPTAGNHYRSNHQP | 3.1.3.-; 3.1.3.106; 3.1.3.4; 3.6.1.75 | null | ceramide metabolic process [GO:0006672]; phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]; sphingosine metabolic process [GO:0006670] | apical plasma membrane [GO:0016324]; caveola [GO:0005901]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | ceramide-1-phosphate phosphatase activity [GO:0106235]; diacylglycerol diphosphate phosphatase activity [GO:0000810]; lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatidate phosphatase activity [GO:0008195]; sphingosine-1-phosphate phosphatase activity [GO:0042392] | PF01569; | 1.20.144.10; | PA-phosphatase related phosphoesterase family | PTM: N-glycosylated. N-linked sugars are of the complex type. N-glycosylation is not required for the phosphatase activity. {ECO:0000250|UniProtKB:Q61469}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane, caveola {ECO:0... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000269|PubMed:18215144}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;... | null | PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:18215144}. | null | null | FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C... | Cavia porcellus (Guinea pig) |
O88958 | GNPI1_MOUSE | MKLIILEHYSQASEWAAKYIRNRIIQFNPGPDKYFTLGLPTGSTPLGCYQKLIEYYKNGDLSFQYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAADLQAECDAFEEKIQAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGDLAKVPTMALTVGVGTVMDAKEVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCDEDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKEIQKSQSAKKPYSD | 3.5.99.6 | null | acrosome reaction [GO:0007340]; fructose 6-phosphate metabolic process [GO:0006002]; fructose biosynthetic process [GO:0046370]; generation of precursor metabolites and energy [GO:0006091]; glucosamine catabolic process [GO:0006043]; glucosamine metabolic process [GO:0006041]; N-acetylglucosamine catabolic process [GO:... | cytoplasm [GO:0005737] | glucosamine-6-phosphate deaminase activity [GO:0004342]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853] | PF01182; | 3.40.50.1360; | Glucosamine/galactosamine-6-phosphate isomerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10481053}. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6; Evidence={ECO:0000250|UniProtKB:P46926}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173; E... | null | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P46926}. | null | null | FUNCTION: Catalyzes the reversible conversion of alpha-D-glucosamine 6-phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and ammonium ion, a regulatory reaction step in de novo uridine diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via hexosamine pathway. Deamination is coupled to aldo-k... | Mus musculus (Mouse) |
O88962 | CP8B1_MOUSE | MTLWCTVLGALLTVVGCLCLSLLLRHRRPWEPPLDKGFVPWLGHSMAFRKNMFEFLKGMRAKHGDVFTVQLGGQYFTFVMDPLSFGPIIKNTEKALDFQSYAKELVLKVFGYQSVDGDHRMIHLASTKHLMGQGLEELNQAMLDSLSLVMLGPKGSSLGASSWCEDGLFHFCYRILFKAGFLSLFGYTKDKQQDLDEADELFRKFRRFDFLFPRFVYSLLGPREWVEVSQLQRLFHQRLSVEQNLEKDGISCWLGYMLQFLREQGIASSMQDKFNFMMLWASQGNTGPTCFWVLLFLLKHQDAMKAVREEATRVMGKARL... | 1.14.14.139 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:O02766}; | bile acid biosynthetic process [GO:0006699]; positive regulation of intestinal cholesterol absorption [GO:0045797] | endoplasmic reticulum membrane [GO:0005789] | 5beta-cholestane-3alpha,7alpha-diol 12alpha-hydroxylase activity [GO:0033779]; 7alpha-hydroxycholest-4-en-3-one 12alpha-hydroxylase activity [GO:0033778]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; sterol 12-alpha-hydroxylase activity [GO:0008397] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:O02766}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=7alpha-hydroxycholest-4-en-3-one + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha,12alpha-dihydroxycholest-4-en-3-one + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:46752, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:C... | null | PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000269|PubMed:12393855, ECO:0000269|PubMed:28377401}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4-cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis (By similarity). Controls biliary balance of cholic acid and chenodeoxycholic acid, ultimately regulating ... | Mus musculus (Mouse) |
O88967 | YMEL1_MOUSE | MFSLSSTVQPQVTIPLSHLINAFHSPKNISVSVNTPVSQKQHRDTVPEHEAPSSEPVLNLRDLGLSELKIGQIDKMVENLLPGFYKDKRVSSCWHTSHISAQSFFENKYGHLDMFSTLRSSSLYRQHPKTLRSICSDLQYFPVFIQSRGFKTLKSRTRRLQSTSERLVEAQNIAPSFVKGFLLRDRGTDLESLDKLMKTKNIPEAHQDAFKTGFAEGFLKAQALTQKTNDSLRRTRLILFVLLLFGIYGLLKNPFLSVRFRTTTGLDSAVDPVQMKNVTFEHVKGVEEAKQELQEVVEFLKNPQKFTVLGGKLPKGILLV... | 3.4.24.-; 3.6.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q96TA2}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q96TA2}; | cell population proliferation [GO:0008283]; mitochondrial protein catabolic process [GO:0035694]; mitochondrial protein processing [GO:0034982]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; protein hexamerization [GO:0034214]; protein quality control for misfolded or i... | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nuclear body [GO:0016604] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent peptidase activity [GO:0004176]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF00004;PF17862;PF01434; | 1.10.8.60;3.40.50.300;1.20.58.760; | AAA ATPase family; Peptidase M41 family | PTM: Proteolytically processed by mitochondrial processing peptidase (MPP) to generate the mature form. Degraded in an OMA1-dependent manner in response to oxidative stress. {ECO:0000250|UniProtKB:Q96TA2}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96TA2}. Mitochondrion {ECO:0000250|UniProtKB:Q96TA2}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q96TA2}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:Q96T... | null | null | null | null | FUNCTION: ATP-dependent metalloprotease that catalyzes the degradation of folded and unfolded proteins with a suitable degron sequence in the mitochondrial intermembrane region (PubMed:17709429, PubMed:24616225, PubMed:24703695, PubMed:26785494, PubMed:27495975, PubMed:33237841). Plays an important role in regulating m... | Mus musculus (Mouse) |
O88974 | SETB1_MOUSE | MSSLPGCMSLAAAPAAADSAEIAELQQAVVEELGISMEELRQYIDEELEKMDCIQQRKKQLAELETWVLQKESEVAYVDRLFDDASREVTNCESLVKDFYSKLGLQYHDSSSEDEASRPTEIIEIPDEDDDVLSIDSGDAGSRTPKDQKLREAMAALRKSAQDVQKFMDAVNKKSSSQDLHKGTLGQVSGELSKDGDLIVSMRILGKKRTKTWHKGTLIAIQTVGLGKKYKVKFDNKGKSLLSGNHIAYDYHPPADKLFVGSRVVAKYKDGNQVWLYAGIVAETPNVKNKLRFLIFFDDGYASYVTQSELYPICRPLKKT... | 2.1.1.366 | null | bone development [GO:0060348]; heterochromatin organization [GO:0070828]; inner cell mass cell proliferation [GO:0001833]; methylation [GO:0032259]; negative regulation of gene expression [GO:0010629]; negative regulation of single stranded viral RNA replication via double stranded DNA intermediate [GO:0045869]; negati... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 monomethyltransferase activity [GO:0140948]; histone H3K9me2 methyltransferase activity [GO:0140947]; promoter-specific chromatin binding [GO:1990841]; zinc ion binding [GO:0008270] | PF18300;PF01429;PF05033;PF00856;PF18358;PF18359; | 2.30.30.140;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, Suvar3-9 subfamily | PTM: Degraded by the proteasome, shielded by interaction with ATF7IP. {ECO:0000250|UniProtKB:Q15047}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29728365}. Chromosome {ECO:0000269|PubMed:29728365}. Note=Associated with non-pericentromeric regions of chromatin. {ECO:0000250|UniProtKB:Q15047}. | CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60288, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15541, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:... | null | null | null | null | FUNCTION: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 (PubMed:11791185, PubMed:22939622). H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euch... | Mus musculus (Mouse) |
O88978 | DAA11_MOUSE | MGRITEDLIRRNAEHNDCVIFSLEELSLHQQEIERLEHIDKWCRDLKILYLQNNLIGKIENVSKLKKLEYLNLALNNIERIENLEGCEWLTKLDLTVNFIGELSSVKTLTHNIHLKELFLMGNPCADFDGYRQFVVVTLQQLKWLDGKEIERSERIQALQNYTSVEQQIREQEKAYCLRRAKEKEEAQRKLEEENESEDKKKSSTGFDGHWYTDIHTACPSATENQDYPQVPETQEEQHNTKESDDIEDDLAFWNKPSLFTPESRLETLRHMEKQRKAQDKLSEKKKKAKPPRTLITEDGKVLNVNEAKLDFSLKDDEKH... | null | null | axonemal dynein complex assembly [GO:0070286]; cerebrospinal fluid circulation [GO:0090660]; cilium movement [GO:0003341]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; epithelial cilium movement involved in extracellular fluid movement [GO:0003351]; establishment of localiz... | apical cytoplasm [GO:0090651]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dynein axonemal particle [GO:0120293]; extracellular region [GO:0005576]; motile cilium [GO:0031514] | null | PF14580; | 3.80.10.10; | TilB family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10775177, ECO:0000269|PubMed:27353389}. Cell projection, cilium {ECO:0000250|UniProtKB:Q86X45}. Dynein axonemal particle {ECO:0000305|PubMed:27353389}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q86X45}. | null | null | null | null | null | FUNCTION: Involved in dynein arm assembly, is important for expression and transporting outer dynein arm (ODA) proteins from the cytoplasm to the cilia (PubMed:27353389). Acts as a crucial component in the formation and motility of spermatozoal flagella (By similarity). {ECO:0000250|UniProtKB:Q86X45, ECO:0000269|PubMed... | Mus musculus (Mouse) |
O88983 | STX8_MOUSE | MAPDPWFSTYDSTCQIAQEIAEKIQERNQCERRGEKTPKLTLTIRTLLKNLKVKIDLLKDLLLRAVSTRQITQLEGDRRQNLLDDLVTRERLLLASFKNEGAEPDLIRSSLMSEEAKRGTPNPWLCEEPEETRGLGFDEIRQQQQKIIQEQDAGLDALSSIISRQKQMGQEIGNELDEQNEIIDDLANLVENTDEKLRTEARRVTLVDRKSTSCGMIMVILLLLVAIVVVAVWPTN | null | null | cellular response to type II interferon [GO:0071346]; early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; regulation of protein localization to plasma membrane [GO:1903076]; vesicle docking [GO:0048278]; vesicle fusion [GO:00... | early endosome [GO:0005769]; endomembrane system [GO:0012505]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; recycling endosome [GO:0055037]; SNARE complex [GO:0031201]; trans-Golgi network... | chloride channel inhibitor activity [GO:0019869]; SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]; ubiquitin protein ligase binding [GO:0031625] | PF05739; | 1.20.5.110; | Syntaxin family | PTM: Ubiquitinated by HECTD3. {ECO:0000269|PubMed:18821010}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Preferentially associated with the early endosome. To a lesser extent, also present in late endosome, the plasma membrane and coated pits (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER. {ECO:0000250}. | Mus musculus (Mouse) |
O88984 | NXF1_RAT | MADEGKSYNEHDDRVSFPQRRKKGRGPFRWKCGVGNRRSGRGGSGIRSSRFEEDDGDVAMNDPQDGPRVRFNPYTTRPNRRRDTWHDRDRIHVTVRRDRAPQERGGAGTSQDGTTKNWFKITIPYGKKYDKMWLLSMIQSKCSVPFNPIEFHYENTRAHFFVENATTASALKAVNYKIQDRENGRISIIINSSAPPYIVQNELKPEQVEQLKLIMSKRYDGSQQALDLKGLRSDPDLVAQNIDVVLNRRGCMAAALRIIEENIPELLSLNLSNNRLYKLDDMSSIVQKAPNLKILNLSGNELKSEWELDKIKGLKLEELW... | null | null | mRNA export from nucleus [GO:0006406]; poly(A)+ mRNA export from nucleus [GO:0016973]; protein transport [GO:0015031]; RNA export from nucleus [GO:0006405] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; nuclear inclusion body [GO:0042405]; nuclear pore [GO:0005643]; nuclear RNA export factor complex [GO:0042272]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; transcription export complex [GO:0000346] | mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF02136;PF09162;PF03943; | 3.10.450.50;3.30.70.330;1.10.8.10;3.80.10.10; | NXF family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus speckle {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm, Stress granule {ECO:0000250|UniPr... | null | null | null | null | null | FUNCTION: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the... | Rattus norvegicus (Rat) |
O88987 | AKAP3_MOUSE | MADRVDWLQSQSGVCKVGVYSPGDNQHQDWKMDTSTDPVRVLSWLRKDLEKSTAGFQDSRFKPGESSFVEEVAYPVDQRKGFCVDYYNTTNKGSPGRLHFEMSHKENPSQGLISHVGNGGSIDEVSFYANRLTNLVIAMARKEINEKIHGAENKCVHQSLYMGDEPTPHKSLSTVASELVNETVTACSKNISSDKAPGSGDRASGSSQAPGLRYTSTLKIKESTKEGKCPDDKPGTKKSFFYKEVFESRNAGDAKEGGRSLPGDQKLFRTSPDNRPDDFSNSISQGIMTYANSVVSDMMVSIMKTLKIQVKDTTIATILL... | null | null | blastocyst hatching [GO:0001835]; protein localization [GO:0008104]; transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178] | acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; motile cilium [GO:0031514]; sperm fibrous sheath [GO:0035686]; sperm midpiece [GO:0097225]; sperm principal piece [GO:0097228] | protein kinase A binding [GO:0051018] | PF05716; | null | AKAP110 family | PTM: Phosphorylated on tyrosine. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:11278869}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:11278869, ECO:0000269|PubMed:37709195}. Note=Dorsal margin of the acrosomal segment (PubMed:11278869). Ribs of the fibrous sheath in the principal piece of the spe... | null | null | null | null | null | FUNCTION: Has a role in the maintenance of acrosome structure. May function as a regulator of both spermatozoa motility and head-associated functions such as capacitation and the acrosome reaction. {ECO:0000250|UniProtKB:O75969}. | Mus musculus (Mouse) |
O88989 | MDHC_RAT | MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLQDVIATDKEEVAFKDLDVAVLVGSMPRREGMERKDLLKANVKIFKSQGAALEKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKSQIALKLGVTADDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFITTVQQRGAAVIKARKLSSAMSAAKAISDHIRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKEL... | 1.1.1.37; 1.1.1.96 | null | malate metabolic process [GO:0006108]; NAD metabolic process [GO:0019674]; NADH metabolic process [GO:0006734]; NADP metabolic process [GO:0006739]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | hydroxyphenylpyruvate reductase activity [GO:0047995]; L-malate dehydrogenase activity [GO:0030060]; malate dehydrogenase activity [GO:0016615]; NAD binding [GO:0051287] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 2 family | PTM: ISGylated. {ECO:0000250|UniProtKB:P40925}.; PTM: Acetylation at Lys-118 dramatically enhances enzymatic activity and promotes adipogenic differentiation. {ECO:0000250|UniProtKB:P40925}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P40925}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000250|UniProtKB:P40925}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21433; Evidence={... | null | null | null | null | FUNCTION: Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH. Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation. Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate, leading t... | Rattus norvegicus (Rat) |
O88990 | ACTN3_MOUSE | MMMVMQPEGLGAGEGPFSGGGGGEYMEQEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRNGLKLMLLLEVISGERLPRPDKGKMRFHKIANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKMLDAEDIVNTPKPDEKAIMTYVSCFYHAFAGAEQAETAANRICKVLAVNQENEKLMEEYEKLASELLEWIRRTVPWLENRVGEPSMS... | null | null | actin cytoskeleton organization [GO:0030036]; bone morphogenesis [GO:0060349]; focal adhesion assembly [GO:0048041]; muscle cell development [GO:0055001]; muscle contraction [GO:0006936]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of cold-induced thermogenesis [GO:012016... | brush border [GO:0005903]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; sarcomere [GO:0030017]; striated muscle thin filament [GO:0005865]; Z disc [GO:0030018] | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; transmembrane transporter binding [GO:0044325] | PF00307;PF08726;PF00435; | 1.20.58.60;1.10.418.10;1.10.238.10; | Alpha-actinin family | null | null | null | null | null | null | null | FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
O88992 | C1QRF_MOUSE | MLLVLVVLIPVLVSSGGPDGHYEMLGTCRMVCDPYPARGPGAGARSDGGDALSEQSGAPPPSTLVQGPQGKPGRTGKPGPPGPPGDRGPPGPVGPPGEKGEPGKPGPPGLPGSGGSGAISTATYTTVPRVAFYAGLKNPHEGYEVLKFDDVVTNLGNNYDAASGKFTCNIPGTYFFTYHVLMRGGDGTSMWADLCKNGQVRASAIAQDADQNYDYASNSVILHLDAGDEVFIKLDGGKAHGGNSNKYSTFSGFIIYSD | null | null | maintenance of synapse structure [GO:0099558]; motor learning [GO:0061743]; neuron remodeling [GO:0016322]; regulation of synapse pruning [GO:1905806] | cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; climbing fiber [GO:0044301]; collagen trimer [GO:0005581]; cytoplasm [GO:0005737]; presynapse [GO:0098793]; synaptic cleft [GO:0043083] | signaling receptor binding [GO:0005102] | PF00386;PF01391; | 2.60.120.40;1.20.5.320; | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses. {ECO:0000269|PubMed:21262840}. | Mus musculus (Mouse) |
O88998 | NOE1_MOUSE | MSVPLLKIGVVLSTMAMITNWMSQTLPSLVGLNTTRLSAASGGTLDRSTGVLPTNPEESWQVYSSAQDSEGRCICTVVAPQQTMCSRDARTKQLRQLLEKVQNMSQSIEVLDRRTQRDLQYVEKMENQMKGLETKFKQVEESHKQHLARQFKAIKAKMDELRPLIPVLEEYKADAKLVLQFKEEVQNLTSVLNELQEEIGAYDYDELQSRVSNLEERLRACMQKLACGKLTGISDPVTVKTSGSRFGSWMTDPLAPEGDNRVWYMDGYHNNRFVREYKSMVDFMNTDNFTSHRLPHPWSGTGQVVYNGSIYFNKFQSHII... | null | null | atrioventricular valve formation [GO:0003190]; cardiac epithelial to mesenchymal transition [GO:0060317]; negative regulation of gene expression [GO:0010629]; neuronal signal transduction [GO:0023041]; positive regulation of apoptotic process [GO:0043065]; positive regulation of epithelial to mesenchymal transition [GO... | AMPA glutamate receptor complex [GO:0032281]; axon [GO:0030424]; axonal growth cone [GO:0044295]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; extrinsic component of synaptic membrane [GO:0099243]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; syn... | null | PF12308;PF02191; | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22923615, ECO:0000305|PubMed:22632720}. Synapse {ECO:0000305|PubMed:22632720}. Endoplasmic reticulum {ECO:0000269|PubMed:22923615}. Cell projection, axon {ECO:0000269|PubMed:22923615, ECO:0000269|PubMed:26107991}. Perikaryon {ECO:0000269|PubMed:22923615}.; SUBCELLULAR ... | null | null | null | null | null | FUNCTION: Contributes to the regulation of axonal growth in the embryonic and adult central nervous system by inhibiting interactions between RTN4R and LINGO1. Inhibits RTN4R-mediated axon growth cone collapse (PubMed:22923615). May play an important role in regulating the production of neural crest cells by the neural... | Mus musculus (Mouse) |
O89000 | DPYD_RAT | MAGVLSRDAPDIESILALNPRIQAHATLRSTMAKKLDKKHWKRNTDKNCFICEKLENNFDDIKHTTLGERGALREAVRCLKCADAPCQKSCPTSLDIKSFITSIANKNYYGAAKLIFSDNPLGLTCGMVCPTSDLCVGGCNLHATEEGPINIGGLQQFATEVFKAMNIPQIRSPLLPPPEHMPEAYSAKIALFGAGPASISCASFLARLGYSDITIFEKQEYVGGLSTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSISTDEMTLSTLKENGYKAAFIGIGLPEPKKDHIFQGLTQVQGFYTSKDFLPLVAKGSKPG... | 1.3.1.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q28943}; Note=Binds 2 FAD. {ECO:0000250|UniProtKB:Q28943}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:Q28943}; Note=Binds 2 FMN. {ECO:0000250|UniProtKB:Q28943}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:... | beta-alanine biosynthetic process [GO:0019483]; circadian rhythm [GO:0007623]; CMP catabolic process [GO:0006248]; dCMP catabolic process [GO:0006249]; dUMP catabolic process [GO:0046079]; purine nucleobase catabolic process [GO:0006145]; pyrimidine nucleobase catabolic process [GO:0006208]; response to glucocorticoid ... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | 4 iron, 4 sulfur cluster binding [GO:0051539]; dihydropyrimidine dehydrogenase (NADP+) activity [GO:0017113]; FAD binding [GO:0071949]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]; uracil binding [GO:0002058] | PF01180;PF14691;PF14697;PF07992; | 3.30.70.20;3.20.20.70;1.10.1060.10;3.50.50.60; | Dihydropyrimidine dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12882}. | CATALYTIC ACTIVITY: Reaction=5,6-dihydrouracil + NADP(+) = H(+) + NADPH + uracil; Xref=Rhea:RHEA:18093, ChEBI:CHEBI:15378, ChEBI:CHEBI:15901, ChEBI:CHEBI:17568, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.2; Evidence={ECO:0000250|UniProtKB:Q12882}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18095; Evidence... | null | PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis. {ECO:0000250|UniProtKB:Q12882}. | null | null | FUNCTION: Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil. {ECO:0000250|UniProtKB:Q12882}. | Rattus norvegicus (Rat) |
O89001 | CBPD_MOUSE | MASGRDERPPWRLGRLRLLPPPPLLLLLLLLRSSAQAAHIKKAEATTTTVGGSEAAEGQFDHYYHEAALGEALEAAAAAGPPGLARLFSIGSSVEGRPLWVLRLTAGLGPPPTAAAGLDAAGPLLPGRPQVKLVGNMHGDETVSRQVLVYLARELASGYRRGDPRLVRLLNTTDVYLLPSLNPDGFERAREGDCGLGDSGPPGTSGRDNSRGRDLNRSFPDQFSTGEPPSLDEVPEVRALIDWIRRNKFVLSGNLHGGSVVASYPFDDSPEHKTTGLYSKTSDDEVFRYLAKAYASNHPIMKTGEPHCPGDEDETFKDGI... | 3.4.17.22 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q90240}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q90240}; | peptide metabolic process [GO:0006518]; protein processing [GO:0016485] | extracellular space [GO:0005615]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | metallocarboxypeptidase activity [GO:0004181]; protein phosphatase 2A binding [GO:0051721]; protein-containing complex binding [GO:0044877]; zinc ion binding [GO:0008270] | PF13620;PF00246; | 2.60.40.1120;3.40.630.10; | Peptidase M14 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q90240}; Single-pass type I membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Releases C-terminal Arg and Lys from polypeptides.; EC=3.4.17.22; | null | null | null | null | null | Mus musculus (Mouse) |
O89016 | ABCD4_MOUSE | MAVPGPTARAGARPRLDLQLVQRFVRIQKVFFPSWSSQNVLMFMTLLCVTLLEQLVIYQVGLIPSQYYGVLGNKDLDGFKALTLLAVTLIVLNSTLKSFDQFTCNLLYVSWRKDLTEHLHHLYFRARVYYTLNVLRDDIDNPDQRISQDVERFCRQLSSVTSKLIISPFTLTYYTYQCFQSTGWLGPVSIFGYFIVGTMVNKTLMGPIVTKLVQQEKLEGDFRFKHMQIRVNAEPAAFYRAGLVEHMRTDRRLQRLLQTQRELMSRELWLYIGINTFDYLGSILSYVVIAIPIFSGVYGDLSPTELSTLVSKNAFVCIYL... | 7.6.2.8 | null | cellular response to leukemia inhibitory factor [GO:1990830]; cobalamin metabolic process [GO:0009235]; cobalamin transport [GO:0015889]; fatty acid beta-oxidation [GO:0006635]; long-chain fatty acid import into peroxisome [GO:0015910]; peroxisome organization [GO:0007031]; very long-chain fatty acid catabolic process ... | endoplasmic reticulum membrane [GO:0005789]; lysosomal membrane [GO:0005765]; peroxisomal membrane [GO:0005778] | ABC-type vitamin B12 transporter activity [GO:0015420]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; identical protein binding [GO:0042802]; long-chain fatty acid transporter activity [GO:0005324] | PF06472;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCD family, Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O14678}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14678}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=an R-cob(III)alamin(out) + ATP + H2O = ADP + an R-cob(III)alamin(in) + H(+) + phosphate; Xref=Rhea:RHEA:17873, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:140785, ChEBI:CHEBI:456216; EC=7.6.2.8; Evidence={ECO:0000250|UniProtKB:O14678}; Physiologic... | null | null | null | null | FUNCTION: Lysosomal membrane protein that transports cobalamin (Vitamin B12) from the lysosomal lumen to the cytosol in an ATP-dependent manner. Targeted by LMBRD1 lysosomal chaperone from the endoplasmic reticulum to the lysosomal membrane. Then forms a complex with lysosomal chaperone LMBRD1 and cytosolic MMACHC to t... | Mus musculus (Mouse) |
O89017 | LGMN_MOUSE | MTWRVAVLLSLVLGAGAVPVGVDDPEDGGKHWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVINRPNGTDVYKGVLKDYTGEDVTPENFLAVLRGDAEAVKGKGSGKVLKSGPRDHVFIYFTDHGATGILVFPNDDLHVKDLNKTIRYMYEHKMYQKMVFYIEACESGSMMNHLPDDINVYATTAANPKESSYACYYDEERGTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSHVMQYGNKSISTMKVMQFQGMKHRASSPISLPPVTHLDLTPSPDVPLTILKRK... | 3.4.22.34 | null | antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; associative learning [GO:0008306]; cellular response to amyloid-beta [GO:1904646]; cellular response to calcium ion [GO:0071277]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; dendritic spine organizat... | apical part of cell [GO:0045177]; extracellular region [GO:0005576]; late endosome [GO:0005770]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; perinuclear region of cytoplasm [GO:0048471] | cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activator activity [GO:0061133]; peptidase activity [GO:0008233] | PF20985;PF01650; | 1.10.132.130;3.40.50.1460; | Peptidase C13 family | PTM: Glycosylated. {ECO:0000305|PubMed:24407422}.; PTM: Activated by autocatalytic processing at pH 4. {ECO:0000250|UniProtKB:Q99538}. | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:21292981, ECO:0000269|PubMed:9742219}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.; EC=3.4.22.34; Evidence={ECO:0000269|PubMed:24407422, ECO:0000269|PubMed:9742219, ECO:0000269|PubMed:9891971}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:9742219}; | null | FUNCTION: Has a strict specificity for hydrolysis of asparaginyl bonds (PubMed:24407422, PubMed:9742219, PubMed:9891971). Can also cleave aspartyl bonds slowly, especially under acidic conditions (PubMed:24407422, PubMed:9742219, PubMed:9891971). Involved in the processing of proteins for MHC class II antigen presentat... | Mus musculus (Mouse) |
O89019 | INVS_MOUSE | MNISEDVLSTGSSLASQVHAAAVNGDKGALQRLIVGNSALRDKEDRFGRTPLMYCVLADRVDCADALLKAGADVNKTDHSRRTALHLAAQKGNYRFMKLLLTRRANWMQKDLEEMTPLHLSTRHRSPKCLALLLKFMAPGEVDTQDKNKQTALHWSAYYNNPEHAKLLIKHDSNIGIPDVEGKIPLHWAANHKDPSAVHTVRCILDAAPTESLLNWQDYEGRTPLHFAVADGNLTVVDVLTSYESCNITSYDNLFRTPLHWAALLGHAQIVHLLLERNKSGTIPSDSQGATPLHYAAQSNFAETVKVFLQHPSVKDDSDL... | null | null | animal organ development [GO:0048513]; embryonic heart tube left/right pattern formation [GO:0060971]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; kidney development [GO:0001822]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; pancreas development [GO... | ciliary base [GO:0097546]; ciliary inversin compartment [GO:0097543]; extracellular region [GO:0005576]; membrane [GO:0016020]; microtubule [GO:0005874]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819] | calmodulin binding [GO:0005516] | PF00023;PF12796;PF00612; | 1.25.40.20; | null | PTM: May be ubiquitinated via its interaction with APC2.; PTM: Hydroxylated at Asn-75, most probably by HIF1AN. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Membrane; Peripheral membrane protein. Nucleus. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle. Note=Associates with several components of the cytoskeleton including ciliary, random and polarized microtubules. During mitosis, it is recruited to ... | null | null | null | null | null | FUNCTION: Required for normal renal development and establishment of left-right axis. Probably acts as a molecular switch between different Wnt signaling pathways. Inhibits the canonical Wnt pathway by targeting cytoplasmic disheveled (DVL1) for degradation by the ubiquitin-proteasome. This suggests that it is required... | Mus musculus (Mouse) |
O89020 | AFAM_MOUSE | MRHLKLTGFIFFLLPLTESLALPTKPQDVDHFNATQKFIDENTTYLAIIAFSQYVQEASFDEVETLVKVMLDYRDRCWADNTLPECSKTANDAIQDMLCDMEGLPQKHNFSHCCGKAGFPRRLCFFYNKKANVGFLPPFPTLDPEEKCQAYKNNSESFLHLYMYEVARRNPFVFAPVLLAVAAWFEEAATTCCEQQQKATCFQAKAAPITQYLKASSSYQRNVCGALIKFGPKVLNSINVAVFSKKFPKIGFKDLTTLLEDVSSMYEGCCEGDVVHCIRSQSQVVNHICSKQDSISSKIKVCCEKKTLEREACIINANKD... | null | null | protein stabilization [GO:0050821]; protein transport within extracellular region [GO:0071693]; vitamin transport [GO:0051180] | blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular space [GO:0005615] | vitamin E binding [GO:0008431] | PF00273; | 1.10.246.10; | ALB/AFP/VDB family | PTM: N-glycosylated; more than 90% of the glycans are sialylated. {ECO:0000250|UniProtKB:P43652}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P43652}. | null | null | null | null | null | FUNCTION: Functions as a carrier for hydrophobic molecules in body fluids. Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B. Binds vitamin E. May transport vitamin E in body fluids under conditions w... | Mus musculus (Mouse) |
O89023 | TPP1_MOUSE | MGLQARLLGLLALVIAGKCTYNPEPDQRWMLPPGWVSLGRVDPEEELSLTFALKQRNLERLSELVQAVSDPSSPQYGKYLTLEDVAELVQPSPLTLLTVQKWLSAAGARNCDSVTTQDFLTCWLSVRQAELLLPGAEFHRYVGGPTKTHVIRSPHPYQLPQALAPHVDFVGGLHRFPPSSPRQRPEPQQVGTVSLHLGVTPSVLRQRYNLTAKDVGSGTTNNSQACAQFLEQYFHNSDLTEFMRLFGGSFTHQASVAKVVGKQGRGRAGIEASLDVEYLMSAGANISTWVYSSPGRHEAQEPFLQWLLLLSNESSLPHVH... | 3.4.14.9 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O14773}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:O14773}; | bone resorption [GO:0045453]; central nervous system development [GO:0007417]; epithelial cell differentiation [GO:0030855]; lysosomal protein catabolic process [GO:1905146]; lysosome organization [GO:0007040]; nervous system development [GO:0007399]; neuromuscular process controlling balance [GO:0050885]; peptide cata... | Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; recycling endosome [GO:0055037] | endopeptidase activity [GO:0004175]; lysophosphatidic acid binding [GO:0035727]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; sulfatide binding [GO:0120146]; tripeptidyl-peptid... | PF00082;PF09286; | 3.40.50.200; | null | PTM: Activated by autocatalytic proteolytical processing upon acidification. N-glycosylation is required for processing and activity (By similarity). {ECO:0000250|UniProtKB:O14773}. | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:19941651}. Melanosome {ECO:0000250|UniProtKB:O14773}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity.; EC=3.4.14.9; Evidence={ECO:0000269|PubMed:28464005}; | null | null | null | null | FUNCTION: Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:28464005). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (By similarity). Requires substrates with an unsubstituted N-terminus (By similarity). {ECO... | Mus musculus (Mouse) |
O89026 | ROBO1_MOUSE | MIAEPAHFYLFGLICLCSGSRLRQEDFPPRIVEHPSDLIVSKGEPATLNCKAEGRPTPTIEWYKGGERVETDKDDPRSHRMLLPSGSLFFLRIVHGRKSRPDEGVYICVARNYLGEAVSHNASLEVAILRDDFRQNPSDVMVAVGEPAVMECQPPRGHPEPTISWKKDGSPLDDKDERITIRGGKLMITYTRKSDAGKYVCVGTNMVGERESEVAELTVLERPSFVKRPSNLAVTVDDSAEFKCEARGDPVPTVRWRKDDGELPKSRYEIRDDHTLKIRKVTAGDMGSYTCVAENMVGKAEASATLTVQEPPHFVVKPRD... | null | null | aorta development [GO:0035904]; aortic valve morphogenesis [GO:0003180]; axon guidance [GO:0007411]; axon midline choice point recognition [GO:0016199]; chemotaxis [GO:0006935]; coronary vasculature development [GO:0060976]; endocardial cushion formation [GO:0003272]; heart development [GO:0007507]; heart induction [GO... | axolemma [GO:0030673]; axon [GO:0030424]; dendrite [GO:0030425]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | axon guidance receptor activity [GO:0008046] | PF00041;PF07679;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, ROBO family | PTM: Ubiquitinated. May be deubiquitinated by USP33. {ECO:0000269|PubMed:19684588}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24560577}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:24560577}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:O55005}; Single-pass membrane protein {ECO:0000250|UniProtKB:O55... | null | null | null | null | null | FUNCTION: Receptor for SLIT1 and SLIT2 that mediates cellular responses to molecular guidance cues in cellular migration, including axonal navigation at the ventral midline of the neural tube and projection of axons to different regions during neuronal development (PubMed:10433822, PubMed:24560577). Interaction with th... | Mus musculus (Mouse) |
O89032 | SPD2A_MOUSE | MLAYCVQDATVVDVEKRRSPSKHYVYIINVTWSDSTSQTIYRRYSKFFDLQMQLLDKFPIEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLKPIDEYCRALVRLPPHISQCDEVFRFFEARPEDVNPPKEDYGSSKRKSVWLSSWAESPKKDVTGADTNAEPMILEQYVVVSNYKKQENSELSLQAGEVVDVIEKNESGWWFVSTSEEQGWVPATYLEAQNGTRDDSDINTSKTGEVSKRRKAHLRRLDRRWTLGGMVNRQHSREEKYVTVQPYTSQSKDEIGFEKGVTVEVIRKNLEGWWYIRYLGKEGWAPASYL... | null | null | in utero embryonic development [GO:0001701]; osteoclast fusion [GO:0072675]; reactive oxygen species metabolic process [GO:0072593]; superoxide anion generation [GO:0042554] | anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; mating projection tip [GO:0043332]; podosome [GO:0002102] | phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:00... | PF00787;PF00018;PF07653; | 3.30.1520.10;2.30.30.40; | SH3PXD2 family | PTM: Tyrosine phosphorylated by SRC. Phosphorylation plays a regulatory role in the protein localization. The intramolecular interaction of the PX domain with the third SH3 domain maintains the protein in the cytoplasm and phosphorylation disrupts this interaction, resulting in the redistribution of the protein from cy... | SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome {ECO:0000250}. Note=Cytoplasmic in normal cells and localizes to podosomes in Src-transformed cells. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Adapter protein involved in invadopodia and podosome formation, extracellular matrix degradation and invasiveness of some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species... | Mus musculus (Mouse) |
O89033 | CDC6_MOUSE | MPQTRSQTQATIGFPKKKLSNTLKKPNSRDCEVKLRNVQPVPTTPCVDVKLLPLSPRKRLGDDNLCNTPRLSPCSPPKLGKKENGPPRSHTWKGCRLVFDDEPTFKASPPKEQDRVRQHQIRSSSAQRSPESKADPEQKCPPEKESVCIRLFKQEGTCYQQAKLVLNTAVPDRLPAREQEMGVIRNFLKEHICGKKAGSLYLSGAPGTGKTACLSRILQDFKKEVKGFKSILLNCMSLRSAQAVFPAIAQEIGREELCRPAGKDLMRKLEKHLTAEKGPMIVLVLDEMDQLDSKGQDVLYTLFEWPWLSNSRLVLIGIAN... | null | null | cell division [GO:0051301]; DNA replication initiation [GO:0006270]; mitotic DNA replication checkpoint signaling [GO:0033314]; positive regulation of fibroblast proliferation [GO:0048146] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; spindle [GO:0005819] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688] | PF13401;PF17872;PF09079; | 1.10.8.60;3.40.50.300;1.10.10.10; | CDC6/cdc18 family | PTM: Ubiquitinated by the SCF(CCNF) E3 ubiquitin-protein ligase complex. {ECO:0000250|UniProtKB:Q99741}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99741}. Cytoplasm {ECO:0000250|UniProtKB:Q99741}. Note=The protein is nuclear in G1 and cytoplasmic in S-phase cells. {ECO:0000250|UniProtKB:Q99741}. | null | null | null | null | null | FUNCTION: Involved in the initiation of DNA replication. Also participates in checkpoint controls that ensure DNA replication is completed before mitosis is initiated. | Mus musculus (Mouse) |
O89035 | DIC_RAT | MAEARTSRWYFGGLASCGAACCTHPLDLLKVHLQTQQEVKLRMTGMALQVVRTDGFLALYNGLSASLCRQMTYSLTRFAIYETMRDYMTKDSQGPLPFYSKVLLGGISGLTGGFVGTPADLVNVRMQNDMKLPLSQRRNYSHALDGLYRVAREEGLKKLFSGATMASSRGALVTVGQLSCYDQAKQLVLSTGYLSDNIFTHFLSSFIAGGCATFLCQPLDVLKTRLMNSKGEYQGVFHCAVETAKLGPQAFFKGLVPAGVRLVPHTVLTFMFLEQLRKHFGIKVAT | null | null | glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; lipid transport [GO:0006869]; malate transmembrane transport [GO:0071423]; malate transport [GO:0015743]; oxaloacetate transport [GO:0015729]; phosphate ion transmembrane transport [GO:0035435]; phosphate ion transport [GO:0006817]; succinate transmembrane t... | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | antiporter activity [GO:0015297]; dicarboxylic acid transmembrane transporter activity [GO:0005310]; malate transmembrane transporter activity [GO:0015140]; oxaloacetate transmembrane transporter activity [GO:0015131]; phosphate ion transmembrane transporter activity [GO:0015114]; secondary active transmembrane transpo... | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:3355813}; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + phosphate(out) = (S)-malate(out) + phosphate(in); Xref=Rhea:RHEA:71607, ChEBI:CHEBI:15589, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:29211846, ECO:0000269|PubMed:3355813, ECO:0000269|PubMed:9733776}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + malonate(out) = (S)-ma... | null | null | null | null | FUNCTION: Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane (PubMed:29211846, PubMed:3355813, PubMed:9733776). Plays an important role in gluc... | Rattus norvegicus (Rat) |
O89038 | MEF2D_RAT | MGRKKIQIQRITDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNHSNKLFQYASTDMDKVLLKYTEYNEPHESRTNADIIETLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGLFRRYGSSVPAPNFAMPVTVPVSNQSSMQFSNPSSSLVTPSLVTSSLTDPRLLSPQQPALQRNSVSPGLPQRPASAGAMLGRDLNSANGACPNPVGNGYVSARASPGLLPVANGNGLNKVIPAKSPPPPTHNTQLGAPSRKPDLRVITSQGGKGLMHHLNNAQRLGVSQSTHSLTTPVVSVATPSLLSQGLPFS... | null | null | adult heart development [GO:0007512]; apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; chondrocyte differentiation [GO:0002062]; endochondral ossification [GO:0001958]; nervous system development [GO:0007399]; osteoblast differentiation [GO:0001649]; positive regulation of DNA-templated transcription ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | 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]; DNA-binding transcription factor binding [GO:0140297]; enzyme bindi... | PF12347;PF00319; | 3.40.1810.10; | null | PTM: Phosphorylated on Ser-430 by CDK5 is required for Lys-425 sumoylation and inhibits transcriptional activity. In neurons, enhanced CDK5 activity induced by neurotoxins promotes caspase 3-mediated cleavage leading to neuron apoptosis. Phosphorylation on Ser-180 can be enhanced by EGF. Phosphorylated and activated by... | SUBCELLULAR LOCATION: Nucleus. Note=Translocated by HDAC4 to nuclear dots. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific, growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays div... | Rattus norvegicus (Rat) |
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