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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P17302 | CXA1_HUMAN | MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVAQTDGVNVDMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSIFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHATSGALSPAKDCGSQKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNRM... | null | null | adult heart development [GO:0007512]; atrial cardiac muscle cell action potential [GO:0086014]; atrial ventricular junction remodeling [GO:0003294]; blood vessel morphogenesis [GO:0048514]; bone development [GO:0060348]; bone remodeling [GO:0046849]; cardiac conduction system development [GO:0003161]; cell communicatio... | apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; cell-cell contact zone [GO:0044291]; connexin complex [GO:0005922]; contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; fascia adherens [GO:0005916]; focal adhesion [GO:0005925]; gap j... | alpha-tubulin binding [GO:0043014]; beta-catenin binding [GO:0008013]; beta-tubulin binding [GO:0048487]; efflux transmembrane transporter activity [GO:0015562]; gap junction channel activity [GO:0005243]; gap junction channel activity involved in cardiac conduction electrical coupling [GO:0086075]; gap junction channe... | PF00029;PF03508; | 1.20.5.1130;1.20.1440.80; | Connexin family, Alpha-type (group II) subfamily | PTM: Phosphorylated at Ser-368 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity (By similarity). Phosphorylation at Ser-325, Ser-328 and Ser-330 by CK1 modulates gap junction assembly. Phosphorylation at Ser-368 by PRKCD triggers its internalization into smal... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22411987, ECO:0000269|PubMed:25398053}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000269|PubMed:22411987, ECO:0000269|PubMed:25398053}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated disk... | null | null | null | null | null | FUNCTION: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by part... | Homo sapiens (Human) |
P17312 | TERL_BPT4 | MEQPINVLNDFHPLNEAGKILIKHPSLAERKDEDGIHWIKSQWDGKWYPEKFSDYLRLHKIVKIPNNSDKPELFQTYKDKNNKRSRYMGLPNLKRANIKTQWTREMVEEWKKCRDDIVYFAETYCAITHIDYGVIKVQLRDYQRDMLKIMSSKRMTVCNLSRQLGKTTVVAIFLAHFVCFNKDKAVGILAHKGSMSAEVLDRTKQAIELLPDFLQPGIVEWNKGSIELDNGSSIGAYASSPDAVRGNSFAMIYIDECAFIPNFHDSWLAIQPVISSGRRSKIIITTTPNGLNHFYDIWTAAVEGKSGFEPYTAIWNSVKE... | 3.1.21.-; 3.6.4.- | COFACTOR: [Isoform Terminase large subunit]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04146, ECO:0000269|PubMed:18627466, ECO:0000305|PubMed:19109896}; Note=ATPase activity requires 1 Mg(2+) ion per subunit (PubMed:17386269). Nuclease activity probably requires 2 Mg(2+) ions per subunit ... | chromosome organization [GO:0051276]; viral DNA genome packaging [GO:0019073]; viral genome packaging [GO:0019072]; viral procapsid maturation [GO:0046797] | viral terminase, large subunit [GO:0098009] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA nuclease activity [GO:0004536]; endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; nuclease activity [GO:0004518] | PF17289;PF03237; | 3.30.420.240;3.40.50.300; | Tequatrovirus large terminase family | PTM: [Isoform Terminase large subunit]: Phosphorylated. {ECO:0000269|PubMed:10967092}. | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=380 uM for ATP {ECO:0000269|PubMed:12466275}; KM=256 uM for ATP {ECO:0000269|PubMed:10967092}; Note=The Km values for the ATPase activity were measured in presence of gp16. {ECO:0000269|PubMed:10967092, ECO:0000269|PubMed:12466275}; | null | null | null | FUNCTION: [Isoform Terminase large subunit]: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction (PubMed:10967092, PubMed:11846554, PubMed:12466275). The t... | Enterobacteria phage T4 (Bacteriophage T4) |
P17325 | JUN_RAT | MTAKMETTFYDDALNASFLQSESGAYGYSNPKILKQSMTLNLADPVGNLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVSGAGMVAPAVASVAGAGGGGGYSASLHSEPPVYANLSNFNPGALSSGGGAPSYGATGLAFPSQPQQQQQPPQPPHHLPQQIPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVN... | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; axon regeneration [GO:0031103]; cell population proliferation [GO:0008283]; cellular response to anisomycin [GO:0072740]; cellular response to cadmium ion [GO:0071276]; cellular response to calcium ion [GO:0071277]; cellular response to hypoxia [GO:0071456]; ce... | chromatin [GO:0000785]; euchromatin [GO:0000791]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | cAMP response element binding [GO:0035497]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0... | PF00170;PF03957; | 1.20.5.170; | BZIP family, Jun subfamily | PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-246; this primes the protein for subsequent phosphorylation by GSK3B at Thr-242. Phosphorylated at Thr-242, Ser-246 and Ser-252 by GSK3B; phosphorylation reduces its abi... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}. | null | null | null | null | null | FUNCTION: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (By similarity). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its trans... | Rattus norvegicus (Rat) |
P17332 | GLYC_LASSG | MGQIVTFFQEVPHVIEEVMNIVLIALSILAILKGLYNVATCGLIGLVTFLLLSGRSCSLIYKGTYELQTLELNMETLNMTMPLSCTKNNSHHYIRVGNETGLELTLTNTSILNHKFCNLSDAHKRNLYDHSLMSIISTFHLSIPNFNQYEAMSCDFNGGKITVQYNLSHSFAVDAAGHCGTLANGVLQTFMRMAWGGSYIALDSGRGNWDCIMTSYQYLIIQNTTWDDHCQFSRPSPIGYLGLLSQRTRDIYISRRLLGTFTWTLSDSEGNETPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNKQ... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleava... | SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Go... | null | null | null | null | null | FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glyc... | Lassa virus (strain GA391) (LASV) |
P17336 | CATA_DROME | MAGRDAASNQLIDYKNSQTVSPGAITTGNGAPIGIKDASQTVGPRGPILLQDVNFLDEMSHFDRERIPERVVHAKGAGAFGYFEVTHDITQYCAAKIFDKVKKRTPLAVRFSTVGGESGSADTARDPRGFAVKFYTEDGVWDLVGNNTPVFFIRDPILFPSFIHTQKRNPQTHLKDPDMFWDFLTLRPESAHQVCILFSDRGTPDGYCHMNGYGSHTFKLINAKGEPIYAKFHFKTDQGIKNLDVKTADQLASTDPDYSIRDLYNRIKTCKFPSWTMYIQVMTYEQAKKFKYNPFDVTKVWSQKEYPLIPVGKMVLDRNP... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04040}; | determination of adult lifespan [GO:0008340]; heart morphogenesis [GO:0003007]; hydrogen peroxide catabolic process [GO:0042744]; intestinal stem cell homeostasis [GO:0036335]; paracrine signaling [GO:0038001]; reactive oxygen species metabolic process [GO:0072593]; regulation of hemocyte proliferation [GO:0035206]; re... | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; peroxisome [GO:0005777] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P04040}. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; | null | null | null | null | FUNCTION: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. {ECO:0000250|UniProtKB:P04040}. | Drosophila melanogaster (Fruit fly) |
P17342 | ANPRC_HUMAN | MPSLLVLTFSPCVLLGWALLAGGTGGGGVGGGGGGAGIGGGRQEREALPPQKIEVLVLLPQDDSYLFSLTRVRPAIEYALRSVEGNGTGRRLLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARGAKPDLILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDSEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEDIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTSGDYAFFNIELFNSSSYGDGSWKRGDKHDFEAKQAYSSLQ... | null | null | angiogenesis [GO:0001525]; blood vessel remodeling [GO:0001974]; negative regulation of cold-induced thermogenesis [GO:0120163]; osteoclast proliferation [GO:0002158]; positive regulation of nitric-oxide synthase activity [GO:0051000]; positive regulation of urine volume [GO:0035810]; regulation of blood pressure [GO:0... | extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | chloride ion binding [GO:0031404]; G protein-coupled peptide receptor activity [GO:0008528]; hormone binding [GO:0042562]; natriuretic peptide receptor activity [GO:0016941]; peptide binding [GO:0042277]; peptide hormone binding [GO:0017046]; protein homodimerization activity [GO:0042803] | PF01094; | 3.40.50.2300; | ANF receptor family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:30032985}; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May ... | Homo sapiens (Human) |
P17347 | VM2EA_ECHCS | IGIAYNRGMCDPKKSVGTVMDHSTEHLSVAVAMAHEMGHNLGMDHDGNQCNCGGAGCVMSEELIESRSYKFSDCSKNQYQNYLTIYKPQCILNQPLRTDTVSTPVSGNELLQNSANPCYDPLTCHPREGEQCESGPCCRNCKFLKEGTICKRARGDDMDDYCNGKTCDCPRNPHKGPATAKGSVLM | 3.4.24.- | null | membrane protein ectodomain proteolysis [GO:0006509] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF00200;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-II subfamily, P-IIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2320569, ECO:0000269|PubMed:3198653}. | null | null | null | null | null | FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the envenomed animal. {ECO:0000250|UniProtKB:Q5XUW8, ECO:0000305}.; FUNCTION: [Disintegrin echistatin]: Potent inhibitor of ligand binding to the integrins alpha-V/beta-3 (ITGAV/ITGB3) (IC(50)=20.7 nM), alpha-IIb/beta-3 (ITGA2B/ITGB3) (IC(50)=51.5 nM), al... | Echis carinatus sochureki (Saw-scaled viper) |
P17349 | VM2E1_PROEL | MIQVLLVTICLAVFPYQGSSIILESGNVDDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEAVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIHNDADSTASISACDGLKGYFKLQGETYLIEPLELSDSEAHAVFKYENVEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIKLAIVVDHGMYTKYSSNFKKIRKRVHQMVSNINEMCRPLNIAITLALLDVWSEKDFITVQADAPTTAGLFGDWRERVLLKKKNHDHAQLLTDTNFARNTIGWAYLGRMCDEKYSVGVVQDH... | 3.4.24.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-II subfamily, P-IIa sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: [Snake venom metalloproteinase]: Impairs hemostasis in the envenomed animal. {ECO:0000250}.; FUNCTION: [Disintegrin elegantin-1a]: Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (IT... | Protobothrops elegans (Elegant pitviper) (Trimeresurus elegans) |
P17362 | PG029_VACCW | MNAYNKADSFSLESDSIKDVIHDYICWLSMTDEMRPSIGNVFKAMETFKIDAVRYYDGNIYELAKDINAMSFDGFIRSLQTIASKKDKLTVYGTMGLLSIVVDINKGCDISNIKFAAGIIILMEYIFDDTDMSHLKVALYRRIQRRDDVDR | null | null | suppression by virus of host type I interferon production [GO:0039501]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity [GO:0039723]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; symbiont-mediate... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; nucleus [GO:0005634] | protein sequestering activity [GO:0140311] | PF06227; | 1.10.437.20; | Orthopoxvirus OPG029 family | null | null | null | null | null | null | null | FUNCTION: Prevents establishment of cellular antiviral state by blocking virus-induced phosphorylation and activation of interferon regulatory factors 3/IRF3 and 7/IRF7, transcription factors critical for the induction of interferons alpha and beta. This blockage is produced through the inhibition of host TBK1, by bind... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P17397 | HBSAG_HBVB2 | MGTNLSVPNPLGFFPDHQLDPAFKANSDNPDWDLNPHKDNWPDSNKVGVGAFGPGFTPPHGGLLGWSPQAQGILTTVPTAPPPASTNRQLGRKPTPLSPPLRDTHPQAMQWNSTTFHQTLQDPRVRALYFPAGGSSSGTVNPVQNTASSISSILSTTGDPVPNMENIASGLLGPLLVLQAGFFSLTKILTIPLSLDSWWTSLNFLGETPVCLGQNSQSQISSHSPTCCPPICPGYRWMCLRRFIIFLCILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCKTCTTPAQGTSMFPSCCCTKPTDGNCTCIPIPSSWA... | null | null | caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Orthohepadnavirus major surface antigen family | PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Hepatitis B virus genotype B2 (isolate Indonesia/pIDW420/1988) (HBV-B) |
P17398 | HBSAG_HBVB1 | MGTNLSVPNPLGFFPDHQLDPAFKANSENPDWDLNPHKDNWPDAHKVGVGAFGPGFTPPHGGLLGWSPQAQGILTSVPAAPPPASTNRQSGRQPTPLSPPLRDTHPQAMQWNSTTFHQTLQDPRVRALYFPAGGSSSGTVSPAQNTVSAISSILSKTGDPVPNMENIASGLLGPLLVLQAGFFLLTKILTIPQSLDSWWTSLNFLGGTPVCLGQNSQSQISSHSPTCCPPICPGYRWMCLRRFIIFLCILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCKTCTTPAQGTSMFPSCCCTKPMDGNCTCIPIPSSWA... | null | null | caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Orthohepadnavirus major surface antigen family | PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Hepatitis B virus genotype B1 subtype adw (isolate Japan/pJDW233/1988) (HBV-B) |
P17399 | HBSAG_HBVB4 | MGTNLSVPNPLGFFPDHQLDPAFKANSENPDWDLNPNKDNWPDANKVGVGAFGPGFTPPHGGLLGWSPQAQGLLTTVPAAPPPASTNRQSGRQPTPLSPPLRDTHPQAMQWNSTTFHQTLQDPGVRALYFPAGGSSSGTVSPAQNTVSAISSILSKTGDPVPNMENIASGLLGPLLVLQAGFFLLTKILTIPQSLDSWWTSLNFLGGTPVCLGQNSQSQISSHSPTCCPPICPGYRWMCLRRFIIFLCILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCKTCTTPAQGTSMFPSCCCTKPTDGNCTCIPIPSSWA... | null | null | caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Orthohepadnavirus major surface antigen family | PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Hepatitis B virus genotype B/C subtype adw (isolate Okinawa/pODW282/1998) (HBV-B) |
P17404 | CNMD_BOVIN | MTENSDKVPIALVGPDDVEFCSPPAYAAVTVKPSSPARLLKVGAVVLISGAVLLLLGAIGAFYFWKGSDNHIYNVHYTMSINGKLQDGSMEIDAGNNLETFKMGSGAEEAVEVNDFQNGITGIRFAGGEKCYIKAQVKARIPEVGTMTKQSISSELEGKIMPVKYEENSLIWVAGDQPVKDNSFLSSKVLELCGDLPIFWLKPTYPKEIQRERRELVRKIVTTTTTRRLRSGPQGTPAPGRPNNGTRPSVQEDAEPFNPDNPYHQQEGESMTFDPRLDHEGICCIECRRSYTHCQKICEPLGGYHPWPYNYQGCRSACRV... | null | null | cartilage development [GO:0051216]; cell differentiation [GO:0030154]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell proliferation [GO:0001937] | endomembrane system [GO:0012505]; extracellular region [GO:0005576]; membrane [GO:0016020] | null | PF04089; | 3.30.390.150; | Chondromodulin-1 family | PTM: After cleavage, the post-translationally modified ChM-I is secreted as a glycoprotein. {ECO:0000269|PubMed:11323410}.; PTM: Two other smaller nonglycosylated chondromodulin forms (9 kDa and 7 kDa) are found either in developing articular cartilage or in chondrocytes. The 9 kDa form could be processed by an extrace... | SUBCELLULAR LOCATION: [Chondromodulin-1]: Secreted, extracellular space, extracellular matrix. Note=Accumulated in the inter-territorial matrix of cartilage.; SUBCELLULAR LOCATION: [Chondrosurfactant protein]: Endomembrane system {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Bifunctional growth regulator that stimulates the growth of cultured chondrocytes in the presence of basic fibroblast growth factor (FGF) but inhibits the growth of cultured vascular endothelial cells. May contribute to the rapid growth of cartilage and vascular invasion prior to the replacement of cartilage ... | Bos taurus (Bovine) |
P17405 | ASM_HUMAN | MPRYGASLRQSCPRSGREQGQDGTAGAPGLLWMGLVLALALALALALALSDSRVLWAPAEAHPLSPQGHPARLHRIVPRLRDVFGWGNLTCPICKGLFTAINLGLKKEPNVARVGSVAIKLCNLLKIAPPAVCQSIVHLFEDDMVEVWRRSVLSPSEACGLLLGSTCGHWDIFSSWNISLPTVPKPPPKPPSPPAPGAPVSRILFLTDLHWDHDYLEGTDPDCADPLCCRRGSGLPPASRPGAGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDQLRALTTVTALVRKFLGPVPVYPAVGN... | 3.1.4.12; 3.1.4.3 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:8702487, ECO:0000269|PubMed:9660788}; Note=Binds 2 Zn(2+) ions per subunit (PubMed:27349982, PubMed:27725636). {ECO:0000269|PubMed:27349982, ECO:0000269|PubMed:27725636, ECO:0000269|PubMed:8702487, ECO:0000269|PubMed:9660788}; | cellular response to calcium ion [GO:0071277]; cellular response to UV [GO:0034644]; ceramide biosynthetic process [GO:0046513]; cholesterol metabolic process [GO:0008203]; glycosphingolipid catabolic process [GO:0046479]; negative regulation of MAP kinase activity [GO:0043407]; nervous system development [GO:0007399];... | endolysosome [GO:0036019]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lamellar body [GO:0042599]; lipid droplet [GO:0005811]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; plasma membrane [GO:0005886] | acid sphingomyelin phosphodiesterase activity [GO:0061750]; hydrolase activity, acting on glycosyl bonds [GO:0016798]; phosphatidylcholine phospholipase C activity [GO:0034480]; sphingomyelin phosphodiesterase activity [GO:0004767]; zinc ion binding [GO:0008270] | PF19272;PF00149; | 3.60.21.10; | Acid sphingomyelinase family | PTM: Proteolytically processed (PubMed:21098024, PubMed:9030779). Mature lysosomal form arises from C-terminal proteolytic processing of pro-sphingomyelin phosphodiesterase (PubMed:21098024). {ECO:0000269|PubMed:21098024, ECO:0000269|PubMed:9030779}.; PTM: [Sphingomyelin phosphodiesterase, processed form]: This form is... | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:16787399, ECO:0000269|PubMed:18815062, ECO:0000269|PubMed:20530211, ECO:0000269|PubMed:20807762, ECO:0000269|PubMed:27659707, ECO:0000269|PubMed:9660788}. Lipid droplet {ECO:0000269|PubMed:25339683}. Secreted {ECO:0000269|PubMed:12563314, ECO:0000269|PubMed:16787399, E... | CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269|PubMed:12563314, ECO:0000269|PubMed:15877209, ECO:0000269|PubMed:... | null | null | null | null | FUNCTION: Converts sphingomyelin to ceramide (PubMed:12563314, PubMed:1840600, PubMed:18815062, PubMed:25339683, PubMed:25920558, PubMed:27659707, PubMed:33163980). Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment,... | Homo sapiens (Human) |
P17411 | CHBF_ECOLI | MSQKLKVVTIGGGSSYTPELLEGFIKRYHELPVSELWLVDVEGGKPKLDIIFDLCQRMIDNAGVPMKLYKTLDRREALKDADFVTTQLRVGQLPARELDERIPLSHGYLGQETNGAGGLFKGLRTIPVIFDIVKDVEELCPNAWVINFTNPAGMVTEAVYRHTGFKRFIGVCNIPIGMKMFIRDVLMLKDSDDLSIDLFGLNHMVFIKDVLINGKSRFAELLDGVASGQLKASSVKNIFDLPFSEGLIRSLNLLPCSYLLYYFKQKEMLAIEMGEYYKGGARAQVVQKVEKQLFELYKNPELKVKPKELEQRGGAYYSDA... | 3.2.1.86 | COFACTOR: Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000269|PubMed:10572139}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10572139}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:10572139}; Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000269|PubMed:105... | carbohydrate metabolic process [GO:0005975]; diacetylchitobiose catabolic process [GO:0052777] | null | 6-phospho-beta-glucosidase activity [GO:0008706]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; methyl beta-D-glucoside 6-phosphate glucohydrolase activity [GO:0103047]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616] | PF02056;PF11975; | 3.90.110.10;3.40.50.720; | Glycosyl hydrolase 4 family | null | null | CATALYTIC ACTIVITY: Reaction=6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate; Xref=Rhea:RHEA:10772, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:58312, ChEBI:CHEBI:61548; EC=3.2.1.86; Evidence={ECO:0000269|PubMed:10572139}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 mM for cellobiose-6P {ECO:0000269|PubMed:10572139}; KM=0.44 mM for salicin-6P {ECO:0000269|PubMed:10572139}; KM=0.35 mM for arbutin-6P {ECO:0000269|PubMed:10572139}; KM=12.5 mM for gentiobiose-6P {ECO:0000269|PubMed:10572139}; KM=2.22 mM for methyl-beta-glucosi... | null | null | null | FUNCTION: Hydrolyzes a wide variety of P-beta-glucosides including cellobiose-6P, salicin-6P, arbutin-6P, gentiobiose-6P, methyl-beta-glucoside-6P and p-nitrophenyl-beta-D-glucopyranoside-6P. Is also able to hydrolyze phospho-N,N'-diacetylchitobiose. {ECO:0000269|PubMed:10572139, ECO:0000269|PubMed:10913117}. | Escherichia coli (strain K12) |
P17412 | FRDA_WOLSU | MKVQYCDSLVIGGGLAGLRAAVATQQKGLSTIVLSLIPVKRSHSAAAQGGMQASLGNSKMSDGDNEDLHFMDTVKGSDWGCDQKVARMFVNTAPKAIRELAAWGVPWTRIHKGDRMAIINAQKTTITEEDFRHGLIHSRDFGGTKKWRTCYTADATGHTMLFAVANECLKLGVSIQDRKEAIALIHQDGKCYGAVVRDLVTGDIIAYVAKGTLIATGGYGRIYKNTTNAVVCEGTGTAIALETGIAQLGNMEAVQFHPTPLFPSGILLTEGCRGDGGILRDVDGHRFMPDYEPEKKELASRDVVSRRMIEHIRKGKGVQS... | 1.3.5.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702}; Note=Binds 1 FAD covalently per subunit. {ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702}; | anaerobic respiration [GO:0009061]; electron transport chain [GO:0022900] | plasma membrane [GO:0005886]; respirasome [GO:0070469] | electron transfer activity [GO:0009055]; flavin adenine dinucleotide binding [GO:0050660]; succinate dehydrogenase (quinone) activity [GO:0008177] | PF00890;PF02910; | 3.10.20.820;3.50.50.60;1.20.58.100;3.90.700.10; | FAD-dependent oxidoreductase 2 family, FRD/SDH subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305|PubMed:10586875}; Cytoplasmic side {ECO:0000305|PubMed:10586875}. | CATALYTIC ACTIVITY: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; | null | null | null | null | FUNCTION: The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. {ECO:0000269|PubMed:11248702, ECO:0000269|PubMed:9492313}. | Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) |
P17413 | FRDC_WOLSU | MTNESILESYSGVTPERKKSRMPAKLDWWQSATGLFLGLFMIGHMFFVSTILLGDNVMLWVTKKFELDFIFEGGKPIVVSFLAAFVFAVFIAHAFLAMRKFPINYRQYLTFKTHKDLMRHGDTTLWWIQAMTGFAMFFLGSVHLYIMMTQPQTIGPVSSSFRMVSEWMWPLYLVLLFAVELHGSVGLYRLAVKWGWFDGETPDKTRANLKKLKTLMSAFLIVLGLLTFGAYVKKGLEQTDPNIDYKYFDYKRTHHR | null | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702}; Note=Binds 2 heme b molecules per subunit, called the proximal (bP) and distal (bD) hemes. {ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702}; | tricarboxylic acid cycle [GO:0006099] | plasma membrane [GO:0005886]; respirasome [GO:0070469] | metal ion binding [GO:0046872]; oxidoreductase activity, acting on the CH-CH group of donors [GO:0016627] | PF01127; | 1.20.1300.10; | Diheme cytochrome b FrdC family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702}. | null | null | null | null | null | FUNCTION: The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. This subunit anchors the complex in the membrane and binds a diheme cytochrome b. {ECO:0000269|PubMed:11248702, ECO:0000269|PubMed:9492313}. | Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) |
P17425 | HMCS1_RAT | MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQARMGFCTDREDINSLCLTVVQKLMERNSLSYDCIGRLEVGTETIIDKSKSVKSNLMQLFEESGNTDIEGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAIYASGNARPTGGVGAVALLIGPNAPVIFDRGLRGTHMQHAYDFYKPDMLSEYPVVDGKLSIQCYLSALDRCYSVYRKKIRAQWQKEGKDKDFTLNDFGFMIFHSPYCKLVQKSLARMFLNDFLNDQNRDKNSIYSGLEAFGDVKLEDTYFDRDVEKAFM... | 2.3.3.10 | null | acetyl-CoA metabolic process [GO:0006084]; cellular response to cholesterol [GO:0071397]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to organic cyclic compound [GO:0071407]; cholesterol biosynthe... | cytoplasm [GO:0005737] | hydroxymethylglutaryl-CoA synthase activity [GO:0004421]; isomerase activity [GO:0016853]; organic acid binding [GO:0043177]; protein homodimerization activity [GO:0042803]; small molecule binding [GO:0036094] | PF08540;PF01154; | 3.40.47.10; | Thiolase-like superfamily, HMG-CoA synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13704}. | CATALYTIC ACTIVITY: Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10; Evidence={ECO:0000250|UniProtKB:Q01581}; PhysiologicalDir... | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3. | null | null | FUNCTION: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate, a precursor for cholesterol synthesis. {ECO:0000250|UniProtKB:P13704}. | Rattus norvegicus (Rat) |
P17426 | AP2A1_MOUSE | MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCISLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHY... | null | null | clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; positive regulation of neuron projection development [GO:0010976]; positive regulation of receptor-mediated endocytosis [GO:0048260]; postsynaptic neurotransmit... | AP-2 adaptor complex [GO:0030122]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; clathrin-coated vesicle [GO:0030136]; cytoplasmic side of plasma membrane [GO:0009898]; filopodium tip [GO:0032433]; membrane coat [GO:0030117]; postsynapse [GO:0098794]; protein-containing complex [GO:0032... | clathrin adaptor activity [GO:0035615]; low-density lipoprotein particle receptor binding [GO:0050750]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877] | PF01602;PF02296;PF02883; | 2.60.40.1230;1.25.10.10;3.30.310.10; | Adaptor complexes large subunit family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O95782}. Membrane, coated pit {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nas... | null | null | null | null | null | FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved i... | Mus musculus (Mouse) |
P17427 | AP2A2_MOUSE | MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHD... | null | null | clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886]; postsynaptic neurotransmitter receptor internalization [GO:0098884]; regulation of hematopoietic stem cell differentiation [GO:1902036]; vesicle-mediated transport [GO:0016192] | AP-2 adaptor complex [GO:0030122]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; membrane coat [GO:0030117]; postsynapse [GO:0098794]; secretory granule [GO:0030141]; synaptic vesicle [GO:0008021] | clathrin adaptor activity [GO:0035615]; disordered domain specific binding [GO:0097718]; kinase binding [GO:0019900]; phosphatidylinositol binding [GO:0035091]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; protein serine/threonine kinase binding [GO:0120283]; protein-containing com... | PF01602;PF02296;PF02883; | 2.60.40.1230;1.25.10.10;3.30.310.10; | Adaptor complexes large subunit family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14530274, ECO:0000269|PubMed:17035303}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Membrane, coated pit {ECO:0000269|PubMed:17035303}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=AP-2 appears to b... | null | null | null | null | null | FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved i... | Mus musculus (Mouse) |
P17429 | AREA_EMENI | MSGLTLGGGSGRVRPTQAAAAFPTSHDFADPDRSSVARNANRPSRRFAAPPQLSDDFSLESPTDSAQVHDNLLQDALFPEWKANSPRGVDSPDEMQKKDPLATQIWKLYSRTKAQLPNQERMENLTWRMMALSLRRQERERAQQQARASSQKSPVPGMSGIAQLRLSDRVSNTPTTTADTVSDAMNLDDFIIPFSPSDHPSPSTTKASEATTGAIPIKARRDQSASEATPVPASFPHPAQDQRRESEFGYVPRRVRKTSIDERQFFNLQIPSRKRPAESSPHVPPVSTSMLAHDPDFSHAVPEYTLDTSHGLSLQNQMNA... | null | null | chromatin remodeling [GO:0006338]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nitrate assimilation [GO:0042128]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of amide catabolic process [GO:0034251]; regulation of arginine metabolic process [GO:0000821];... | 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]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF07573;PF08550;PF00320; | 3.30.50.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription activator that binds the consensus DNA element 5'-CGATAG-3' and mediates nitrogen metabolite repression. Activates the transcription of uapA. {ECO:0000269|PubMed:1970293}. | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
P17431 | TISB_RAT | MTTTLVSATIFDLSEVLCKGNKMLNYSTPSAGGCLLDRKAVGTPAGGGFPRRHSVTLPSSKFHQNQLLSSLKGEPAPTLSSRDSRFRDRSFSEGGERLLPTQKQPGSGQVNSSRYKTELCRPFEENGACKYGDKCQFAHGIHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRALAGGRDLSADRPRLQHSFSFAGFPSAAATAAATGLLDSPTSITPPPILSADDLLGSPTLPDGTNNPFAFSSQELASLFAPSMGLPGGGSPTTFLFRPMSESPHMFDSPPSPQDSLSDHEGYLSSSSSSHSGSDSPT... | null | null | 3'-UTR-mediated mRNA destabilization [GO:0061158]; apoptotic process [GO:0006915]; cell population proliferation [GO:0008283]; cellular response to cAMP [GO:0071320]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular respons... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]; ribonucleoprotein complex [GO:1990904] | 14-3-3 protein binding [GO:0071889]; DNA binding [GO:0003677]; metal ion binding [GO:0046872]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA binding [GO:0003729] | PF04553;PF00642; | 4.10.1000.10; | null | PTM: Phosphorylated. Phosphorylated by RPS6KA1 at Ser-334 upon phorbol 12-myristate 13-acetate (PMA) treatment; this phosphorylation results in dissociation of the CCR4-NOT deadenylase complex and induces p38 MAPK-mediated stabilization of the low-density lipoprotein receptor LDLR mRNA. Phosphorylated by protein kinase... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q07352}. Cytoplasm {ECO:0000250|UniProtKB:Q07352}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q07352}. Cytoplasm, P-body {ECO:0000250|UniProtKB:Q07352}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. Component of cytoplasmic stre... | null | null | null | null | null | FUNCTION: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (PubMed:10751406, PubMed:12748283). Acts as a 3'-untranslated region... | Rattus norvegicus (Rat) |
P17433 | SPI1_MOUSE | MLQACKMEGFSLTAPPSDDLVTYDSELYQRPMHDYYSFVGSDGESHSDHYWDFSAHHVHNNEFENFPENHFTELQSVQPPQLQQLYRHMELEQMHVLDTPMVPPHTGLSHQVSYMPRMCFPYQTLSPAHQQSSDEEEGERQSPPLEVSDGEADGLEPGPGLLHGETGSKKKIRLYQFLLDLLRSGDMKDSIWWVDKDKGTFQFSSKHKEALAHRWGIQKGNRKKMTYQKMARALRNYGKTGEVKKVKKKLTYQFSGEVLGRGGLAERRLPPH | null | null | anatomical structure regression [GO:0060033]; apoptotic process involved in blood vessel morphogenesis [GO:1902262]; endothelial to hematopoietic transition [GO:0098508]; erythrocyte differentiation [GO:0030218]; follicular B cell differentiation [GO:0002316]; germinal center B cell differentiation [GO:0002314]; granul... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polyme... | PF00178; | 1.10.10.10; | ETS family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17947}. | null | null | null | null | null | FUNCTION: Pioneer transcription factor, which controls hematopoietic cell fate by decompacting stem cell heterochromatin and allowing other transcription factors to enter otherwise inaccessible genomic sites (PubMed:8079170). Once in open chromatin, can directly control gene expression by binding genetic regulatory ele... | Mus musculus (Mouse) |
P17439 | GBA1_MOUSE | MAARLIGFFLFQAVSWAYGAQPCIPKSFGYSSVVCVCNASYCDSLDPVTLPALGTFSRYESTRRGRRMELSVGAIQANRTGTGLLLTLQPEKKFQKVKGFGGAMTDATALNILALSPPTQKLLLRSYFSTNGIEYNIIRVPMASCDFSIRVYTYADTPNDFQLSNFSLPEEDTKLKIPLIHQALKMSSRPISLFASPWTSPTWLKTNGRVNGKGSLKGQPGDIFHQTWANYFVKFLDAYAKYGLRFWAVTAENEPTAGLFTGYPFQCLGFTPEHQRDFISRDLGPALANSSHDVKLLMLDDQRLLLPRWAEVVLSDPEAA... | 2.4.1.-; 3.2.1.-; 3.2.1.45; 3.2.1.46 | null | antigen processing and presentation [GO:0019882]; autophagosome organization [GO:1905037]; autophagy [GO:0006914]; beta-glucoside catabolic process [GO:1901805]; brain morphogenesis [GO:0048854]; cell maturation [GO:0048469]; cellular response to starvation [GO:0009267]; cellular response to tumor necrosis factor [GO:0... | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lysosomal lumen [GO:0043202]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; trans-Golgi network [GO:0005802] | beta-glucosidase activity [GO:0008422]; galactosylceramidase activity [GO:0004336]; glucosylceramidase activity [GO:0004348]; glucosyltransferase activity [GO:0046527]; hydrolase activity [GO:0016787]; scavenger receptor binding [GO:0005124]; signaling receptor binding [GO:0005102]; steryl-beta-glucosidase activity [GO... | PF02055;PF17189; | 3.20.20.80; | Glycosyl hydrolase 30 family | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P04062}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04062}; Lumenal side {ECO:0000250|UniProtKB:P04062}. Note=Interaction with saposin-C promotes membrane [?]association. Targeting to lysosomes occurs through an alternative MPR-independent mechanis... | CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H2O = an N-acylsphing-4-enine + D-glucose; Xref=Rhea:RHEA:13269, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377, ChEBI:CHEBI:22801, ChEBI:CHEBI:52639; EC=3.2.1.45; Evidence={ECO:0000269|PubMed:24211208}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | null | PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:24211208}.; PATHWAY: Sphingolipid metabolism. {ECO:0000269|PubMed:24211208}. | null | null | FUNCTION: Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:24211208). Plays a central role in the degradation of complex lipids a... | Mus musculus (Mouse) |
P17442 | PHO81_YEAST | MKFGKYLEARQLELAEYNSHFIDYKALKKLIKQLAIPTLKASSDLDLHLTLDDIDEKIIHQRLQENKAAFFFKLERELEKVNGYYLARESDLRIKFNILHSKYKDYKINGKLNSNQATSFKNLYAAFKKFQKDLRNLEQYVELNKTGFSKALKKWDKRSQSHDKDFYLATVVSIQPIFTRDGPLKLNDETLHILLELNDIDNNNRRADIQSSTFTNDDDDDNNTSNNNKHNNNNNNNNNNNNNNNNNNILHNNYELTTSKISENQLEHLFQASSSSLDMEMEIENWYKEILNIATVKDVQRKHALLRNFRETKIFTYLLQ... | null | null | lipid metabolic process [GO:0006629]; phosphate-containing compound metabolic process [GO:0006796] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; phosphoric diester hydrolase activity [GO:0008081] | PF12796;PF03105; | 1.25.40.20;3.20.20.190; | null | PTM: Phosphorylated by the cyclin-CDK PHO80-PHO85. Phosphorylation mediates the formation of a stable interaction with the cyclin-CDK and is required for function as an active inhibitor of the complex under phosphate starvation conditions. {ECO:0000269|PubMed:15057567, ECO:0000269|PubMed:15127225}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localizes predominantly to the nucleus in both high- and low-phosphate conditions. | null | null | null | null | null | FUNCTION: Inhibits the kinase activity of the cyclin-CDKs PHO80-PHO85 and PCL7-PHO85 under low-phosphate conditions. {ECO:0000269|PubMed:11069666, ECO:0000269|PubMed:7939631, ECO:0000269|PubMed:7957107}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17443 | MURG_ECOLI | MSGQGKRLMVMAGGTGGHVFPGLAVAHHLMAQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGIKALIAAPLRIFNAWRQARAIMKAYKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAFPNAEVVGNPVRTDVLALPLPQQRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDSVTIWHQSGKGSQQSVEQAYAEAGQPQHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIIEQPQLSVDAVANTLAG... | 2.4.1.227 | null | carbohydrate metabolic process [GO:0005975]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell wall organization [GO:0071555]; lipid glycosylation [GO:0030259]; peptidoglycan biosynthetic process [GO:0009252]; regulation of cell shape [GO:0008360] | plasma membrane [GO:0005886] | UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity [GO:0051991]; undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity [GO:0050511] | PF04101;PF03033; | 3.40.50.2000; | Glycosyltransferase 28 family, MurG subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000269|PubMed:1649817, ECO:0000269|PubMed:17640276, ECO:0000269|PubMed:8449890}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000269|PubMed:1649817, ECO:0000269|PubMed:17640276, ECO:0000269|PubMed:8449890}; Cytoplasmi... | CATALYTIC ACTIVITY: Reaction=di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutam... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.053 mM for lipid I {ECO:0000269|PubMed:12538870}; KM=0.053 mM for UDP-N-acetyl-alpha-D-glucosamine {ECO:0000269|PubMed:12538870}; Note=kcat is 837 min(-1). {ECO:0000269|PubMed:12538870}; | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00033, ECO:0000269|PubMed:1649817}. | null | null | FUNCTION: Cell wall formation (PubMed:1649817). Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II) (PubMed:12538870, PubMed:1649817). Strongly prefers UDP to CDP, GDP... | Escherichia coli (strain K12) |
P17444 | BETA_ECOLI | MQFDYIIIGAGSAGNVLATRLTEDPNTSVLLLEAGGPDYRFDFRTQMPAALAFPLQGKRYNWAYETEPEPFMNNRRMECGRGKGLGGSSLINGMCYIRGNALDLDNWAQEPGLENWSYLDCLPYYRKAETRDMGENDYHGGDGPVSVTTSKPGVNPLFEAMIEAGVQAGYPRTDDLNGYQQEGFGPMDRTVTPQGRRASTARGYLDQAKSRPNLTIRTHAMTDHIIFDGKRAVGVEWLEGDSTIPTRATANKEVLLCAGAIASPQILQRSGVGNAELLAEFDIPLVHELPGVGENLQDHLEMYLQYECKEPVSLYPALQW... | 1.1.99.1; 1.2.1.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_00750}; | glycine betaine biosynthetic process from choline [GO:0019285]; response to osmotic stress [GO:0006970] | membrane [GO:0016020]; plasma membrane [GO:0005886] | betaine-aldehyde dehydrogenase activity [GO:0008802]; choline dehydrogenase activity [GO:0008812]; flavin adenine dinucleotide binding [GO:0050660] | PF05199;PF00732; | 3.50.50.60;3.30.560.10; | GMC oxidoreductase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3512525}; Peripheral membrane protein {ECO:0000269|PubMed:3512525}. | CATALYTIC ACTIVITY: Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433, ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710, ChEBI:CHEBI:17499; EC=1.1.99.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00750, ECO:0000269|PubMed:3512525}; CATALYTIC ACTIVITY: Reaction=betaine aldehyde + H2O + NAD(+) = glycine... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 mM for NAD (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:3512525}; KM=0.13 mM for glycine betaine aldehyde (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:3512525}; KM=0.5 mM for NADP (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:35125... | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00750}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5 for choline dehydrogenase and is between 7.5 and 9.5 for glycine betaine-aldehyde dehydrogenase. {ECO:0000269|PubMed:3512525}; | null | FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. {ECO:0000255|HAMAP-Rule:MF_00750, ECO:0000269|PubMed:3512525, ECO:0000269|PubMed:3512526}. | Escherichia coli (strain K12) |
P17445 | BETB_ECOLI | MSRMAEQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIWASMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLIPALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYSEAGLPDGVFNVLPGVGAETGQYLTEHPGIAKVSFTGGVASGKKVMANSAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKAAFEQKILARVERIRAGDVFD... | 1.2.1.8 | COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-Rule:MF_00804}; Note=Binds 2 potassium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00804}; | glycine betaine biosynthetic process from choline [GO:0019285]; protein homotetramerization [GO:0051289]; response to osmotic stress [GO:0006970]; response to X-ray [GO:0010165] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | 4-trimethylammoniobutyraldehyde dehydrogenase activity [GO:0047105]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; betaine-aldehyde dehydrogenase activity [GO:0008802]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF00171; | null | Aldehyde dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) + NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:2194570, ECO:0... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=99 uM for NAD (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2194570}; KM=160 uM for betaine aldehyde (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2194570}; KM=400 uM for NADP (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:2194570}; KM=60 ... | PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00804}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 7.5 and 9.5. {ECO:0000269|PubMed:2194570, ECO:0000269|PubMed:3512525}; | null | FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the irreversible oxidation of betaine aldehyde to the corresponding acid. It is highly specific for betaine and has a significantly higher affinity for NAD than for NADP. {ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:2194570,... | Escherichia coli (strain K12) |
P17454 | LBP_RABIT | MGTWARALLGSTLLSLLLAAAPGALGTNPGLITRITDKGLEYAAREGLLALQRKLLEVTLPDSDGDFRIKHFGRAQYKFYSLKIPRFELLRGTLRPLPGQGLSLDISDAYIHVRGSWKVRKAFLRLKNSFDLYVKGLTISVHLVLGSESSGRPTVTTSSCSSDIQNVELDIEGDLEELLNLLQSQIDARLREVLESKICRQIEEAVTAHLQPYLQTLPVTTQIDSFAGIDYSLMEAPRATAGMLDVMFKGEIFPLDHRSPVDFLAPAMNLPEAHSRMVYFSISDYVFNTASLAYHKSGYWNFSITDAMVPADLNIRRTTK... | null | null | acute-phase response [GO:0006953]; cellular defense response [GO:0006968]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; lipid transport [GO:0006869]; lipopolysaccharide-mediated signaling pathway [GO:0031663]; ma... | extracellular space [GO:0005615] | lipopolysaccharide binding [GO:0001530]; signaling receptor binding [GO:0005102] | PF01273;PF02886; | null | BPI/LBP/Plunc superfamily, BPI/LBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2402637, ECO:0000269|PubMed:2427635}. | null | null | null | null | null | FUNCTION: Plays a role in the innate immune response (PubMed:2402637). Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:2427635). Acts as an affinity enhancer for CD14, facilitating its association with LPS (By similarit... | Oryctolagus cuniculus (Rabbit) |
P17455 | CAPSD_PAVCD | MAPPAKRARRGLVPPGYKYLGPGNSLDQGEPTNPSDAAAKEHDEAYAAYLRSGKNPYLYFSPADQRFIDQTKDAKDWGGKIGHYFFRAKKAIAPVLTDTPDHPSTSRPTKPTKRSKPPPHIFINLAKKKKAGAGQVKRDNLAPMSDGAVQPDGGQPAVRNERATGSGNGSGGGGGGGSGGVGISTGTFNNQTEFKFLENGWVEITANSSRLVHLNMPESENYRRVVVNNMDKTAVNGNMALDDIHAQIVTPWSLVDANAWGVWFNPGDWQLIVNTMSELHLVSFEQEIFNVVLKTVSESATQPPTKVYNNDLTASLMVAL... | null | null | adhesion receptor-mediated virion attachment to host cell [GO:0098671]; clathrin-dependent endocytosis of virus by host cell [GO:0075512]; entry receptor-mediated virion attachment to host cell [GO:0098670]; microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; permeabilization o... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; T=1 icosahedral viral capsid [GO:0039615] | metal ion binding [GO:0046872]; structural molecule activity [GO:0005198] | PF00740;PF08398; | 2.170.30.10; | Parvoviridae capsid protein family | null | SUBCELLULAR LOCATION: Virion. Host nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Capsid protein self-assembles to form an icosahedral capsid with a T=1 symmetry, about 22 nm in diameter, and consisting of 60 copies of two size variants of the capsid proteins, VP1 and VP2, which differ by the presence of an N-terminal extension in the minor protein VP1. The capsid encapsulates the genomic ... | Canine parvovirustype 2 (isolate Dog/United States/CPV-d/1988) (CPV-2) |
P17473 | ICP4_EHV1K | MASQRSDFAPDLYDFIESNDFGEDPLIRAASAAEEGFTQPAAPDLLYGSQNMFGVDDAPLSTPVVVIPPPSPAPEPRGGKAKRSPSAAGSGGPPTPAAAAQPASPAPSPAPGLAAMLKMVHSSVAPGNGRRATGSSSPGGGDAADPVALDSDTETCPGSPQPEFPSSASPGGGSPAPRVRSISISSSSSSSSSMDEDDQADGAGASSSSSSSSDDSDSDEGGEEETPRPRHSQNAAKTPSAAGSPGPSSGGDRPAAGAATPKSCRSGAASPGAPAPAPASAPAPSRPGGGLLPPGARILEYLEGVREANLAKTLERPEPP... | null | null | DNA-templated viral transcription [GO:0039695]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of viral transcription [GO:0050434] | host cell nucleoplasm [GO:0044095]; host cell nucleus [GO:0042025] | DNA binding [GO:0003677] | PF03585;PF03584; | null | Herpesviridae ICP4 family | PTM: A long stretch of serine residues may be a major site of phosphorylation. | SUBCELLULAR LOCATION: Host nucleus. | null | null | null | null | null | FUNCTION: This IE protein is a multifunctional protein capable of migrating to the nucleus, binding to DNA, trans-activating other viral genes, and autoregulating its own synthesis. | Equine herpesvirus 1 (strain Kentucky A) (EHV-1) (Equine abortion virus) |
P17475 | A1AT_RAT | MAPSISRGLLLLAALCCLAPSFLAEDAQETDTSQQDQSPTYRKISSNLADFAFSLYRELVHQSNTSNIFFSPMSITTAFAMLSLGSKGDTRKQILEGLEFNLTQIPEADIHKAFHHLLQTLNRPDSELQLNTGNGLFVNKNLKLVEKFLEEVKNNYHSEAFSVNFADSEEAKKVINDYVEKGTQGKIVDLMKQLDEDTVFALVNYIFFKGKWKRPFNPEHTRDADFHVDKSTTVKVPMMNRLGMFDMHYCSTLSSWVLMMDYLGNATAIFLLPDDGKMQHLEQTLTKDLISRFLLNRQTRSAILYFPKLSISGTYNLKTL... | null | null | acute-phase response [GO:0006953]; response to chromate [GO:0046687]; response to cytokine [GO:0034097]; response to estradiol [GO:0032355]; response to hypoxia [GO:0001666]; response to inorganic substance [GO:0010035]; response to lead ion [GO:0010288]; response to lipopolysaccharide [GO:0032496]; response to methano... | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794] | endopeptidase inhibitor activity [GO:0004866]; identical protein binding [GO:0042802]; protease binding [GO:0002020]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10;2.10.310.10; | Serpin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibitor of serine proteases. The primary target is elastase, but also has a moderate affinity for plasmin and thrombin. | Rattus norvegicus (Rat) |
P17480 | UBF1_HUMAN | MNGEADCPTDLEMAAPKGQDRWSQEDMLTLLECMKNNLPSNDSSKFKTTESHMDWEKVAFKDFSGDMCKLKWVEISNEVRKFRTLTELILDAQEHVKNPYKGKKLKKHPDFPKKPLTPYFRFFMEKRAKYAKLHPEMSNLDLTKILSKKYKELPEKKKMKYIQDFQREKQEFERNLARFREDHPDLIQNAKKSDIPEKPKTPQQLWYTHEKKVYLKVRPDATTKEVKDSLGKQWSQLSDKKRLKWIHKALEQRKEYEEIMRDYIQKHPELNISEEGITKSTLTKAERQLKDKFDGRPTKPPPNSYSLYCAELMANMKDVP... | null | null | positive regulation of transcription by RNA polymerase I [GO:0045943]; transcription by RNA polymerase I [GO:0006360]; transcription initiation at RNA polymerase I promoter [GO:0006361] | fibrillar center [GO:0001650]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; RNA binding [GO:0003723]; RNA polymerase I cis-regulatory region sequence-specific DNA binding [GO:0001165]; RNA polymerase I core promoter sequence-specific DNA binding [GO:0001164]; RNA polymerase I general transcription initiation factor activity [GO:0001181]; scaffold protein binding... | PF00505;PF09011;PF14887; | 1.10.30.10; | null | PTM: Phosphorylated and activated by PIK3CA. {ECO:0000250|UniProtKB:P25976}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P25976}. | null | null | null | null | null | FUNCTION: Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I (Pol I) through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element and can activate Pol I promoter escape. {ECO:0000269|PubMed:11250... | Homo sapiens (Human) |
P17481 | HXB8_HUMAN | MSSYFVNSLFSKYKTGESLRPNYYDCGFAQDLGGRPTVVYGPSSGGSFQHPSQIQEFYHGPSSLSTAPYQQNPCAVACHGDPGNFYGYDPLQRQSLFGAQDPDLVQYADCKLAAASGLGEEAEGSEQSPSPTQLFPWMRPQAAAGRRRGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKFPSSKCEQEELEKQKLERAPEAADEGDAQKGDKK | null | null | adult locomotory behavior [GO:0008344]; anterior/posterior pattern specification [GO:0009952]; dorsal spinal cord development [GO:0021516]; embryonic skeletal system morphogenesis [GO:0048704]; grooming behavior [GO:0007625]; negative regulation of myeloid cell differentiation [GO:0045638]; regulation of transcription ... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific double-stranded DNA binding [GO:19908... | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P17482 | HXB9_HUMAN | MSISGTLSSYYVDSIISHESEDAPPAKFPSGQYASSRQPGHAEHLEFPSCSFQPKAPVFGASWAPLSPHASGSLPSVYHPYIQPQGVPPAESRYLRTWLEPAPRGEAAPGQGQAAVKAEPLLGAPGELLKQGTPEYSLETSAGREAVLSNQRPGYGDNKICEGSEDKERPDQTNPSANWLHARSSRKKRCPYTKYQTLELEKEFLFNMYLTRDRRHEVARLLNLSERQVKIWFQNRRMKMKKMNKEQGKE | null | null | anterior/posterior pattern specification [GO:0009952]; cell chemotaxis [GO:0060326]; DNA-templated transcription [GO:0006351]; embryonic skeletal system morphogenesis [GO:0048704]; mammary gland development [GO:0030879]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proximal/distal pattern for... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | 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-specific double-stranded DNA binding [GO:1990837] | PF00046;PF04617; | 1.10.10.60; | Abd-B homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P17483 | HXB4_HUMAN | MAMSSFLINSNYVDPKFPPCEEYSQSDYLPSDHSPGYYAGGQRRESSFQPEAGFGRRAACTVQRYAACRDPGPPPPPPPPPPPPPPPGLSPRAPAPPPAGALLPEPGQRCEAVSSSPPPPPCAQNPLHPSPSHSACKEPVVYPWMRKVHVSTVNPNYAGGEPKRSRTAYTRQQVLELEKEFHYNRYLTRRRRVEIAHALCLSERQIKIWFQNRRMKWKKDHKLPNTKIRSGGAAGSAGGPPGRPNGGPRAL | null | null | anterior/posterior pattern specification [GO:0009952]; bone marrow development [GO:0048539]; definitive hemopoiesis [GO:0060216]; embryonic skeletal system morphogenesis [GO:0048704]; hematopoietic stem cell differentiation [GO:0060218]; hematopoietic stem cell proliferation [GO:0071425]; morphogenesis of an epithelial... | centrosome [GO:0005813]; chromatin [GO:0000785]; nucleoplasm [GO:0005654] | 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 double-stranded DNA binding [GO:1990837] | PF00046; | 1.10.10.60; | Antp homeobox family, Deformed subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P17486 | EGL5_CAEEL | MNTSTSAFDFGSSTASSAATSTTSSQPDANDHLSRLAAMTQGVGKEDPETSSTPSTEASLYPGISAAYMQSYGWPQNYNYFGQPLGPATFPGWPQCYPNTAWPNYGELFASSKKGRQTYQRYQTSVLEAKFQQSSYVSKKQREELRLQTQLTDRQIKIWFQNRRMKAKKEKQRVDDHTEHTPLLPANPPKGMGMDMDDEKKWQMAHWPPAAAHNPYQYPLCPP | null | null | anterior/posterior pattern specification [GO:0009952]; cell fate specification [GO:0001708]; defense response to bacterium [GO:0042742]; hindgut development [GO:0061525]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode male tail tip morphogenesis [GO:0045138]; neuron migration [GO:00017... | 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]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF00046; | 1.10.10.60; | Abd-B homeobox family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10049576}. | null | null | null | null | null | FUNCTION: Involved in control of cell fate and pattern formation along the anterior-posterior axis, acting mainly in the tail (PubMed:10049576, PubMed:1879361, PubMed:8101474). Required during embryonic and postembryonic development (PubMed:1879361). Essential for the determination of specific neurons, including the PL... | Caenorhabditis elegans |
P17490 | INHA_RAT | MVIQPSLLLLLLLTLQDVDSCQGPELVRELVLAKVKALFLDALGPPAMDGEGGGPGIRRLPRRHALGGFMHRTSEPEEEDVSQAILFPATGATCEDQAAAGGLAQEPEEGLFTYVFRPSQHIRSHQVTSAQLWFHTGLDRKSTAASNSSRPLLDLLVLSSGGPMAVPVSLGQSPPRWAVLHLAASAFPLLTHPILVLLLRCPLCSCSGRPETTPFLVAHTRARAPSAGERARRSAPSMPWPWSPAALRLLQRPPEEPSAHAFCHRAALNISFQELGWDRWIVHPPSFIFHYCHGSCGMPTSDLPLPVPGAPPTPAQPLFL... | null | null | hemoglobin biosynthetic process [GO:0042541]; male gonad development [GO:0008584]; negative regulation of follicle-stimulating hormone secretion [GO:0046882]; ovarian follicle development [GO:0001541]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127] | extracellular space [GO:0005615]; inhibin A complex [GO:0043512]; inhibin B complex [GO:0043513]; inhibin-betaglycan-ActRII complex [GO:0034673]; neuronal cell body [GO:0043025]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; inhibin binding [GO:0034711]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF00019; | 2.10.90.10; | TGF-beta family | PTM: Proteolytic processing yields a number of bioactive forms, consisting either solely of the mature alpha chain, of the most N-terminal propeptide linked through a disulfide bond to the mature alpha chain, or of the entire proprotein. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, eryth... | Rattus norvegicus (Rat) |
P17491 | INHBB_RAT | MDGLPGRALGAACLLLLAAGWLGPEAWGSPTPPPSPAAPPPPPPPGAPGGSQDTCTSCGGGGGGFRRPEELGRVDGDFLEAVKRHILSRLQLRGRPNITHAVPKAAMVTALRKLHAGKVREDGRVEIPHLDGHASPGADGQERVSEIISFAETDGLASSRVRLYFFVSNEGNQNLFVVQASLWLYLKLLPYVLEKGSRRKVRVKVYFQEQGHGDRWNVVEKKVDLKRSGWHTFPITEAIQALFERGERRLNLDVQCDSCQELAVVPVFVDPGEESHRPFVVVQARLGDSRHRIRKRGLECDGRTSLCCRQQFFIDFRLIG... | null | null | activin receptor signaling pathway [GO:0032924]; apoptotic signaling pathway [GO:0097190]; cellular response to calcium ion [GO:0071277]; cellular response to cAMP [GO:0071320]; cellular response to cholesterol [GO:0071397]; cellular response to insulin stimulus [GO:0032869]; cellular response to interleukin-1 [GO:0071... | cell periphery [GO:0071944]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; protein homodimerization activity [GO:0042803] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, eryth... | Rattus norvegicus (Rat) |
P17501 | FUS_NPVAC | MVSAIVLYVLLAAAAHSAFAAEHCNAQMKTGPYKIKNLDITPPKETLQKDVEITIVETDYNENVIIGYKGYYQAYAYNGGSLDPNTRVEETMKTLNVGKEDLLMWSIRQQCEVGEELIDRWGSDSDDCFRDNEGRGQWVKGKELVKRQNNNHFAHHTCNKSWRCGISTSKMYSRLECQDDTDECQVYILDAEGNPINVTVDTVLHRDGVSMILKQKSTFTTRQIKAACLLIKDDKNNPESVTREHCLIDNDIYDLSKNTWNCKFNRCIKRKVEHRVKKRPPTWRHNVRAKYTEGDTATKGDLMHIQEELMYENDLLKMNI... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; membrane fusion involved in viral entry into host cell [GO:0039663]; modulation by virus of host process [GO:0019048]; symbiont entry into host cell [GO:0046718]; viral budding from plasma membrane [GO:0046761] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | identical protein binding [GO:0042802] | PF03273; | 2.40.50.710;6.10.250.2130;6.10.250.3010;6.20.460.10; | Baculoviridae gp64 family | PTM: Palmitoylated. {ECO:0000269|PubMed:12743283, ECO:0000269|PubMed:2672565}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:25142609}; Single-pass membrane protein {ECO:0000305}. Host cell membrane {ECO:0000269|PubMed:12743283}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Class III viral fusion protein. Envelope phosphoglycoprotein which mediates the fusion of viral and host endosomal membranes leading to virus entry into the host cell. After receptor-mediated internalization of the virus, gp64 undergoes conformational change into a fusion-competent state at low pH, and the nu... | Autographa californica nuclear polyhedrosis virus (AcMNPV) |
P17505 | MDHM_YEAST | MLSRVAKRAFSSTVANPYKVTVLGAGGGIGQPLSLLLKLNHKVTDLRLYDLKGAKGVATDLSHIPTNSVVKGFTPEEPDGLNNALKDTDMVLIPAGVPRKPGMTRDDLFAINASIVRDLAAATAESAPNAAILVISNPVNSTVPIVAQVLKNKGVYNPKKLFGVTTLDSIRAARFISEVENTDPTQERVNVIGGHSGITIIPLISQTNHKLMSDDKRHELIHRIQFGGDEVVKAKNGAGSATLSMAHAGAKFANAVLSGFKGERDVIEPSFVDSPLFKSEGIEFFASPVTLGPDGIEKIHPIGELSSEEEEMLQKCKETL... | 1.1.1.37 | null | aerobic respiration [GO:0009060]; malate metabolic process [GO:0006108]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | L-malate dehydrogenase activity [GO:0030060]; mRNA binding [GO:0003729] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 1 family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11502169}. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; Evidence={ECO:0000255|PROSITE-ProRule:PRU10004}; | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17509 | HXB6_HUMAN | MSSYFVNSTFPVTLASGQESFLGQLPLYSSGYADPLRHYPAPYGPGPGQDKGFATSSYYPPAGGGYGRAAPCDYGPAPAFYREKESACALSGADEQPPFHPEPRKSDCAQDKSVFGETEEQKCSTPVYPWMQRMNSCNSSSFGPSGRRGRQTYTRYQTLELEKEFHYNRYLTRRRRIEIAHALCLTERQIKIWFQNRRMKWKKESKLLSASQLSAEEEEEKQAE | null | null | anterior/posterior pattern specification [GO:0009952]; embryonic skeletal system morphogenesis [GO:0048704]; erythrocyte homeostasis [GO:0034101]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P17515 | CXL10_MOUSE | MNPSAAVIFCLILLGLSGTQGIPLARTVRCNCIHIDDGPVRMRAIGKLEIIPASLSCPRVEIIATMKKNDEQRCLNPESKTIKNLMKAFSQKRSKRAP | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; antiviral innate immune response [GO:0140374]; cellular response to interleukin-17 [GO:0097398]; cellular response to lipopolysaccharide [GO:00712... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615] | chemoattractant activity [GO:0042056]; chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248]; heparin binding [GO:0008201] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02778}. | null | null | null | null | null | FUNCTION: Pro-inflammatory cytokine that is involved in a wide variety of processes such as chemotaxis, differentiation, and activation of peripheral immune cells, regulation of cell growth, apoptosis and modulation of angiostatic effects (By similarity) (PubMed:28623423). Plays thereby an important role during viral i... | Mus musculus (Mouse) |
P17516 | AK1C4_HUMAN | MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVVMDFLMDHPDYPFS... | 1.1.1.-; 1.1.1.209; 1.1.1.210; 1.1.1.225; 1.1.1.357; 1.1.1.51; 1.1.1.53; 1.1.1.62 | null | androgen metabolic process [GO:0008209]; bile acid and bile salt transport [GO:0015721]; bile acid biosynthetic process [GO:0006699]; cellular response to jasmonic acid stimulus [GO:0071395]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; progesterone metabolic process [GO:0042... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062] | 5alpha-androstane-3beta,17beta-diol dehydrogenase activity [GO:0047024]; alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; androstan-3-alpha,17-beta-diol dehydrogenase activity [GO:0047044]; androsterone dehydrogenase activity [GO:0047023]; bile acid binding [GO:003... | PF00248; | 3.20.20.100; | Aldo/keto reductase family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q04828}. | CATALYTIC ACTIVITY: Reaction=a 3alpha-hydroxysteroid + NADP(+) = a 3-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:34783, ChEBI:CHEBI:15378, ChEBI:CHEBI:36835, ChEBI:CHEBI:47788, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.357; Evidence={ECO:0000269|PubMed:10634139, ECO:0000269|PubMed:10998348, ECO:0000269|PubMed:111580... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.5 uM for 5alpha-androstane-3alpha,17beta-diol {ECO:0000269|PubMed:10998348}; KM=8.3 uM for 17beta-hydroxy-5alpha-androstan-3-one {ECO:0000269|PubMed:10998348}; KM=0.8 uM for 17beta-hydroxy-5alpha-androstan-3-one {ECO:0000269|PubMed:11158055}; KM=1.44 uM for 5alp... | PATHWAY: Steroid metabolism. {ECO:0000269|PubMed:14672942}. | null | null | FUNCTION: Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Liver specific enzyme that acts as an NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid nucleus and side chain (PubMed:10634139, PubMed:10998348, PubMed:11158055, PubMe... | Homo sapiens (Human) |
P17519 | P1_PLRV1 | MNRFTAYAALFFMFSLCSTAKEAGFLHPAFNFRGTSTMSASSGDYSAAPTPLYKSWALPSSLNLTTQPPPPLTDRSYYELVQALTSKMRLDCQTVGDMTWRHLSEMLFASWNSVKEVSLKAASVTLWAIINIWFGLYWTLARLITLFLWTFSIEALCLILLGCITSLIYKGALSLSEHLPVFLFMSPLKIIWRAAFSKRNYKNERAVEGYKGFSVPQKPPKSAVIELQHENGSHLGYANCIRLYSGENALVTAEHCLEGAFATSLKTGNRIPMSTFFPIFKSARNDISILVGPPNWEGLLSVKGAHFITADKIGKGPASF... | 3.4.21.- | null | proteolysis [GO:0006508]; viral process [GO:0016032] | membrane [GO:0016020] | RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; serine-type exopeptidase activity [GO:0070008] | PF02122; | 2.40.10.10; | Peptidase S39B family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The protease probably cleaves itself and releases the VPg protein. The VPg protein is probably further cleaved in its C-terminus. {ECO:0000269|PubMed:9268161}. | SUBCELLULAR LOCATION: [Protein P1]: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Precursor from which the VPg molecule is probably released at the onset of the RNA synthesis. Essential for virus replication. Participates, together with the proteins P0 and P7, in the inhibition of the induction of aphid-induced host phytohormones (PubMed:31758809). This could play a role in the attraction ... | Potato leafroll virus (strain Potato/Scotland/strain 1/1984) (PLrV) |
P17532 | TPH1_MOUSE | MIEDNKENKENKDHSSERGRVTLIFSLENEVGGLIKVLKIFQENHVSLLHIESRKSKQRNSEFEIFVDCDISREQLNDIFPLLKSHATVLSVDSPDQLTAKEDVMETVPWFPKKISDLDFCANRVLLYGSELDADHPGFKDNVYRRRRKYFAELAMNYKHGDPIPKIEFTEEEIKTWGTIFRELNKLYPTHACREYLRNLPLLSKYCGYREDNIPQLEDVSNFLKERTGFSIRPVAGYLSPRDFLSGLAFRVFHCTQYVRHSSDPLYTPEPDTCHELLGHVPLLAEPSFAQFSQEIGLASLGASEETVQKLATCYFFTVE... | 1.14.16.4 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P17752}; | aromatic amino acid metabolic process [GO:0009072]; bone remodeling [GO:0046849]; circadian rhythm [GO:0007623]; mammary gland alveolus development [GO:0060749]; negative regulation of ossification [GO:0030279]; platelet degranulation [GO:0002576]; positive regulation of fat cell differentiation [GO:0045600]; regulatio... | cytoplasm [GO:0005737]; neuron projection [GO:0043005] | iron ion binding [GO:0005506]; tryptophan 5-monooxygenase activity [GO:0004510] | PF01842;PF00351; | 1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitinated is triggered by phosphorylation. {ECO:0000250|UniProtKB:P09810}.; PTM: Phosphorylated; triggering degradation by the proteasome. {ECO:0000250|UniProtKB:P09810}. | null | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tryptophan + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + 5-hydroxy-L-tryptophan; Xref=Rhea:RHEA:16709, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57912, ChEBI:CHEBI:58266, ChEBI:CHEBI:59560; EC=1.14.16.4; Evidence={E... | null | PATHWAY: Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2. {ECO:0000305|PubMed:2110547}. | null | null | FUNCTION: Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis. {ECO:0000269|PubMed:14697203, ECO:0000305|PubMed:2110547}. | Mus musculus (Mouse) |
P17534 | DFAR2_MOUSE | MKKLVLLFALVLLAFQVQADSIQNTDEETKTEEQPGEKDQAVSVSFGDPQGSALQDAALGWGRRCPQCPRCPSCPSCPRCPRCPRCKCNPK | null | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; secretory granule [GO:0030141] | null | PF00879; | null | Alpha-defensin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Apparent precursor of a secreted, cationic, proline- and cysteine-rich peptide that contains Cys-Pro-Xaa repeats. Unlike cryptdin, the proposed mature peptide region lacks the structural motif characteristic of defensins. It may have microbicidal activities. | Mus musculus (Mouse) |
P17535 | JUND_HUMAN | METPFYGDEALSGLGGGASGSGGSFASPGRLFPGAPPTAAAGSMMKKDALTLSLSEQVAAALKPAAAPPPTPLRADGAPSAAPPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSSQFLYPKVAASEEQEFAEGFVKALEDLHKQNQLGAGAAAAAAAAAAGGPSGTATGSAPPGELAPAAAAPEAPVYANLSSYAGGAGGAGGAATVAFAAEPVPFPPPPPPGALGPPRLAALKDEPQTVPDVPSFGESPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQ... | null | null | cellular response to calcium ion [GO:0071277]; gene expression [GO:0010467]; negative regulation of transcription by RNA polymerase II [GO:0000122]; osteoblast development [GO:0002076]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of transcription by RNA polymerase II [GO:0045944]... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; enzyme binding [GO:0019899]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DN... | PF00170;PF03957; | 1.20.5.170; | BZIP family, Jun subfamily | PTM: Phosphorylated by MAP kinases MAPK8 and MAPK10; phosphorylation is inhibited in the presence of MEN1. {ECO:0000269|PubMed:22327296}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor binding AP-1 sites (PubMed:9989505). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing their transcriptional activity (PubMed:28981703, Pub... | Homo sapiens (Human) |
P17540 | KCRS_HUMAN | MASIFSKLLTGRNASLLFATMGTSVLTTGYLLNRQKVCAEVREQPRLFPPSADYPDLRKHNNCMAECLTPAIYAKLRNKVTPNGYTLDQCIQTGVDNPGHPFIKTVGMVAGDEESYEVFADLFDPVIKLRHNGYDPRVMKHTTDLDASKITQGQFDEHYVLSSRVRTGRSIRGLSLPPACTRAERREVENVAITALEGLKGDLAGRYYKLSEMTEQDQQRLIDDHFLFDKPVSPLLTCAGMARDWPDARGIWHNYDKTFLIWINEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQERGWEFMWNERLGYILTCPSN... | 2.7.3.2 | null | muscle contraction [GO:0006936]; phosphocreatine biosynthetic process [GO:0046314]; phosphorylation [GO:0016310] | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; creatine kinase activity [GO:0004111] | PF00217;PF02807; | 1.10.135.10;3.30.590.10; | ATP:guanido phosphotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. | CATALYTIC ACTIVITY: Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10029}; | null | null | null | null | FUNCTION: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. | Homo sapiens (Human) |
P17542 | TAL1_HUMAN | MTERPPSEAARSDPQLEGRDAAEASMAPPHLVLLNGVAKETSRAAAAEPPVIELGARGGPGGGPAGGGGAARDLKGRDAATAEARHRVPTTELCRPPGPAPAPAPASVTAELPGDGRMVQLSPPALAAPAAPGRALLYSLSQPLASLGSGFFGEPDAFPMFTTNNRVKRRPSPYEMEITDGPHTKVVRRIFTNSRERWRQQNVNGAFAELRKLIPTHPPDKKLSKNEILRLAMKYINFLAKLLNDQEEEGTQRAKTGKDPVVGAGGGGGGGGGGAPPDDLLQDVLSPNSSCGSSLDGAASPDSYTEEPAPKHTARSLHPA... | null | null | angiogenesis [GO:0001525]; astrocyte fate commitment [GO:0060018]; basophil differentiation [GO:0030221]; cell fate commitment [GO:0045165]; definitive hemopoiesis [GO:0060216]; embryonic hemopoiesis [GO:0035162]; erythrocyte differentiation [GO:0030218]; erythrocyte maturation [GO:0043249]; hemangioblast cell differen... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; enzyme binding [GO:0019899]; histone deacetylase binding [GO:0042826]; protein dimerization activity [GO:0046983]; RNA p... | PF00010; | 4.10.280.10; | null | PTM: Phosphorylated on serine residues. Phosphorylation of Ser-122 is strongly stimulated by hypoxia (By similarity). {ECO:0000250}.; PTM: Ubiquitinated; subsequent to hypoxia-dependent phosphorylation of Ser-122, ubiquitination targets the protein for rapid degradation via the ubiquitin system. This process may be cha... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | FUNCTION: Implicated in the genesis of hemopoietic malignancies. It may play an important role in hemopoietic differentiation. Serves as a positive regulator of erythroid differentiation (By similarity). {ECO:0000250, ECO:0000269|PubMed:1396592}. | Homo sapiens (Human) |
P17544 | ATF7_HUMAN | MGDDRPFVCNAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARTDSVIIADQTPTPTRFLKNCEEVGLFNELASSFEHEFKKAADEDEKKAAAGPLDMSLPSTPDIKIKEEEPVEVDSSPPDSPASSPCSPPLKEKEVTPKPVLISTPTPTIVRPGSLPLHLGYDPLHPTLPSPTSVITQAPPSNRQMGSPTGSLPLVMHLANGQTMPVLPGPPVQMPSVISLARPVSMVPNIPGIPGPPVNSSGSISPSGHPIPSEAKMRLKATLTHQVSSINGGCGMVVGTASTMVTARPEQSQILIQHPDAPSPAQPQVSPAQPTPSTG... | null | null | negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | cAMP response element binding [GO:0035497]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; enzyme binding [GO:0019899]; metal ion binding [G... | PF00170; | 1.20.5.170;3.30.160.60; | BZIP family | PTM: On EGF stimulation, phosphorylated first on Thr-53 allowing subsequent phosphorylation on Thr-51. This latter phosphorylation prevents sumoylation, increases binding to TAF12 and enhances transcriptional activity. {ECO:0000269|PubMed:18950637}.; PTM: Sumoylation delays nuclear localization and inhibits transactiva... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:17264123}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17264123}. Chromosome, telomere {ECO:0000269|PubMed:29490055}. Note=Mainly nucleoplasmic. Restricted distribution to the perinuculear region. The sumoylated form locates to the nuc... | null | null | null | null | null | FUNCTION: Stress-responsive chromatin regulator that plays a role in various biological processes including innate immunological memory, adipocyte differentiation or telomerase regulation (PubMed:29490055). In absence of stress, contributes to the formation of heterochromatin and heterochromatin-like structure by recru... | Homo sapiens (Human) |
P17549 | BPHA_ASPNG | MLALLLSPYGAYLGLALLVLYYLLPYLKRAHLRDIPAPGLAAFTNFWLLLQTRRGHRFVVVDNAHKKYGKLVRIAPRHTSIADDGAIQAVYGHGNGFLKSDFYDAFVSIHRGLFNTRDRAEHTRKRKTVSHTFSMKSIGQFEQYIHGNIELFVKQWNRMADTQRNPKTGFASLDALNWFNYLAFDIIGDLAFGAPFGMLDKGKDFAEMRKTPDSPPSYVQAVEVLNRRGEVSATLGCYPALKPFAKYLPDSFFRDGIQAVEDLAGIAVARVNERLRPEVMANNTRVDLLARLMEGKDSNGEKLGRAELTAEALTQLIAGS... | 1.14.14.92 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798}; | null | intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | benzoate 4-monooxygenase activity [GO:0018664]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=benzoate + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxybenzoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:18033, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16150, ChEBI:CHEBI:17879,... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.083 mM for benzoate {ECO:0000269|PubMed:11594739}; KM=0.097 mM for 2-fluorobenzoate {ECO:0000269|PubMed:11594739}; KM=0.31 mM for 2-chlorobenzoate {ECO:0000269|PubMed:11594739}; KM=0.28 mM for 2-hydroxybenzoate {ECO:0000269|PubMed:11594739}; KM=1.6 mM for 2-methy... | null | null | null | FUNCTION: Cytochrome P450 monooxygenase; part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway (PubMed:11594739, Ref.6). Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its... | Aspergillus niger |
P17553 | WNT3_MOUSE | MEPHLLGLLLGLLLSGTRVLAGYPIWWSLALGQQYTSLASQPLLCGSIPGLVPKQLRFCRNYIEIMPSVAEGVKLGIQECQHQFRGRRWNCTTIDDSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGTSTICGCDSHHKGPPGEGWKWGGCSEDADFGVLVSREFADARENRPDARSAMNKHNNEAGRTTILDHMHLKCKCHGLSGSCEVKTCWWAQPDFRAIGDFLKDKYDSASEMVVEKHRESRGWVETLRAKYALFKPPTERDLVYYENSPNFCEPNPETGSFGTRDRTCNVTSHGIDGCDLLCCGRGHN... | null | null | anatomical structure formation involved in morphogenesis [GO:0048646]; animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification [GO:0009948]; anterior/posterior pattern specification [GO:0009952]; axon guidance [GO:0007411]; canonical Wnt signaling pathway [GO:0060070]; canonical Wnt signaling pat... | endoplasmic reticulum lumen [GO:0005788]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; protein domain specific binding [GO:0019904]; signaling receptor binding [GO:0005102] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P56703}. Secreted {ECO:0000250|UniProtKB:P56703}. | null | null | null | null | null | FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (By similarity). Required for normal gastrulation, formation of the primitive streak, and for the fo... | Mus musculus (Mouse) |
P17555 | CAP_YEAST | MPDSKYTMQGYNLVKLLKRLEEATARLEDVTIYQEGYIQNKLEASKNNKPSDSGADANTTNEPSAENAPEVEQDPKCITAFQSYIGENIDPLVELSGKIDTVVLDALQLLKGGFQSQLTFLRAAVRSRKPDYSSQTFADSLRPINENIIKLGQLKESNRQSKYFAYLSALSEGAPLFSWVAVDTPVSMVTDFKDAAQFWTNRILKEYRESDPNAVEWVKKFLASFDNLKAYIKEYHTTGVSWKKDGMDFADAMAQSTKNTGATSSPSPASATAAPAPPPPPPAPPASVFEISNDTPATSSDANKGGIGAVFAELNQGENI... | null | null | actin filament depolymerization [GO:0030042]; actin filament organization [GO:0007015]; actin filament severing [GO:0051014]; cAMP-mediated signaling [GO:0019933]; cell morphogenesis [GO:0000902]; positive regulation of actin filament depolymerization [GO:0030836]; positive regulation of mitochondrial fission [GO:00901... | actin cortical patch [GO:0030479]; cytoplasm [GO:0005737]; mating projection tip [GO:0043332] | actin binding [GO:0003779]; adenylate cyclase binding [GO:0008179]; identical protein binding [GO:0042802] | PF08603;PF01213; | 2.160.20.70;1.25.40.330; | CAP family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:8552082}. Note=Cortical actin patches. | null | null | null | null | null | FUNCTION: The N-terminal domain binds to adenylyl cyclase, thereby enabling adenylyl cyclase to be activated by upstream regulatory signals, such as Ras. The C-terminal domain is required for normal cellular morphology and growth control. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17556 | DHA_LYSSH | MKIGIPKEIKNNENRVAMTPAGVVSLTHAGHERLAIETGGGIGSSFTDAEYVAAGAAYRCIGKEAWAQEMILKVKEPVASEYDYFYEGQILFTYLHLAPRAELTQALIDKKVVGIAYETVQLANGSLPLLTPMSEVAGKMATQIGAQYLEKNHGGKGILLGGVSGVHARKVTVIGGGIAGTNAAKIAVGMGADVTVIDLSPERLRQLEDMFGRDVQTLMSNPYNIAESVKHSDLVVGAVLIPGAKAPKLVSEEMIQSMQPGSVVVDIAIDQGGIFATSDRVTTHDDPTYVKHGVVHYAVANMPGAVPRTSTIALTNNTIP... | 1.4.1.1 | null | alanine catabolic process [GO:0006524]; L-alanine catabolic process [GO:0042853]; sporulation resulting in formation of a cellular spore [GO:0030435] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | alanine dehydrogenase activity [GO:0000286]; nucleotide binding [GO:0000166] | PF01262;PF05222; | 3.40.50.720; | AlaDH/PNT family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0QVQ8}. | CATALYTIC ACTIVITY: Reaction=H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate; Xref=Rhea:RHEA:18405, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57972; EC=1.4.1.1; Evidence={ECO:0000269|PubMed:488097}; PhysiologicalDirection=lef... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18.9 uM for oxidative deamination of L-alanine {ECO:0000269|PubMed:488097}; KM=330 uM for oxidative deamination of L-2-aminobutyrate {ECO:0000269|PubMed:488097}; KM=39 uM for oxidative deamination of L-serine {ECO:0000269|PubMed:488097}; KM=20 uM for oxidative deam... | PATHWAY: Amino-acid degradation; L-alanine degradation via dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 10.0-10.5 for the oxidative deamination of L-alanine and about 9.0 for reductive amination of pyruvate. {ECO:0000269|PubMed:488097}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Loses about 50% of its initial activity when heated at 65 degrees Celsius for 5 minutes. {ECO:0000269|PubMed:2340274, ECO:0000269|PubMed:488097}; | FUNCTION: Catalyzes the reversible reductive amination of pyruvate to L-alanine. Prefers L-alanine for oxidative deamination, other substrates are poorly reactive. In the other direction 2-oxobutyrate is almost as reactive as pyruvate. Ammonia is the sole amino donor for the reductive amination of pyruvate, NADPH is in... | Lysinibacillus sphaericus (Bacillus sphaericus) |
P17559 | UTER_RAT | MKIAITITVLMLSICCSSASSDICPGFLQVLEALLLGSESNYEAALKPFNPASDLQNAGTQLKRLVDTLPQETRINIVKLTEKILTSPLCEQDLRV | null | null | negative regulation of interleukin-13 production [GO:0032696]; negative regulation of interleukin-4 production [GO:0032713]; negative regulation of interleukin-5 production [GO:0032714]; negative regulation of T cell proliferation [GO:0042130]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neg... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nuclear envelope [GO:0005635]; secretory granule [GO:0030141] | phospholipase A2 inhibitor activity [GO:0019834]; polychlorinated biphenyl binding [GO:0097160] | PF01099; | 1.10.210.10; | Secretoglobin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2. | Rattus norvegicus (Rat) |
P17560 | RENBP_PIG | MEKERETLQAWKERVGQELDRVMAFWLEHSHDREHGGFFTCLGRDGRVYDDLKYVWLQGRQVWMYCRLYRKLERFHRPELLDAAKAGGEFLLRHARVAPPEKKCAFVLTRDGRPVKVQRSIFSECFYTMAMNELWRVTAEARYQSEAVDMMDQIVHWVREDPSGLGRPQLPGAVASESMAVPMMLLCLVEQLGEEDEELAGRYAQLGHWCARRILQHVQRDGQAVLENVSEDGEELSGCLGRHQNPGHALEAGWFLLRHSSRSGDAKLRAHVIDTFLLLPFRSGWDADHGGLFYFQDADGLCPTQLEWAMKLWWPHSEAM... | 5.1.3.8 | null | 6-sulfoquinovose(1-) catabolic process to glycerone phosphate and 3-sulfolactaldehyde [GO:0061720]; carbohydrate metabolic process [GO:0005975]; N-acetylglucosamine metabolic process [GO:0006044]; N-acetylmannosamine metabolic process [GO:0006051]; N-acetylneuraminate catabolic process [GO:0019262] | null | identical protein binding [GO:0042802]; N-acylglucosamine 2-epimerase activity [GO:0050121]; peptidase inhibitor activity [GO:0030414]; sulfoquinovose isomerase activity [GO:0061593] | PF07221; | 1.50.10.10; | N-acylglucosamine 2-epimerase family | null | null | CATALYTIC ACTIVITY: Reaction=an N-acyl-D-glucosamine = an N-acyl-D-mannosamine; Xref=Rhea:RHEA:19033, ChEBI:CHEBI:16062, ChEBI:CHEBI:17274; EC=5.1.3.8; Evidence={ECO:0000269|PubMed:8663114}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19034; Evidence={ECO:0000305|PubMed:8663114}; PhysiologicalDirection=right-t... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.4 mM for N-acetyl-D-glucosamine {ECO:0000269|PubMed:8663114}; KM=6.3 mM for N-acetyl-D-mannosamine {ECO:0000269|PubMed:8663114}; | PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation. {ECO:0000250|UniProtKB:P51606}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.8. {ECO:0000269|PubMed:8663114}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 47 degrees Celsius. {ECO:0000269|PubMed:8663114}; | FUNCTION: Catalyzes the interconversion of N-acetylglucosamine to N-acetylmannosamine (PubMed:8663114). Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (By similarity). {ECO:0000250|UniProtKB:P82343, ECO:0000269|PubMed:8663114}. | Sus scrofa (Pig) |
P17562 | METK2_ARATH | METFLFTSESVNEGHPDKLCDQISDAVLDACLEQDPDSKVACETCTKTNMVMVFGEITTKATIDYEKIVRDTCRSIGFISDDVGLDADKCKVLVNIEQQSPDIAQGVHGHFTKRPEDIGAGDQGHMFGYATDETPELMPLSHVLATKIGARLTEVRKNGTCRWLRPDGKTQVTVEYYNDNGAMVPVRVHTVLISTQHDETVTNDEIARDLKEHVIKPIIPEKYLDDKTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVANGMARRALVQVSYAIGVPEPLSVFV... | 2.5.1.6 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q96551}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:16365035}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q96551}; Note=Binds 2 divalent ions per subunit. The metal ions interact primarily wit... | one-carbon metabolic process [GO:0006730]; S-adenosylmethionine biosynthetic process [GO:0006556] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleolus [GO:0005730]; plant-type cell wall [GO:0009505]; plasmodesma [GO:0009506] | ATP binding [GO:0005524]; copper ion binding [GO:0005507]; methionine adenosyltransferase activity [GO:0004478] | PF02773;PF02772;PF00438; | 3.30.300.10; | AdoMet synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9LUT2}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000269|PubMed:16365035}; | null | PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. {ECO:0000269|PubMed:16365035}. | null | null | FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. {ECO:0000269|PubMed:16365035}. | Arabidopsis thaliana (Mouse-ear cress) |
P17563 | SBP1_MOUSE | MATKCTKCGPGYSTPLEAMKGPREEIVYLPCIYRNTGTEAPDYLATVDVDPKSPQYSQVIHRLPMPYLKDELHHSGWNTCSSCFGDSTKSRNKLILPGLISSRIYVVDVGSEPRAPKLHKVIEASEIQAKCNVSSLHTSHCLASGEVMVSTLGDLQGNGKGSFVLLDGETFEVKGTWEKPGDAAPMGYDFWYQPRHNVMVSTEWAAPNVFKDGFNPAHVEAGLYGSRIFVWDWQRHEIIQTLQMTDGLIPLEIRFLHDPSATQGFVGCALSSNIQRFYKNAEGTWSVEKVIQVPSKKVKGWMLPEMPGLITDILLSLDDR... | 1.8.3.4 | null | brown fat cell differentiation [GO:0050873]; protein transport [GO:0015031] | cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634] | methanethiol oxidase activity [GO:0018549]; selenium binding [GO:0008430] | PF05694; | null | Selenium-binding protein family | PTM: The N-terminus is blocked. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13228}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13228}. Membrane {ECO:0000250|UniProtKB:Q8VIF7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8VIF7}. Note=May associate with Golgi membrane (By similarity). May associate with the membrane of autophagosomes ... | CATALYTIC ACTIVITY: Reaction=H2O + methanethiol + O2 = formaldehyde + H(+) + H2O2 + hydrogen sulfide; Xref=Rhea:RHEA:11812, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16007, ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:29919; EC=1.8.3.4; Evidence={ECO:0000269|PubMed:29255262}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5 nM for methanethiol {ECO:0000269|PubMed:29255262}; | PATHWAY: Organosulfur degradation. {ECO:0000269|PubMed:29255262}. | null | null | FUNCTION: Catalyzes the oxidation of methanethiol, an organosulfur compound known to be produced in substantial amounts by gut bacteria (PubMed:29255262). Selenium-binding protein which may be involved in the sensing of reactive xenobiotics in the cytoplasm. May be involved in intra-Golgi protein transport (By similari... | Mus musculus (Mouse) |
P17564 | PR15A_MOUSE | MAPSPRPQHVLHWRDAHNFYLLSPLMGLLSRAWSRLRGPEVPEAWLAKTVTGADQIEAAALLTPTPVSGNLLPHGETEESGSPEQSQAAQRLCLVEAESSPPETWGLSNVDEYNAKPGQDDLREKEMERTAGKATLQPAGLQGADKRLGEVVAREEGVAEPAYPTSQLEGGPAENEEDGETVKTYQASAASIAPGYKPSTPVPFLGEAEHQATEEKGTENKADPSNSPSSGSHSRAWEYYSREKPKQEGEAKVEAHRAGQGHPCRNAEAEEGGPETTFVCTGNAFLKAWVYRPGEDTEEEDNSDSDSAEEDTAQTGATPH... | null | null | apoptotic process [GO:0006915]; endoplasmic reticulum unfolded protein response [GO:0030968]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; negative regulation of protein processing [GO:0010955]; negative regulation of transcri... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial outer membrane [GO:0005741]; protein phosphatase type 1 complex [GO:0000164] | protein phosphatase 1 binding [GO:0008157]; protein phosphatase binding [GO:0019903]; protein phosphatase regulator activity [GO:0019888] | PF10488; | null | PPP1R15 family | PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity. Phosphorylation at Tyr-239 enhances proteasomal degradation, this position is dephosphorylated by PTPN2. {ECO:0000250|UniProtKB:O75807}.; PTM: Polyubiquitinated. Exhibits a rapid proteasoma... | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}. Note=Associates with membranes via an N-terminal amphipathic intramembrane regio... | null | null | null | null | null | FUNCTION: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress (PubMed:11381086, PubMed:1... | Mus musculus (Mouse) |
P17568 | NDUB7_HUMAN | MGAHLVRRYLGDASVEPDPLQMPTFPPDYGFPERKEREMVATQQEMMDAQLRLQLRDYCAHHLIRLLKCKRDSFPNFLACKQERHDWDYCEHRDYVMRMKEFERERRLLQRKKRREKKAAELAKGQGPGEVDPKVAL | null | null | aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776] | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739] | NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF05676; | null | Complex I NDUFB7 subunit family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:21310150}; Peripheral membrane protein {ECO:0000269|PubMed:21310150}. Mitochondrion intermembrane space {ECO:0000269|PubMed:21310150}. | null | null | null | null | null | FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ... | Homo sapiens (Human) |
P17571 | NIA1_MAIZE | GFPVRVIIPGCIGGRMVKWLKRIIVTPAESDNYYHFKDNRVLPSHVDAELANAEAWWYKPEYIINELNINSVITTPCHDEILPINAFTTQRPYTLKGYAYSGGGKKVTRVEVTLDGGETWLVCTDHPEKPTKYGKYWCWCFWSLEVEVLDLLSAKEIAVRAWDESLNTQPEKLIWNVMGMMNNCWFRVKTNVCKPHKGEIGIVFDHPTLPGNESGGWMAKEKHLETAEAAAPGLKRSTSTPFMNTTDVGKEFTMSEVRKHASQESAWIVVHGHVYDCTKFLKDHPGGADSILINAGTDCTEEFDAIHSDKAKALLDTYRI... | 1.7.1.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:7812715}; Note=Binds 1 FAD. {ECO:0000269|PubMed:7812715}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Note=Binds 1 heme group. The heme group is called cytochrome b-557.; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000... | nitrate assimilation [GO:0042128]; nitric oxide biosynthetic process [GO:0006809] | null | FAD binding [GO:0071949]; heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; nitrate reductase (NADH) activity [GO:0009703] | PF00173;PF00970;PF03404;PF00175;PF00174; | 2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10; | Nitrate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + nitrite = H(+) + NADH + nitrate; Xref=Rhea:RHEA:17913, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.7.1.1; Evidence={ECO:0000269|PubMed:2189408, ECO:0000269|PubMed:8188655}; | null | null | null | null | FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. {ECO:0000269|PubMed:2189408}. | Zea mays (Maize) |
P17572 | PRL_MELGA | MSNTGASLKGLLLAVLLVSNMLLTKEGVTSLPICSSGSVNCQVSLGELFDRAVRLSHYIHFLSSEIFNEFDERYAQGRGFITKAVNGCHTSSLTTPEDKEQTQQIHHEELLNLILGVLRSWNDPLIHLASEVQRIKEAPDTILWKAVEIEEQNKRLLEGMEKIVGRIHSGDAGNEVFSQWDGLPSLQLADEDSRLFAFYNLLHCLRRDSHKIDNYLKVLKCRLIHDNNC | null | null | estrogen biosynthetic process [GO:0006703]; negative regulation of endothelial cell proliferation [GO:0001937]; photoperiodism [GO:0009648]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of lactation [G... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | PTM: Three forms are found, non-glycosylated, glycosylated and one form seems to be only O-glycosylated. {ECO:0000269|PubMed:1769204}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | null | Meleagris gallopavo (Wild turkey) |
P17573 | LIP1_GEOCN | MVSKTFFLAAALNVVGTLAQAPTAVLNGNEVISGVLEGKVDTFKGIPFADPPVGDLRFKHPQPFTGSYQGLKANDFSSACMQLDPGNAISLLDKVVGLGKIIPDNLRGPLYDMAQGSVSMNEDCLYLNVFRPAGTKPDAKLPVMVWIYGGAFVFGSSASYPGNGYVKESVEMGQPVVFVSINYRTGPYGFLGGDAITAEGNTNAGLHDQRKGLEWVSDNIANFGGDPDKVMIFGESAGAMSVAHQLVAYGGDNTYNGKQLFHSAILQSGGPLPYFDSTSVGPESAYSRFAQYAGCDASAGDNETLACLRSKSSDVLHSAQ... | 3.1.1.3 | null | lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | triglyceride lipase activity [GO:0004806] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; | null | null | null | null | FUNCTION: Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated... | Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum) |
P17585 | AADK_BACSU | MRSEQEMMDIFLDFALNDERIRLVTLEGSRTNRNIPPDNFQDYDISYFVTDVESFKENDQWLEIFGKRIMMQKPEDMELFPPELGNWFSYIILFEDGNKLDLTLIPIREAEDYFANNDGLVKVLLDKDSFINYKVTPNDRQYWIKRPTAREFDDCCNEFWMVSTYVVKGLARNEILFAIDHLNEIVRPNLLRMMAWHIASQKGYSFSMGKNYKFMKRYLSNKEWEELMSTYSVNGYQEMWKSLFTCYALFRKYSKAVSEGLAYKYPDYDEGITKYTEGIYCSVK | 2.7.7.- | null | cellular response to streptomycin [GO:0071239] | cytoplasm [GO:0005737] | adenylyltransferase activity [GO:0070566]; protein homodimerization activity [GO:0042803] | PF04439; | 3.30.460.10;1.20.120.330; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|Ref.5}. | CATALYTIC ACTIVITY: Reaction=ATP + streptomycin = 6-O-adenylylstreptomycin + diphosphate; Xref=Rhea:RHEA:63236, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58007, ChEBI:CHEBI:146262; Evidence={ECO:0000269|PubMed:15984036, ECO:0000269|PubMed:17609790, ECO:0000269|Ref.5}; CATALYTIC ACTIVITY: Reaction=GTP + streptom... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.08 uM for streptomycin {ECO:0000269|Ref.5}; KM=0.04 mM for streptomycin (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:17609790}; KM=0.6 mM for streptidine (at pH 7.5 and 25 degrees Celsius) {ECO:0000269|PubMed:17609790}; Vmax=4 pmol/min/mg enzyme with st... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|Ref.5}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|Ref.5}; | FUNCTION: Mediates bacterial resistance to streptomycin (PubMed:17609790, PubMed:3137862). Adenylates streptomycin on the O-6 residue (PubMed:15984036, PubMed:17609790, PubMed:3137862). Adenylates streptidine on the O-6 residue (PubMed:17609790). Does not act on spectinomycin, neomycin-B or kanamycin (PubMed:15984036, ... | Bacillus subtilis (strain 168) |
P17593 | POLG_EMCVB | MATTMEQEICAHSLTLKGCPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPELDMEVVFELQGNSTSSDKNNSSSDGNEGVIINNFYSNQYQNSIDLSANATGSDPPRTYGQFSNLLSGAVNAFSNMIPLLADQNTEEMENLSDRVLQDTAGNTVTNTQSTVGRLVGYGAVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGAALRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDAFAMDNRWSKDNLPNGTKTQTNRKGPFAMDHQNFWQWTLYPHQFL... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytop... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF00548;PF00680;PF00073;PF00910;PF08935;PF11475; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P12296}. Host cyto... | 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=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2... | null | null | null | null | FUNCTION: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (By similarity). Proteins with NLS signals f... | Encephalomyocarditis virus (strain emc-b nondiabetogenic) |
P17594 | POLG_EMCVD | MATTMEQEICAHSLTFKGCPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPELDMEVVFELQGNSTSSDKNNSSSDGNEGVIINNFYSNQYQNSIDLSANATGSDPPRTYGQFSNLLSGAVNAFSNMIPLLADQNTEEMENLSDRVLQDTAGNTVTNTQSTVGRLVGYGAVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGAALRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDAFAMDNRWSKDNLPNGTKTQTNRKGPFAMDHQNFWQWTLYPHQFL... | 2.7.7.48; 3.4.22.28; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:0039522]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytop... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF00548;PF00680;PF00073;PF00910;PF08935;PF11475; | 1.20.960.20;2.60.120.20;3.30.70.270;4.10.90.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P12296}. Host cyto... | 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=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=ATP + H2... | null | null | null | null | FUNCTION: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (By similarity). Proteins with NLS signals f... | Encephalomyocarditis virus (strain emc-d diabetogenic) |
P17596 | FRDB_WOLSU | MGRMLTIRVFKYDPQSAVSKPHFQEYKIEEAPSMTIFIVLNMIRETYDPDLNFDFVCRAGICGSCGMMINGRPSLACRTLTKDFEDGVITLLPLPAFKLIKDLSVDTGNWFNGMSQRVESWIHAQKEHDISKLEERIEPEVAQEVFELDRCIECGCCIAACGTKIMREDFVGAAGLNRVVRFMIDPHDERTDEDYYELIGDDDGVFGCMTLLACHDVCPKNLPLQSKIAYLRRKMVSVN | 1.3.5.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000269|PubMed:10586875, ECO:00... | respiratory electron transport chain [GO:0022904]; tricarboxylic acid cycle [GO:0006099] | plasma membrane [GO:0005886]; respirasome [GO:0070469] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491] | PF13085;PF13183; | 3.10.20.30;1.10.1060.10; | Succinate dehydrogenase/fumarate reductase iron-sulfur protein family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305|PubMed:10586875}; Cytoplasmic side {ECO:0000305|PubMed:10586875}. | CATALYTIC ACTIVITY: Reaction=a menaquinone + succinate = a menaquinol + fumarate; Xref=Rhea:RHEA:27834, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539, ChEBI:CHEBI:16374, ChEBI:CHEBI:18151, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031; EC=1.3.5.1; Evidence={ECO:0000250|UniProtKB:P0AC47}; | null | null | null | null | FUNCTION: The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. {ECO:0000269|PubMed:10586875, ECO:0000269|PubMed:11248702, ECO:0000269|PubMed:9492313}. | Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W) (Vibrio succinogenes) |
P17597 | ILVB_ARATH | MAAATTTTTTSSSISFSTKPSPSSSKSPLPISRFSLPFSLNPNKSSSSSRRRGIKSSSPSSISAVLNTTTNVTTTPSPTKPTKPETFISRFAPDQPRKGADILVEALERQGVETVFAYPGGASMEIHQALTRSSSIRNVLPRHEQGGVFAAEGYARSSGKPGICIATSGPGATNLVSGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNYLVMDVEDIPRIIEEAFFLATSGRPGPVLVDVPKDIQQQLAIPNWEQAMRLPGYMSRMPKPPEDSHLEQIVRLISESKKPVLYVGGGCLNSSDELGRF... | 2.2.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32640464}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:32640464}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:32640464}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:000026... | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; response to herbicide [GO:0009635]; valine biosynthetic process [GO:0009099] | acetolactate synthase complex [GO:0005948]; chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; mitochondrion [GO:0005739] | acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976] | PF02775;PF00205;PF02776; | 3.40.50.970;3.40.50.1220; | TPP enzyme family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6; | null | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:9355748, ECO:0000269|PubMed:9677339}; | null | FUNCTION: Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis. {ECO:0000269|PubMed:10386618, ECO:0000269|PubMed:16665813, ECO:0000269|PubMed:16667374, ECO:0000269|PubMed:16668488, ECO:0000269|PubMed:2336405, ECO:0000269|PubMed:8913312, ECO:0000269|PubMed:9355748, ... | Arabidopsis thaliana (Mouse-ear cress) |
P17598 | CATA1_GOSHI | MDPYKHRPSSAFNSPFWTTNSGAPVWNNNSSLTVGPRGQYLLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISHLTCADFLRAPGVQTPVIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFIRDGMKFPDMVHALKPNPKSHIQENWRILDFFSHHPESLHMFTFLFDDLGVPQDYRHMEGSGVNTYTLINKAGKAHYVKFHWKPTCGVKCLLEDEAIKVGGANHSHATQDLYDSIAAGNYPEWKLFIQTIDPDHEDKFDFDPLDVTKTWPEDILPLQPVGRLVLNKNIDNFFAENE... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | hydrogen peroxide catabolic process [GO:0042744]; response to hydrogen peroxide [GO:0042542]; seed germination [GO:0009845] | cytoplasm [GO:0005737]; glyoxysome [GO:0009514]; nucleus [GO:0005634]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Peroxisome. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; | null | null | null | null | FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. | Gossypium hirsutum (Upland cotton) (Gossypium mexicanum) |
P17600 | SYN1_HUMAN | MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPGAHSPGATPGPGTATAERSSGVAPAASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAASRVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIG... | null | null | chemical synaptic transmission [GO:0007268]; neuron development [GO:0048666]; neurotransmitter secretion [GO:0007269]; regulation of neurotransmitter secretion [GO:0046928]; regulation of synaptic vesicle cycle [GO:0098693]; regulation of synaptic vesicle exocytosis [GO:2000300]; synapse organization [GO:0050808]; syna... | axon [GO:0030424]; cell body [GO:0044297]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; extrinsic component of synaptic vesicle membrane [GO:0098850]; Golgi apparatus [GO:0005794]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; Schaffer collateral - CA1 synapse [G... | actin binding [GO:0003779]; ATP binding [GO:0005524]; calcium-dependent protein binding [GO:0048306]; cytoskeletal protein-membrane anchor activity [GO:0106006]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901] | PF02078;PF02750;PF10581; | 3.40.50.20;3.30.1490.20;3.30.470.20; | Synapsin family | PTM: Substrate of different protein kinases. Phosphorylated by CaMK2 and MAPK1 (PubMed:21441247). Phosphorylation, including phosphorylation at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, regulates its rate of dispersion, and controls the kinetics of vesicle pool turnover and neurotransmitter releas... | SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:O88935}. Golgi apparatus {ECO:0000250|UniProtKB:O88935}. Presynapse {ECO:0000269|PubMed:21441247}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P09951}. Note=Dissociates from synaptic vesicles and redistributes into the axon during ... | null | null | null | null | null | FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (PubMed:21441247, PubMed:23406870). Also involved in the regulation of axon outgrowth and ... | Homo sapiens (Human) |
P17605 | AT5G1_SHEEP | MQTTGALLISPALIRSCTRGLIRPVSASFLSRPEIPSVQPSYSSGPLQVARREFQTSVVSRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM | null | null | proton motive force-driven ATP synthesis [GO:0015986] | mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276] | lipid binding [GO:0008289]; proton transmembrane transporter activity [GO:0015078] | PF00137; | 1.20.20.10; | ATPase C chain family | PTM: Trimethylated by ATPSCKMT at Lys-104. Methylation is required for proper incorporation of the C subunit into the ATP synthase complex and mitochondrial respiration. {ECO:0000250|UniProtKB:P05496}. | SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Ovis aries (Sheep) |
P17606 | MDHP1_SORBI | MGLSTAYSPVGSHLAPAPLGHRRSAQLHRPRRALLATVRCSVDAAKQVQDGVATAEAPATRKDCFGVFCTTYDLKAEDKTKSWKKLVNIAVSGAAGMISNHLLFKLASGEVFGQDQPIALKLLGSERSFQALEGVAMELEDSLYPLLREVSIGIDPYEVFEDVDWALLIGAKPRGPGMERAALLDINGQIFADQGKALNAVASKNVKVLVVGNPCNTNALICLKNAPDIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNVTIWGNHSTTQVPDFLNAKIDGRPVKEVIKDTKWLEEEFTITVQKRGGALIQKWGRSS... | 1.1.1.82 | null | malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | chloroplast [GO:0009507] | L-malate dehydrogenase activity [GO:0030060]; malate dehydrogenase (NADP+) activity [GO:0046554] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 2 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate; Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.82; | null | null | null | null | FUNCTION: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells. | Sorghum bicolor (Sorghum) (Sorghum vulgare) |
P17607 | LYSC1_SHEEP | MKALIILGLLCLSVAVQGKVFERCELARTLKELGLDGYKGVSLANWLCLTKWESSYNTKATNYNPGSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCSELMENNIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCSL | 3.2.1.17 | null | defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; digestion [GO:0007586]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | extracellular region [GO:0005576] | lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; | null | null | null | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. | Ovis aries (Sheep) |
P17608 | RYH1_SCHPO | MSENYSFSLRKFKLVFLGEQSVGKTSLITRFMYDQFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAIIVYDITNHNSFVNTEKWIEDVRAERGDDVIIVLVGNKTDLADKRQVTQEEGEKKAKELKIMHMETSAKAGHNVKLLFRKIAQMLPGMENVETQSTQMIDVSIQPNENESSCNC | null | null | intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; positive regulation of TORC2 signaling [GO:1904515]; protein localization to phagophore assembly site [GO:0034497]; retrograde transport, endosome to Golgi [GO:0042147]; retrograde vesicle-mediated transport, Golgi to end... | cytosol [GO:0005829]; endomembrane system [GO:0012505]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:16483310}; Lipid-anchor {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:16483310}; Lipid-anchor {ECO:0000305}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Has a role in retrograde traffricking of proteins from the endosome to the Golgi. Involved in protein transport to the plasma membrane. Involved in the secretory pathway where it has a role in acid phosphatase secretion. Required also in normal glycosylation trafficking pathways. {ECO:0000269|PubMed:16483310}... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P17609 | YPT2_SCHPO | MSTKSYDYLIKLLLIGDSGVGKSCLLLRFSEDSFTPSFITTIGIDFKIRTIELDGKRIKLQIWDTAGQERFRTITTAYYRGAMGILLLYDVTDKKSFDNVRTWFSNVEQHASENVYKILIGNKCDCEDQRQVSFEQGQALADELGVKFLEASAKTNVNVDEAFFTLAREIKKQKIDAENEFSNQANNVDLGNDRTVKRCC | null | null | endocytic recycling [GO:0032456]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; Golgi vesicle fusion to target membrane [GO:0048210]; intracellular protein transport [GO:0006886]; protein localization to plasma membrane [GO:0072659]; protein secretion [GO:0009306]; regulation of exocytosis [... | cytosol [GO:0005829]; endosome [GO:0005768]; meiotic spindle pole body [GO:0035974]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; prospore membrane [GO:0005628]; trans-Golgi network transport vesicle [GO:0030140] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | null | null | null | null | null | FUNCTION: Protein transport. Probably involved in vesicular traffic (By similarity). {ECO:0000250}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P17610 | YPT3_SCHPO | MCQEDEYDYLFKTVLIGDSGVGKSNLLMRFTRNEFNIESKSTIGVEFATRNIVLDNKKIKAQIWDTAGQERYRAITSAYYRGAVGALIVYDITKQSSFDNVGRWLKELREHADSNIVIMLVGNKTDLLHLRAVSTEEAQAFAAENNLSFIETSAMDASNVEEAFQTVLTEIFRIVSNRSLEAGDDGVHPTAGQTLNIAPTMNDLNKKKSSSQCC | null | null | ascospore-type prospore membrane formation [GO:0032120]; exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; membrane addition at site of mitotic cytokinesis [GO:0061796]; mitotic cytokinesis [GO:0000281]; protein localization to cell cortex of cell tip [GO:1990896]; protein localization to meiotic s... | cleavage furrow leading edge [GO:0090689]; cortical dynamic polarity patch [GO:0090726]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; growing cell tip [GO:0035838]; meiotic spindle pole [GO:0090619]; meiotic spindle pole body [G... | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305|PubMed:1597466}; Cytoplasmic side {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:12181359, ECO:0000269|PubMed:16483310}; Lipid-anchor {ECO:0000305|PubMed:1597466}. Golgi apparatus membrane {ECO:0000269|PubMed:12181359, ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Has a role in retrograde traffricking of proteins from the endosome to the Golgi. Involved in the secretory pathway where it has a role in acid phosphatase secretion. {ECO:0000269|PubMed:12181359, ECO:0000269|PubMed:16483310}. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P17612 | KAPCA_HUMAN | MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFK... | 2.7.11.11 | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell communication by electrical coupling involved in cardiac conduction [GO:0086064]; cellular response to cold [GO:0070417]; cellular response to epinephr... | acrosomal vesicle [GO:0001669]; calcium channel complex [GO:0034704]; cAMP-dependent protein kinase complex [GO:0005952]; centrosome [GO:0005813]; ciliary base [GO:0097546]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]... | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; protein domain specific binding [GO:0019904]; protein kinase A regulatory subunit binding [GO:0034237]; protein kinas... | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin K(2) (PubMed:12372837, PubMed:17909264). Phosphorylated on threonine and serine residues. Phosphorylation on Thr-198 is required for full activity (PubMed:16765046, PubMed:20137943, PubMed:20481595, PubMed:20732331, PubMed:21774789, Ref.43). Phosphorylated... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21085490, ECO:0000269|PubMed:21423175}. Cell membrane {ECO:0000269|PubMed:19210988, ECO:0000269|PubMed:21423175}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Nucleus {ECO:0000269|PubMed:21085490}. Mitochondrion {ECO:0000250|UniProtKB:P05132}. Note=Translocates... | 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=2.7.11.11; Evidence={ECO:0000269|PubMed:21812984, ECO:00002... | null | null | null | null | FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984, PubMed:31112131). Phosphoryl... | Homo sapiens (Human) |
P17618 | RIBD_BACSU | MEEYYMKLALDLAKQGEGQTESNPLVGAVVVKDGQIVGMGAHLKYGEAHAEVHAIHMAGAHAEGADIYVTLEPCSHYGKTPPCAELIINSGIKRVFVAMRDPNPLVAGRGISMMKEAGIEVREGILADQAERLNEKFLHFMRTGLPYVTLKAAASLDGKIATSTGDSKWITSEAARQDAQQYRKTHQSILVGVGTVKADNPSLTCRLPNVTKQPVRVILDTVLSIPEDAKVICDQIAPTWIFTTARADEEKKKRLSAFGVNIFTLETERIQIPDVLKILAEEGIMSVYVEGGSAVHGSFVKEGCFQEIIFYFAPKLIGGT... | 1.1.1.193; 3.5.4.26 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16308316}; Note=Binds 1 zinc ion. {ECO:0000269|PubMed:16308316}; | riboflavin biosynthetic process [GO:0009231] | null | 5-amino-6-(5-phosphoribosylamino)uracil reductase activity [GO:0008703]; diaminohydroxyphosphoribosylaminopyrimidine deaminase activity [GO:0008835]; NADP binding [GO:0050661]; zinc ion binding [GO:0008270] | PF00383;PF01872; | 3.40.140.10;3.40.430.10; | Cytidine and deoxycytidylate deaminase family; HTP reductase family | null | null | CATALYTIC ACTIVITY: Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+); Xref=Rhea:RHEA:21868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58453, ChEBI:CHEBI:58614; EC=3.5.4.26; CATALYTIC ACTIVITY: Reaction=5-ami... | null | PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.; PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4. | null | null | FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate. | Bacillus subtilis (strain 168) |
P17625 | GYS2_RAT | MLRGRSLSVTSLGGLPAWEAERLPVEDLLLFEVSWEVTNKVGGICTVIQSKAKTTANEWGENYFLIGPYFEHNVKTQVEPCEPANDAVRKAVDAMNKHGCQVHFGRWLIEGSPYVVLFDISSSVWNLDRWKGDFWEACGVGIPHDDREANDMLIFGSLTAWFLKEVTDHADGKHVIAQFHEWQAGTGLILSRARKLPIATIFTTHATLLGRYLCAANIDFYNQLDKFNIDKEAGERQIYHRYCMERASVHCAHVFTTVSEITAIEADHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHATYKARIQDFVRGHFYGHLDFDL... | 2.4.1.11 | null | glycogen biosynthetic process [GO:0005978]; glycogen metabolic process [GO:0005977]; response to glucose [GO:0009749] | cell cortex [GO:0005938]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829] | glucose binding [GO:0005536]; glycogen (starch) synthase activity [GO:0004373] | PF05693; | 3.40.50.2000; | Glycosyltransferase 3 family | PTM: Primed phosphorylation at Ser-657 (site 5) by CSNK2A1 and CSNK2A2 is required for inhibitory phosphorylation at Ser-641 (site 3a), Ser-645 (site 3b), Ser-649 (site 3c) and Ser-653 (site 4) by GSK3A an GSK3B. Dephosphorylation at Ser-641 and Ser-645 by PP1 activates the enzyme (By similarity). Phosphorylation at Se... | null | CATALYTIC ACTIVITY: Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11; Evidence={ECO:0000269|PubMed:1731614}; P... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 mM for UDP-alpha-D-glucose (UDPG) (in the absence of glucose-6-phosphate) (poorly or non-phosphorylated state) {ECO:0000269|PubMed:1731614}; KM=1 mM for UDP-alpha-D-glucose (UDPG) (in the presence of 50 uM glucose-6-phosphate) (poorly or non-phosphorylated stat... | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:1731614}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.5 (at 25 degrees Celsius) (non-phosphorylated state). Optimum pH is 8.5 (at 25 degrees Celsius) (most phosphorylated state). {ECO:0000269|PubMed:1731614}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-40 degrees Celsius. {ECO:0000269|PubMed:1731614}; | FUNCTION: Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to ... | Rattus norvegicus (Rat) |
P17629 | HPR1_YEAST | MSNTEELIQNSIGFLQKTFKALPVSFDSIRHEPLPSSMLHASVLNFEWEPLEKNISAIHDRDSLIDIILKRFIIDSMTNAIEDEEENNLEKGLLNSCIGLDFVYNSRFNRSNPASWGNTFFELFSTIIDLLNSPSTFLKFWPYAESRIEWFKMNTSVEPVSLGESNLISYKQPLYEKLRHWNDILAKLENNDILNTVKHYNMKYKLENFLSELLPINEESNFNRSASISALQESDNEWNRSARERESNRSSDVIFAADYNFVFYHLIICPIEFAFSDLEYKNDVDRSLSPLLDAILEIEENFYSKIKMNNRTRYSLEEAL... | null | null | DNA recombination [GO:0006310]; mRNA 3'-end processing [GO:0031124]; mRNA export from nucleus [GO:0006406]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of transcription elongation by RNA polymerase I [GO:2001209]; transcription elongation by RNA polymerase II [GO:0006368];... | Cdc73/Paf1 complex [GO:0016593]; chromosome, telomeric region [GO:0000781]; nucleoplasmic THO complex [GO:0000446]; THO complex part of transcription export complex [GO:0000445]; transcription export complex [GO:0000346] | molecular adaptor activity [GO:0060090]; nucleic acid binding [GO:0003676] | PF11957; | null | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11060033, ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymera... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17633 | MBHS_RUBGE | METFYEVMRRQGISRRSFLKYCSLTATSLGLAPSFVPQIAHAMETKPRTPVLWLHGLECTCCSESFIRSAHPLAKDAVLSMISLDYDDTLMAAAGHQAEAILDEIMAKYKGNYILAVEGNPPLNEDGMFCIQRQALPREAQAVAADCKAVIAWGSCASWGCVQAAKPNPTQATPIHKVITDKPIIKVPGCPPIAEVMTGVITYMLTFDRIPELDRQGRPKMFYSQRIHDKCYRRPHFDAGQFVESFDDENARKGFCLYKVGCKGPTTYNACSTVMWNEGTSFPIKAGHGCTGCSEDGFWDKGSFYDRLTNIHQFGIEASA... | 1.12.99.6 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P21853}; Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P21853}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250|UniProtKB:P21853}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P21853... | anaerobic respiration [GO:0009061] | [Ni-Fe] hydrogenase complex [GO:0044569]; ferredoxin hydrogenase complex [GO:0009375]; plasma membrane [GO:0005886] | 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; ferredoxin hydrogenase activity [GO:0008901]; hydrogenase (acceptor) activity [GO:0033748]; metal ion binding [GO:0046872] | PF14720;PF01058; | 4.10.480.10;3.40.50.700; | [NiFe]/[NiFeSe] hydrogenase small subunit family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6; | null | null | null | null | FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. | Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas gelatinosa) |
P17635 | FMO2_RABIT | MAKKVAVIGAGVSGLISLKCCVDEGLEPTCFERTEDIGGLWRFKENVEDGRASIYQSVITNTSKEMSCFSDFPMPEDFPNFLHNSKLLEYFRIFAKKFDLLKYIQFQTTVISVKKRPDFASSGQWEVVTQSNSKQQSAVFDAVMVCSGHHILPNIPLKSFPGIEKFKGQYFHSRQYKHPAGLEGKRILVIGIGNSASDIAVELSKKAAQVYISTRKGSWVMSRISEDGYPWDMVFHTRFSSMLRNVLPRMIVKWMMEQQMNRWFNHENYGLAPENKYLMKEPVLNDDLPSRILYGTIKVKRRVKELTESAAIFEDGTVEE... | 1.14.13.-; 1.14.13.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | NADPH oxidation [GO:0070995] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | flavin adenine dinucleotide binding [GO:0050660]; hypotaurine dehydrogenase activity [GO:0047822]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661] | PF00743; | 3.50.50.60; | FMO family | null | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:16620765}; Single-pass membrane protein {ECO:0000269|PubMed:16620765}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:16620765}; Single-pass membrane protein {ECO:0000269|PubMed:16620765}. | CATALYTIC ACTIVITY: Reaction=H(+) + N,N-dimethylaniline + NADPH + O2 = H2O + N,N-dimethylaniline N-oxide + NADP(+); Xref=Rhea:RHEA:24468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16269, ChEBI:CHEBI:17735, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.8; Evidence={ECO:0000269|PubMed:113029... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 uM for thiourea {ECO:0000269|PubMed:15144220}; KM=21 uM for ethylenethiourea {ECO:0000269|PubMed:15144220}; KM=82 uM for N-phenylthiourea {ECO:0000269|PubMed:15144220}; KM=25 uM for ANTU {ECO:0000269|PubMed:15144220}; KM=310 uM for N,N-dimethylaniline {ECO:00002... | null | null | null | FUNCTION: Catalyzes the oxidative metabolism of numerous xenobiotics, including mainly therapeutic drugs and insecticides that contain a soft nucleophile, most commonly nitrogen and sulfur and participates to their bioactivation (PubMed:10950853, PubMed:11302936, PubMed:15144220, PubMed:15294458, PubMed:16620765, PubMe... | Oryctolagus cuniculus (Rabbit) |
P17636 | FMO1_RABIT | MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYSDFPFPEDYPNYVPNSQFLDYLKMYADRFSLLKSIQFKTTVFSITKCQDFNVSGQWEVVTLHEGKQESAIFDAVMVCTGFLTNPHLPLGCFPGIKTFKGQYFHSRQYKHPDIFKDKRVLVVGMGNSGTDIAVEASHVAKKVFLSTTGGAWVISRVFDSGYPWDMVFTTRFQNFIRNSLPTPIVTWLVAKKMNSWFNHANYGLVPKDRIQLKEPVLNDELPGRIITGKVFIRPSIKEVKENSVVFGNAHNTP... | 1.14.13.148; 1.14.13.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q01740}; | taurine biosynthetic process [GO:0042412] | endoplasmic reticulum membrane [GO:0005789] | flavin adenine dinucleotide binding [GO:0050660]; hypotaurine dehydrogenase activity [GO:0047822]; N,N-dimethylaniline monooxygenase activity [GO:0004499]; NADP binding [GO:0050661]; trimethylamine monooxygenase activity [GO:0034899] | PF00743; | 3.50.50.60; | FMO family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:2505769}; Single-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=H(+) + hypotaurine + NADPH + O2 = H2O + NADP(+) + taurine; Xref=Rhea:RHEA:69819, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:57853, ChEBI:CHEBI:58349, ChEBI:CHEBI:507393; EC=1.14.13.8; Evidence={ECO:0000250|UniProtKB:Q01740}; PhysiologicalDirectio... | null | null | null | null | FUNCTION: Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics (By similarity). Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytopr... | Oryctolagus cuniculus (Rabbit) |
P17643 | TYRP1_HUMAN | MSAPKLLSLGCIFFPLLLFQQARAQFPRQCATVEALRSGMCCPDLSPVSGPGTDRCGSSSGRGRCEAVTADSRPHSPQYPHDGRDDREVWPLRFFNRTCHCNGNFSGHNCGTCRPGWRGAACDQRVLIVRRNLLDLSKEEKNHFVRALDMAKRTTHPLFVIATRRSEEILGPDGNTPQFENISIYNYFVWTHYYSVKKTFLGVGQESFGEVDFSHEGPAFLTWHRYHLLRLEKDMQEMLQEPSFSLPYWNFATGKNVCDICTDDLMGSRSNFDSTLISPNSVFSQWRVVCDSLEDYDTLGTLCNSTEDGPIRRNPAGNVA... | 1.14.18.- | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000269|PubMed:28661582}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:28661582}; Note=Contains bound zinc ions after heterologous expression in insect cells, giving rise to a protein that lacks DHICA oxidase activity. {ECO:0000269|PubMed... | acetoacetic acid metabolic process [GO:0043438]; melanin biosynthetic process [GO:0042438]; melanocyte differentiation [GO:0030318]; melanosome organization [GO:0032438]; positive regulation of melanin biosynthetic process [GO:0048023] | clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; endosome membrane [GO:0010008]; intracellular vesicle [GO:0097708]; melanosome [GO:0042470]; melanosome membrane [GO:0033162] | metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; protein homodimerization activity [GO:0042803]; tyrosinase activity [GO:0004503] | PF00264; | 1.10.1280.10; | Tyrosinase family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P07147}. | SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P07147}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P07147}. Note=Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. Proper trafficking to mel... | CATALYTIC ACTIVITY: Reaction=2 5,6-dihydroxyindole-2-carboxylate + O2 = 2 H2O + 2 indole-5,6-quinone-2-carboxylate; Xref=Rhea:RHEA:68388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16875, ChEBI:CHEBI:177869; Evidence={ECO:0000269|PubMed:28661582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68389; Evide... | null | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:16704458, ECO:0000269|PubMed:22556244, ECO:0000269|PubMed:23504663}. | null | null | FUNCTION: Plays a role in melanin biosynthesis (PubMed:16704458, PubMed:22556244, PubMed:23504663). Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid in the presence of bound Cu(2+) ions, but not in the presence of Zn(2+) (PubMed:28661582). May regulate o... | Homo sapiens (Human) |
P17644 | ACH2_DROME | MAPGCCTTRPRPIALLAHIWRHCKPLCLLLVLLLLCETVQANPDAKRLYDDLLSNYNRLIRPVSNNTDTVLVKLGLRLSQLIDLNLKDQILTTNVWLEHEWQDHKFKWDPSEYGGVTELYVPSEHIWLPDIVLYNNADGEYVVTTMTKAILHYTGKVVWTPPAIFKSSCEIDVRYFPFDQQTCFMKFGSWTYDGDQIDLKHISQKNDKDNKVEIGIDLREYYPSVEWDILGVPAERHEKYYPCCAEPYPDIFFNITLRRKTLFYTVNLIIPCVGISYLSVLVFYLPADSGEKIALCISILLSQTMFFLLISEIIPSTSLA... | null | null | monoatomic cation transmembrane transport [GO:0098655]; synaptic transmission, cholinergic [GO:0007271] | acetylcholine-gated channel complex [GO:0005892]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202] | acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; transmembrane signaling receptor activity [GO:0004888]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane pot... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. {ECO:0000250}. | Drosophila melanogaster (Fruit fly) |
P17649 | GABAT_YEAST | MSICEQYYPEEPTKPTVKTESIPGPESQKQLKELGEVFDTRPAYFLADYEKSLGNYITDVDGNTYLDLYAQISSIALGYNNPALIKAAQSPEMIRALVDRPALGNFPSKDLDKILKQILKSAPKGQDHVWSGLSGADANELAFKAAFIYYRAKQRGYDADFSEKENLSVMDNDAPGAPHLAVLSFKRAFHGRLFASGSTTCSKPIHKLDFPAFHWPHAEYPSYQYPLDENSDANRKEDDHCLAIVEELIKTWSIPVAALIIEPIQSEGGDNHASKYFLQKLRDITLKYNVVYIIDEVQTGVGATGKLWCHEYADIQPPVD... | 2.6.1.19 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:17355287}; | gamma-aminobutyric acid catabolic process [GO:0009450] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | 4-aminobutyrate transaminase activity [GO:0003867]; 4-aminobutyrate:2-oxoglutarate transaminase activity [GO:0034386]; pyridoxal phosphate binding [GO:0030170] | PF00202; | 3.90.1150.10;3.40.640.10; | Class-III pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19; Evidence={ECO:0000269|PubMed:17355287, ECO:0000305|PubMed:3888627}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.2 mM for 4-aminobutanoate {ECO:0000269|PubMed:17355287}; KM=0.22 mM for 2-oxoglutarate {ECO:0000269|PubMed:17355287}; Vmax=12.8 umol/min/mg enzyme {ECO:0000269|PubMed:17355287}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.3. {ECO:0000269|PubMed:3888627}; | null | FUNCTION: Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source and for oxidative stress tolerance. Deaminates GABA to succinate semialdehyde, which in turn is converted to succinate by the succinate-semialdehyde dehydrogenase UGA2. Cannot transami... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P17654 | AMY1_ORYSJ | MQVLNTMVNKHFLSLSVLIVLLGLSSNLTAGQVLFQGFNWESWKENGGWYNFLMGKVDDIAAAGITHVWLPPPSHSVGEQGYMPGRLYDLDASKYGNEAQLKSLIEAFHGKGVQVIADIVINHRTAEHKDGRGIYCLFEGGTPDSRLDWGPHMICRDDPYGDGTGNPDTGADFAAAPDIDHLNKRVQRELIGWLDWLKMDIGFDAWRLDFAKGYSADMAKIYIDATEPSFAVAEIWTSMANGGDGKPNYDQNAHRQELVNWVDRVGGANSNATAFDFTTKGILNVAVEGELWRLRGEDGKAPGMIGWWPAKATTFVDNHD... | 3.2.1.1 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00693}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P00693}; | starch catabolic process [GO:0005983]; sucrose catabolic process [GO:0005987] | null | alpha-amylase activity [GO:0004556]; calcium ion binding [GO:0005509] | PF07821;PF00128; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 13 family | PTM: Only cereal amylase known to be glycosylated. | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000250|UniProtKB:P00693}; | null | null | null | null | FUNCTION: Important for breakdown of endosperm starch during germination. | Oryza sativa subsp. japonica (Rice) |
P17655 | CAN2_HUMAN | MAGIAAKLAKDREAAEGLGSHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHE... | 3.4.22.53 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 7 Ca(2+) ions. {ECO:0000250}; | behavioral response to pain [GO:0048266]; blastocyst development [GO:0001824]; cellular response to amino acid stimulus [GO:0071230]; cellular response to interferon-beta [GO:0035458]; cellular response to lipopolysaccharide [GO:0071222]; female pregnancy [GO:0007565]; myoblast fusion [GO:0007520]; positive regulation ... | calpain complex [GO:0110158]; chromatin [GO:0000785]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi a... | calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; cysteine-type peptidase activity [GO:0008234]; cytoskeletal protein binding [GO:0008092]; enzyme binding [GO:0019899]; protein-containing complex binding [GO:0044877] | PF01067;PF13833;PF00648; | 2.60.120.380;3.90.70.10;1.10.238.10; | Peptidase C2 family | null | SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding. | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.53; | 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 MYOC at 'Arg-226' (PubMed:17650508). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translat... | Homo sapiens (Human) |
P17658 | KCNA6_HUMAN | MRSEKSLTLAAPGEVRGPEGEQQDAGDFPEAGGGGGCCSSERLVINISGLRFETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFLEEIRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRVDGRGGNNGGVSRVSPVSRGSQEEEEDEDDSYTFHHGITPGEMGTGGSSSLSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKPAFFRNIMNIIDLVAIFPYFITLGTELVQQQE... | null | null | potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260] | axon terminus [GO:0043679]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; potassium channel complex [GO:0034705]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251]; voltage-gated potassium channel activity [GO:0005249] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Kv1.6/KCNA6 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14575698, ECO:0000269|PubMed:2347305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (PubMed:14575698, PubMed:2347305). The channel alternates between opened and... | Homo sapiens (Human) |
P17659 | KCNA6_RAT | MRSEKSLTLAAPGEVRGPEGEQQDAGEFQEAEGGGGCCSSERLVINISGLRYETQLRTLSLFPDTLLGDPGRRVRFFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDIFMEEIRFYQLGDEALAAFREDEGCLPEGGEDEKPLPSQPFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPQFRADGRGGSNEGSGTRMSPASRGSHEEEDEDEDSYAFPGSIPSGGLGTGGTSSFSTLGGSFFTDPFFLVETLCIVWFTFELLVRFSACPSKAAFFRNIMNIIDLVAIFPYFITLGTELVQRH... | null | null | potassium ion transmembrane transport [GO:0071805]; protein homooligomerization [GO:0051260] | axon [GO:0030424]; axon terminus [GO:0043679]; plasma membrane [GO:0005886]; potassium channel complex [GO:0034705]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Kv1.6/KCNA6 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1993474}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response ... | Rattus norvegicus (Rat) |
P17661 | DESM_HUMAN | MSQAYSSSQRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGFGSKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGTTRTPSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQE... | null | null | cytoskeleton organization [GO:0007010]; intermediate filament organization [GO:0045109]; muscle contraction [GO:0006936]; nuclear envelope organization [GO:0006998]; regulation of heart contraction [GO:0008016]; skeletal muscle organ development [GO:0060538] | cardiac myofibril [GO:0097512]; cell tip [GO:0051286]; cell-cell junction [GO:0005911]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; fascia adherens [GO:0005916]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; neuromuscular junction [GO:... | cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; structural constituent of cytoskeleton [GO:0005200] | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: ADP-ribosylation prevents ability to form intermediate filaments. {ECO:0000250|UniProtKB:P48675}.; PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by ROCK1 contribute to efficient separation of desmin intermediate filaments during mitosis. ... | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:24200904, ECO:0000269|PubMed:26724190, ECO:0000269|PubMed:30262925}. Cytoplasm {ECO:0000269|PubMed:25394388}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25394388}. Nucleus {ECO:0000250|UniProtKB:P31001}. Cell tip {ECO:0000250|UniProtKB... | null | null | null | null | null | FUNCTION: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mito... | Homo sapiens (Human) |
P17664 | NEF_SIVCZ | MGTKWSKSSLVGWPEVRRRIREAPTAAEGVGEVSKDLERHGAITSRNTPETNQTLAWLEEMDNEEVGFPVRPQVPTRPMTYKAAFDLSHFLKEKGGLEGLVYSRRRQEILDLWVYHTQGFFPDWQNYTTGPGTRFPLCFGWCFKLVPLTEEQVEQANEGDNNCLLHPICQHGMEDEDKEVLVWRFDSRLALRHIAREQHPEYYKD | null | null | suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated pertu... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | GTP binding [GO:0005525]; SH3 domain binding [GO:0017124] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Simian immunodeficiency virus (isolate CPZ GAB1) (SIV-cpz) (Chimpanzee immunodeficiency virus) |
P17671 | E75BC_DROME | MLMSADSSDSAKTSVICSTVSASMLAPPAPEQPSTTAPPILGVTGRSHLENALKLPPNTSVSAYYQHNSKLGMGQNYNPEFRSLVAPVTDLDTVPPTGVTMASSSNSPNSSVKLPHSGVIFVSKSSAVSTTDGPTAVLQQQQPQQQMPQHFESLPHHHPQQEHQPQQQQQQHHLQHHPHPHVMYPHGYQQANLHHSGGIAVVPADSRPQTPEYIKSYPVMDTTVASSVKGEPELNIEFDGTTVLCRVCGDKASGFHYGVHSCEGCKGFFRRSIQQKIQYRPCTKNQQCSILRINRNRCQYCRLKKCIAVGMSRDAVRFGR... | null | null | cell differentiation [GO:0030154]; ecdysis, chitin-based cuticle [GO:0018990]; hormone-mediated signaling pathway [GO:0009755]; molting cycle, chitin-based cuticle [GO:0007591]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oogenesis [GO:0048477]; positive regulation of transcription by RNA po... | nucleus [GO:0005634] | DNA binding [GO:0003677]; heme binding [GO:0020037]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Implicated in the regulation of ecdysone-triggered gene hierarchies. Probably plays a key role in mediating the regulation of the larval molt by 20-OH-ecdysone. {ECO:0000269|PubMed:8223281}. | Drosophila melanogaster (Fruit fly) |
P17672 | E75BA_DROME | MVCAMQEVAAVQHQQQQQQLQLPQQQQQQQQTTQQQHATTIVLLTGNGGGNLHIVATPQQHQPMHQLHHQHQHQHQHQQQAKSQQLKQQHSALVKLLESAPIKQQQQTPKQIVYLQQQQQQPQRKRLKNEAAIVQQQQQTPATLVKTTTTSNSNSNNTQTTNSISQQQQQHQIVLQHQQPAAAATPKPCADLSAKNDSESGIDEDSPNSDEDCPNANPAGTSLEDSSYEQYQCPWKKIRYARELKQRELEQQQTTGGSNAQQQVEAKPAAIPTSNIKQLHCDSPFSAQTHKEIANLLRQQSQQQQVVATQQQQQQQQQHQ... | null | null | cell differentiation [GO:0030154]; ecdysis, chitin-based cuticle [GO:0018990]; hormone-mediated signaling pathway [GO:0009755]; molting cycle, chitin-based cuticle [GO:0007591]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oogenesis [GO:0048477]; positive regulation of transcription by RNA po... | nucleus [GO:0005634] | DNA binding [GO:0003677]; heme binding [GO:0020037]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Implicated in the regulation of ecdysone-triggered gene hierarchies. Probably plays a key role in mediating the regulation of the larval molt by 20-OH-ecdysone. {ECO:0000269|PubMed:8223281}. | Drosophila melanogaster (Fruit fly) |
P17676 | CEBPB_HUMAN | MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQL... | null | null | acute-phase response [GO:0006953]; brown fat cell differentiation [GO:0050873]; cellular response to amino acid stimulus [GO:0071230]; defense response to bacterium [GO:0042742]; embryonic placenta development [GO:0001892]; granuloma formation [GO:0002432]; hepatocyte proliferation [GO:0072574]; immune response [GO:000... | C/EBP complex [GO:1990647]; CHOP-C/EBP complex [GO:0036488]; chromatin [GO:0000785]; condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repre... | PF07716; | 1.20.5.170; | BZIP family, C/EBP subfamily | PTM: Methylated. Methylation at Arg-3 by CARM1 and at Lys-43 by EHMT2 inhibit transactivation activity. Methylation is probably inhibited by phosphorylation at Thr-235. {ECO:0000305|PubMed:18647749, ECO:0000305|PubMed:20111005}.; PTM: Sumoylated by polymeric chains of SUMO2 or SUMO3 (PubMed:12810706). Sumoylation at Ly... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829347}. Cytoplasm {ECO:0000269|PubMed:9374525}. Note=Translocates to the nucleus when phosphorylated at Ser-288. In T-cells when sumoylated drawn to pericentric heterochromatin thereby allowing proliferation (By similarity). {ECO:0000250|UniProtKB:P28033, ECO:0000269... | null | null | null | null | null | FUNCTION: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The... | Homo sapiens (Human) |
P17677 | NEUM_HUMAN | MLCCMRRTKQVEKNDDDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKDDVQAAEAEANKKDEAPVADGVEKKGEGTTTAEAAPATGSKPDEPGKAGETPSEEKKGEGDAATEQAAPQAPASSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATTPAAEDAAAKATAQPPTETGESSQAEENIEAVDETKPKESARQDEGKEEEPEADQEHA | null | null | astrocyte differentiation [GO:0048708]; axon choice point recognition [GO:0016198]; axon regeneration [GO:0031103]; cell fate commitment [GO:0045165]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; radial glial cell differentiation [GO:0060019]; regulation of filopodium assembly ... | cytoplasm [GO:0005737]; dendrite [GO:0030425]; filopodium membrane [GO:0031527]; GABA-ergic synapse [GO:0098982]; growth cone membrane [GO:0032584]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; presynapse [GO:0098793] | calmodulin binding [GO:0005516]; lysophosphatidic acid binding [GO:0035727]; phosphatidylinositol phosphate binding [GO:1901981]; phosphatidylserine binding [GO:0001786] | PF00612;PF06614;PF10580; | 1.20.5.190; | Neuromodulin family | PTM: Phosphorylated (By similarity). Phosphorylation of this protein by a protein kinase C is specifically correlated with certain forms of synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:P07936}.; PTM: Palmitoylated by ZDHHC3 (By similarity). Palmitoylation is regulated by ARF6 and is essential for plasma ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14978216}; Peripheral membrane protein {ECO:0000269|PubMed:14978216}; Cytoplasmic side {ECO:0000269|PubMed:14978216}. Cell projection, growth cone membrane {ECO:0000269|PubMed:14978216}; Peripheral membrane protein {ECO:0000269|PubMed:14978216}; Cytoplasmic side {... | null | null | null | null | null | FUNCTION: This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction. {ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:21152083}. | Homo sapiens (Human) |
P17678 | GATA1_CHICK | MEFVALGGPDAGSPTPFPDEAGAFLGLGGGERTEAGGLLASYPPSGRVSLVPWADTGTLGTPQWVPPATQMEPPHYLELLQPPRGSPPHPSSGPLLPLSSGPPPCEARECVNCGATATPLWRRDGTGHYLCNACGLYHRLNGQNRPLIRPKKRLLVSKRAGTVCSNCQTSTTTLWRRSPMGDPVCNACGLYYKLHQVNRPLTMRKDGIQTRNRKVSSKGKKRRPPGGGNPSATAGGGAPMGGGGDPSMPPPPPPPAAAPPQSDALYALGPVVLSGHFLPFGNSGGFFGGGAGGYTAPPGLSPQI | null | null | cell fate commitment [GO:0045165]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944] | 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]; transcription coactivator binding [GO:0001223]; zinc ion binding [GO:0008270] | PF00320; | 3.30.50.10; | null | PTM: Acetylated on Lys-158, Lys-214, Lys-218 and Lys-220 by EP300. Acetylation increases DNA binding and stimulates transcriptional activity. {ECO:0000269|PubMed:9859997}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P15976}. | null | null | null | null | null | FUNCTION: Transcriptional activator or repressor which serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. {ECO:0000250|UniProtKB:P15976}. | Gallus gallus (Chicken) |
P17679 | GATA1_MOUSE | MDFPGLGALGTSEPLPQFVDSALVSSPSDSTGFFSSGPEGLDAASSSTSPNAATAAASALAYYREAEAYRHSPVFQVYPLLNSMEGIPGGSPYASWAYGKTALYPASTVCPSHEDAPSQALEDQEGKSNNTFLDTLKTERLSPDLLTLGTALPASLPVTGSAYGGADFPSPFFSPTGSPLSSAAYSSPKFHGSLPLAPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRMIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYFKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSN... | null | null | animal organ regeneration [GO:0031100]; basophil differentiation [GO:0030221]; bone mineralization [GO:0030282]; cell development [GO:0048468]; cell fate commitment [GO:0045165]; cell population proliferation [GO:0008283]; cell-cell signaling [GO:0007267]; cellular response to cAMP [GO:0071320]; cellular response to fo... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription repressor complex [GO:0017053] | C2H2 zinc finger domain binding [GO:0070742]; chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription f... | PF00320; | 3.30.50.10; | null | PTM: Highly phosphorylated on serine residues. Phosphorylation on Ser-310 is enhanced on erythroid differentiation. Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity). {ECO:0000250}.; PTM: Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16888089}. | null | null | null | null | null | FUNCTION: Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of gene... | Mus musculus (Mouse) |
P17693 | HLAG_HUMAN | MVVMAPRTLFLLLSGALTLTETWAGSHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRFDSDSACPRMEPRAPWVEQEGPEYWEEETRNTKAHAQTDRMNLQTLRGYYNQSEASSHTLQWMIGCDLGSDGRLLRGYEQYAYDGKDYLALNEDLRSWTAADTAAQISKRKCEAANVAEQRRAYLEGTCVEWLHRYLENGKEMLQRADPPKTHVTHHPVFDYEATLRCWALGFYPAEIILTWQRDGEDQTQDVELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLRWKQSSLPTIPIMGIVAGLVVLAA... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; cellular defense response [GO:0006968]; immune response [GO:0006955]; immune response-inhibitin... | cis-Golgi network membrane [GO:0033106]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; filopodium membrane [GO:0031527]; Golgi membrane [GO:0000139]; lumenal side of... | CD8 receptor binding [GO:0042610]; identical protein binding [GO:0042802]; peptide antigen binding [GO:0042605]; protein homodimerization activity [GO:0042803]; signaling receptor binding [GO:0005102] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | MHC class I family | PTM: N-glycosylated. {ECO:0000269|PubMed:11290782}.; PTM: [Soluble HLA class I histocompatibility antigen, alpha chain G]: Produced by proteolytic cleavage at the cell surface (shedding) by matrix metalloproteinase MMP2. {ECO:0000269|PubMed:23737137}. | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:20448110, ECO:0000269|PubMed:7584149}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11520457}. Early endosome membrane {ECO:0000269|PubMed:16366734}.; SUBCELLULAR LOCATION: [Soluble HLA class I ... | null | null | null | null | null | FUNCTION: [Isoform 1]: Non-classical major histocompatibility class Ib molecule involved in immune regulatory processes at the maternal-fetal interface (PubMed:19304799, PubMed:23184984, PubMed:29262349). In complex with B2M/beta-2 microglobulin binds a limited repertoire of nonamer self-peptides derived from intracell... | Homo sapiens (Human) |
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