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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O35089 | CNIH2_MOUSE | MAFTFAAFCYMLTLVLCASLIFFVIWHIIAFDELRTDFKNPIDQGNPARARERLKNIERICCLLRKLVVPEYSIHGLFCLMFLCAAEWVTLGLNIPLLFYHLWRYFHRPADGSEVMYDAVSIMNADILNYCQKESWCKLAFYLLSFFYYLYSMVYTLVSF | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; localization within membrane [GO:0051668]; negative regulation of anterograde synaptic vesicle transport [GO:1903743]; negative regulation of receptor localization to synapse [GO:1902684]; regulation of AMPA receptor activity [GO:2000311]; regulati... | AMPA glutamate receptor complex [GO:0032281]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; endoplasmic reticulum membrane [GO:0005789]; glutamatergic synapse [GO:0098978]; postsynaptic density [GO:0014069]; postsynaptic densi... | channel regulator activity [GO:0016247] | PF03311; | null | Cornichon family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:21172611}. Cell projection, dendrite {ECO:0000269|PubMed:21172611}. Cell projection, dendritic spine {ECO:0000269|PubMed:21172611}. Postsynaptic cell membrane {ECO:0000... | null | null | null | null | null | FUNCTION: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. Blocks CACNG8-mediated resensitization of ... | Mus musculus (Mouse) |
O35095 | NCDN_RAT | MSCCDLAAAGQLGKAGIMASDCEPALNQAESRNPTLERYLGALREAKNDSEQFAALLLVTKAVKAGDIDAKTRRRIFDAVGFTFPNRLLTTKEAPDGCPDHVLRALGVALLACFCSDPELASHPQVLNKIPILCTFLTARGDPDDAARRSMIDDTYQCLTAVAGTPRGPRHLIAGGTVSALCQAYLGHGYGFDQALALLVGLLAAAETQCWKEAEPDLLAVLRGLSEDFQRAEDASKFELCQLLPLFLPPTTVPPECHRDLQAGLARILGSKLSSWQRNPALKLAARLAHACGSDWIPVGSSGSKFLALLVNLACVEVRL... | null | null | bone resorption [GO:0045453]; neuron projection development [GO:0031175]; regulation of neuronal synaptic plasticity [GO:0048168] | cytosol [GO:0005829]; dendrite [GO:0030425]; endosome membrane [GO:0010008]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; postsynapse [GO:0098794] | null | PF05536; | null | Neurochondrin family | PTM: Palmitoylated (PubMed:23687301). Palmitoylation by ZDHHC1, ZDHHC3 and ZDHHC11 regulates the association of NCDN with endosome membranes (PubMed:23687301). May also be palmitoylated by ZDHHC7 (PubMed:23687301). {ECO:0000269|PubMed:23687301}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10521593}. Endosome membrane {ECO:0000269|PubMed:23687301}; Lipid-anchor {ECO:0000305|PubMed:23687301}. Cell projection, dendrite {ECO:0000269|PubMed:10521593, ECO:0000269|PubMed:23687301}. Postsynapse {ECO:0000269|PubMed:23687301}. Note=Localizes to somatic ... | null | null | null | null | null | FUNCTION: Probably involved in signal transduction, in the nervous system, via increasing cell surface localization of GRM5 and positively regulating its signaling. Required for the spatial learning process. Acts as a negative regulator of Ca(2+)-calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May play a... | Rattus norvegicus (Rat) |
O35099 | M3K5_MOUSE | MGTEAGEGITFSVPPFASVGFCTIPEGGSCRRGGGAATAAEGEPSLQPLLVPPPPPPPGSFWNVESAAAPGTSCPTTAPGSSATRGRGNSGSGGGRRTTVAYVINEASQGQLVVAESEALQSLREACEAVGATLETLHFGKLDFGETAVLDRFYNADIAVVEMSDAFRQPSLFYHLGVRESFSMANNIILYCDTNSDSLQSLKEIICQKNTVCTGNYTFIPYMVTPHNKVYCCDSSFMKGLTELMQPNFELLLGPICLPLVDRFVQLLKVAQASSSQYFRESILSDIRKARNLYTGKELAAELARIRQRVDNIEVLTADI... | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cellular response to amino acid starvation [GO:0034198]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to reactive nitrogen species [GO:1902170]; cellular response to tumor necrosis factor [GO:0071356]; endothelial cell apoptotic process [GO:0072577]; innate immune response [GO:0045087]; intrin... | external side of plasma membrane [GO:0009897]; IRE1-TRAF2-ASK1 complex [GO:1990604]; protein kinase complex [GO:1902911] | ATP binding [GO:0005524]; JUN kinase kinase kinase activity [GO:0004706]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; protein domain specific binding [GO:0019904]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein phosphatase binding [GO... | PF19039;PF20309;PF20302;PF13281;PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | PTM: Ser-90 and Ser-1040 are inactivating phosphorylation sites, the former of which is phosphorylated by AKT1 (By similarity). Phosphorylated at Ser-973 which induces association of MAP3K5/ASK1 with the 14-3-3 family proteins and suppresses MAP3K5/ASK1 activity (PubMed:16648474). Calcineurin (CN) dephosphorylates this... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99683}. Endoplasmic reticulum {ECO:0000250}. Note=Interaction with 14-3-3 proteins alters the distribution of MAP3K5/ASK1 and restricts it to the perinuclear endoplasmic reticulum region. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000269|PubMed:16648474}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucia... | Mus musculus (Mouse) |
O35111 | KCNK3_MOUSE | MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPEMIERQRLELRQLELRARYNLSEGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVRYLLHRAKRGLGMRHAEVSMANMVLIGFVSCISTLCIGAAAFSYYERWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTHNGQAVGLGGLSCLSGSLGDGVRPRDPVTCAAAAGGVGVGVGGSGFRNVYAEVLH... | null | null | cellular response to hypoxia [GO:0071456]; cellular response to zinc ion [GO:0071294]; cochlea development [GO:0090102]; negative regulation of cytosolic calcium ion concentration [GO:0051481]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of resting membrane poten... | plasma membrane [GO:0005886] | open rectifier potassium channel activity [GO:0005252]; outward rectifier potassium channel activity [GO:0015271]; potassium ion leak channel activity [GO:0022841]; S100 protein binding [GO:0044548] | PF07885; | 1.10.287.70; | Two pore domain potassium channel (TC 1.A.1.8) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14649}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14649}. | null | null | null | null | null | FUNCTION: pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward.... | Mus musculus (Mouse) |
O35112 | CD166_RAT | MASKGSPSCRLVFCLLISAAVLRPGLGWYTVNSAYGDTIVMPCRLDVPQNLMFGKWKYEKPDGSPVFIAFRSSTKKSVQYDDVPEYKDRLSLSENYTLSINNAKISDEKRFVCMLVTEDNVFEAPTLVKVFKQPSKPEIVNRAAFLETEQLKKLGDCISRDSYPDGNITWYRNGKVLQPVDGEVSILFKKEIDPGTQLYTMTSSLEYKTTKSDIQMPFTCSVTYYGPSGQKTIYSEQAIFDIYYPTEQVTIQVLPPKNAIKEGDNITLQCLGNGNPPPEEFMFYLPGQAEGIRSSNTYTLTDVRRNATGDYKCSLIDQRN... | null | null | adaptive immune response [GO:0002250]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; motor neuron axon guidance [GO:0008045]; neuron projection extension [GO:1990138... | axon [GO:0030424]; dendrite [GO:0030425]; external side of plasma membrane [GO:0009897]; immunological synapse [GO:0001772]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; T cell receptor complex [GO:0042101] | identical protein binding [GO:0042802] | PF08205;PF13927; | 2.60.40.10; | null | PTM: The N-terminus is blocked.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q13740}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q61490}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q61490}. Cell projection, axon {ECO:0000250|UniProtKB:Q61490}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61490}. Note=Detected at the immunological synapse, i.e, at the contact zone bet... | null | null | null | null | null | FUNCTION: Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts. Promotes T-cell activation and proliferation via its interactions with CD6 (By similarity). Contributes to the formation and maturation of the immunological synapse v... | Rattus norvegicus (Rat) |
O35114 | SCRB2_MOUSE | MGRCCFYTAGTLSLLLLVTSVTLLVARVFQKAVDQTIEKNMVLQNGTKVFNSWEKPPLPVYIQFYFFNVTNPEEILQGEIPLLEEVGPYTYRELRNKANIQFGENGTTISAVTNKAYVFERNQSVGDPNVDLIRTINIPLLTVVDLAQLTLLRELIEAMLKAYQQKLFVIHTVHELLWGYKDEILSLVHIFKPDVSPNFGLFYERNGTNDGEYVFLTGEDNYLNFSKIVEWNGKTSLDWWTTDTCNMINGTDGDSFHPLISKDEVLYLFPSDLCRSVHITFSSFENVEGLPAFRYKVPAEILANTSENAGFCIPEGNCMD... | null | null | aminophospholipid transport [GO:0015917]; endosome to plasma membrane protein transport [GO:0099638]; positive regulation of neuron projection development [GO:0010976]; protein targeting to lysosome [GO:0006622]; receptor-mediated endocytosis [GO:0006898]; regulation of carbohydrate catabolic process [GO:0043470]; regu... | cytoplasm [GO:0005737]; endocytic vesicle membrane [GO:0030666]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886] | cargo receptor activity [GO:0038024]; cholesterol binding [GO:0015485]; enzyme binding [GO:0019899]; phosphatidylcholine binding [GO:0031210]; phosphatidylserine binding [GO:0001786]; protein homodimerization activity [GO:0042803]; protein-folding chaperone binding [GO:0051087]; scavenger receptor activity [GO:0005044] | PF01130; | null | CD36 family | PTM: Acylated by palmitic acid group(s). {ECO:0000250}.; PTM: Heavily glycosylated. {ECO:0000269|PubMed:19349973}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}; Multi-pass membrane protein {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}. | null | null | null | null | null | FUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting. {ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:24162852}. | Mus musculus (Mouse) |
O35115 | FHL2_RAT | MTERFDCHHCNESLYGKKYILKEENPHCVACFEELYANTCEECGTPIGCDCKDLSYKDRHWHEGCFHCSRCGSSLVDKPFAAKEEQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFTCQRCQQPIGTKSFIPKENQNFCVPCYEKQYALQCVQCKKPITTGGVTYRDQPWHRECFVCTACKKQLSGQRFTARDEFPYCLTCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI | null | null | atrial cardiac muscle cell development [GO:0055014]; heart trabecula formation [GO:0060347]; negative regulation of apoptotic process [GO:0043066]; negative regulation of calcineurin-NFAT signaling cascade [GO:0070885]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast differentiation [... | M band [GO:0031430]; nucleus [GO:0005634]; Z disc [GO:0030018] | bHLH transcription factor binding [GO:0043425]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134] | PF00412; | 2.10.110.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14192}. Nucleus {ECO:0000250|UniProtKB:Q14192}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22851699}. | null | null | null | null | null | FUNCTION: May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 wit... | Rattus norvegicus (Rat) |
O35116 | CTND2_RAT | FPSVQSNAAAYLQHLCFGDNKIKAEIRRQGGIQLLVDLLDHRMTEVHRSACGALRNLVYGKANDDNKIALKNCGGIPALVRLLRKTTDLEIRELVTGVLWNLSSCDALKMPIIQDALAVLTNAVIIPHSGWENSPLQDDRKIQLHSSQVLRNATGCLRNVSSAGEEARRRMRECDGLTDALLYVIQSALGSSEIDSKTVENCVCILRNLSYRLAAETSQGQHMGTDELDGLLCGEANGKDAESSGCWGKKKKKKKSQDQWDGVG | null | null | cell-cell adhesion [GO:0098609]; cell-cell junction assembly [GO:0007043]; dendritic spine morphogenesis [GO:0060997]; learning [GO:0007612]; morphogenesis of a branching structure [GO:0001763]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of postsynaptic membrane neurotransmitter receptor lev... | adherens junction [GO:0005912]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069] | beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; structural constituent of postsynaptic density [GO:0098919] | PF00514; | 1.25.10.10; | Beta-catenin family | PTM: O-glycosylated. {ECO:0000250}.; PTM: Phosphorylated by CDK5 (PubMed:17009320). Phosphorylated by GSK3B (By similarity). {ECO:0000250|UniProtKB:O35927, ECO:0000269|PubMed:17009320}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O35927}. Cell junction, adherens junction {ECO:0000250|UniProtKB:O35927}. Cell projection, dendrite {ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:20623542}. Perikaryon {ECO:0000269|PubMed:17009320, ECO:0000269|PubMed:20623542}. | null | null | null | null | null | FUNCTION: Has a critical role in neuronal development, particularly in the formation and/or maintenance of dendritic spines and synapses (PubMed:25807484). Involved in the regulation of canonical Wnt signaling (By similarity). It probably acts on beta-catenin turnover, facilitating beta-catenin interaction with GSK3B, ... | Rattus norvegicus (Rat) |
O35118 | GFRA3_MOUSE | MGLSWSPRPPLLMILLLVLSLWLPLGAGNSLATENRFVNSCTQARKKCEANPACKAAYQHLGSCTSSLSRPLPLEESAMSADCLEAAEQLRNSSLIDCRCHRRMKHQATCLDIYWTVHPARSLGDYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLHDKCDRLRKAYGEACSGIRCQRHLCLAQLRSFFEKAAESHAQGLLLCPCAPEDAGCGERRRNTIAPSCALPSVTPNCLDLRSFCRADPLCRSRLMDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFISKVNTTVALSCTCRGSGN... | null | null | axon guidance [GO:0007411]; glial cell-derived neurotrophic factor receptor signaling pathway [GO:0035860]; nervous system development [GO:0007399]; neuron development [GO:0048666]; neuron migration [GO:0001764]; sympathetic nervous system development [GO:0048485]; transmembrane receptor protein tyrosine kinase signali... | cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235] | axon guidance receptor activity [GO:0008046]; coreceptor activity [GO:0015026]; glial cell-derived neurotrophic factor receptor activity [GO:0016167]; signaling receptor activity [GO:0038023] | PF02351; | 1.10.220.110; | GDNFR family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O60609}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O60609}. | null | null | null | null | null | FUNCTION: Receptor for artemin (ARTN), a growth factor that supports the survival of sensory and sympathetic peripheral neurons. ARTN-binding leads to autophosphorylation and activation of the RET receptor. {ECO:0000250|UniProtKB:O60609}. | Mus musculus (Mouse) |
O35119 | TRPC4_RAT | MAQFYYKRNVNAPYRDRIPLRIVRAESELSPSEKAYLNAVEKGDYASVKKSLEEAEIYFKININCIDPLGRTALLIAIENENLELIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKKPSGEKQVPPILLDKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPRPHEVRCNCVECVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKSEYEELSRQCKQFAKDLLDQTRSSRELEIILNYRDDNSLIEEQSGNDLARLKLAIKYRQKEFVAQPNCQQLLASRWYDEFPG... | null | null | calcium ion import [GO:0070509]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; gamma-aminobutyric acid secretion [GO:0014051]; oligodendrocyte differentiation [GO:0048709]; positive regulation of store-operated calcium entry [GO:0106129]; regulation of action potential firing rat... | basolateral plasma membrane [GO:0016323]; calcium channel complex [GO:0034704]; cation channel complex [GO:0034703]; caveola [GO:0005901]; cell surface [GO:0009986]; cortical cytoskeleton [GO:0030863]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; calcium channel activity [GO:0005262]; inositol 1,4,5 trisphosphate binding [GO:0070679]; store-operated calcium channel activity [GO:0015279] | PF00023;PF12796;PF00520;PF08344; | 1.25.40.20; | Transient receptor (TC 1.A.4) family, STrpC subfamily, TRPC4 sub-subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Thought to form non-selective a receptor-activated calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Has also be... | Rattus norvegicus (Rat) |
O35126 | ATN1_MOUSE | MKTRQNKDSMSMRSGRKKEAPGPREELRSRGRASPGGVSTSSSDGKAEKSRQTAKKARIEEPSAPKASKQGRSEEISESESEETSAPKKTKTEQELPRPQSPSDLDSLDGRSINDDGSSDPRDIDQDNRSTSPSIYSPGSVENDSDSSSGLSQGPARPYHPPPLFPPSPPPPDSTPRQPESGFEPHPSVPPTGYHAPMEPPTSRLFQGPPPGAPPTHPQLYPGNASGGVLSGPPMGPKGGAAASSVGAPSGGKQHPPPTTPIPISSSGASGAPPAKPPSAPVGGGSLPSAPPPASFPHVTPNLPPPPALRPLNNASASPP... | null | null | cell killing [GO:0001906]; cell migration [GO:0016477]; determination of adult lifespan [GO:0008340]; maintenance of cell polarity [GO:0030011]; male gonad development [GO:0008584]; multicellular organism growth [GO:0035264]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron apoptotic proce... | anchoring junction [GO:0070161]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | JUN kinase binding [GO:0008432]; protein domain specific binding [GO:0019904]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714] | PF03154; | null | null | PTM: Phosphorylated in vitro by MAPK8/JNK1 on Ser-724. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P54258}. Cell junction {ECO:0000250|UniProtKB:P54258}. Nucleus {ECO:0000250|UniProtKB:P54258}. Note=Shuttles between nucleus and cytoplasm. Colocalizes with FAT1 in the perinuclear area, at cell-cell junctions and leading edges of cells. Colocal... | null | null | null | null | null | FUNCTION: Transcriptional corepressor. Corepressor of MTG8 transcriptional repression. Has some intrinsic repression activity which is independent of the number of the poly-Q repeats (By similarity). Recruits NR2E1 to repress transcription. Promotes vascular smooth cell (VSMC) migration and orientation. {ECO:0000250|Un... | Mus musculus (Mouse) |
O35129 | PHB2_MOUSE | MAQNLKDLAGRLPAGPRGMGTALKLLLGAGAVAYGVRESVFTVEGGHRAIFFNRIGGVQQDTILAEGLHFRIPWFQYPIIYDIRARPRKISSPTGSKDLQMVNISLRVLSRPNAQELPSMYQRLGLDYEERVLPSIVNEVLKSVVAKFNASQLITQRAQVSLLIRRELTERAKDFSLILDDVAITELSFSREYTAAVEAKQVAQQEAQRAQFLVEKAKQEQRQKIVQAEGEAEAAKMLGEALSKNPGYIKLRKIRAAQNISKTIATSQNRIYLTADNLVLNLQDESFTRGSDSLIKGKK | null | null | activation of phospholipase C activity [GO:0007202]; activation of protein kinase C activity [GO:1990051]; antiviral innate immune response [GO:0140374]; B cell activation [GO:0042113]; CD40 signaling pathway [GO:0023035]; cell migration [GO:0016477]; cellular response to hypoxia [GO:0071456]; cellular response to reti... | axon [GO:0030424]; cell surface [GO:0009986]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; inner mitochondrial membrane protein complex [GO:0098800]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrial prohibitin complex [GO:0035632]; mitochondrion... | amide binding [GO:0033218]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; sphingolipid binding [GO:0046625] | PF01145; | 3.30.479.30; | Prohibitin family | PTM: Phosphorylated. Tyrosine phosphorylation is indirectly stimulated by IGFBP6. {ECO:0000250|UniProtKB:Q99623}. | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11302691, ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:24856930}. Cytoplasm {ECO:0000269|PubMed:15140878}. Nucleus {ECO:0000269|PubMed:15140878, ECO:0000269|PubMed:20959514}. Cell membrane {ECO:0000250|UniProtKB:Q99623}. | null | null | null | null | null | FUNCTION: Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors and sex steroid hormones in the nucleus. {ECO:0000269|PubMed... | Mus musculus (Mouse) |
O35130 | NEP1_MOUSE | MSAASGGFQPRERRFSVQEQDWETTPPKKLRLGAGSKCGGRRLIVVLEGASLETVKVGKTYELLNCDRHKSMLLKNGRDPGEVRPDITHQSLLMLMDSPLNRAGLLQVYIHTQKNVLIEVNPQTRIPRTFDRFCGLMVQLLHKLSVRAADGPQKLLKVIKNPVSDHFPVGCMKIGTSFSVEDISDIRELVPSSDPVVFVVGAFAHGKVSVEYTEKMVSISNYPLSAALTCAKVTTAFEEVWGVI | 2.1.1.- | null | blastocyst development [GO:0001824]; nucleologenesis [GO:0017126]; ribosomal small subunit biogenesis [GO:0042274]; rRNA base methylation [GO:0070475] | chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040] | identical protein binding [GO:0042802]; rRNA (pseudouridine) methyltransferase activity [GO:0070037]; rRNA binding [GO:0019843] | PF03587; | 3.40.1280.10; | Class IV-like SAM-binding methyltransferase superfamily, RNA methyltransferase NEP1 family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92979}. | CATALYTIC ACTIVITY: Reaction=pseudouridine(1248) in human 18S rRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylpseudouridine(1248) in human 18S rRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:46712, Rhea:RHEA-COMP:11638, Rhea:RHEA-COMP:11639, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:65314... | null | null | null | null | FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at t... | Mus musculus (Mouse) |
O35132 | CP27B_RAT | MTQAVKLASRVFHRVQLPSQLGSDSVLRSLSDIPGPSTPSFLAELFCKGGLSRLHELQVHGAARYGPIWSGSFGTLRTVYVADPALVEQLLRQESHCPERCSFSSWSEHRRRHQRACGLLTADGEEWQRLRSLLAPLLLRPQAAAGYAGTLDSVVSDLVRRLRRQRGRGSGLPDLVLDVAGEFYKFGLEGIGAVLLGSRLGCLEAEVPPDTETFIEAVGSVFVSTLLTMAMPSWLHRLIPGPWARLCRDWDQMFAFAQKHVEQREGEAAVRNQGKPEEDLPTGHHLTHFLFREKVSVQSIVGNVTELLLAGVDTVSNTLS... | 1.14.15.18 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | bone mineralization [GO:0030282]; C21-steroid hormone biosynthetic process [GO:0006700]; calcitriol biosynthetic process from calciol [GO:0036378]; calcium ion homeostasis [GO:0055074]; calcium ion transport [GO:0006816]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol metabolic process [GO:0008... | cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | calcidiol 1-monooxygenase activity [GO:0004498]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; secalciferol 1-monooxygenase activity [GO:0062185] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion membrane. | CATALYTIC ACTIVITY: Reaction=calcidiol + 2 H(+) + O2 + 2 reduced [adrenodoxin] = calcitriol + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:20573, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17823, ChEBI:CHEBI:17933, ChEBI:CHEBI:33737, ChEBI:CHEBI:3373... | null | PATHWAY: Hormone biosynthesis; cholecalciferol biosynthesis. | null | null | FUNCTION: Catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)(2)D3), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). Is also active with 25-hydroxy-24-oxo-vitamin D3. Plays an important role in norm... | Rattus norvegicus (Rat) |
O35134 | RPA1_MOUSE | MLASKHTPWRRLQGISFGMYSAEELKKLSVKSITNPRYVDYLGNPSANGLYDLALGPADSKEVCATCVQDFNNCSGHLGHIDLPLTVYNPFLFDKLYLLLRGSCLSCHMLTCPRAAIYLLISQLRVLEVGALQAVYELERILSRFLEETGDPSAFEIQEELEEYTSKILQNNLLGSQGTHVKNVCESRSKLVAQFWKTHMAAKQCPHCKTGRSVVRKEHNSKLIITYPATVHKKSDQEGTELPEGVPEAPGIDKAQMGKRGYLTPSSAQEHLFAIWKNEGFFLNYLFSGLDDIGPESSFNPSMFFLDFIVVPPSRYRPVN... | 2.7.7.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O95602}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:O95602}; | negative regulation of protein localization to nucleolus [GO:1904750]; rRNA transcription [GO:0009303] | chromosome [GO:0005694]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase I complex [GO:0005736] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; DNA/RNA hybrid binding [GO:0071667]; magnesium ion binding [GO:0000287]; RNA polymerase I activity [GO:0001054]; zinc ion binding [GO:0008270] | PF04997;PF00623;PF04983;PF05000;PF04998; | 1.10.132.30;1.10.357.120;2.40.40.20;3.30.70.2850;6.10.250.2940;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: Phosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:O95602}. Chromosome {ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:O95602, ECO:0000269|PubMed:10589839}; PhysiologicalDire... | null | null | null | null | FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (By similarity... | Mus musculus (Mouse) |
O35136 | NCAM2_MOUSE | MSLLLSFYLLGLLVRSGQALLQVTISLSKVELSVGESKFFTCTAIGEPESIDWYNPQGEKIISTQRVMLQKEGVRSRLTIYNANIEDAGIYRCQATDAKGQTQEATVVLEIYQKLTFREVVSPQEFKQGEDAEVVCRVSSSPAPAVSWLYHNEEVTTIPDNRFAVLANNNLQILNINKSDEGIYRCEGRVEARGEIDFRDIIVIVNVPPAIMMPQKSFNATAERGEEMTLTCKASGSPDPTISWFRNGKLIEENEKYILKGSNTELTVRNIINKDGGSYVCKATNKAGEDQKQAFLQVFVQPHILQLKNETTSENGHVTL... | null | null | axonal fasciculation [GO:0007413]; cell adhesion [GO:0007155] | axon [GO:0030424]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | identical protein binding [GO:0042802] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform Short]: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | null | null | FUNCTION: May play important roles in selective fasciculation and zone-to-zone projection of the primary olfactory axons. | Mus musculus (Mouse) |
O35137 | ALX4_MOUSE | MNAETCVSYCESPAAAMDAYYSPVSQSREGSSPFRGFPGGDKFGTTFLSAGAKGQGFGDAKSRARYGAGQQDLAAPLESSSGARGSFNKFQPQPPTPQPPPAPPAPPAHLYLQRGACKTPPDGSLKLQEGSGGHNAALQVPCYAKESNLGEPELPPDSEPVGMDNSYLSVKETGAKGPQDRASAEIPSPLEKTDSESNKGKKRRNRTTFTSYQLEELEKVFQKTHYPDVYAREQLAMRTDLTEARVQVWFQNRRAKWRKRERFGQMQQVRTHFSTAYELPLLTRAENYAQIQNPSWIGNNGAASPVPACVVPCDPVPACM... | null | null | anterior/posterior pattern specification [GO:0009952]; digestive tract development [GO:0048565]; embryonic digit morphogenesis [GO:0042733]; embryonic forelimb morphogenesis [GO:0035115]; embryonic hindlimb morphogenesis [GO:0035116]; embryonic skeletal system morphogenesis [GO:0048704]; hair follicle development [GO:0... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; HMG box domain binding [GO:0071837]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565] | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor involved in skull and limb development. | Mus musculus (Mouse) |
O35142 | COPB2_RAT | MPLRLDIKRKLTAMSDRVKSVDLHPTEPWMLASLYNGSVCVWNHETQTLVKTFEVCDLPVRAAKFVARKNWVVTGADDMQIRVFNYNTLERVHMFEAHSDYIRCIAVHPTQPFILTSSDDMLIKLWDWDKKWSCSQVFEGHTHYVMQIVINPKDNNQFASASLDRTIKVWQLGSSSPNFTLEGHEKGVNCIDYYSGGDKPYLISGADDRLVKIWDYQNKTCVQTPEGHAQNVSCATFHPELPIIITGSEDGTVRIWHSSTYRLESTLNYGMERVWCVASLRGSNNVALGYDEGSIIVKLGREEPAMSMDANGKIIWAKHS... | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890] | COPI vesicle coat [GO:0030126]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | protein kinase C binding [GO:0005080]; structural molecule activity [GO:0005198] | PF04053;PF00400; | 1.25.40.470;2.130.10.10; | WD repeat COPB2 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus membrane {ECO:0000269|PubMed:17360540}; Peripheral membrane protein {ECO:0000269|PubMed:17360540}; Cytoplasmic side {ECO:0000269|PubMed:17360540}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:000... | null | null | null | null | null | FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membra... | Rattus norvegicus (Rat) |
O35143 | ATIF1_MOUSE | MAGSALAVRARFGVWGMKVLQTRGFVSDSSDSMDTGAGSIREAGGAFGKREKAEEDRYFREKTKEQLAALRKHHEDEIDHHSKEIERLQKQIERHKKKIQQLKNNH | null | null | erythrocyte differentiation [GO:0030218]; heme biosynthetic process [GO:0006783]; mitochondrial depolarization [GO:0051882]; negative regulation of endothelial cell proliferation [GO:0001937]; negative regulation of hydrolase activity [GO:0051346]; positive regulation of autophagy of mitochondrion in response to mitoch... | cell surface [GO:0009986]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991] | angiostatin binding [GO:0043532]; ATPase binding [GO:0051117]; ATPase inhibitor activity [GO:0042030]; calmodulin binding [GO:0005516]; identical protein binding [GO:0042802]; mitochondrial proton-transporting ATP synthase complex binding [GO:0140260] | PF04568; | 1.20.5.500; | ATPase inhibitor family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. | null | null | null | null | null | FUNCTION: Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase e... | Mus musculus (Mouse) |
O35144 | TERF2_MOUSE | MAAGAGTAGPASGPGVVRDPMASQPRKRPSREGGEGGEGERRSNTMAGGGGSSDSSGRAASRRASRSGGRARRGRHEPGLGGAAERGAGEARLEEAVNRWVLKFYFHEALRAFRSSRYRDFRQIRDIMQALLVRPLGKEHTVSRLLRVMQCLSRIEEGENLDCSFDMEAELTPLESAINVLEMIKTEFTLTDSMVESSRKLVKEAAVIICIKNKEFEKASKILKKYMSKDPTTQKLRTDLLNIIREKNLAHPVIQNFSYEVFQQKMLRFLESHLDDTEPYLLTMAKKALKSESAASSTMREEKHPEPVEKPLREPPSRQP... | null | null | anterograde axonal transport [GO:0008089]; axonal transport of messenger ribonucleoprotein complex [GO:0099088]; cell cycle [GO:0007049]; in utero embryonic development [GO:0001701]; negative regulation of cellular senescence [GO:2000773]; negative regulation of gene expression [GO:0010629]; negative regulation of t-ci... | axon cytoplasm [GO:1904115]; chromosome, telomeric region [GO:0000781]; male germ cell nucleus [GO:0001673]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; shelterin complex [GO:0070187]; telomere cap complex [GO:0000782] | double-stranded telomeric DNA binding [GO:0003691]; enzyme binding [GO:0019899]; G-rich strand telomeric DNA binding [GO:0098505]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; telomerase activity [GO:0003720]; telomeric DNA binding [GO:0042162] | PF00249;PF16772;PF08558; | 1.10.10.60;1.25.40.210; | null | PTM: Phosphorylated upon DNA damage, most probably by ATM. Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly localizes to damage sites (By similarity). {ECO:0000250|UniProtKB:Q15554}.; PTM: Methylated by PRMT1 at multiple arginines within the N-terminal Arg-rich region. Methylation may control association... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:20339076}. Chromosome, telomere {ECO:0000269|PubMed:20339076}. Note=Colocalizes with telomeric DNA in interphase cells and is located at chromosome ends during metaphase. {ECO:0000269|PubMed:20339076}. | null | null | null | null | null | FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes (PubMed:20339076, PubMed:20619712, PubMed:20622870, PubMed:28216226). In addition to its telomeric DNA-binding role, required to recruit a number of ... | Mus musculus (Mouse) |
O35147 | BAD_RAT | MGTPKQPSLAPAHALGLRKSDPGIRSLGSDAGGRRWRPAAQSMFQIPEFEPSEQEDASTTDRGLGPSLTEDQPGPYLAPGLLGSIVQQQPGQAANNSHHGGAGTMETRSRHSSYPAGTEEDEGMEEELSPFRGRSRSAPPNLWAAQRYGRELRRMSDEFEGSFKGLPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ | null | null | activation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0006919]; ADP metabolic process [GO:0046031]; apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; ATP metabolic process [GO:0046034]; cellular response to chromate [GO:0071247]; cellular response to hypoxia [GO:00... | BAD-BCL-2 complex [GO:0097138]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | 14-3-3 protein binding [GO:0071889]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; lipid binding [GO:0008289]; phospholipid binding [GO:0005543]; protein kinase B binding [GO:0043422]; protein kinase binding [GO:0019901]; protein phosphatase 2B binding [GO:0030346]; protein ... | PF10514; | null | Bcl-2 family | PTM: Phosphorylated at one or more of Ser-113, Ser-137, Ser-156 and Ser-171 in response to survival stimuli, which blocks its pro-apoptotic activity. Phosphorylation on Ser-137 or Ser-113 promotes heterodimerization with 14-3-3 proteins. This interaction then facilitates the phosphorylation at Ser-156, a site within th... | SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm {ECO:0000250|UniProtKB:Q61337}. Note=Colocalizes with HIF3A in the cytoplasm. Upon phosphorylation, locates to the cytoplasm. {ECO:0000250|UniProtKB:Q61337}. | null | null | null | null | null | FUNCTION: Promotes cell death. Successfully competes for the binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level of heterodimerization of these proteins with BAX. Can reverse the death repressor activity of Bcl-X(L), but not that of Bcl-2 (By similarity). Appears to act as a link between growth factor rec... | Rattus norvegicus (Rat) |
O35149 | ZNT4_MOUSE | MAGPGAWKRLKSLLRKDDTPLFLNDTSAFDFSDEVSDEGLSRFNKLRVVVADDDSEAPERPVNGAHPALQADDDSLLDQDLPLTNSQLSLKMDPCDNCSKRRELLKQRKVKTRLTIAAVLYLLFMIGELVGGYMANSLAIMTDALHMLTDLSAIILTLLALWLSSKSPTRRFTFGFHRLEVLSAMISVMLVYVLMGFLLYEAVQRTIHMNYEINGDVMLITAAVGVAVNVIMGFLLNQSGHHHSHAHSHSLPSNSPSMVSSGHNHGQDSLAVRAAFVHALGDLVQSVGVLIAAYIIRFKPEYKIADPICTYIFSLLVAFT... | null | null | response to toxic substance [GO:0009636]; response to zinc ion [GO:0010043]; zinc export across plasma membrane [GO:0140882]; zinc ion import into lysosome [GO:0140916]; zinc ion transmembrane transport [GO:0071577] | endosome membrane [GO:0010008]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886] | antiporter activity [GO:0015297]; metal ion binding [GO:0046872]; zinc ion transmembrane transporter activity [GO:0005385] | PF01545; | 1.20.1510.10; | Cation diffusion facilitator (CDF) transporter (TC 2.A.4) family, SLC30A subfamily | null | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250|UniProtKB:O55174}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:O14863}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched ... | CATALYTIC ACTIVITY: Reaction=2 H(+)(out) + Zn(2+)(in) = 2 H(+)(in) + Zn(2+)(out); Xref=Rhea:RHEA:72627, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:9354792}; | null | null | null | null | FUNCTION: Probable proton-coupled zinc ion antiporter mediating zinc import from cytoplasm potentially into the endocytic compartment (PubMed:9354792). Controls zinc deposition in milk (PubMed:9354792). {ECO:0000269|PubMed:9354792}. | Mus musculus (Mouse) |
O35152 | BET1L_RAT | MADWTRAQSSGAVEEIVDRENKRMADSLASKVTRLKSLALDIDRDTEDQNRYLDGMDSDFTSVTGLLTGSVKRFSTVARSGRDTRKLLCGMAVVLIVAFFILSYLFSRTRT | null | null | protein transport [GO:0015031]; regulation of retrograde vesicle-mediated transport, Golgi to ER [GO:2000156]; retrograde transport, endosome to Golgi [GO:0042147] | cytosol [GO:0005829]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; Golgi-associated vesicle [GO:0005798]; SNARE complex [GO:0031201]; trans-Golgi network [GO:0005802] | SNAP receptor activity [GO:0005484] | null | 1.20.5.110; | null | null | SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type IV membrane protein. Golgi apparatus, trans-Golgi network membrane. Note=Present throughout the Golgi apparatus, with strongly increasing concentration from cis-Golgi to the trans-Golgi face of the stacks. | null | null | null | null | null | FUNCTION: Vesicle SNARE required for targeting and fusion of retrograde transport vesicles with the Golgi complex. Required for the integrity of the Golgi complex. {ECO:0000269|PubMed:12388752, ECO:0000269|PubMed:14742712}. | Rattus norvegicus (Rat) |
O35158 | CDON_RAT | MHPDLGPLWKLLYVLVILCSSVSSDLATYFISEPLSAVQKLGRPVVLHCSAKPVTARISWLHNGKRLDRNTEQIKIHRGTLTILSLNPSLSGCYQCVANNSVGAVVSGPATVSADALADFDSSTMHVITAEKKNTGFIGCRVPESNPKAEVRYKIRGKWLMYSTGNYIILPSGNLQILNVSSKDKGSYKCAAYNPVTSELKVEPAGRKLLVSRPSSDGFHILHPALSQALAVLPHSPVTLECVVSGVPASQVYWLKDGQDCLSGSNWRRLYSHLATASIDPADSGNYSCVVGNNSSGDVKHVTYTVNVLEHASISKGLHD... | null | null | anterior/posterior pattern specification [GO:0009952]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cell fate specification [GO:0001708]; cell-cell adhesion [GO:0098609]; cerebral cortex development [GO:0021987]; embryonic body morphogenesis [GO:0010172]; embryonic morphogenesis [GO:0048598]; embryonic retin... | axon [GO:0030424]; cell surface [GO:0009986]; plasma membrane [GO:0005886] | cell-cell adhesion mediator activity [GO:0098632] | PF00041;PF07679;PF13927; | 2.60.40.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:9214393}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21802063, ECO:0000269|PubMed:9214393}; Single-pass membrane protein {ECO:0000269|PubMed:21802063, ECO:0000269|PubMed:9214393}. | null | null | null | null | null | FUNCTION: Component of a cell-surface receptor complex that mediates cell-cell interactions between muscle precursor cells. Promotes differentiation of myogenic cells (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
O35160 | PITX3_MOUSE | MEFGLLGEAEARSPALSLSDAGTPHPPLPEHGCKGQEHSDSEKASASLPGGSPEDGSLKKKQRRQRTHFTSQQLQELEATFQRNRYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWRKRERSQQAELCKGGFAAPLGGLVPPYEEVYPGYSYGNWPPKALAPPLAAKTFPFAFNSVNVGPLASQPVFSPPSSIAASMVPSAAAAPGTVPGPGALQGLGGAPPGLAPAAVSSGAVSCPYASAAAAAAAAASSPYVYRDPCNSSLASLRLKAKQHASFSYPAVPGPPPAANLSPCQYAVERPV | null | null | anatomical structure morphogenesis [GO:0009653]; cellular response to glial cell derived neurotrophic factor [GO:1990792]; dopaminergic neuron differentiation [GO:0071542]; lens development in camera-type eye [GO:0002088]; lens fiber cell differentiation [GO:0070306]; lens morphogenesis in camera-type eye [GO:0002089];... | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00046;PF03826; | 1.10.10.60; | Paired homeobox family, Bicoid subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138, ECO:0000269|PubMed:17184956}. | null | null | null | null | null | FUNCTION: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-med... | Mus musculus (Mouse) |
O35161 | CELR1_MOUSE | MAPSSPRVLPALVLLAAAALPALELGAAAWELRVPGGARAFALGPGWSYRLDTTRTPRELLDVSREGPAAGRRLGLGAGTLGCARLAGRLLPLQVRLVARGAPTAPSLVLRARAYGARCGVRLLRRSARGAELRSPAVRSVPGLGDALCFPAAGGGAASLTSVLEAITNFPACSCPPVAGTGCRRGPICLRPGGSAELRLVCALGRAAGAVWVELVIEATSGTPSESPSVSPSLLNLSQPRAGVVRRSRRGTGSSTSPQFPLPSYQVSVPENEPAGTAVIELRAHDPDEGDAGRLSYQMEALFDERSNGYFLIDAATGAV... | null | null | anterior/posterior pattern specification [GO:0009952]; apical protein localization [GO:0045176]; cell-cell adhesion [GO:0098609]; establishment of body hair planar orientation [GO:0048105]; establishment of planar polarity [GO:0001736]; establishment of planar polarity of embryonic epithelium [GO:0042249]; hair follicl... | membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; G protein-coupled receptor activity [GO:0004930] | PF00002;PF00028;PF00008;PF16489;PF01825;PF02793;PF00053;PF02210; | 2.60.120.200;2.60.220.50;2.60.40.60;4.10.1240.10;2.10.25.10;1.20.1070.10;2.170.300.10; | G-protein coupled receptor 2 family, LN-TM7 subfamily | PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor that may have an important role in cell/cell signaling during nervous system formation. | Mus musculus (Mouse) |
O35165 | GOSR2_RAT | MEPLYQQTHKQVHEIQSHMGRLETADKQSVHLVENEIQASIDQIFSHLERLEILSSKEPPNRRQNAKLRVDQLKYDVQHLQTALRNFQHRRQAKEQQERQRDELLSRTFTTNDSDTTIPMDESLQFNSSLQNIHHGMDDLIGGGHSILEGLRAQRLTLKGTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCAVMFLVVQYLT | null | null | intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; nucleoplasm [GO:0005654]; SNARE complex [GO:0031201] | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149] | PF12352; | 1.20.58.400; | GOSR2 family | null | SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:14742712}; Single-pass type IV membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:14742712}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:9094723}. Note=Concentrated most in the intermediate compartment... | null | null | null | null | null | FUNCTION: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network. {ECO:0000269|PubMed:9094723}. | Rattus norvegicus (Rat) |
O35166 | GOSR2_MOUSE | MEPLYQQTNKQVQEIQSHMGRLERADKQSVHLVENEIQASIEQIFSHLERLEILSSKEPLNRRQNAKLRVDQLKYDVQHLQTALRNFQHRRQVREQQERQRDELLSRTFTTNDSDTTIPMDESLQFNSSLHNIHHGMDDLIGGGHSILEGLRAQRLTLKGTQKKILDIANMLGLSNTVMRLIEKRAFQDKYFMIGGMLLTCAVMFLVVQYLT | null | null | endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; nucleoplasm [GO:0005654]; SNARE complex [GO:0031201] | SNAP receptor activity [GO:0005484]; SNARE binding [GO:0000149] | PF12352; | null | GOSR2 family | null | SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:O35165}; Single-pass type IV membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O35165}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35165}. Note=Concentrated most in the intermediate compart... | null | null | null | null | null | FUNCTION: Involved in transport of proteins from the cis/medial-Golgi to the trans-Golgi network. {ECO:0000250|UniProtKB:O35165}. | Mus musculus (Mouse) |
O35167 | COLQ_RAT | MAVLNPMTLGIYLQLFFCSIVSQPTFINSVLPISAALPGLDQKKRGNHKACCLLMPPPPPLFPPPFFRGSRSPLLSPDMKNLLELEASPSPCMQGSLGSPGPPGPQGPPGLPGKAGPKGEKGDLGRPGRKGRPGPPGVPGEPGPVGWPGPEGPRGEKGDVGMMGLPGSRGPMGSKGFPGSRGEKGSRGERGDLGPKGEKGFPGFPGMLGQKGEMGPKGESGIAGHRGPTGRPGKRGKQGQKGDSGIMGPPGKPGPSGQPGRQGPPGPPGPPSAGQLVMGLKGERGFPGPPGRCLCGPPANVNNPSYGDPMYGRGSPRVPA... | null | null | establishment of protein localization to membrane [GO:0090150]; extracellular matrix organization [GO:0030198]; regulation of synaptic assembly at neuromuscular junction [GO:0008582]; skeletal muscle acetylcholine-gated channel clustering [GO:0071340] | basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; heparin binding [GO:0008201]; structural molecule activity [GO:0005198] | PF01391; | null | COLQ family | PTM: The triple-helical tail is stabilized by disulfide bonds at each end. | SUBCELLULAR LOCATION: Synapse {ECO:0000250}. | null | null | null | null | null | FUNCTION: Anchors the catalytic subunits of asymmetric AChE to the synaptic basal lamina. {ECO:0000250}. | Rattus norvegicus (Rat) |
O35173 | KCNS1_MOUSE | MVSEFPGPGSRVPWRPRDEALRVNVGGVRRLLSARALARFPGTRLGRLQAAASEEQARRLCDDYDAAAHEFYFDRHPGFFLGLLHFYRTGHLHVLDELCVFAFGQEADYWGLGENALATCCRARYLERRVARPRAWDEDSDAPSSVDPCPDEISDVQRELARYGAARCGRLRRRLWLTMENPGYSLPSKLFSCVSIGVVLASIAAMCIHSLPEYQAREAAAAVAAVAAGRSAEEVRDDPVLRRLEYFCIAWFSFEVSSRLLLAPSTRNFFCHPLNLIDIVSVLPFYLTLLAGAALGDQRGASGEELGDLGKVVQVFRLMR... | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; regulation of delayed rectifier potassium channel activity [GO:1902259] | perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251]; potassium channel regulator activity [GO:0015459] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, S (TC 1.A.1.2) subfamily, Kv9.1/KCNS1 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9305895}; Multi-pass membrane protein {ECO:0000305}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}. | null | null | null | null | null | FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}. | Mus musculus (Mouse) |
O35174 | KCNS2_MOUSE | MTRQSLWDVSDTDVEDGEIRINVGGFKRRLRSHTLLRFPETRLGRLLLCHSREAILELCDDYDDVQREFYFDRNPELFPYVLHFYHTGKLHVMAELCVFSFSQEIEYWGINEFFIDSCCSYSYHGRKVEPEQEKWDEQSDQESTTSSFDEILAFYNDASKFDGQPLGNFRRQLWLALDNPGYSVLSRVFSVLSILVVLGSIITMCLNSLPDFQIPDSQGNPGEDPRFEIVEHFGIAWFTFELVARFAVAPDFLKFFKNALNLIDLMSIVPFYITLVVNLVVESSPTLANLGRVAQVLRLMRIFRILKLARHSTGLRSLGA... | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; regulation of delayed rectifier potassium channel activity [GO:1902259] | perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076] | voltage-gated potassium channel activity [GO:0005249] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, S (TC 1.A.1.2) subfamily, Kv9.2/KCNS2 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9305895}; Multi-pass membrane protein {ECO:0000305}. Note=May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}. | null | null | null | null | null | FUNCTION: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 (PubMed:9305895). {ECO:0000269|PubMed:9305895}. | Mus musculus (Mouse) |
O35177 | CASL_MOUSE | MWARNLMARALYDNVPECAEELAFRKGDILTVIEQNTGGLEGWWLCSLHGRQGIVPGNRVKLLIGPVQETPGHEQPTPGPMHQTFGQQKLYQVPNSQAASRDTIYQVPPSYQNQGIYQVPTGHGTPEQDVYQVPPSVQRNIGGTNGPLLSKKVITPVRTGHGYVYEYPSRYQKDVYDVPPSHSTQGVYDIPPSSVKGPVFSVPVGEIKPQGVYDIPPTQGVYAIPPSACRDEAGLREKEYDFPPPMKQDGKPDTRPEGVYDIPPTSTKTAGKDLHIKFPCDAPGGVEPMARRHQSFSLHHAPSQLGQSGDTQSDAYDVPR... | null | null | cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell migration [GO:0016477]; cilium disassembly [GO:0061523]; learning or memory [GO:0007611]; lymphocyte migration into lymphoid organs [GO:0097021]; negative regulation of cell migration [GO:0030336]; positive regulation of cell migratio... | basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; immunological synapse [GO:0001772]; lamellipodium [GO:0030027]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005... | protein tyrosine kinase binding [GO:1990782] | PF12026;PF08824;PF14604; | 1.20.120.230;1.20.120.830;2.30.30.40; | CAS family | PTM: Polyubiquitinated by ITCH/AIP4, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q14511}.; PTM: PTK2/FAK1 phosphorylates the protein at the YDYVHL motif (conserved among all cas proteins) following integrin stimulation (By similarity). The SRC family kinases (FYN, SRC, LCK and CRK) are recruited to the p... | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q14511}. Nucleus {ECO:0000250|UniProtKB:Q14511}. Golgi apparatus {ECO:0000250|UniProtKB:Q14511}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q14511}. Cytoplasm {ECO:0000250|UniProtKB:Q14511}. Cell junction, focal adhesion {ECO:0000269|PubMed:... | null | null | null | null | null | FUNCTION: Scaffolding protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion (By similarity). As a focal adhesion protein, plays a role in embryonic fibroblast migration (PubMed:25059660). May play an important role in integrin beta-1 or B cell antigen receptor (BCR... | Mus musculus (Mouse) |
O35179 | SH3G2_RAT | MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDMEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFATGDGTQPNGGLSHTGTPKPAGVQMDQPCCRALYDFEPENEGELGFKEGDIITLT... | null | null | cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; dendrite extension [GO:0097484]; lipid tube assembly [GO:0060988]; membrane bending [GO:0097753]; membrane tubulation [GO:0097749]; negative regulation of blood-brain barrier permeability [GO:1905604]; negative regulation of gene expression [... | basal dendrite [GO:0097441]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; photoreceptor ribbon synapse [GO:0098684]; plasma membrane [GO:0005886... | identical protein binding [GO:0042802]; lipid binding [GO:0008289]; protein kinase binding [GO:0019901]; transmembrane transporter binding [GO:0044325] | PF03114;PF00018; | 1.20.1270.60;2.30.30.40; | Endophilin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9238017, ECO:0000269|PubMed:9341169}. Membrane {ECO:0000269|PubMed:9238017}; Peripheral membrane protein {ECO:0000269|PubMed:9238017}. Early endosome {ECO:0000250|UniProtKB:Q62420}. Presynapse {ECO:0000269|PubMed:9341169}. | null | null | null | null | null | FUNCTION: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes (By similarity). {ECO:0000250|UniProtKB:Q62420, E... | Rattus norvegicus (Rat) |
O35180 | SH3G3_RAT | MSVAGLKKQFHKASQLFSEKISGAEGTKLDEEFLDMEKKIDITSKAVAEILSKATEYLQPNPAYRAKLGMLNTMSKLRGQVKATGYPQTEGLLGDCMLKYGRELGEDSAFGNSLVEVGEALKLMAEVKDSLDINVKQTFIDPLQLLQDKDLKEIGHHLRKLEGRRLDYDYKKKRVGKIPEEEIRQAVEKFEESKELAERSMFNFLENDVEQVSQLAVFVEAALDYHRQSTEILQELQNKLELRIALASQVPRRDYMPKPVNTSSTNANGVEPSSSSKLTGTDIPSDQPCCRGLYDFEPENEGELGFKEGDIITLTNQIDE... | null | null | negative regulation of clathrin-dependent endocytosis [GO:1900186]; positive regulation of neuron differentiation [GO:0045666]; regulation of clathrin-dependent endocytosis [GO:2000369]; synaptic vesicle uncoating [GO:0016191] | acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; glutamatergic synapse [GO:0098978]; postsynaptic density, intracellular component [GO:0099092]; postsynaptic endosome [GO:0098845]; presynapse [GO:0098793] | identical protein binding [GO:0042802]; lipid binding [GO:0008289] | PF03114;PF00018; | 1.20.1270.60;2.30.30.40; | Endophilin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17088211, ECO:0000269|PubMed:9238017}. Early endosome membrane {ECO:0000269|PubMed:17088211}; Peripheral membrane protein {ECO:0000305|PubMed:17088211}. Note=Associated with postsynaptic endosomes in hippocampal neurons. Associated with presynaptic endosomes in olfact... | null | null | null | null | null | FUNCTION: Implicated in endocytosis. May recruit other proteins to membranes with high curvature. {ECO:0000269|PubMed:15066995}. | Rattus norvegicus (Rat) |
O35181 | NRG3_MOUSE | MSEGAAGASPPGAASAAAASAEEGTAAAAAAAAAGGGPDGGGEGAAEPPRELRCSDCIVWNRQQTWLCVVPLFIGFIGLGLSLMLLKWIVVGSVKEYVPTDLVDSKGMGQDPFFLSKPSSFPKAMETTTTTTSTTSPATPSAGGAASSRTPNRISTRLTTITRAPTRFPGHRVPIRASPRSTTARNTAAPPTVLSTTAPFFSSSTPGSRPPMPGAPSTQAMPSWPTAAYATSSYLHDSTPSWTLSPFQDAAAASSSSPSSTSSTTTTPETSTSPKFHTTTYSTERSEHFKPCRDKDLAYCLNDGECFVIETLTGSHKHCR... | null | null | animal organ development [GO:0048513]; chemorepulsion involved in interneuron migration from the subpallium to the cortex [GO:0021842]; ERBB4 signaling pathway [GO:0038130]; ERBB4-ERBB4 signaling pathway [GO:0038138]; intracellular signal transduction [GO:0035556]; mammary gland development [GO:0030879]; mammary placod... | extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; synapse [GO:0045202] | chemorepellent activity [GO:0045499]; growth factor activity [GO:0008083]; receptor ligand activity [GO:0048018] | null | 2.10.25.10; | Neuregulin family | PTM: Proteolytic cleavage close to the plasma membrane on the external face leads to the release of the soluble growth factor form. {ECO:0000250}.; PTM: Extensive glycosylation precedes the proteolytic cleavage. {ECO:0000250}. | SUBCELLULAR LOCATION: [Pro-neuregulin-3, membrane-bound isoform]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Does not seem to be active. {ECO:0000250}.; SUBCELLULAR LOCATION: [Neuregulin-3]: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Direct ligand for the ERBB4 tyrosine kinase receptor. Binding results in ligand-stimulated tyrosine phosphorylation and activation of the receptor. Does not bind to the EGF receptor, ERBB2 or ERBB3 receptors. {ECO:0000269|PubMed:9275162}. | Mus musculus (Mouse) |
O35182 | SMAD6_MOUSE | MFRSKRSGLVRRLWRSRVVPDREEGSGGGGGVDEDGSLGSRAEPAPRAREGGGCSRSEVRSVAPRRPRDAVGPRGAAIAGRRRRTGGLPRPVSESGAGAGGSPLDVAEPGGPGWLPESDCETVTCCLFSERDAAGAPRDSGDPQARQSPEPEEGGGPRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFTAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPPDQYKPLDLSDSTLSYTETEATNSLITAPGEFSDA... | null | null | anatomical structure morphogenesis [GO:0009653]; aorta development [GO:0035904]; aortic valve morphogenesis [GO:0003180]; BMP signaling pathway [GO:0030509]; cardiac vascular smooth muscle cell development [GO:0060948]; cell differentiation [GO:0030154]; cell-substrate adhesion [GO:0031589]; coronary vasculature develo... | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; heteromeric SMAD protein complex [GO:0071144]; nuclear body [GO:0016604]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | chromatin binding [GO:0003682]; co-SMAD binding [GO:0070410]; I-SMAD binding [GO:0070411]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein sequestering activity [GO:0140311]; R-SMAD binding [GO:0070412]; transcription cis-regulatory region binding [GO:0000976]; transcription regulator in... | PF03165;PF03166; | 2.60.200.10;3.90.520.10; | Dwarfin/SMAD family | PTM: Monoubiquitinated at Lys-174 by the E2/E3 hybrid ubiquitin-protein ligase UBE2O, leading to reduced binding affinity for the activated BMP type I receptor ACVR1/ALK2, thereby enhancing BMP7 and regulating adipocyte differentiation (By similarity). Ubiquitinated by WWP1 (PubMed:15221015). Ubiquitinated by ARK2C, pr... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transforming growth factor-beta superfamily receptors signaling occurs through the Smad family of intracellular mediators. SMAD6 is an inhibitory Smad (i-Smad) that negatively regulates signaling downstream of type I transforming growth factor-beta (By similarity). Acts as a mediator of TGF-beta and BMP anti-... | Mus musculus (Mouse) |
O35185 | BHE40_MOUSE | MERIPSAQPPPTCLPKAPGLEHGDLSGMDFAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGDLSGRNLEAGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGASRKPLDSAPKAVDLKEKPSFLAKGSEGPGKNCVPVIQRTFAPSGGEQSGSDTDTDSGYGGELEKGDLRSEQPYFKSDHGRRFAVGERVSTIKQESEEPPTKKSRMQLSEEEGHFAGSDLMGSPFLGPHPHQPP... | null | null | anterior/posterior pattern specification [GO:0009952]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; entrainment of circadian clock by photoperiod [GO:0043153]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase ... | cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; MRF binding [GO:0043426]; protein domain specific binding [GO:0019904]; protein heterodimerizat... | PF07527;PF00010; | 6.10.250.980;4.10.280.10; | null | PTM: Ubiquitinated; which may lead to proteasomal degradation. {ECO:0000250}.; PTM: Sumoylation inhibits its ubiquitination and promotes its negative regulation of the CLOCK-BMAL1 heterodimer transcriptional activator activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14503}. Nucleus {ECO:0000250|UniProtKB:O14503}. Note=Predominantly localized in the nucleus (By similarity). {ECO:0000250|UniProtKB:O14503}. | null | null | null | null | null | FUNCTION: Transcriptional repressor involved in the regulation of the circadian rhythm by negatively regulating the activity of the clock genes and clock-controlled genes (PubMed:18411297). Acts as the negative limb of a novel autoregulatory feedback loop (DEC loop) which differs from the one formed by the PER and CRY ... | Mus musculus (Mouse) |
O35186 | CATK_RAT | MWVFKFLLLPVVSFALSPEETLDTQWELWKKTHGKQYNSKVDEISRRLIWEKNLKKISVHNLEASLGAHTYELAMNHLGDMTSEEVVQKMTGLRVPPSRSFSNDTLYTPEWEGRVPDSIDYRKKGYVTPVKNQGQCGSCWAFSSAGALEGQLKKKTGKLLALSPQNLVDCVSENYGCGGGYMTTAFQYVQQNGGIDSEDAYPYVGQDESCMYNATAKAAKCRGYREIPVGNEKALKRAVARVGPVSVSIDASLTSFQFYSRGVYYDENCDRDNVNHAVLVVGYGTQKGNKYWIIKNSWGESWGNKGYVLLARNKNNACGI... | 3.4.22.38 | null | bone resorption [GO:0045453]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to zinc ion starvation [GO:0034224]; collagen catabolic process [GO:0030574]; immune response [GO:0006955]; intramembranous ossification [G... | apical plasma membrane [GO:0016324]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; nucleoplasm [GO:0005654] | collagen binding [GO:0005518]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; fibronectin binding [GO:0001968]; proteoglycan binding [GO:0043394] | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P43235}. Secreted {ECO:0000250|UniProtKB:P43235}. Apical cell membrane {ECO:0000250|UniProtKB:P43235}; Peripheral membrane protein {ECO:0000250|UniProtKB:P43235}; Extracellular side {ECO:0000250|UniProtKB:P43235}. Note=Localizes to the lumen of thyroid follicles and... | CATALYTIC ACTIVITY: Reaction=Broad proteolytic activity. With small-molecule substrates and inhibitors, the major determinant of specificity is P2, which is preferably Leu, Met > Phe, and not Arg.; EC=3.4.22.38; | null | null | null | null | FUNCTION: Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T... | Rattus norvegicus (Rat) |
O35188 | X3CL1_MOUSE | MAPSPLAWLLRLAAFFHLCTLLPGQHLGMTKCEIMCDKMTSRIPVALLIRYQLNQESCGKRAIVLETTQHRRFCADPKEKWVQDAMKHLDHQAAALTKNGGKFEKRVDNVTPGITLATRGLSPSALTKPESATLEDLALELTTISQEARGTMGTSQEPPAAVTGSSLSTSEAQDAGLTAKPQSIGSFEAADISTTVWPSPAVYQSGSSSWAEEKATESPSTTAPSPQVSTTSPSTPEENVGSEGQPPWVQGQDLSPEKSLGSEEINPVHTDNFQERGPGNTVHPSVAPISSEETPSPELVASGSQAPKIEEPIHATADPQ... | null | null | angiogenesis involved in wound healing [GO:0060055]; autocrine signaling [GO:0035425]; cell-cell adhesion [GO:0098609]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO... | cell body [GO:0044297]; cell projection [GO:0042995]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsy... | CCR chemokine receptor binding [GO:0048020]; chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; CX3C chemokine receptor binding [GO:0031737]; CXCR1 chemokine receptor binding [GO:0045237]; integrin binding [GO:0005178] | PF00048; | 2.40.50.40; | Intercrine delta family | PTM: A soluble short 80 kDa form may be released by proteolytic cleavage from the long membrane-anchored form. {ECO:0000269|PubMed:10382755}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9177350}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Processed fractalkine]: Secreted {ECO:0000269|PubMed:10382755}. | null | null | null | null | null | FUNCTION: Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1 (PubMed:10187784, PubMed:18971423). The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:10187784, PubMed:103... | Mus musculus (Mouse) |
O35206 | COFA1_MOUSE | MTHRRTAQGRRPRWLLSIISALLSAVLQTRAATGSASQVHLDLTVLIGVPLPSSVSFTTGYGGFPAYSFGPGANVGRPARTLIPPTFFRDFAIGVAVKPNSAQGGVLFAITDAFQKVIYLGLRLSSVEDGRQRVILYYTEPGSHVSREAAVFSVPVMTNRWNRFAVTVQGEEVALFMDCEEQSQVRFQRSSWPLTFEPSAGIFVGNAGAMGLERFTGSIQQLTIYSDPRTPEELCEAQESSASGEASGFQEMDEVAEIMEAVTYTQAPPKESHVDPISVPPTSSSPAEDSELSGEPVPEGTPETNLSIIGHSSPEQGSGE... | null | null | cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198] | basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01391;PF20010;PF06482;PF13385; | 2.60.120.200;3.40.1620.70;3.10.100.10; | Multiplexin collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}.; PTM: O-glycosylated; contains chondroitin sulfate. {ECO:0000250|UniProtKB:P39059}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. Secreted {ECO:0000250|UniProtKB:P39059}. | null | null | null | null | null | FUNCTION: Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.; FUNCTION: Restin potently inhibits angiogenesis. | Mus musculus (Mouse) |
O35216 | CENPA_MOUSE | MGPRRKPQTPRRRPSSPAPGPSRQSSSVGSQTLRRRQKFMWLKEIKTLQKSTDLLFRKKPFSMVVREICEKFSRGVDFWWQAQALLALQEAAEAFLIHLFEDAYLLSLHAGRVTLFPKDIQLTRRIRGFEGGLP | null | null | CENP-A containing chromatin assembly [GO:0034080]; establishment of mitotic spindle orientation [GO:0000132]; kinetochore assembly [GO:0051382]; mitotic cytokinesis [GO:0000281]; protein localization to CENP-A containing chromatin [GO:0061644]; protein localization to chromosome, centromeric region [GO:0071459] | CENP-A containing chromatin [GO:0061638]; CENP-A containing nucleosome [GO:0043505]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Poly-ADP-ribosylated by PARP1.; PTM: Trimethylated by NTMT1 at the N-terminal glycine after cleavage of Met-1. Methylation is low before incorporation into nucleosomes and increases with cell cycle progression, with the highest levels in mitotic nucleosomes. {ECO:0000250|UniProtKB:P49450}.; PTM: Phosphorylated by ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49450}. Chromosome, centromere {ECO:0000250|UniProtKB:P49450}. Note=Localizes exclusively to sites of kinetochore assembly in centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constriction but encom... | null | null | null | null | null | FUNCTION: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapp... | Mus musculus (Mouse) |
O35217 | MINP1_RAT | MLRGARSHLSASVALAAVLAAALLSSFARCSLPGRGDPVASVLSPYFGTKTRYEDVNPWLLGDPVAPRRDPELLAGTCTPVQLVALIRHGTRYPTTKQIRKLRQLQGLLQTRESVDGGSRVAAALDQWPLWYDDWMDGQLVEKGRQDMRQLALRLAALFPDLFCRENYGRLRLITSSKHRCVDSSAAFLQGLWQHYHPGLPPPDVSDMECDPPRVNDKLMRFFDHCEKFLTEVERNATALYHVEAFKTGPEMQTVLKKVAATLQVPVNNLNADLIQVAFFTCSFDLAIQGVHSPWCDVFDVDDAKVLEYLNDLKQYWKRS... | 3.1.3.62; 3.1.3.80 | null | intracellular monoatomic cation homeostasis [GO:0030003]; phosphatidylinositol-mediated signaling [GO:0048015] | endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | 3-phytase activity [GO:0016158]; 4-phytase activity [GO:0008707]; acid phosphatase activity [GO:0003993]; bisphosphoglycerate 3-phosphatase activity [GO:0034417]; inositol bisphosphate phosphatase activity [GO:0016312]; inositol hexakisphosphate 2-phosphatase activity [GO:0052826]; inositol pentakisphosphate phosphatas... | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family, MINPP1 subfamily | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UNW1}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:8384201}. Secreted {ECO:0000250|UniProtKB:Q9UNW1}. Cell membrane {ECO:0000250|UniProtKB:Q9Z2L6}. Note=Also associated with the plasma membrane in erythrocytes. {ECO:0000250|UniProtKB:Q9Z2L6}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, ChEBI:CHEBI:58130; EC=3.1.3.62; Evidence={ECO:0000269|PubMed:1653239}; PhysiologicalDirection=left-to-right; Xref=... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=40 nM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate {ECO:0000269|PubMed:1653239}; KM=0.3 nM for 1D-myo-inositol hexakisphosphate {ECO:0000269|PubMed:1653239}; Vmax=211 nmol/min/mg enzyme with 1D-myo-inositol 1,3,4,5,6-pentakisphosphate as substrate {ECO:0000269|P... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-9 with 1D-myo-inositol 1,3,4,5,6-pentakisphosphate or 1D-myo-inositol hexakisphosphate as substrate in absence of magnesium. Optimum pH is 7.4 with 1D-myo-inositol hexakisphosphate as substrate in presence of 1 mM magnesium. {ECO:0000269|PubMed:1653239}; | null | FUNCTION: Multiple inositol polyphosphate phosphatase that hydrolyzes 1D-myo-inositol 1,3,4,5,6-pentakisphosphate (InsP5[2OH]) and 1D-myo-inositol hexakisphosphate (InsP6) to a range of less phosphorylated inositol phosphates. This regulates the availability of these various small molecule second messengers and metal c... | Rattus norvegicus (Rat) |
O35219 | KCNH2_MOUSE | MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAVIYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQIAQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVIMFILNFEVVMEKDMVGSPAHDTNHRGPSTSWLASGRAKTFRLKLPALLALTARESSVRTGSMHSAGAPGAVVVDVDLTPAAPSSESLALDEVSAMDNHVAGLGPAEERRALVGPGSASPVASIRGPHPSPRAQSLNPDASGSSCSLARTRSRESCASVRRASSADDIEAMRAGALPPPPRHASTGAMHPLRSGLLNS... | null | null | membrane repolarization during cardiac muscle cell action potential [GO:0086013]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane potential [GO:0042391]; regulation of ventricular cardiac muscle... | monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886] | inward rectifier potassium channel activity [GO:0005242]; monoatomic ion channel activity [GO:0005216]; potassium channel activity [GO:0005267]; protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; voltage-gated potassium channel activity [GO:0005249] | PF00027;PF00520;PF13426; | 1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20; | Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv11.1/KCNH2 sub-subfamily | PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel. Channel properties are modulated by cAMP and subunit assembly. Mediates the rapidly activating component of the delayed rectifying potassium current in heart (IKr) (By similarity). {ECO:0000250|UniProtKB:Q12809}. | Mus musculus (Mouse) |
O35226 | PSMD4_MOUSE | MVLESTMVCVDNSEYMRNGDFLPTRLQAQQDAVNIVCHSKTRSNPENNVGLITLANDCEVLTTLTPDTGRILSKLHTVQPKGKITFCTGIRVAHLALKHRQGKNHKMRIIAFVGSPVEDNEKDLVKLAKRLKKEKVNVDIINFGEEEVNTEKLTAFVNTLNGKDGTGSHLVTVPPGPSLADALISSPILAGEGGAMLGLGASDFEFGVDPSADPELALALRVSMEEQRQRQEEEARRAAAASAAEAGIATPGTEDSDDALLKMTINQQEFGRPGLPDLSSMTEEEQIAYAMQMSLQGTEFSQESADMDASSAMDTSDPVK... | null | null | proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome accessory complex [GO:0022624]; proteasome regulatory particle, base subcomplex [GO:0008540] | identical protein binding [GO:0042802]; polyubiquitin modification-dependent protein binding [GO:0031593] | PF02809;PF13519; | 6.10.250.380;6.10.300.40;3.40.50.410; | Proteasome subunit S5A family | null | null | null | null | null | null | null | FUNCTION: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose ... | Mus musculus (Mouse) |
O35227 | ADAM7_MOUSE | MLTTGIFWMTVLISHIQERGIVGVEGQELVHPKKLPLLHKRDLERIHDSDIPEEYEEELLYEIKLGKKTLILHLLKAREFLSSNYSETYYNVKREVFTKHPQILDHCFYQGSIIHEFDSAASISTCNGLRGFFRVNDQRYLIEPVKYSDDGEHLVYKYNVKAPYATNHSCVGLNFTKKSALIDVENIEEHNAEDHHKEKFIELFVVADEYVYRRNNKPQNKLRKRIWGMVNFVNMIYKTLNIHVTLAGFEIWSAGDKIEIVSNLESTLLHFSTWQETVLKKRKDFDHVILLSGKWLYTSMQGIAYPGGICQILRSCSVVK... | null | null | epididymis development [GO:1905867]; epithelial cell morphogenesis [GO:0003382]; positive regulation of flagellated sperm motility [GO:1902093]; positive regulation of sperm capacitation [GO:1902492]; proteolysis [GO:0006508] | apical part of cell [GO:0045177]; plasma membrane [GO:0005886] | endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222] | PF08516;PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:20945367}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Required for normal male fertility via maintenance of epithelial cell morphology in the caput epididymis and subsequently correct epididymis lumen structure required for sperm development (PubMed:26246218). Plays a role in sperm motility, flagella morphology and tyrosine phosphorylation during sperm capacitan... | Mus musculus (Mouse) |
O35231 | KIFC3_MOUSE | MVPSRRTWNLGATPSLRGLWRVGRVQEPKPGMARPAPASPAARPFPHTGQGRLRTGRGKDILPSGEEDSTSRTAARPSLAQCRALSVDWPGPRSPHRLYLTVQVENLKEKLISQAQEVSRLRSELGGTDAEKHRDRLMVENEQLRQELRRCEVELQELRAQPVVPCEGCEHSQESSQLRDKLSQLQLEVAENKGMLSELNLEVQQKTDRLAEVELRLKDCLAEKAQEEERLSRRLRDSHETIASLRAQSPPVKYVIKTVEVESSKTKQALSESQTRNQHLQEQVAMQRQVLKEMEQQLQNSHQLTVQLRAQIAMYEAELE... | null | null | epithelial cell-cell adhesion [GO:0090136]; Golgi organization [GO:0007030]; microtubule-based movement [GO:0007018]; microtubule-based process [GO:0007017]; zonula adherens maintenance [GO:0045218] | centrosome [GO:0005813]; cytoplasmic vesicle membrane [GO:0030659]; Golgi apparatus [GO:0005794]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; zonula adherens [GO:0005915] | ATP binding [GO:0005524]; microtubule binding [GO:0008017]; minus-end-directed microtubule motor activity [GO:0008569] | PF00225; | 3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11581287}. Cytoplasmic vesicle membrane {ECO:0000305|PubMed:11581287}; Peripheral membrane protein {ECO:0000305|PubMed:11581287}. Cell junction, adherens junction {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000... | null | null | null | null | null | FUNCTION: Minus-end microtubule-dependent motor protein. Involved in apically targeted transport. Required for zonula adherens maintenance. {ECO:0000269|PubMed:11581287}. | Mus musculus (Mouse) |
O35235 | TNF11_MOUSE | MRRASRDYGKYLRSSEEMGSGPGVPHEGPLHPAPSAPAPAPPPAASRSMFLALLGLGLGQVVCSIALFLYFRAQMDPNRISEDSTHCFYRILRLHENADLQDSTLESEDTLPDSCRRMKQAFQGAVQKELQHIVGPQRFSGAPAMMEGSWLDVAQRGKPEAQPFAHLTINAASIPSGSHKVTLSSWYHDRGWAKISNMTLSNGKLRVNQDGFYYLYANICFRHHETSGSVPTDYLQLMVYVVKTSIKIPSSHNLMKGGSTKNWSGNSEFHFYSINVGGFFKLRAGEEISIQVSNPSLLDPDQDATYFGAFKVQDID | null | null | animal organ morphogenesis [GO:0009887]; bone development [GO:0060348]; bone resorption [GO:0045453]; calcium ion homeostasis [GO:0055074]; calcium-mediated signaling [GO:0019722]; cellular response to leukemia inhibitory factor [GO:1990830]; ERK1 and ERK2 cascade [GO:0070371]; immune response [GO:0006955]; JNK cascade... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | cytokine activity [GO:0005125]; identical protein binding [GO:0042802]; receptor ligand activity [GO:0048018]; tumor necrosis factor receptor binding [GO:0005164]; tumor necrosis factor receptor superfamily binding [GO:0032813] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: N-glycosylated. {ECO:0000269|PubMed:10224132}.; PTM: The soluble form of isoform 1 derives from the membrane form by proteolytic processing. The cleavage may be catalyzed by ADAM17. A further shorter soluble form was observed. {ECO:0000269|PubMed:10224132}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 11, soluble form]: Secre... | null | null | null | null | null | FUNCTION: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor (PubMed:22437732). Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role... | Mus musculus (Mouse) |
O35240 | ASIC3_RAT | MKPRSGLEEAQRRQASDIRVFASSCTMHGLGHIFGPGGLTLRRGLWATAVLLSLAAFLYQVAERVRYYGEFHHKTTLDERESHQLTFPAVTLCNINPLRRSRLTPNDLHWAGTALLGLDPAEHAAYLRALGQPPAPPGFMPSPTFDMAQLYARAGHSLEDMLLDCRYRGQPCGPENFTVIFTRMGQCYTFNSGAHGAELLTTPKGGAGNGLEIMLDVQQEEYLPIWKDMEETPFEVGIRVQIHSQDEPPAIDQLGFGAAPGHQTFVSCQQQQLSFLPPPWGDCNTASLDPDDFDPEPSDPLGSPRPRPSPPYSLIGCRLA... | null | null | detection of chemical stimulus involved in sensory perception [GO:0050907]; detection of chemical stimulus involved in sensory perception of pain [GO:0050968]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; detection of mechanical stimulus involved in sensory perception of pain [GO:005096... | perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | enterobactin transmembrane transporter activity [GO:0042931]; ligand-gated sodium channel activity [GO:0015280]; monoatomic cation channel activity [GO:0005261]; pH-gated monoatomic ion channel activity [GO:0160128] | PF00858; | 1.10.3590.10;1.10.287.820;1.10.287.770; | Amiloride-sensitive sodium channel (TC 1.A.6) family, ASIC3 subfamily | PTM: Phosphorylated by PKA (By similarity). Phosphorylated by PKC. In vitro, PRKCABP/PICK-1 is necessary for PKC phosphorylation and activation of a ASIC3/ACCN3-ASIC2/ASIC2b channel, but does not activate a homomeric ASIC3/ACCN3 channel. {ECO:0000250, ECO:0000269|PubMed:14976185}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=In part cytoplasmic in cochlea cells (By similarity). Cell surface expression may be stabilized by interaction with LIN7B and cytoplasmic retention by interaction with DLG4. {ECO:0000250, ECO:0000... | null | null | null | null | null | FUNCTION: Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damag... | Rattus norvegicus (Rat) |
O35244 | PRDX6_RAT | MPGGLLLGDEAPNFEANTTIGHIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHFAWSKDINAYNGAAPTEKLPFPIIDDKDRDLAILLGMLDPAEKDEKGMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTASNPVATPVDWKKGESVMVLPTLPEEEAKQLFPKGVFTKELPSGKKYLRYTPQP | 1.11.1.27; 2.3.1.23; 3.1.1.4 | null | bleb assembly [GO:0032060]; cell redox homeostasis [GO:0045454]; cellular oxidant detoxification [GO:0098869]; cellular response to oxidative stress [GO:0034599]; glycerophospholipid catabolic process [GO:0046475]; hydrogen peroxide catabolic process [GO:0042744]; positive regulation of mRNA splicing, via spliceosome [... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | 1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; calcium-independent phospholipase A2 activity [GO:0047499]; glutathione peroxidase activity [GO:0004602]; identical protein binding [GO:0042802]; peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; phospholipase A2 activity [GO:0004... | PF10417;PF00578; | 3.40.30.10; | Peroxiredoxin family, Prx6 subfamily | PTM: Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (PubMed:19140803). Phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (PubMed:26830860). {ECO:0000269|PubMed:19140803, ECO:0000269|PubMed:2683086... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19700648}. Lysosome {ECO:0000269|PubMed:19700648}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000269|PubMed:19700648}. | CATALYTIC ACTIVITY: Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.27; Evidence={ECO:0000269|PubMed:15004285}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for dipalmitoyl phosphatidylcholine {ECO:0000269|PubMed:8999971}; Vmax=1.89 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine {ECO:0000269|PubMed:8999971}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4 (for phospholipase activity). {ECO:0000269|PubMed:8999971}; | null | FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15004285). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, can therefore... | Rattus norvegicus (Rat) |
O35245 | PKD2_MOUSE | MVNSRRVQPQPPGDAGRSPAPRASGPGRLVAGGAGLAVPGGLGEQRGLEIEMERIRQAAARDPPAGASASPSPPLSSCSRQAWSRDNPGFEAEEDDDDDEVEGEEGGMVVEMDVEWRPGSRRSASSSAVSSVGARGRGLGSYRGAAHLSGRRRRLEDQGAQCPSPAGGGDPLHRHLPLEGQPPRVAWAERLVRGLRGLWGTRLMEESNANREKYLKSVLRELVTYLFFLVVLCILTYGMMSSNVYYYTRTLSQLFIDTPVSKTEKTNFKTLSSMEDFWKFTEGSFLDGLYWKAQTSNHTQADNRSFIFYENLLLGVPRLR... | null | null | aorta development [GO:0035904]; branching involved in ureteric bud morphogenesis [GO:0001658]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; cell-cell signaling by wnt [GO:0198738]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular re... | basal cortex [GO:0045180]; basolateral plasma membrane [GO:0016323]; cation channel complex [GO:0034703]; ciliary basal body [GO:0036064]; ciliary membrane [GO:0060170]; cilium [GO:0005929]; cytoplasm [GO:0005737]; cytoplasmic side of endoplasmic reticulum membrane [GO:0098554]; cytoplasmic vesicle membrane [GO:0030659... | alpha-actinin binding [GO:0051393]; ATPase binding [GO:0051117]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; channel activity [GO:0015267]; HLH domain binding [GO:0043398]; identical protein binding [GO:0042802]; muscle alpha-actinin bi... | PF18109;PF08016;PF20519; | 1.10.287.70;1.20.5.340;1.10.238.10;1.20.120.350; | Polycystin family | PTM: N-glycosylated (PubMed:11854751). The four subunits in a tetramer probably differ in the extent of glycosylation; simultaneous glycosylation of all experimentally validated sites would probably create steric hindrance (By similarity). {ECO:0000250|UniProtKB:Q13563, ECO:0000269|PubMed:11854751}.; PTM: Phosphorylate... | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:12514735, ECO:0000269|PubMed:18695040, ECO:0000269|PubMed:21307093, ECO:0000269|PubMed:22983710, ECO:0000269|PubMed:25405894, ECO:0000269|PubMed:27760766}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cell membrane {ECO:0000269|Pu... | null | null | null | null | null | FUNCTION: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel (PubMed:27214281). Functions as a cation channel involved in fluid-flow mechan... | Mus musculus (Mouse) |
O35250 | EXOC7_MOUSE | MIPPQEASARRREIEDKLKQEEETLSFIRDSLEKSDQLTRNMVSILSSFESRLMKLENSIIPVHKQTENLQRLQENVEKTLSCLDHVISYYHVASDTEKIIREGPTGRLEEYLGSMAKIQKAVEYFQDNSPDSPELNKVKLLFERGKESLESEFRSLMTRHSKVVSPVLLLDLISADDELEVQEDVVLEHLPESVLRDVVRISRWLVEYGRNQDFMNVYYQIRSSQLDRSIKGLKEHFRKSSSSSGVPYSPAIPNKRKDTPTKKPIKRPGTIRKAQNLLKQYSQHGLDGKKGGSNLIPLEGRDDMLDVETDAYIHCVSAF... | null | null | exocytosis [GO:0006887]; membrane fission [GO:0090148]; mitotic cytokinesis [GO:0000281]; protein transmembrane transport [GO:0071806]; regulation of entry of bacterium into host cell [GO:2000535]; vesicle docking involved in exocytosis [GO:0006904]; vesicle tethering involved in exocytosis [GO:0090522] | centriolar satellite [GO:0034451]; cytosol [GO:0005829]; exocyst [GO:0000145]; Flemming body [GO:0090543]; growth cone membrane [GO:0032584]; plasma membrane [GO:0005886] | phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF03081;PF20669; | 1.20.1280.170; | EXO70 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12687004}. Cell membrane {ECO:0000269|PubMed:12687004}; Peripheral membrane protein. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q9UPT5}. Note=Translocates, as a preformed complex with SEC6 and SEC8, to the plasma membrane in response to insulin through the ... | null | null | null | null | null | FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion. It is required for... | Mus musculus (Mouse) |
O35251 | VEGFD_RAT | MYGEWAAVNILMMSYVYLVQGFSIEHRAVKDVSLERSSRSVLERSEQQIRAASTLEELLQVAHSEDWKLWRCRLKLKSLANVDSRSTSHRSTRFAATFYDTETLKVIDEEWQRTQCSPRETCVEVASELGKTTNTFFKPPCVNVFRCGGCCNEESVMCMNTSTSYISKQLFEISVPLTSVPELVPVKIANHTGCKCLPTGPRHPYSIIRRSIQIPEEDQCPHSKKLCPVDMLWDNTKCKCVLQDENPLPGTEDHSYLQEPALCGPHMMFDEDRCECVCKAPCPGDLIQHPENCSCFECKESLESCCQKHKMFHPDTCRSM... | null | null | dopaminergic neuron differentiation [GO:0071542]; fibroblast proliferation [GO:0048144]; induction of positive chemotaxis [GO:0050930]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulat... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020] | chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; vascular endothelial growth factor receptor 3 binding [GO:0043185]; vascular endothelial growth factor receptor binding [GO:0005172] | PF03128;PF00341; | 2.10.90.10; | PDGF/VEGF growth factor family | PTM: Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3 and VEGFR-2. VEGF-D first form an antiparallel homodimer linked by disulfide bonds before secretion. The fully processed VEGF-D is composed mostly of two VEGF homology domains (VH... | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the mainten... | Rattus norvegicus (Rat) |
O35253 | SMAD7_MOUSE | MFRTKRSALVRRLWRSRAPGGEDEEEGVGGGGGGGELRGEGATDGRAYGAGGGGAGRAGCCLGKAVRGAKGHHHPHPPTSGAGAAGGAEADLKALTHSVLKKLKERQLELLLQAVESRGGTRTACLLLPGRLDCRLGPGAPASAQPAQPPSSYSLPLLLCKVFRWPDLRHSSEVKRLCCCESYGKINPELVCCNPHHLSRLCELESPPPPYSRYPMDFLKPTAGCPDAVPSSAETGGTNYLAPGGLSDSQLLLEPGDRSHWCVVAYWEEKTRVGRLYCVQEPSLDIFYDLPQGNGFCLGQLNSDNKSQLVQKVRSKIGCG... | null | null | adherens junction assembly [GO:0034333]; anatomical structure morphogenesis [GO:0009653]; artery morphogenesis [GO:0048844]; cell differentiation [GO:0030154]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to transforming growth factor beta stimulus [GO:0071560]; intracellular signal t... | adherens junction [GO:0005912]; centrosome [GO:0005813]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; heteromeric SMAD protein complex [GO:0071144]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | activin receptor binding [GO:0070697]; beta-catenin binding [GO:0008013]; collagen binding [GO:0005518]; I-SMAD binding [GO:0070411]; metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]; transcription regulator inhibitor activity [GO:0140416]; type I transforming growth factor beta receptor ... | PF03165;PF03166; | 2.60.200.10;3.90.520.10; | Dwarfin/SMAD family | PTM: Phosphorylation on Ser-249 does not affect its stability, nuclear localization or inhibitory function in TGFB signaling; however it affects its ability to regulate transcription (PubMed:11278814). Phosphorylated by PDPK1 (By similarity). {ECO:0000250|UniProtKB:O15105, ECO:0000269|PubMed:11278814}.; PTM: Ubiquitina... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}. Cytoplasm {ECO:0000269|PubMed:11278814, ECO:0000269|PubMed:15496141}. Note=Interaction with NEDD4L or RNF111 induces translocation from the nucleus to the cytoplasm (PubMed:15496141). TGF-beta stimulates its translocation from the... | null | null | null | null | null | FUNCTION: Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access. Functions as an adapter to recruit SMURF2 to the TGF-bet... | Mus musculus (Mouse) |
O35254 | GORS1_RAT | MGLGASSEQPAGGEGFHLHGVQENSPAQQAGLEPYFDFIITIGHSRLNKENDTLKALLKANVEKPVKLEVFNMKTMRVREVEVVPSNMWGGQGLLGASVRFCSFRRASEHVWHVLDVEPSSPAALAGLRPYTDYIVGSDQILQESEDFFTLIESHEGKPLKLMVYNSESDSCREVTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPSSQYKKPPSASSPGTPAKTPQPNAFPLGAPPPWPIPQDSSGPELGSRQSDYMEALPQVPGGFMEEQLPGPGSPGHGTADYGGCLHSMEIPLQPPPPVQRVMDPGFLDVSGMSLLD... | null | null | establishment of protein localization to plasma membrane [GO:0061951]; Golgi organization [GO:0007030]; Golgi ribbon formation [GO:0090161]; negative regulation of dendrite morphogenesis [GO:0050774]; protein N-linked glycosylation [GO:0006487]; protein transport [GO:0015031] | Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139] | metal ion binding [GO:0046872] | PF04495; | 2.30.42.10; | GORASP family | PTM: Phosphorylated by CDC2/B1 and PLK kinases during mitosis. Phosphorylation cycle correlates with the cisternal stacking cycle. Phosphorylation of the homodimer prevents the association of dimers into higher-order oligomers, leading to cisternal unstacking. {ECO:0000269|PubMed:11050165, ECO:0000269|PubMed:12839990, ... | SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane {ECO:0000269|PubMed:11706049, ECO:0000269|PubMed:11739401, ECO:0000269|PubMed:12015985, ECO:0000269|PubMed:12839990, ECO:0000269|PubMed:9346242}; Peripheral membrane protein {ECO:0000269|PubMed:9346242}; Cytoplasmic side {ECO:0000269|PubMed:9346242}. | null | null | null | null | null | FUNCTION: Key structural protein of the Golgi apparatus (By similarity). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (By similarity). Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of th... | Rattus norvegicus (Rat) |
O35260 | NACC1_RAT | MAQTLQMEIPNFGNSILECLNEQRLQGLYCDVSVVVKGHAFKAHRAVLAASSSYFRDLFNSSRSAVVELPAAVQPQSFQQILTFCYTGRLSMNMGDQFLLIYTAGFLQIQEIMEKGTEFFLKVSSPSCDSQGLHPEEAPSSEPQSPVAQILGWPACSTPLPLVSRVKTEQELDSVQCTPMAKRLWDSSQKEAGGSGGNNGSRKMAKFSTPDLAPNRMPQPVSVATATAAVAVVAVGGCVSGPSMSERTSPGTSSAYTSDSPSSYHNEEDEEEDAGEEGTDEQYRQICNMYTMYSMLNVGQTVEKVEALPEQVVLESHSRI... | null | null | negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of cell population proliferation [GO:0008284]; regulation of transcription by RNA polymerase II [GO:0006357] | cell junction [GO:0030054]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF10523;PF00651; | 1.10.10.2590; | null | PTM: Phosphorylated by protein kinase C (PKC). {ECO:0000269|PubMed:16045493}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Punctate distribution in nucleus. In differentiated PC12 cells diffusely distributed in the cytoplasm and is dependent on phosphorylation. | null | null | null | null | null | FUNCTION: Functions as a transcriptional repressor. Isoform 1 is a stronger transcriptional repressor than isoform 2. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be medi... | Rattus norvegicus (Rat) |
O35261 | E2F3_MOUSE | MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAPGTYIQILTTNPSTTSCATSLQSGALTAGPLLPSVPGTEPAASSLYTTPQGPSSRVGLLQQPPAPGRGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKAPPETRLEV... | null | null | G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of fat cell proliferation [GO:0070345]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of vascular associated smooth muscle cell apoptotic proc... | RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-r... | PF16421;PF02319; | 6.10.250.540;1.10.10.10; | E2F/DP family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle pr... | Mus musculus (Mouse) |
O35263 | PA1B3_RAT | MSGEGENPASKPTPVQDVQGDGRWMSLHHRFVADSKDKEPEVVFIGDSLVQLMHQCEIWRELFSPLHALNFGIGGDSTQHVLWRLENGELEHIRPKIVVVWVGTNNHSHTAEQVTGGIKAIVQLVNKLQPQARVVVLGLLPRGQHPNPLREKNRQVNELVRAALAGYPRAHFLDADPGFVHSDGTISHHDMYDYLHLSRLGYTPVCRALHSLLLRLLAQDQGQGIPLPETAP | 3.1.1.47 | null | lipid catabolic process [GO:0016042]; spermatogenesis [GO:0007283] | 1-alkyl-2-acetylglycerophosphocholine esterase complex [GO:0008247]; cytoplasm [GO:0005737] | 1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; identical protein binding [GO:0042802]; platelet-activating factor acetyltransferase activity [GO:0047179]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:00448... | PF13472; | 3.40.50.1110; | 'GDSL' lipolytic enzyme family, Platelet-activating factor acetylhydrolase IB beta/gamma subunits subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000269|PubMed:9660828}; Physiolog... | null | null | null | null | FUNCTION: Alpha1 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF (PubMed:9660828). The activity and substrate speci... | Rattus norvegicus (Rat) |
O35264 | PA1B2_RAT | MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA | 3.1.1.47 | null | lipid catabolic process [GO:0016042]; positive regulation of macroautophagy [GO:0016239]; spermatogenesis [GO:0007283] | 1-alkyl-2-acetylglycerophosphocholine esterase complex [GO:0008247]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; plasma membrane [GO:0005886] | 1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; identical protein binding [GO:0042802]; platelet-activating factor acetyltransferase activity [GO:0047179]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:00448... | PF13472; | 3.40.50.1110; | 'GDSL' lipolytic enzyme family, Platelet-activating factor acetylhydrolase IB beta/gamma subunits subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-glycero-3-phosphocholine + acetate + H(+); Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47; Evidence={ECO:0000269|PubMed:9660828}; Physiolog... | null | null | null | null | FUNCTION: Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF (PubMed:9660828). The activity and substrate speci... | Rattus norvegicus (Rat) |
O35274 | NEB2_RAT | MMKTEPRGPGGPLRSASPHRSAYEAGIQALKPPDAPGPDEAPKAAHHKKYGSNVHRIKSMFLQMGTTTGPPGEAGGASGMAEAPRASDRGVRLSLPRASSLNENVDHSALLKLGTSVSERVSRFDSKPAPSAQPAPPPHPPSRLQETRKLFERSVPAASGGDKEAVARRLLRQERASLQDRKLDVVVRFNGSTEALDKLDADAVSPTVSQLSAVFEKADSRTGLHRAPGPPRAAGAPQVNSKLVTKRSRVFQPPPPPPAPSGDAATEKDRGPGGQQPPQHRVAPARPPPKPREVRKIKPVEVEESGESEAESAPGEVIQA... | null | null | actin filament depolymerization [GO:0030042]; actin filament organization [GO:0007015]; calcium-mediated signaling [GO:0019722]; cell migration [GO:0016477]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to estradiol stimulus [GO:0071392]; cellular response to morphine [GO:007131... | actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoplasmic side of dendritic spine plasma membrane [GO:1990780]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dendritic spine head [GO:0044327]; dendritic spine membrane [GO:003259... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; D2 dopamine receptor binding [GO:0031749]; kinase binding [GO:0019900]; nucleic acid binding [GO:0003676]; protein kinase activity [GO:0004672]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase inhibitor activity [GO:0004864]; protein-conta... | PF00595;PF17817; | 2.30.42.10; | null | PTM: Stimulation of D1 (but not D2) dopamine receptors induces Ser-94 and Ser-177 phosphorylation. Dephosphorylation of these residues is mediated by PP1 and possibly PP2A. Spinophilin unphosphorylated or phosphorylated at Ser-94 is concentrated in the postsynaptic density, whereas spinophilin phosphorylated at Ser-177... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:15514983}. Cell junction, adherens junction. Cell projection, dendritic spine {ECO:0000269|PubMed:15514983}. Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. ... | null | null | null | null | null | FUNCTION: Seems to act as a scaffold protein in multiple signaling pathways. Modulates excitatory synaptic transmission and dendritic spine morphology. Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May play an important role in linking the actin cytoskeleton ... | Rattus norvegicus (Rat) |
O35276 | NRP2_RAT | MDMFPLTWIFLALYFSGHKVRSQQDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWVVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSVLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPRMEIILQFLTFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSKLRSSTGILSLTFHTDMAVAKDGFSARYYLVHQEPPENFQCNAPLGMESGRIANEQISASSTFSDGRWTPQQSRLHGDDNGWTP... | null | null | angiogenesis [GO:0001525]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cellular response to leukemia inhibitory factor [GO:1990830]; dorsal root ganglion morphogenesis [GO:1904835]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375];... | axon [GO:0030424]; glutamatergic synapse [GO:0098978]; postsynaptic membrane [GO:0045211] | heparin binding [GO:0008201]; metal ion binding [GO:0046872]; semaphorin receptor activity [GO:0017154]; vascular endothelial growth factor receptor activity [GO:0005021] | PF00431;PF11980;PF00754;PF00629; | 2.60.120.200;2.60.120.260;2.60.120.290; | Neuropilin family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O60462}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60462}. | null | null | null | null | null | FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF. | Rattus norvegicus (Rat) |
O35280 | CHK1_MOUSE | MAVPFVEDWDLVQTLGEGAYGEVQLAVNRITEEAVAVKIVDMKRAIDCPENIKKEICINKMLSHENVVKFYGHRREGHIQYLFLEYCSGGELFDRIEPDIGMPEQDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRHNNRERLLNKMCGTLPYVAPELLKRKEFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVETPSARITIPDIKKDRWYNKPLNRGAKRPRATSGGMSESSSGFSKHIHSNLDFSPVNNGSSEETVKFSSSQPE... | 2.7.11.1 | null | apoptotic process involved in development [GO:1902742]; cellular response to caffeine [GO:0071313]; cellular response to mechanical stimulus [GO:0071260]; chromatin remodeling [GO:0006338]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; G2/M transition of mitoti... | centrosome [GO:0005813]; chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657] | ATP binding [GO:0005524]; histone H3T11 kinase activity [GO:0035402]; protein domain specific binding [GO:0019904]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 3.30.310.80;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, NIM1 subfamily | PTM: Phosphorylated by ATR in a RAD17-dependent manner in response to ultraviolet irradiation and inhibition of DNA replication. Phosphorylated by ATM in response to ionizing irradiation. ATM and ATR can both phosphorylate Ser-317 and Ser-345 and this results in enhanced kinase activity. Phosphorylation at Ser-345 indu... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15710331, ECO:0000269|PubMed:9382850}. Chromosome {ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:9382850}. Cytoplasm {ECO:0000250|UniProtKB:O14757}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O14757}. Note=Nuclear export ... | 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:18243098}; CATALYTIC... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:10859163, PubMed:10859164, PubMed:15261141). May also negatively regulate cell cycle progression during unperturbed cel... | Mus musculus (Mouse) |
O35284 | BATF_MOUSE | MPHSSDSSDSSFSRSPPPGKQDSSDDVRKVQRREKNRIAAQKSRQRQTQKADTLHLESEDLEKQNAALRKEIKQLTEELKYFTSVLSSHEPLCSVLASGTPSPPEVVYSAHAFHQPHISSPRFQP | null | null | defense response to protozoan [GO:0042832]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; hematopoietic stem cell differentiation [GO:0060218]; isotype switching [GO:0045190]; lymphoid progenitor cell differentiation [GO:0002320]; myeloid dendritic cell d... | cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-... | PF00170; | 1.20.5.170; | BZIP family | PTM: Phosphorylated on serine and threonine residues and at least one tyrosine residue. Phosphorylation at Ser-43 inhibit DNA binding activity and transforms it as a negative regulator of AP-1 mediated transcription. {ECO:0000269|PubMed:12809553}. | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Present in the nucleus and cytoplasm, but shows increased nuclear translocation after activation of T-cells. | null | null | null | null | null | FUNCTION: AP-1 family transcription factor that controls the differentiation of lineage-specific cells in the immune system: specifically mediates the differentiation of T-helper 17 cells (Th17), follicular T-helper cells (TfH), CD8(+) dendritic cells and class-switch recombination (CSR) in B-cells. Acts via the format... | Mus musculus (Mouse) |
O35286 | DHX15_MOUSE | MSKRHRLDLGEDYPSGKKRAGTDGKDRERDRDREDRSKDRDRERDRGDREREREKEKEKELRASTNAMLISAGLPPLKASHSAHSTHSAHSTHSTHSAHSTHTGHTGHTSLPQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVE... | 3.6.4.13 | null | antiviral innate immune response [GO:0140374]; defense response to bacterium [GO:0042742]; defense response to virus [GO:0051607]; mRNA processing [GO:0006397]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; response to alkaloid [GO:0043279]; response to toxic substance [GO:0009636]; RNA s... | nuclear speck [GO:0016607]; nucleolus [GO:0005730]; spliceosomal complex [GO:0005681]; U12-type spliceosomal complex [GO:0005689]; U2-type post-mRNA release spliceosomal complex [GO:0071008] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; helicase activity [GO:0004386]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00270;PF21010;PF04408;PF00271;PF07717; | 1.20.120.1080;3.40.50.300; | DEAD box helicase family, DEAH subfamily, DDX15/PRP43 sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9342318}. Nucleus, nucleolus {ECO:0000269|PubMed:9342318}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000250|UniProtKB:O43143}; | null | null | null | null | FUNCTION: RNA helicase involved in mRNA processing and antiviral innate immunity (PubMed:26494172, PubMed:34161762). Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA (By similarity). In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 ... | Mus musculus (Mouse) |
O35291 | RNAS2_MOUSE | MGPKLLESRLCLLLLLGLVLMLASCQAQILSQKFYTQHIYNSTYPRCDAVMRVVNRYRPRCKDINTFLHTSFADVVAVCGHPNITCNNLTRKNCHASSFQVFITFCNLTMPTRICTQCRYQTTGSVKYYRVACENRTPQDTPMYPVVPVHLDGTF | 4.6.1.18 | null | chemotaxis [GO:0006935]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response in mucosa [GO:0002227] | extracellular space [GO:0005615]; lysosome [GO:0005764] | lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule. | CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000250|UniProtKB:P47784}; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleoti... | null | null | null | null | FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities. | Mus musculus (Mouse) |
O35293 | CP2F2_RAT | MDGVSTAILLLLLAVISLSLTFTSWGKGQLPPGPKPLPILGNLLQLRSQDLLTSLTKLSKDYGSVFTVYLGPRRVIVLSGYQTVKEALVDKGEEFSGRGSYPIFFNFTKGNGIAFSDGERWKILRRFSVQILRNFGMGKRSIEERILEEGSFLLDVLRKTEGKPFDPVFILSRSVSNIICSVIFGSRFDYDDERLLTIIHFINDNFQIMSSPWGEMYNIFPSLLDWVPGPHRRVFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMVQEKQDPLSHFNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKV... | 1.14.14.- | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | epoxygenase P450 pathway [GO:0019373]; naphthalene catabolic process [GO:1901170]; response to toxic substance [GO:0009636]; trichloroethylene metabolic process [GO:0018979]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one ... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | null | null | null | null | null | FUNCTION: Involved in the regio- and stereoselective transformation of naphthalene to trans-1R-hydroxy-2R-glutathionyl-1,2-dihydronaphthalene in the presence of glutathione and glutathione S-transferases. It specifically catalyzes the production of a very reactive and potentially toxic intermediate, the 2R,2S arene oxi... | Rattus norvegicus (Rat) |
O35295 | PURB_MOUSE | MADGDSGSERGGGGGGGGGPGGFQPAPRGGGGGGGGPGGEQETQELASKRLDIQNKRFYLDVKQNAKGRFLKIAEVGAGGSKSRLTLSMAVAAEFRDSLGDFIEHYAQLGPSSPEQLAAGAEEGGGPRRALKSEFLVRENRKYYLDLKENQRGRFLRIRQTVNRGGGGFGGGPGPGGLQSGQTIALPAQGLIEFRDALAKLIDDYGGDEDELAGGPGGGAGGPGGGLYGELPEGTSITVDSKRFFFDVGCNKYGVFLRVSEVKPSYRNAITVPFKAWGKFGGAFCRYADEMKEIQERQRDKLYERRGGGSGGGDESEGEE... | null | null | DNA unwinding involved in DNA replication [GO:0006268]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:00... | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | 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]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; double-stranded DNA binding [GO:000369... | PF04845; | 3.10.450.700;3.30.2450.30; | PUR DNA-binding protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33743134}. | null | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:27064749}; | FUNCTION: Transcriptional regulator which can act as an activator or a repressor (PubMed:11751932, PubMed:12874279, PubMed:27064749, PubMed:31918924, PubMed:33743134, PubMed:9334258). Represses the transcription of ACTA2 in fibroblasts and smooth muscle cells via its ability to interact with the purine-rich strand of a... | Mus musculus (Mouse) |
O35298 | AOAH_MOUSE | MKFPWKVFKTTLLLLLLSHSLASVPSEDQPGDSYSHGQSCLGCVVLVSVIEQLAEVHNSSVQVAMERLCSYLPEKLFLKTACYFLVQTFGSDIIKLLDEAMKADVVCYALEFCKRGAVQPQCHLYPLPQEAWESALEKARQVLRRSSTMKYPRSGRNICSLPFLTKICQKIELSIKKAVPFKDIDSDKHSVFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDIHQDSNCNGIWGIDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTASQMSVNSFLNLPSALTDELNWPQLSGVTGFLDSTSGIEEKSIYH... | 3.1.1.77 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29343645}; Note=Binds 3 Ca(2+) ions per subunit. The calcium ions probably have a structural role. {ECO:0000269|PubMed:29343645}; | fatty acid metabolic process [GO:0006631]; lipopolysaccharide catabolic process [GO:0009104]; lipopolysaccharide metabolic process [GO:0008653]; negative regulation of inflammatory response [GO:0050728] | cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576] | acyloxyacyl hydrolase activity [GO:0050528]; calcium ion binding [GO:0005509] | PF00657;PF20825; | 1.10.225.10;3.40.50.1110; | null | PTM: Cleaved into a large and a small subunit. {ECO:0000250|UniProtKB:P28039}.; PTM: The small subunit is N-glycosylated. {ECO:0000250|UniProtKB:P28039}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15155618}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in urine. {ECO:0000269|PubMed:15155618}. | CATALYTIC ACTIVITY: Reaction=a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+); Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:136853, ChEBI:CHEBI:140675; EC=3.1.1.77; Evidence={ECO:0000305|PubMed:1281069... | null | null | null | null | FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS) (PubMed:12810692, PubMed:15155618, PubMed:17322564, PubMed:19860560). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflam... | Mus musculus (Mouse) |
O35303 | DNM1L_RAT | MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGVVTRRPLILQLVHVSPEDKRKTTGEENDPATWKNSRHLSKGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKVFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTR... | 3.6.5.5 | null | calcium ion transport [GO:0006816]; cellular response to hypoxia [GO:0071456]; cellular response to lipid [GO:0071396]; endocytosis [GO:0006897]; heart contraction [GO:0060047]; intracellular distribution of mitochondria [GO:0048312]; membrane fusion [GO:0061025]; mitochondrial fission [GO:0000266]; mitochondrial fragm... | brush border [GO:0005903]; clathrin-coated pit [GO:0005905]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; microtubule [GO:0005874]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]... | BH2 domain binding [GO:0051433]; clathrin binding [GO:0030276]; GTP binding [GO:0005525]; GTP-dependent protein binding [GO:0030742]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; protei... | PF01031;PF00350;PF02212; | 1.20.120.1240;3.40.50.300; | TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family | PTM: Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission (By similarity). Phosphorylation on Ser-656 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation (By similarity). Dephosphorylated on th... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:22745122}. Golgi apparatus {ECO:0000250|UniProtKB:O00429}. Endomembrane system {ECO:0000250|UniProtKB:O00429}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8K1M6}. Mitochondrion outer membrane {ECO:0000269|PubMed:12861026, ... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5; Evidence={ECO:0000250|UniProtKB:O00429}; | null | null | null | null | FUNCTION: Functions in mitochondrial and peroxisomal division (PubMed:11553726, PubMed:12499366, PubMed:12861026, PubMed:17301055, PubMed:18250306). Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial m... | Rattus norvegicus (Rat) |
O35304 | VACHT_MOUSE | MEPTAPTGQARAAATKLSEAVGAALQEPQRQRRLVLVIVCVALLLDNMLYMVIVPIVPDYIAHMRGGSESPTLISEVWEPTLPPPTLANASAYLANTSASPTAAGSARSILRPRYPTESEDVKIGVLFASKAILQLLVNPLSGPFIDRMSYDVPLLIGLGVMFASTVMFAFAEDYATFFAARSLQGLGSAFADTSGIAMIADKYPEEPERSRALGVALAFISFGSLVAPPFGGILYEFAGKRVPFLVLAAVSLFDALLLLAVAKPFSAAARARANLPVGTPIHRLMLDPYIAVVAGALTTCNIPLAFLEPTIATWMKHTM... | null | null | acetylcholine transport [GO:0015870]; acetylcholine uptake [GO:0051630]; chemical synaptic transmission [GO:0007268]; neurotransmitter loading into synaptic vesicle [GO:0098700]; positive regulation of acetylcholine secretion, neurotransmission [GO:0014057]; positive regulation of long-term synaptic potentiation [GO:19... | AP-1 adaptor complex [GO:0030121]; AP-2 adaptor complex [GO:0030122]; axon [GO:0030424]; axon terminus [GO:0043679]; cholinergic synapse [GO:0098981]; cytoplasm [GO:0005737]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]; termi... | acetylcholine transmembrane transporter activity [GO:0005277]; acetylcholine:proton antiporter activity [GO:0005278]; monoamine transmembrane transporter activity [GO:0008504] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Vesicular transporter family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q62666}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=acetylcholine(out) + 2 H(+)(in) = acetylcholine(in) + 2 H(+)(out); Xref=Rhea:RHEA:72891, ChEBI:CHEBI:15355, ChEBI:CHEBI:15378; Evidence={ECO:0000250|UniProtKB:Q16572}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72892; Evidence={ECO:0000250|UniProtKB:Q16572}; CATALYTIC ACTIVITY: Re... | null | null | null | null | FUNCTION: Electrogenic antiporter that exchanges one cholinergic neurotransmitter, acetylcholine or choline, with two intravesicular protons across the membrane of synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to store neurotransmitters inside the vesicles prio... | Mus musculus (Mouse) |
O35305 | TNR11_MOUSE | MAPRARRRRQLPAPLLALCVLLVPLQVTLQVTPPCTQERHYEHLGRCCSRCEPGKYLSSKCTPTSDSVCLPCGPDEYLDTWNEEDKCLLHKVCDAGKALVAVDPGNHTAPRRCACTAGYHWNSDCECCRRNTECAPGFGAQHPLQLNKDTVCTPCLLGFFSDVFSSTDKCKPWTNCTLLGKLEAHQGTTESDVVCSSSMTLRRPPKEAQAYLPSLIVLLLFISVVVVAAIIFGVYYRKGGKALTANLWNWVNDACSSLSGNKESSGDRCAGSHSATSSQQEVCEGILLMTREEKMVPEDGAGVCGPVCAAGGPWAEVRDS... | null | null | adaptive immune response [GO:0002250]; cellular response to zinc ion starvation [GO:0034224]; circadian temperature homeostasis [GO:0060086]; lymph node development [GO:0048535]; mammary gland alveolus development [GO:0060749]; multinuclear osteoclast differentiation [GO:0072674]; ossification [GO:0001503]; positive re... | cell surface [GO:0009986]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121] | cytokine binding [GO:0019955]; metal ion binding [GO:0046872]; tumor necrosis factor receptor activity [GO:0005031] | PF18278;PF00020; | 2.10.50.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y6Q6}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:23478294}. | null | null | null | null | null | FUNCTION: Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis (PubMed:20483727, PubMed:23478294, PubMed:9878548). Its interaction with EEIG1 promotes osteoclastogenesis via facilitating the transcription of NFATC1 and activation of PLCG2 (PubMed:23478294). Involved in the regulation ... | Mus musculus (Mouse) |
O35309 | NMI_MOUSE | MDADKDNIKQACDERSAEMDDMRGEQSMGLVHEIMSENKELDEEIKKLEAELQSDAREFQIKENVPEKKLKLTSVESPKDGCHFSNSSCSFQVSSQILYELQEGQALITFEKEEVAQNVISMGNHVVQMEGTPVKVSAHPVPLNTGVRFQVHVDISKMKINVTGIPDELSEEQTRDKLELSFCKSRNGGGEVESVDYDRKSRSAVITFVETGVVDKILKKKTYPLYMNQKCHSVAVSPCIERCLEKYQVFSAVSKKTVLLTGLEGIPVDEETGEDLLNIHFQRKNNGGGEVEVVKCSLDQSFAAYFKEEARETI | null | null | innate immune response [GO:0045087]; macrophage activation involved in immune response [GO:0002281]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of innate immune response [GO:0045824]; negative regulation of interferon-alpha production [GO:0032687]; negative regulation of inte... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | identical protein binding [GO:0042802] | PF07334;PF07292; | 3.30.70.330; | NMI family | PTM: May be ubiquitinated. {ECO:0000250|UniProtKB:Q13287}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13287}. Nucleus {ECO:0000250|UniProtKB:Q13287}. Secreted {ECO:0000250|UniProtKB:Q13287}. Note=Cytoplasmic NMI localizes in punctate granular structures. Nuclear localization increased following IFN-alpha treatment. Extracelullar following secretion by macrophage. ... | null | null | null | null | null | FUNCTION: Acts as a signaling pathway regulator involved in innate immune system response (PubMed:23956435). In response to interleukin 2/IL2 and interferon IFN-gamma/IFNG, interacts with signal transducer and activator of transcription/STAT which activate the transcription of downstream genes involved in a multitude o... | Mus musculus (Mouse) |
O35310 | HS3S1_MOUSE | MTLLLLGAVLLVAQPQLVHSHPAAPGPGLKQQELLRKVIILPEDTGEGTASNGSTQQLPQTIIIGVRKGGTRALLEMLSLHPDVAAAENEVHFFDWEEHYSQGLGWYLTQMPFSSPHQLTVEKTPAYFTSPKVPERIHSMNPTIRLLLILRDPSERVLSDYTQVLYNHLQKHKPYPPIEDLLMRDGRLNLDYKALNRSLYHAHMLNWLRFFPLGHIHIVDGDRLIRDPFPEIQKVERFLKLSPQINASNFYFNKTKGFYCLRDSGKDRCLHESKGRAHPQVDPKLLDKLHEYFHEPNKKFFKLVGRTFDWH | 2.8.2.23 | null | glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012] | Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796] | [heparan sulfate]-glucosamine 3-sulfotransferase 1 activity [GO:0008467] | PF00685; | 3.40.50.300; | Sulfotransferase 1 family | null | SUBCELLULAR LOCATION: Golgi apparatus lumen {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 3-sulfo-alpha-D-glucosaminyl-[heparan sulfate](n) + adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:15461, Rhea:RHEA-COMP:9830, Rhea:RHEA-COMP:9831, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CH... | null | null | null | null | FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan (PubMed:15060080, PubMed:9346953). Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact) (PubMed:15060080, PubMed:9346953). ... | Mus musculus (Mouse) |
O35312 | GDF8_RAT | MIQKPQMYVYIYLFVLIAAGPVDLNEDSEREANVEKEGLCNACAWRQNTRYSRIEAIKIQILSKLRLETAPNISKDAIRQLLPRAPPLRELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLMQADGKPKCCFFKFSSKIQYNKVVKAQLWIYLRAVKTPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMSPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPGPGEDGLNPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQ... | null | null | cellular response to dexamethasone stimulus [GO:0071549]; cellular response to hypoxia [GO:0071456]; muscle cell cellular homeostasis [GO:0046716]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of insulin receptor signaling pathway [GO:0046627]; negative regulation of mus... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}. | null | null | null | null | null | FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000250|UniProtKB:O08689}. | Rattus norvegicus (Rat) |
O35314 | SCG1_RAT | MQRAMLLGLLGAAALAAVISAPVDNRDHNEEMVTRCIIEVLSNALSKSSAPTITPECRQVLRKSGKEVKGEEKGENENSKFEVRLLRDPSDASVGRWASSREETGAPVEDSPGQAKVDNEEWTGGGGHSREAVDDQESLHPSNQQVSKEAKIRHSEERGGKEEEEEEGKIYPKGEHRGDAGEEKKHTEESGEKHNAFSNKRSEASAKKKEESVARAEAHFVELEKTHSREQSSQESGEETRRQEKPQELPDQDQSEEESEEGEEGEEGATSEVTKRRPRHHHWRSQSNKPSYEGRRPLSEERKHAAGESKDANVATANLG... | null | null | null | extracellular space [GO:0005615]; secretory granule [GO:0030141] | null | PF01271; | null | Chromogranin/secretogranin protein family | PTM: Extensively processed in glucagonoma tissue by limited proteolysis at conserved basic residues. Alternative processing are seen in different tissues. The proglucagon-converting enzymes present in transformed alpha-cells are likely candidates to be involved in tissue-specific processing. | SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine secretory granules. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides. | Rattus norvegicus (Rat) |
O35316 | SC6A6_MOUSE | MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEADGKPPQREKWSSKIDFVLSVAGGFVGLGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEVIIGQYTSEGGITCWEKICPLFSGIGYASIVIVSLLNVYYIVILAWATYYLFHSFQKDLPWAHCNHSWNTPQCMEDTLRRNESHWVSLSTANFTSPVIEFWERNVLSLSSGIDNPGSLKWDLALCLLLVWLVCFFCIWKGVRSTGKVVYFTATFPFAMLLVLLVRGLTLPGAGEGIKFYLYPDISRLGDPQVWIDAGTQIFFSYAICLGAMTSLGSYNKYKY... | null | null | amino acid import across plasma membrane [GO:0089718]; amino acid transport [GO:0006865]; gamma-aminobutyric acid import [GO:0051939]; import across plasma membrane [GO:0098739]; modulation of chemical synaptic transmission [GO:0050804]; neurotransmitter transport [GO:0006836]; positive regulation of cell differentiati... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell projection [GO:0042995]; dendrite [GO:0030425]; GABA-ergic synapse [GO:0098982]; microvillus membrane [GO:0031528]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane protein complex [GO:0098797]; postsynapti... | alanine transmembrane transporter activity [GO:0022858]; amino acid:sodium symporter activity [GO:0005283]; gamma-aminobutyric acid transmembrane transporter activity [GO:0015185]; gamma-aminobutyric acid:sodium:chloride symporter activity [GO:0005332]; taurine binding [GO:0030977]; taurine transmembrane transporter ac... | PF00209; | null | Sodium:neurotransmitter symporter (SNF) (TC 2.A.22) family, SLC6A6 subfamily | PTM: Taurine transport activity is down-regulated upon Ser-322 phosphorylation. {ECO:0000250|UniProtKB:Q00589}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P31641}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=4-aminobutanoate(out) + chloride(out) + 2 Na(+)(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na(+)(in); Xref=Rhea:RHEA:70687, ChEBI:CHEBI:17996, ChEBI:CHEBI:29101, ChEBI:CHEBI:59888; Evidence={ECO:0000269|PubMed:30270321, ECO:0000269|PubMed:9375654}; PhysiologicalDirection=left-to-right; ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.5 uM for taurine {ECO:0000269|PubMed:1465453}; KM=13.2 uM for taurine {ECO:0000269|PubMed:9375654}; KM=10.7 uM for hypotaurine {ECO:0000269|PubMed:30270321}; KM=56 uM for beta-alanine {ECO:0000269|PubMed:1465453}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0 (for taurine transport). {ECO:0000269|PubMed:9375654}; | null | FUNCTION: Mediates sodium- and chloride-dependent transport of taurine (PubMed:1465453, PubMed:30270321, PubMed:9375654). Can also mediate transport of hypotaurine, beta-alanine and gamma-aminobutyric acid (GABA) (PubMed:1465453, PubMed:30270321, PubMed:9375654). {ECO:0000269|PubMed:1465453, ECO:0000269|PubMed:30270321... | Mus musculus (Mouse) |
O35317 | PBX3_MOUSE | MDDQSRMLQTLAGVNLAGHSVQGGMALPPPPHGHEGADGDGRKQDIGDILHQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRGAQEEDPPDPQLMRLDNMLLAEGVSGPEKGGGSAAAAAAAAASGGSSDNSIEHSDYRAKLTQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVGIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEILNEYFYSHLSNPYPSEEAKEELAKKCSITVSQVSNWFGNKRIRYKKNIGKFQEEANLYAAKTAVTAAHAVA... | null | null | adult locomotory behavior [GO:0008344]; animal organ morphogenesis [GO:0009887]; brain development [GO:0007420]; dorsal spinal cord development [GO:0021516]; embryonic organ development [GO:0048568]; eye development [GO:0001654]; neuron development [GO:0048666]; positive regulation of transcription by RNA polymerase II... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF05920;PF03792; | 1.10.10.60; | TALE/PBX homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. | null | null | null | null | null | FUNCTION: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. {ECO:0000250}. | Mus musculus (Mouse) |
O35324 | SH21B_MOUSE | MDLPYYHGCLTKRECEALLLKGGVDGNFLIRDSESVPGALCLCVSFKKLVYSYRIFREKHGYYRIETDAHTPRTIFPNLQELVSKYGKPGQGLVVHLSNPIMRNNLCQRGRRMELELNVYENTDEEYVDVLP | null | null | adaptive immune response [GO:0002250]; leukocyte activation involved in immune response [GO:0002366]; natural killer cell inhibitory signaling pathway [GO:0002769]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of bone resorption [GO:0045779]; negative regulation of natural killer cell med... | cytosol [GO:0005829] | phosphotyrosine residue binding [GO:0001784]; signaling adaptor activity [GO:0035591] | PF00017; | 3.30.505.10; | null | PTM: Phosphorylated on tyrosine residues; probably at Tyr-120 and/or Tyr-127. {ECO:0000269|PubMed:16127454}. | null | null | null | null | null | null | FUNCTION: Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as CD84, SLAMF1, LY9 and CD244. In SLAM signaling seems to cooperate with SH2D1A/SAP. Plays a role in regulation of effector functions of natural killer (NK) cells by controlling signal transduction th... | Mus musculus (Mouse) |
O35326 | SRSF5_MOUSE | MSGCRVFIGRLNPAAREKDVERFFKGYGRIRDIDLKRGFGFVEFEDPRDADDAVYELDGKELCSERVTIEHARARSRGGRGRGRYSDRFSSRRPRNDRRNAPPVRTENRLIVENLSSRVSWQDLKDFMRQAGEVTFADAHRPKLNEGVVEFASYGDLKNAIEKLSGKEINGRKIKLIEGSKRHRSRSRSRSRTRSSSRSRSRSRSRRSKSYSRSRSRSRSRSKSRSGSRSPVPEKSQKRGSSSRSKSPASVDRQRSRSRSRSRSVDSGN | null | null | mRNA splicing, via spliceosome [GO:0000398]; positive regulation of RNA splicing [GO:0033120]; response to insulin [GO:0032868]; response to wounding [GO:0009611] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607] | mRNA binding [GO:0003729]; protein kinase B binding [GO:0043422]; RNA binding [GO:0003723]; RS domain binding [GO:0050733] | PF00076; | 3.30.70.330; | Splicing factor SR family | PTM: Extensively phosphorylated on serine residues in the RS domain. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be required for progression through G1 and entry into S phase of cell growth. May play a regulatory role in pre-mRNA splicing. Autoregulates its own expression. Plays a role in constitutive splicing and can modulate the selection of alternative splice sites (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
O35331 | PDXK_RAT | MEGECRVLSIQSHVVRGYVGNRAAMFPLQVLGFEVDAVNSVQFSNHTGYAHWKGQVLTSQELHALYEGLKANNVNKYDYVLTGYTRDKSFLGMVVDIVQELKQQNSRLVYVCDPVMGDKWNGEGSMYVPQDLLPVYREKVVPMADIITPNQFEAELLSGRKIHSQEEAFAVMDVLHRMGPDTVVITSSDLPSPKGSDYLMALGSQRMRKPDGSTVTQRIRMEMRKVDPVFVGTGDLFAAMLLAWTHKHPDNLKVACEKTVSAMQHVLQRTIRCAKAEAGEGQKPSPAQLELRMVQSRKDIEDPEIVVQATVL | 2.7.1.35 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P82197}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O00764}; | negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; pyridoxal 5'-phosphate salvage [GO:0009443]; pyridoxal metabolic process [GO:0042817]; pyridoxal phosphate biosynthetic process [GO:0042823]; pyridoxal phosphate metabolic process [GO:0042822]; pyridoxamine metabolic process [GO:004281... | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; organic cyclic compound binding [GO:0097159]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]; pyridoxal binding [GO:0070280]; pyridoxal kinase activity [GO:0008478]; small molecule binding [GO:0036094] | PF08543; | 3.40.1190.20; | Pyridoxine kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00764}. | CATALYTIC ACTIVITY: Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; Evidence={ECO:0000250|UniProtKB:O00764}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10225; Evi... | null | PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1. {ECO:0000250|UniProtKB:O00764}.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000250|UniProtKB:O00764}.; PATHWAY: Cofactor metabolism; ... | null | null | FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (By similarity). PLP is the active form of vitamin B6, and acts as a cofa... | Rattus norvegicus (Rat) |
O35343 | IMA3_MOUSE | MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPQEDICEDSDIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQ... | null | null | NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606]; response to hydrogen peroxide [GO:0042542] | cytosol [GO:0005829]; male germ cell nucleus [GO:0001673]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin... | Mus musculus (Mouse) |
O35345 | IMA7_MOUSE | METMASPGKDNYRMKSYKNNALNPEEMRRRREEEGIQLRKQKREQQLFKRRNVELINEEAAMFDSLLMDSYVSSTTGESVITREMVEMLFSDDSDLQLATTQKFRKLLSKEPSPPIDEVINTPGVVDRFVEFLKRNENCTLQFEAAWALTNIASGTSQQTKIVIEAGAVPIFIELLNSDFEDVQEQAVWALGNIAGDSSLCRDYVLNCSILNPLLTLLTKSTRLTMTRNAVWALSNLCRGKNPPPEFAKVSPCLPVLSRLLFSSDSDLLADACWALSYLSDGPNEKIQAVIDSGVCRRLVELLMHNDYKVASPALRAVGN... | null | null | entry of viral genome into host nucleus through nuclear pore complex via importin [GO:0075506]; maternal process involved in female pregnancy [GO:0060135]; NLS-bearing protein import into nucleus [GO:0006607]; positive regulation of cytokine production involved in inflammatory response [GO:1900017]; positive regulation... | cytosol [GO:0005829]; host cell [GO:0043657]; NLS-dependent protein nuclear import complex [GO:0042564]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin... | Mus musculus (Mouse) |
O35346 | FAK1_RAT | MAAAYLDPNLNHTPSSSTKTHLGTGTERSPGAMERVLKVFHYFESSNEPTTWASIIRHGDATDVRGIIQKIVDSHKVKHVACYGFRLSHLRSEEVHWLHVDMGVSSVREKYELAHPPEEWKYELRIRYLPKGFLNQFTEDKPTLNFFYQQVKSDYMLEIADQVDQDIALKLGCLEIRRSYWEMRGNALEKKSNYEVLEKDVGLKRFFPKSLLDSVKAKTLRKLIQQTFRQFANLNREESILKFFEILSPVYRFDKECFKCALGSSWIISVELAIGPEEGISYLTDKGCNPTHLADFNQVQTIQYSNSEDKDRKGMLQLKI... | 2.7.10.2 | null | angiogenesis [GO:0001525]; axonogenesis [GO:0007409]; blood vessel development [GO:0001568]; cell migration [GO:0016477]; cellular response to transforming growth factor beta stimulus [GO:0071560]; central nervous system neuron axonogenesis [GO:0021955]; endothelial cell migration [GO:0043542]; ephrin receptor signalin... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell cortex [GO:0005938]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; intercalated dis... | actin binding [GO:0003779]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; JUN kinase binding [GO:0008432]; molecular function activator activity [GO:0140677]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphatase binding [GO:0019902]; phospha... | PF21477;PF00373;PF18038;PF03623;PF07714; | 1.20.80.10;1.20.120.330;2.30.29.30;1.20.5.540;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, FAK subfamily | PTM: Phosphorylated on tyrosine residues upon activation, e.g. upon integrin signaling. Tyr-397 is the major autophosphorylation site, but other kinases can also phosphorylate this residue. Phosphorylation at Tyr-397 promotes interaction with SRC and SRC family members, leading to phosphorylation at Tyr-576, Tyr-577 an... | SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q00944}. Cell membrane {ECO:0000250|UniProtKB:Q00944}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00944}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q00944}. Cytoplasm, cell cor... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryon... | Rattus norvegicus (Rat) |
O35350 | CAN1_MOUSE | MTEELITPVYCTGVSAQVQKKRDKELGLGRHENAIKYLGQDYETLRARCLQSGVLFQDEAFPPVSHSLGFKELGPHSSKTYGIKWKRPTELMSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNETILHRVVPYGQSFQDGYAGIFHFQLWQFGEWVDVVIDDLLPTKDGKLVFVHSAQGNEFWSALLEKAYAKVNGSYEALSGGCTSEAFEDFTGGVTEWYDLQKAPSDLYQIILKALERGSLLGCSINISDIRDLEAITFKNLVRGHAYSVTGAKQVTYQGQRVNLIRMRNPWGEVEWKGPWSDSSYEWNKVDPY... | 3.4.22.52 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P07384}; Note=Binds 4 Ca(2+) ions. {ECO:0000250|UniProtKB:P07384}; | cellular response to hydrogen peroxide [GO:0070301]; mammary gland involution [GO:0060056]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; posit... | calpain complex [GO:0110158]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; cytoskeletal protein binding [GO:0008092]; enzyme binding [GO:0019899] | PF01067;PF13833;PF00648; | 2.60.120.380;3.90.70.10;1.10.238.10; | Peptidase C2 family | PTM: Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms (By similarity). {ECO:0000250|UniProtKB:P07384}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07384}. Cell membrane {ECO:0000250|UniProtKB:P07384}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250|UniProtKB:P07384}. | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52; Evidence={ECO:0000250|UniProtKB:P07384}; | null | null | null | null | FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-388' and 'His-410'. Cleaves and activates caspase-7 (CASP7). {ECO:0000250|UniProtKB:P07384}. | Mus musculus (Mouse) |
O35375 | NRP2_MOUSE | MDMFPLTWVFLALYFSGHEVRSQQDPPCGGRLNSKDAGYITSPGYPQDYPSHQNCEWIVYAPEPNQKIVLNFNPHFEIEKHDCKYDFIEIRDGDSESADLLGKHCGNIAPPTIISSGSVLYIKFTSDYARQGAGFSLRYEIFKTGSEDCSKNFTSPNGTIESPGFPEKYPHNLDCTFTILAKPRMEIILQFLTFDLEHDPLQVGEGDCKYDWLDIWDGIPHVGPLIGKYCGTKTPSKLRSSTGILSLTFHTDMAVAKDGFSARYYLIHQEPPENFQCNVPLGMESGRIANEQISASSTFSDGRWTPQQSRLHGDDNGWTP... | null | null | angiogenesis [GO:0001525]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cellular response to leukemia inhibitory factor [GO:1990830]; dorsal root ganglion morphogenesis [GO:1904835]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375];... | axon [GO:0030424]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211] | heparin binding [GO:0008201]; metal ion binding [GO:0046872]; semaphorin receptor activity [GO:0017154]; vascular endothelial growth factor receptor activity [GO:0005021] | PF00431;PF11980;PF00754;PF00629; | 2.60.120.200;2.60.120.260;2.60.120.290; | Neuropilin family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:O60462}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60462}. | null | null | null | null | null | FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF. | Mus musculus (Mouse) |
O35379 | MRP1_MOUSE | MALRSFCSADGSDPLWDWNVTWHTSNPDFTKCFQNTVLTWVPCFYLWSCFPLYFFYLSRHDRGYIQMTHLNKTKTALGFFLWIICWADLFYSFWERSQGVLRAPVLLVSPTLLGITMLLATFLIQLERRKGVQSSGIMLTFWLVALLCALAILRSKIISALKKDAHVDVFRDSTFYLYFTLVLVQLVLSCFSDCSPLFSETVHDRNPCPESSASFLSRITFWWITGMMVHGYRQPLESSDLWSLNKEDTSEEVVPVLVNNWKKECDKSRKQPVRIVYAPPKDPSKPKGSSQLDVNEEVEALIVKSPHKDREPSLFKVLYK... | 7.6.2.2; 7.6.2.3 | null | astrocyte differentiation [GO:0048708]; cell chemotaxis [GO:0060326]; cellular response to amyloid-beta [GO:1904646]; cobalamin transport [GO:0015889]; cyclic nucleotide transport [GO:0070729]; export across plasma membrane [GO:0140115]; glial cell differentiation [GO:0010001]; glutathione transmembrane transport [GO:0... | apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886] | ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ABC-type transporter activity [GO:0140359]; ABC-type vitamin B12 transporter activity [GO:0015420]; ABC-type xenobiotic transporter activity [GO:0008559]; amide transmembrane transporter activity [GO:0042887]; ATP binding [GO:0005524]; ATP hydrolysis a... | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:9359705}; CATALYTIC ACTIVITY: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 nM for leukotriene C4 {ECO:0000269|PubMed:9281595}; KM=3.3 nM for S-(2,4-dinitrophenyl)glutathione {ECO:0000269|PubMed:9359705}; Vmax=350 pmol/min/mg enzyme for leukotriene C4 transport {ECO:0000269|PubMed:9281595}; | null | null | null | FUNCTION: Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs by decreasing accumulation of... | Mus musculus (Mouse) |
O35381 | AN32A_MOUSE | MEMDKRIYLELRNRTPSDVKELVLDNCKSIEGKIEGLTDEFEELEFLSTINVGLTSISNLPKLNKLKKLELSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNAYRENVFKLLPQVMYLDGYDRDNKEAPDSDVEGYVEDDDEEDEDEEEYDEYAQLVEDEEEEDEEEEGEEEDVSGEEEEDEEGYNDGEVDDEEDEEEAGEEEGSQKRKREPDDEGEEDD | null | null | nucleocytoplasmic transport [GO:0006913]; regulation of apoptotic process [GO:0042981] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | histone binding [GO:0042393] | PF14580; | 3.80.10.10; | ANP32 family | PTM: Phosphorylated on serine residues, at least in part by casein kinase 2/CK2. {ECO:0000250|UniProtKB:P39687}.; PTM: Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12807913}. Cytoplasm {ECO:0000269|PubMed:12807913}. Endoplasmic reticulum {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. Translocates to the cytoplasm during the process of neuritogenesis. | null | null | null | null | null | FUNCTION: Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription. Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation. In addition, plays a role in the modulation of hist... | Mus musculus (Mouse) |
O35382 | EXOC4_MOUSE | MAAEAAGGKYRSTVSKSKDPSGLLISVIRTLSTSDDVEDRENEKGRLEEAYEKCDRDLDELIVQHYTELTTAIRTYQSITERITNSRNKIKQVKENLLSCKMLLHCKRDELRKLWIEGIEHKHVLNLLDEIENIKQVPQKLEQCMASKHYLSATDMLVSAVESLEGPLLQVEGLSDLRLELHSKKMNLHLVLIEELHRHLYIKSTSRVVQRNKEKGKMSSHGKDPSPGPLIDVSNIPTPRKFLDASQYSAAGGSSVREMNLQDVKEDLECDPEENSTLFMGILIQGLARLKKIPETVKAIKERLEQELKQIVKRSTTQVA... | null | null | chemical synaptic transmission [GO:0007268]; establishment of cell polarity [GO:0030010]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; Golgi to transport vesicle transport [GO:0055108]; membrane biogenesis [GO:0044091]; membrane fission [GO:0090148]; mitotic cytokinesis [GO:0000281]; oligod... | cell leading edge [GO:0031252]; centrosome [GO:0005813]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; exocyst [GO:0000145]; Flemming body [GO:0090543]; growth cone [GO:0030426]; growth cone membrane [GO:0032584]; microvillus [GO:0005902]; myelin sheath abaxonal region [GO:0035748]; neuron projection [GO:0043005... | ionotropic glutamate receptor binding [GO:0035255]; PDZ domain binding [GO:0030165]; protein-containing complex binding [GO:0044877] | PF20652;PF04048; | null | SEC8 family | null | SUBCELLULAR LOCATION: Midbody, Midbody ring {ECO:0000250|UniProtKB:Q96A65}. Cell projection {ECO:0000250|UniProtKB:Q62824}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q96A65}. Note=Colocalizes with CNTRL/centriolin at the midbody ring (By similarity). Localizes at the lead... | null | null | null | null | null | FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000250|UniProtKB:Q62824}. | Mus musculus (Mouse) |
O35385 | PPE2_MOUSE | MGSSSSTQHHFAFQNAEKAFKAAALIQRWYRRYMARLEMRRRCTWNIFQSIEYAGQQDQVKLHEFFSYLVDHFTPSSHHERDFLNRMFTEERFAQDVETEEGGDFESIEVPDSYTGPRLSFPLLPDHATALVEAFRLRQQLHARYVLNLLYETRKHLAQLPNINRVSTCYSEEVTVCGDLHGQLDDLIFIFYKNGLPSPERAYVFNGDFVDRGKDSVEVLMVLFAFMLVYPKEFHLNRGNHEDHLVNLRYGFTKEVMHKYKIHGKKILRTLQDVFCWLPLATLVDEKVLVLHGGVSDKTDLELLAKLDRHKIVSTMRCKT... | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; | detection of stimulus involved in sensory perception [GO:0050906]; negative regulation of MAPK cascade [GO:0043409]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; visual perception [GO:0007601] | cytosol [GO:0005829]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; manganese ion binding [GO:0030145]; mitogen-activated protein kinase kinase kinase binding [GO:0031435]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase... | PF13499;PF00149;PF08321; | 3.60.21.10;1.10.238.10; | PPP phosphatase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-... | null | null | null | null | FUNCTION: May play a role in phototransduction. May dephosphorylate photoactivated rhodopsin. May function as a calcium sensing regulator of ionic currents, energy production or synaptic transmission. | Mus musculus (Mouse) |
O35386 | PAHX_MOUSE | MNLTRAGARLQVLLGHLGRPSAPTIVAQPVSGLASPASFQPEQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVSDDDIQRFRAEFERICREEVKPPGIVIMRDVALAKQDYMPSDRMVSKIQDFQEDEELFRYCLLPEILKYVECFTGPNIMALHGMLINKPPDVGKKTSRHPLHQDLHYFPFRPSNLIVCAWTAMEHIDRNNGCLVVLPGTHKGTLKPHDYPKWEGGVNKMYHGIQDYDPNSPRVHLVMEKGDTVFFHPLLIHGSGRNKTQGFRKAISCHFGSSDCQCIDVSGTSQENIAREVVEMAEKKYGFQGVMDF... | 1.14.11.18 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evid... | 2-oxobutyrate catabolic process [GO:0019606]; 2-oxoglutarate metabolic process [GO:0006103]; fatty acid alpha-oxidation [GO:0001561]; isoprenoid metabolic process [GO:0006720]; methyl-branched fatty acid metabolic process [GO:0097089] | 9+0 non-motile cilium [GO:0097731]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | catalytic activity [GO:0003824]; ferrous iron binding [GO:0008198]; L-ascorbic acid binding [GO:0031418]; phytanoyl-CoA dioxygenase activity [GO:0048244] | PF05721; | 2.60.120.620; | PhyH family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O14832}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:16065, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57334, ChEBI:CHEBI:57391; EC=1.14.11.18; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirect... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. | null | null | FUNCTION: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon at... | Mus musculus (Mouse) |
O35387 | HAX1_MOUSE | MSVFDLFRGFFGFPGPRSHRDPFFGGMTRDDDDDDDDDDEAEEDRGAWGRESYAFDGSQPPEEFGFSFSPRGGMRFHGNFGFDDLVRDFNSIFSEMGAWTLPSHSPELPGPESETPGERLREGQTLRDSMLKYPDSHQPRIFEGVLESHAKPESPKPAPDWGSQGPFHRLDDTWPVSPHSRAKEDKDLDSQVSQEGLGPLLQPQPKSYFKSISVTKITKPDGTVEERRTVVDSEGRRETTVTHQEAHDSSRSDPDSQRSSALDDPFSILDLLLGRWFRSR | null | null | cell surface receptor signaling pathway [GO:0007166]; granulocyte colony-stimulating factor signaling pathway [GO:0038158]; negative regulation of apoptotic process [GO:0043066]; positive regulation of granulocyte differentiation [GO:0030854]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; posit... | actin cytoskeleton [GO:0015629]; apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; lamellipodium [GO:0030027]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrial o... | interleukin-1 binding [GO:0019966]; protein domain specific binding [GO:0019904]; signaling adaptor activity [GO:0035591] | null | null | HAX1 family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:16814492, ECO:0000269|PubMed:26915802}. Endoplasmic reticulum {ECO:0000269|PubMed:10760273}. Nucleus membrane {ECO:0000305|PubMed:16814492}. Cytoplasmic vesicle {ECO:0000269|PubMed:10760273, ECO:0000269|PubMed:16814492}. Cytoplasm, cell cortex {ECO:0000250|... | null | null | null | null | null | FUNCTION: Recruits the Arp2/3 complex to the cell cortex and regulates reorganization of the cortical actin cytoskeleton via its interaction with KCNC3 and the Arp2/3 complex. Slows down the rate of inactivation of KCNC3 channels. Promotes GNA13-mediated cell migration. Involved in the clathrin-mediated endocytosis pat... | Mus musculus (Mouse) |
O35393 | EFNB3_MOUSE | MGAPHFGPGGVQVGALLLLGFAGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSAEPGRDTIPGDPSSNATSRGAEGPLPPPSMPAVAGAAGGMALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGTADPPFCPHYEKVSGDYGH... | null | null | adult walking behavior [GO:0007628]; axon choice point recognition [GO:0016198]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; negative regulation of axonogenesis [GO:0050771]; positive regulation of presynapse assembly [GO:1905608]; positive regulation of synaptic transmission [GO:0050806... | glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734] | ephrin receptor binding [GO:0046875] | PF00812; | 2.60.40.420; | Ephrin family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional sign... | Mus musculus (Mouse) |
O35394 | PRAF1_RAT | MAAQKDQQKDAEVEGLSATTLLPKLIPSGAGREWLERRRATIRPWGTFVDQQRFSRPRNVGELCQRLVRNVEYYQSNYVFVFLGLILYCVVTSPMLLVALAVFFGACYILYLRTLQSKLVLFGREVSPAHQYALAGGVSFPFFWLAGAGSAVFWVLGATLVLIGSHAAFHQIEPADGEELQMEPV | null | null | vesicle-mediated transport [GO:0016192] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; plasma membrane [GO:0005886]; synapse [GO:0045202]; synaptic vesicle [GO:0008021] | GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; proline-rich region binding [GO:0070064]; protein-macromolecule adaptor activity [GO:0030674] | PF03208; | null | PRA1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10751420}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:10751420}. Golgi apparatus {ECO:0000269|PubMed:10751420, ECO:0000269|PubMed:11096102, ECO:0000269|PubMed:12107180}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:00... | null | null | null | null | null | FUNCTION: General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI1. {ECO:0000269|PubMed:10751420, ECO:0000269|Pub... | Rattus norvegicus (Rat) |
O35397 | CASP6_RAT | MTETDGFYRSREVLDPAEQYKMDHKRRGTALIFNHERFFWHLALPERRGTNADRDNPTRRFSELGFEVKCFNDLRAEELLLKIHEVSTSSHVDADCFLCVFLSHGEGNHIYAYDAKIEIQTLTGLFKGDKCQSLVGKPKIFIIQACRGSQHDVPLVPLDVVDHQTDKLDDNVTQVDAASVYTLPAGADFLMCYSVAEGYYSHRETVNGSWYIQDLSEMLARHGSSLEFTELLTLVNRKVSQRRVDFCKDPGAIGKKQVPCFASMLTKKLHFCPKPSK | 3.4.22.59 | null | activation of innate immune response [GO:0002218]; acute inflammatory response to non-antigenic stimulus [GO:0002525]; axonal fasciculation [GO:0007413]; cellular response to staurosporine [GO:0072734]; epithelial cell differentiation [GO:0030855]; hepatocyte apoptotic process [GO:0097284]; intrinsic apoptotic signalin... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuronal cell body [GO:0043025]; nucleus [GO:0005634] | cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200]; endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802] | PF00656; | 3.40.50.1460; | Peptidase C14A family | PTM: Phosphorylated by NUAK1; phosphorylation inhibits self-activation. Phosphorylation at Ser-240 by AMP-activated protein kinase (PRKAA1 or PRKAA2) inhibits autocleavage, preventing caspase activation, thereby preventing hepatocyte apoptosis. {ECO:0000250|UniProtKB:P55212}.; PTM: Palmitoylation by ZDHHC17 blocks dime... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P55212}. Nucleus {ECO:0000250|UniProtKB:P55212}. | CATALYTIC ACTIVITY: Reaction=Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59; Evidence={ECO:0000250|UniProtKB:P55212}; | null | null | null | null | FUNCTION: Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity (By similarity). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein NUMA1 and lamin A/LMNA thereby inducing... | Rattus norvegicus (Rat) |
O35400 | ST2B1_MOUSE | MDGPQPRALWSSSEKNVSEMSWNFGGEYFRYKGIPFPVGMYSPESLSLAENTSNVRDDDIFIVTYPKSGTNWMIEIVCLILKDGDPSWIRSEPIWQRAPWCETIISAFNVLDRPSPRIMSSHLPIELFTKAFFSSKAKVIYVGRNPRDVVVSLYYYSKIAGQLKDPGTPDQFLQNFLKGEVQFGSWFDHIKGWIRMQNQENFLFITYEELQQDLRGSVQRICEFLGRPLGEEALSSVVAHSAFAAMKANTMSNYSLLPASLLDHRQGEFLRKGISGDWKNHFTVAQSEAFDSVYREQMHGVQRFPWDTSEEDSSPDGQPD... | 2.8.2.2 | null | cholesterol metabolic process [GO:0008203]; sulfate assimilation [GO:0000103]; sulfation [GO:0051923] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634] | cholesterol sulfotransferase activity [GO:0051922]; sulfotransferase activity [GO:0008146] | PF00685; | 3.40.50.300; | Sulfotransferase 1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O00204}. Microsome {ECO:0000250|UniProtKB:O00204}. Nucleus {ECO:0000250|UniProtKB:O00204}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2; Evidence={ECO:0000269|PubMed:12639899}; CATALYTIC ACTIVITY: Reac... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.88 uM for cholesterol (isoform 2) {ECO:0000269|PubMed:12639899}; KM=17.7 uM for pregnenolone (isoform 2) {ECO:0000269|PubMed:12639899}; KM=0.87 uM for cholesterol (isoform 1) {ECO:0000269|PubMed:12639899}; KM=16.7 uM for pregnenolone (isoform 1) {ECO:0000269|PubM... | null | null | null | FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Preferentially sulfonates cholesterol (PubMed:12639899). Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA). Cholester... | Mus musculus (Mouse) |
O35405 | PLD3_MOUSE | MKPKLMYQELKVPVEEPAGELPLNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLWEYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLEFPNATTSNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLQQLQALAPRGVKVRIAVSKPNGPLADLQSLLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDLTKIFEAYWFLGQAGSSIPSTWPRSFDTRYNQETPMEICLNGTPALAYLASAPPPLCPSGRTPDLKALLNVVDSARSFI... | 3.1.16.1 | null | inflammatory response [GO:0006954]; innate immune response [GO:0045087]; myotube differentiation [GO:0014902]; regulation of cytokine production involved in inflammatory response [GO:1900015] | early endosome membrane [GO:0031901]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765] | phospholipase D activity [GO:0004630]; single-stranded DNA 5'-3' DNA exonuclease activity [GO:0045145] | PF13918; | 3.30.870.10; | Phospholipase D family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8IV08}.; PTM: Proteolytically processed to a soluble form that is stable within endosomes and lysosomes. During transport through the secretory pathway becomes proteolysed by cysteine proteases, thereby releasing a stable soluble lysosomal lumenal polypeptide, whereas the tr... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8IV08}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8IV08}. Lysosome lumen {ECO:0000250|UniProtKB:Q8IV08}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IV08}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8I... | CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.; EC=3.1.16.1; Evidence={ECO:0000269|PubMed:30111894}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-5. {ECO:0000269|PubMed:30111894}; | null | FUNCTION: 5'->3' DNA exonuclease which digests single-stranded DNA (ssDNA) (PubMed:30111894). Regulates inflammatory cytokine responses via the degradation of nucleic acids, by reducing the concentration of ssDNA able to stimulate TLR9, a nucleotide-sensing receptor in collaboration with PLD4 (PubMed:30111894). May be ... | Mus musculus (Mouse) |
O35409 | FOLH1_MOUSE | MWNALQDRDSAEVLGHRQRWLRVGTLVLALTGTFLIGFLFGWFIKPSNEATGNVSHSGMKKEFLHELKAENIKKFLYNFTRTPHLAGTQNNFELAKQIHDQWKEFGLDLVELSHYDVLLSYPNKTHPNYISIINEDGNEIFKTSLSEQPPPGYENISDVVPPYSAFSPQGTPEGDLVYVNYARTEDFFKLEREMKISCSGKIVIARYGKVFRGNMVKNAQLAGAKGMILYSDPADYFVPAVKSYPDGWNLPGGGVQRGNVLNLNGAGDPLTPGYPANEHAYRHELTNAVGLPSIPVHPIGYDDAQKLLEHMGGPAPPDSS... | 3.4.17.21 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.; | folic acid-containing compound metabolic process [GO:0006760]; positive regulation of apoptotic process [GO:0043065]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508] | cell surface [GO:0009986]; membrane [GO:0016020]; plasma membrane [GO:0005886] | Ac-Asp-Glu binding [GO:1904492]; carboxypeptidase activity [GO:0004180]; dipeptidase activity [GO:0016805]; metal ion binding [GO:0046872]; metallocarboxypeptidase activity [GO:0004181]; peptidase activity [GO:0008233]; tetrahydrofolyl-poly(glutamate) polymer binding [GO:1904493] | PF02225;PF04389;PF04253; | 3.50.30.30;1.20.930.40;3.40.630.10; | Peptidase M28 family, M28B subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q04609}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q04609}. | CATALYTIC ACTIVITY: Reaction=Release of an unsubstituted, C-terminal glutamyl residue, typically from Ac-Asp-Glu or folylpoly-gamma-glutamates.; EC=3.4.17.21; | null | null | null | null | FUNCTION: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides (By similarity). In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropepti... | Mus musculus (Mouse) |
O35412 | SI1L1_RAT | MTSLKRSQTERPVTADRASVVSTDGTPKVHTDDFYMRRFRSQNGSLGSSVMAAVGPPRSEGPHHITSTPGVPKMGVRARIADWPPRKENVKESSRSSQEIETSSCLESLSSKGSPVSQGSSVSLNSNDSAMLKSIQNTLKNKTGPAESMDSRFLMPEAYPSSPRKALRRIRQRSNSDITISELDVDSFDECISPTYKSGPSLHREYGSTSSIDKQGTSGESFFGLLKGYKDDRADRGPTPTKLSDFLITGGGKGSGFSLDVIDGPISQRENLRLFKEREKPLKRRSKSETGDSSIFRKLRNAKGEELGKSSDLEDNRSED... | null | null | actin cytoskeleton organization [GO:0030036]; activation of GTPase activity [GO:0090630]; ephrin receptor signaling pathway [GO:0048013]; postsynaptic actin cytoskeleton organization [GO:0098974]; regulation of axonogenesis [GO:0050770]; regulation of dendrite morphogenesis [GO:0048814]; regulation of dendritic spine m... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; postsynapse [GO:0098794]; postsynaptic density [GO:0014069]; protein-containing complex [GO:0032991] | actin filament binding [GO:0051015]; ephrin receptor binding [GO:0046875]; GTPase activator activity [GO:0005096]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]; ubiquitin protein ligase binding [GO:0031625] | PF00595;PF21022;PF02145;PF11881; | 2.30.42.10;3.30.1120.160;3.40.50.11210; | null | PTM: Ubiquitinated and degraded by the SCF(BTRC) following phosphorylation by PLK2.; PTM: Phosphorylated at Ser-1367 by CDK5, creating a docking site for the POLO box domains of PLK2. Subsequently, PLK2 binds and phosphorylates SIPA1L1, leading to ubiquitination and degradation by the proteasome. {ECO:0000269|PubMed:18... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Postsynaptic density. Synapse, synaptosome. Note=Associated with the actin cytoskeleton. Detected at synapses and dendritic spines of cultured hippocampal neurons. | null | null | null | null | null | FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes reorganization of the actin cytoskeleton and recruits DLG4 to F-actin. Contributes to the regulation of dendritic spine morphogenesis. {ECO:0000269|PubMed:11502259}. | Rattus norvegicus (Rat) |
O35413 | SRBS2_RAT | MNTDSGGCARKRAAMSVTLTSVKRVQSSPNLLAAGRESHSPDSAWRSYNGRNPETLNGDATYSSLAAKGFRSVRPNLQDKKSPTQSHITINGNSGGAVSPVSYYQRPFSPSAYSLPASLNSSIIMPHGRSLDSAETYSQHAQSLDGTMGSSIPLYRSSEEEKRVTVIKAPHYPGIGPVDESGIPTAIRTTVDRPKDWYKTMFKQIHMVHKPDEDTDMYNTPYTYNAGLYNSPYSAQSHPAAKTQTYRPLSKSHSDNGTDAFKEATSPVPPPHVPPRPRDQSSTEKHDWDPPDRKVDTRKFRSEPRSIFEYEPGKSSILQH... | null | null | acetylcholine receptor signaling pathway [GO:0095500]; cell growth involved in cardiac muscle cell development [GO:0061049]; Notch signaling pathway [GO:0007219]; regulation of skeletal muscle acetylcholine-gated channel clustering [GO:1904393] | apical plasma membrane [GO:0016324]; dendrite [GO:0030425]; focal adhesion [GO:0005925]; lamellipodium [GO:0030027]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; synapse [GO:0045202] | protein domain specific binding [GO:0019904] | PF00018;PF14604;PF02208; | 2.30.30.40; | null | PTM: Ubiquitinated by CBL. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10521485, ECO:0000269|PubMed:15128873, ECO:0000269|PubMed:15659545, ECO:0000269|PubMed:16125169}. Apical cell membrane {ECO:0000250|UniProtKB:O94875}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:O94875}. Cell projection, lamellipodium {ECO... | null | null | null | null | null | FUNCTION: Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 (By similarity). May play a role in the regulation of pancreatic cell adhesion, possibl... | Rattus norvegicus (Rat) |
O35417 | PDYN_MOUSE | MAWSRLMLAACLLVMPSNVMADCLSLCSLCAVRIQDGPRPINPLICSLECQDLVPPSEEWETCRGFSSFLTLTVSGLRGKDDLEDEVALEEGISAHAKLLEPVLKELEKSRLLTSVPEEKFRGLSSSFGNGKESELAGADRMNDEAAQGRTVHFNEEDLRKQAKRYGGFLRKYPKRSSEMARDEDGGQDGDQVGHEDLYKRYGGFLRRIRPKLKWDNQKRYGGFLRRQFKVVTRSQENPNTYSEDLDV | null | null | chemical synaptic transmission [GO:0007268]; neuropeptide signaling pathway [GO:0007218]; sensory perception [GO:0007600] | axon terminus [GO:0043679]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; dense core granule [GO:0031045]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; neuronal cell body [GO:0043025]; neuronal dense core vesicle lumen [GO:0099013]; plasma membrane [GO:0005886]; synaptic vesicle [GO:0008021] | neuropeptide hormone activity [GO:0005184]; opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628] | PF01160; | null | Opioid neuropeptide precursor family | PTM: The N-terminal domain contains 6 conserved cysteines thought to be involved in disulfide bonding and/or processing. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity). {ECO:0000250}.; FUNCTION: Dynorphin peptides differentially regulate the kappa opioid receptor. Dynorphin A(1-13) has a ... | Mus musculus (Mouse) |
O35423 | AGT1_MOUSE | MFRMLAKASVTLGSRAAGWVRTMGSYQLLVPPPEALSKPLSVPTRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMLQIMEEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLTGTNGIWGMRAAEIADRIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLVHGESSTGVVQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDIMYSSSQKVLNAPPGISLISFNDKAKYKVYSRKTKPVSFYTDITYLAKLWGCEGETRVIHHTTPVTSLYCLRESLALIAEQGLENCWRRHREATAHL... | 2.6.1.44; 2.6.1.51 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P21549}; | glycine biosynthetic process, by transamination of glyoxylate [GO:0019265]; glyoxylate catabolic process [GO:0009436]; glyoxylate metabolic process [GO:0046487]; L-alanine catabolic process [GO:0042853]; L-cysteine catabolic process [GO:0019448]; L-serine metabolic process [GO:0006563]; Notch signaling pathway [GO:0007... | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | alanine-glyoxylate transaminase activity [GO:0008453]; amino acid binding [GO:0016597]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621]; pyridoxal phosphate binding [GO:0030170]; serine-pyruvate transaminase activity [GO:0004760] | PF00266; | 3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: [Isoform Peroxisomal]: Peroxisome {ECO:0000250|UniProtKB:P21549}.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion matrix {ECO:0000250|UniProtKB:P09139}. | CATALYTIC ACTIVITY: [Isoform Mitochondrial]: Reaction=L-serine + pyruvate = 3-hydroxypyruvate + L-alanine; Xref=Rhea:RHEA:22852, ChEBI:CHEBI:15361, ChEBI:CHEBI:17180, ChEBI:CHEBI:33384, ChEBI:CHEBI:57972; EC=2.6.1.51; Evidence={ECO:0000250|UniProtKB:P09139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22853; E... | null | null | null | null | FUNCTION: [Isoform Peroxisomal]: Catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification. {ECO:0000250|UniProtKB:P21549}.; FUNCTION: [Isoform Mitochondrial]: Catalyzes the transamination between L-serine and pyruvate and weakly contributes to gluconeogenesis from the L-ser... | Mus musculus (Mouse) |
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