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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P12478 | NEF_HV1Z2 | MGGRWSKSSIVGWPAIRERIRRTDPAADGVGAVSRDLEKHGAITSSNTRGTNADCAWLEAQEESEEVGFPVRPQVPLRPMTYKGALDLSHFLKEKGG | null | null | virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell perinuclear region of cytoplasm [GO:0044220]; 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 (By similarity). {ECO:0000250}.; PTM: Phosphorylated on serine residues, probably by host PKC. | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Host cytoplasm, host perinuclear region {ECO:0000250}. Virion {ECO:0000250}. Secreted {ECO:0000250}. Note=Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PA... | 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... | Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34) (HIV-1) |
P12479 | NEF_HV1BN | MGGKWSKMAGWSTVRERMRRAEPARERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEDEEVGFPVKPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQQRQDILDLWVYHTQGYFPDWQNYTPGPGVRYPLTFGWCFKLVPVEPEKIEEANEGENNSLLHPMSQHGMDDPEREVLQWRFDSRLAFHHMARELHPEYYKNC | 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... | Human immunodeficiency virus type 1 group M subtype B (isolate BRVA) (HIV-1) |
P12487 | ENV_HV1Z2 | MRVRGIERNCQNLWKWGIMLLGILMTCSNADNLWVTVYYGVPVWKEATTTLFCASDAKSYKTEAHNIWATHACVPTDPNPQEIELENVTENFNMWRNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDEVMENVTMKNNNVTEEIRMKNCSFNITTVVRDKTKQVHALFYRLDIVPIDNDNSTNSTNYRLINCNTSAITQACPKVSFEPIPIHYCAPAGFAILKCRDKRFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEIIIRSENLTNNAKIIIVQLNESVAINCTRPYRNIRQRTSIGLGQALYTTK... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34) (HIV-1) |
P12488 | ENV_HV1BN | MRVKGIKKNYQHLWRWGGMMLLGILMICSATDKLWVTVYYGVPVWKEANTTLFCASDAKAYDTEIHNVWATHACVPTDPNPQELVMGNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCHDFNATNATSNSGKMMEGGEMKNCSFNITTSIRDKMQKEYALFYKLDIVPIDNDKTNTRYRLISCNTSVITQACPKVTFEPIPIHYCAPAGFAILKCNNKKFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSENFTNNVKTIIVQLNESVEINCTRPNNNTRKRITMGPGRVYYTTGQ... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate BRVA) (HIV-1) |
P12489 | ENV_HV1J3 | MRVKGIRKNYQHLWRWGTMLLGILMICSAAEQLWVTVYYGVPVWKEAATTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLENVTEKFNMWKNNMVEQMHEDIISLWDQSLKPCVKLTPLCVTLNCIDWGNDTSPNATNTTSSGGEKMEKGEMKNCSFNITTSIRDKVQKEHALFYKHDVVPINNSTKDNIKNDNSTRYRLISCNTSVITQACPKISFEPIPIHYCAPAGFAIIKCNDKKFNGTGPCTNVSTVQCTHGIKPVVSTQLLLNGSLAEEEVVIRSENFTDNAKTIIVQLKEPVVINCTRPSKTTRRRIH... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polariz... | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20;1.20.5.490; | HIV-1 env protein family | PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic ... | SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-... | null | null | null | null | null | FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like... | Human immunodeficiency virus type 1 group M subtype B (isolate JH32) (HIV-1) |
P12492 | ENV_SIVS4 | MGCLGNQLLIALLLVSVLEICCVQYVTVFYGVPAWKNATIPLFCATKNRDTWGTTQCLPDNDDYSELAINVTEAFDAWDNTVTEQAIEDVWNLFETSIKPCVKLTPLCIAMRCNKTETDRWGLTGNAGTTTTAITTTATPSVAENVINESNPCIKNNSCAGLEQEPMIGCKFNMTGLNRDKKKEYNETWYSRDLICEQSANESESKCYMHHCNTSVIQESCDKHYWDAIRFRYCAPPGYALLRCNDSNYLGFAPNCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGKSNRTIISLNKYYNLTMRCRRPENKTV... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 t... | Simian immunodeficiency virus (isolate F236/smH4) (SIV-sm) (Simian immunodeficiency virus sooty mangabey monkey) |
P12493 | GAG_HV1N5 | MGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000269|PubMed:22334652}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|UniP... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane; Lipid-anchor {ECO:0000269|PubMed:14722309}. Host endosome, host multivesicular body. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve ... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1) |
P12494 | GAG_HV1J3 | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPSLLETSEGCRQILGQLQPSLQTGSEELKSLFNTVATLYCVHQRIEVKDTKEALEKIEEEQNKSKKKAQQAAADTGNSSKVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPAQAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPSSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate JH32) (HIV-1) |
P12495 | GAG_HV1Z2 | MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETSDGCKQIIGQLQPAIRTGSEELRSLFNTVATLYCVHERIEVKDTKEALEKMEEEQNKSKNKKAQQAAADAGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIAWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKGWMTE... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF19317;PF08705;PF00098; | 1.10.1200.30;6.10.250.390;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34) (HIV-1) |
P12496 | GAG_SIVS4 | MGARNSVLSGKEADELEKVRLRPNGKKKYMLKHVVWAANELDRFGLAESLLDNKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVVETGTADRMPATSRPTAPPSGRGGNYPVQQVGGNYVHLPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGEHQAAMQIIREIINEEAADWDLQHPQPGPLPAGQLREPRGSDIAGTTSTVDEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Capsid protein p24 is phosphorylated. {ECO:0000250}.; PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding, this process is termed maturation (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | null | null | null | null | null | FUNCTION: Matrix protein p17 targets Gag and Gag-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex. Implicated in the release from host cell mediated by Vpu (By similarity). {EC... | Simian immunodeficiency virus (isolate F236/smH4) (SIV-sm) (Simian immunodeficiency virus sooty mangabey monkey) |
P12497 | POL_HV1N5 | MGARASVLSGGELDKWEKIRLRPGGKKQYKLKHIVWASRELERFAVNPGLLETSEGCRQILGQLQPSLQTGSEELRSLYNTIAVLYCVHQRIDVKDTKEALDKIEEEQNKSKKKAQQAAADTGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTHNPPIPVGEIYKRWIILGLNKIVRMYSPTSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor {ECO:0000269|PubMed:19297499}. Host endosome, host multivesicular body {ECO:0000269|PubMed:19297499}. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosoma... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1) |
P12498 | POL_HV1J3 | MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHIVWASRELERFAVNPSLLETSEGCRQILGQLQPSLQTGSEELKSLFNTVATLYCVHQRIEVKDTKEALEKIEEEQNKSKKKAQQAAADTGNSSKVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPAQAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPSSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTET... | 3.4.23.16 | null | proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral process [GO:0016032] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; lipid binding [GO:0008289]; RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00077;PF00098; | 1.10.1200.30;2.40.70.10;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | null | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. Nucleocapsid p... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype B (isolate JH32) (HIV-1) |
P12499 | POL_HV1Z2 | MGARASVLSGGKLDAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETSDGCKQIIGQLQPAIRTGSEELRSLFNTVATLYCVHERIEVKDTKEALEKMEEEQNKSKNKKAQQAAADAGNNSQVSQNYPIVQNLQGQMVHQAISPRTLNAWVKVIEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPVHAGPIAPGQMREPRGSDIAGTTSTLQEQIAWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKGWMTE... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34) (HIV-1) |
P12502 | POL_SIVS4 | MGARNSVLSGKEADELEKVRLRPNGKKKYMLKHVVWAANELDRFGLAESLLDNKEGCQKILSVLAPLVPTGSENLKSLYNTVCVIWCIHAEEKVKHTEEAKQIVQRHLVVETGTADRMPATSRPTAPPSGRGGNYPVQQVGGNYVHLPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGEHQAAMQIIREIINEEAADWDLQHPQPGPLPAGQLREPRGSDIAGTTSTVDEQIQWMYRQQNPIPVGNIYRRWIQLGLQKCVRMYNPTNILDVKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.16 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; structural mo... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT subunit. {ECO:0000255|P... | SUBCELLULAR LOCATION: [Matrix protein p17]: Virion {ECO:0000305}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Following virus entry, the nuclear localization signal (NLS) of the matrix protein participates with Vpr to the nuclear localizat... | CATALYTIC ACTIVITY: Reaction=Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.; EC=3.4.23.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RN... | null | null | null | null | FUNCTION: Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shut off translation (By similarity). {ECO:000... | Simian immunodeficiency virus (isolate F236/smH4) (SIV-sm) (Simian immunodeficiency virus sooty mangabey monkey) |
P12504 | VIF_HV1N5 | MENRWQVMIVWQVDRMRINTWKRLVKHHMYISRKAKDWFYRHHYESTNPKISSEVHIPLGDAKLVITTYWGLHTGERDWHLGQGVSIEWRKKRYSTQVDPDLADQLIHLHYFDCFSESAIRNTILGRIVSPRCEYQAGHNKVGSLQYLALAALIKPKQIKPPLPSVRKLTEDRWNKPQKTKGHRGSHTMNGH | null | null | viral life cycle [GO:0019058] | host cell cytoplasm [GO:0030430]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | RNA binding [GO:0003723] | PF00559; | null | Primate lentivirus group Vif protein family | PTM: Highly phosphorylated on serine and threonine residues. Thr-96 and Ser-165 are phosphorylated by the mitogen activated kinase MAP4K1. As the HIV-1 replication can be activated by stress and mitogens, these phosphorylations could be involved in this process. Ser-144 phosphorylation may inhibit elongin BC complex bi... | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04081}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04081}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04081}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04081}. Virion {ECO:0000255|HAMAP-Rule:MF_04081}. Note=In the cytoplasm, seems to coloc... | null | null | null | null | null | FUNCTION: Counteracts the innate antiviral activity of host APOBEC3F and APOBEC3G. Forms a complex with host APOBEC3F and APOBEC3G thus preventing the entry of these lethally hypermutating enzymes into progeny virions. Recruits an active E3 ubiquitin ligase complex composed of elongin BC, CUL5, and RBX2 to induce polyu... | Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1) |
P12506 | TAT_HV1Z2 | MDPVDPNIEPWNHPGSQPKTACNRCHCKKCCYHCQVCFITKGLGISYGRKKRRQRRRPSQGGQTHQDPIPKQPSSQPRGDPTGPKE | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; regulatory region RNA binding [GO:0001069]; RNA-binding transcription regulator activity [GO:0001070]; trans-acti... | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34) (HIV-1) |
P12520 | VPR_HV1N5 | MEQAPEDQGPQREPYNEWTLELLEELKSEAVRHFPRIWLHNLGQHIYETYGDTWAGVEAIIRILQQLLFIHFRIGCRHSRIGVTRQRRARNGASRS | null | null | cell cycle [GO:0007049]; DNA-templated transcription [GO:0006351]; monoatomic ion transmembrane transport [GO:0034220]; protein homooligomerization [GO:0051260]; regulation of DNA-templated transcription [GO:0006355]; symbiont entry into host cell [GO:0046718]; symbiont-mediated arrest of host cell cycle during G2/M tr... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host extracellular space [GO:0043655]; virion component [GO:0044423] | null | PF00522; | 6.10.210.10;1.20.5.90; | HIV-1 VPR protein family | PTM: Phosphorylated on several residues by host. These phosphorylations regulate VPR activity for the nuclear import of the HIV-1 pre-integration complex. {ECO:0000255|HAMAP-Rule:MF_04080}. | SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04080}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04080}. Host extracellular space {ECO:0000255|HAMAP-Rule:MF_04080}. Note=Incorporation into virion is dependent on p6 GAG sequences. Lacks a canonical nuclear localization signal, thus import into nucleus may functio... | null | null | null | null | null | FUNCTION: During virus replication, may deplete host UNG protein, and incude G2-M cell cycle arrest. Acts by targeting specific host proteins for degradation by the 26S proteasome, through association with the cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host VPRPB/DCAF-1. Cell cycle arrest reported... | Human immunodeficiency virus type 1 group M subtype B (isolate NY5) (HIV-1) |
P12524 | MYCL_HUMAN | MDYDSYQHYFYDYDCGEDFYRSTAPSEDIWKKFELVPSPPTSPPWGLGPGAGDPAPGIGPPEPWPGGCTGDEAESRGHSKGWGRNYASIIRRDCMWSGFSARERLERAVSDRLAPGAPRGNPPKASAAPDCTPSLEAGNPAPAAPCPLGEPKTQACSGSESPSDSENEEIDVVTVEKRQSLGIRKPVTITVRADPLDPCMKHFHISIHQQQHNYAARFPPESCSQEEASERGPQEEVLERDAAGEKEDEEDEEIVSPPPVESEAAQSCHPKPVSSDTEDVTKRKNHNFLERKRRNDLRSRFLALRDQVPTLASCSKAPKV... | null | null | regulation of inner ear auditory receptor cell differentiation [GO:0045607]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; chromosome [GO:0005694]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00010;PF01056; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:2548855}. | null | null | null | null | null | null | Homo sapiens (Human) |
P12526 | MAS_RAT | MDQSNMTSFAEEKAMNTSSRNASLGTSHPPIPIVHWVIMSISPLGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKHQSAFVCALLWALSCLVTTMEYVMCIDSGEESHSQSDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRVLYLLYYEYWSTFGNLHNISLLFSTINSSANPFIYFFVGSSKKKRFRESLKVVLTRAFKDEMQPRRQEGNGNTVSI... | null | null | cellular response to peptide hormone stimulus [GO:0071375]; G protein-coupled receptor signaling pathway [GO:0007186]; hippocampus development [GO:0021766]; male gonad development [GO:0008584]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of canonical NF-kappaB signal transduction [G... | cell surface [GO:0009986]; plasma membrane [GO:0005886] | angiotensin receptor activity [GO:0001595]; G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for angiotensin 1-7 (By similarity). Acts specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 receptor), although it up-regulates AGTR1 receptor levels. Positive regulation of AGTR1 levels occurs through activation of the G-proteins GNA11 and GNAQ, and stimulation of the protein ki... | Rattus norvegicus (Rat) |
P12527 | LOX5_RAT | MPSYTVTVATGSQWFAGTDDYIYLSLIGSAGCSEKHLLDKAFYNDFERGGRDSYDVTVDEELGEIYLVKIEKRKYRLHDDWYLKYITLKTPHDYIEFPCYRWITGEGEIVLRDGCAKLARDDQIHILKQHRRKELETRQKQYRWMEWNPGFPLSIDAKCHKDLPRDIQFDSEKGVDFVLNYSKAMENLFINRFMHMFQSSWHDFADFEKIFVKISNTISERVKNHWQEDLMFGYQFLNGCNPVLIKRCTELPKKLPVTTEMVECSLERQLSLEQEVQEGNIFIVDYELLDGIDANKTDPCTHQFLAAPICLLYKNLANKI... | 1.13.11.-; 1.13.11.34 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P09917, ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:P09917, ECO:0000255|PROSITE-ProRule:PRU00726}; | arachidonic acid metabolic process [GO:0019369]; dendritic cell migration [GO:0036336]; glucose homeostasis [GO:0042593]; hepoxilin biosynthetic process [GO:0051122]; humoral immune response [GO:0006959]; inflammatory response [GO:0006954]; leukocyte chemotaxis involved in inflammatory response [GO:0002232]; leukocyte ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; nuclear envelope [GO:0005635]; nuclear envelope lumen [GO:0005641]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383] | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 5-lipoxygenase activity [GO:0004051]; arachidonate 8(S)-lipoxygenase activity [GO:0036403]; hydrolase activity [GO:0016787]; iron ion binding [GO:0005506] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | PTM: Serine phosphorylation by MAPKAPK2 is stimulated by arachidonic acid. Phosphorylation on Ser-523 by PKA has an inhibitory effect. Phosphorylation on Ser-271 prevents export from the nucleus. Phosphorylation at Ser-523 is stimulated by 8-bromo-3',5'-cyclic AMP or prostaglandin E2. {ECO:0000250|UniProtKB:P09917}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P09917, ECO:0000250|UniProtKB:P48999}. Nucleus matrix {ECO:0000250|UniProtKB:P09917}. Nucleus membrane {ECO:0000250|UniProtKB:P09917}; Peripheral membrane protein {ECO:0000250|UniProtKB:P09917}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P09917}. Cytoplas... | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = H2O + leukotriene A4; Xref=Rhea:RHEA:32307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57463; EC=1.13.11.34; Evidence={ECO:0000250|UniProtKB:P09917}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32308; Evidence={ECO:... | null | PATHWAY: Lipid metabolism; leukotriene A4 biosynthesis. {ECO:0000250|UniProtKB:P09917}. | null | null | FUNCTION: Catalyzes the oxygenation of arachidonate to 5-hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation. Also catalyzes the oxygenation of arachid... | Rattus norvegicus (Rat) |
P12528 | FIBER_BPP22 | MTDITANVVVSNPRPIFTESRSFKAVANGKIYIGQIDTDPVNPANQIPVYIENEDGSHVQITQPLIINAAGKIVYNGQLVKIVTVQGHSMAIYDANGSQVDYIANVLKYDPDQYSIEADKKFKYSVKLSDYPTLQDAASAAVDGLLIDRDYNFYGGETVDFGGKVLTIECKAKFIGDGNLIFTKLGKGSRIAGVFMESTTTPWVIKPWTDDNQWLTDAAAVVATLKQSKTDGYQPTVSDYVKFPGIETLLPPNAKGQNITSTLEIRECIGVEVHRASGLMAGFLFRGCHFCKMVDANNPSGGKDGIITFENLSGDWGKGN... | 3.2.1.- | null | adhesion receptor-mediated virion attachment to host cell [GO:0098671]; metabolic process [GO:0008152]; symbiont entry into host [GO:0044409]; symbiont entry into host cell via disruption of host cell envelope [GO:0098994]; symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide [GO:009899... | virus tail, fiber [GO:0098024] | endo-1,3-alpha-L-rhamnosidase activity [GO:0052775] | PF09008;PF09251; | 2.160.20.20;2.170.14.10; | P22likevirus tail fiber protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. | null | null | null | null | null | FUNCTION: Structural component of the short non-contractile tail. The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polys... | Salmonella phage P22 (Bacteriophage P22) |
P12530 | LOX15_RABIT | MGVYRVCVSTGASIYAGSKNKVELWLVGQHGEVELGSCLRPTRNKEEEFKVNVSKYLGSLLFVRLRKKHFLKEDAWFCNWISVQALGAAEDKYWFPCYRWVVGDGVQSLPVGTGCTTVGDPQGLFQKHREQELEERRKLYQWGSWKEGLILNVAGSKLTDLPVDERFLEDKKIDFEASLAWGLAELALKNSLNILAPWKTLDDFNRIFWCGRSKLARRVRDSWQEDSLFGYQFLNGANPMLLRRSVQLPARLVFPPGMEELQAQLEKELKAGTLFEADFALLDNIKANVILYCQQYLAAPLVMLKLQPDGKLMPMVIQLH... | 1.13.11.-; 1.13.11.12; 1.13.11.31; 1.13.11.33 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P16469, ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:P16469, ECO:0000255|PROSITE-ProRule:PRU00726}; | apoptotic cell clearance [GO:0043277]; arachidonic acid metabolic process [GO:0019369]; bone mineralization [GO:0030282]; cellular response to calcium ion [GO:0071277]; cellular response to interleukin-13 [GO:0035963]; fatty acid oxidation [GO:0019395]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabol... | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; plasma membrane [GO:0005886] | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9414270}. Cell membrane {ECO:0000269|PubMed:9414270}; Peripheral membrane protein {ECO:0000269|PubMed:9414270}. Lipid droplet {ECO:0000250|UniProtKB:P16050}. Note=Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates from t... | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444; EC=1.13.11.31; Evidence={ECO:0000269|PubMed:9600854}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10429; Evid... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:17493578}; KM=49 uM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine {ECO:0000269|PubMed:17493578}; KM=98 uM for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine {ECO:0000269|PubMed:17493578}; KM=48 uM for N-(... | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:9600854}. | null | null | FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators (PubMed:15123652, PubMed:17493578, PubMed:18311922, PubMed:9414270, PubMed:9600854). It inserts peroxyl groups at C12 or C1... | Oryctolagus cuniculus (Rabbit) |
P12531 | TOP2_TRYBB | MAEAHKYKKLTPIEHVLTRPEMYIGSLDTTATPMFIYDEQKGHMVWETVKLNHGLLKIVDEILLNASDNISNRSARMTYIRVTITDTGEITIENDGAGIPIVRSREHKLYIPEMVFGHLLTSSNYDDDNQNAVAGRHGYGAKLTNILSLSFSVCCRTNGREFHMSWQDHMRKATAPRVSNVGTKEKNVTRVKFLPDYERFGMKEKKISNDMKRVLYKRIMDLSAMFPNIQITLNGSSFGFKSFKDYATLYSAMTPKGEKPPPPYVYESKSGCVAFIPSVVPGVRRMFGVVNGVVTYNGGTHCNAAQDILTGCLDGVEREL... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Note=Binds two Mg(2+) per subunit. The magnesium ion... | DNA topological change [GO:0006265]; resolution of meiotic recombination intermediates [GO:0000712]; sister chromatid segregation [GO:0000819] | kinetoplast [GO:0020023]; nucleus [GO:0005634] | ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; metal ion binding [GO:0046872] | PF00204;PF00521;PF01751;PF16898; | 3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10; | Type II topoisomerase family | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; | null | null | null | null | FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. | Trypanosoma brucei brucei |
P12532 | KCRU_HUMAN | MAGPFSRLLSARPGLRLLALAGAGSLAAGFLLRPEPVRAASERRRLYPPSAEYPDLRKHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFADLFDPVIQERHNGYDPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEVERLIQERGWEFMWNERLGYILTCPSNL... | 2.7.3.2 | null | 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) |
P12544 | GRAA_HUMAN | MRNSYRFLASSLSVVVSLLLIPEDVCEKIIGGNEVTPHSRPYMVLLSLDRKTICAGALIAKDWVLTAAHCNLNKRSQVILGAHSITREEPTKQIMLVKKEFPYPCYDPATREGDLKLLQLMEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDRNHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCEGVFRGVTSFGLENKCGDPRGPGVYILLSKKHLNWIIMTIKGAV | 3.4.21.78 | null | apoptotic process [GO:0006915]; cytotoxic T cell pyroptotic process [GO:1902483]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; immune response [GO:0006955]; killing of cells of another organism [GO:0031640]; negative regulation of DNA binding [GO:0043392]; negative regulation of endodeoxyribo... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; immunological synapse [GO:0001772]; nucleus [GO:0005634] | protein homodimerization activity [GO:0042803]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Granzyme subfamily | null | SUBCELLULAR LOCATION: [Isoform alpha]: Secreted {ECO:0000269|PubMed:3257574}. Cytoplasmic granule {ECO:0000269|PubMed:3257574}. Note=Delivered into the target cell by perforin. {ECO:0000269|PubMed:20038786, ECO:0000269|PubMed:32299851}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-Xaa-, -Lys-|-Xaa- >> -Phe-|-Xaa- in small molecule substrates.; EC=3.4.21.78; Evidence={ECO:0000269|PubMed:12819770, ECO:0000269|PubMed:32299851, ECO:0000269|PubMed:34022140, ECO:000... | null | null | null | null | FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:12819770, PubMed:32299851, PubMed:3257574, PubMed:3262682, PubMed:3263427). It cleaves after Lys or Arg (Pu... | Homo sapiens (Human) |
P12545 | PLMN_MACMU | MEHKEVVLLLLLFLKSGQGEPLDDYVNTKGASLFSITKKQLGAGSIEECAAKCEEEEEFTCRSFQYHSKEQQCVIMAENRKSSIVFRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTRTGITCQKWSSTSPHRPTFSPATHPSEGLEENYCRNPDNDGQGPWCYTTDPEERFDYCDIPECEDECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDGEPRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGDVAVTVSGHTCHGWSAQTPHTHNRTPENFPCKNLD... | 3.4.21.7 | null | blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]; proteolysis [GO:0006508]; tissue remodeling [GO:0048771] | extracellular space [GO:0005615] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102] | PF00051;PF00024;PF00089; | 3.50.4.10;2.40.20.10;2.40.10.10; | Peptidase S1 family, Plasminogen subfamily | PTM: In the presence of the inhibitor, the activation involves only cleavage after Arg-580, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.; EC=3.4.21.7; | null | null | null | null | FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, co... | Macaca mulatta (Rhesus macaque) |
P12547 | ORYZ_ASPOR | MQSIKRTLLLLGAILPAVLGAPVQETRRAAEKLPGKYIVTFKPGIDEAKIQEHTTWATNIHQRSLERRGATGGDLPVGIERNYKINKFAAYAGSFDDATIEEIRKNEDVAYVEEDQIYYLDGLTTQKSAPWGLGSISHKGQQSTDYIYDTSAGEGTYAYVVDSGVNVDHEEFEGRASKAYNAAGGQHVDSIGHGTHVSGTIAGKTYGIAKKASILSVKVFQGESSSTSVILDGFNWAANDIVSKKRTSKAAINMSLGGGYSKAFNDAVENAFEQGVLSVVAAGNENSDAGQTSPASAPDAITVAAIQKSNNRASFSNFGK... | 3.4.21.63 | null | proteolysis [GO:0006508] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF05922;PF00082; | 3.30.70.80;3.40.50.200; | Peptidase S8 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.; EC=3.4.21.63; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:18226921}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:18226921}; | FUNCTION: Secreted alkaline protease that allows assimilation of proteinaceous substrates. {ECO:0000269|PubMed:18226921}. | Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
P12568 | FUS_HRSV | MELPILKANAITTILAAVTFCFASSQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLINQELDKYKNAVTELQLLMQSTTAANNRARRELPRFMNYTLNNTKKTNVTLSKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCRISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSP... | null | null | entry receptor-mediated virion attachment to host cell [GO:0098670]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of syncytium formation by virus [GO:0060141]; symbiont entry into host cell [GO:0046718] | host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00523; | 1.10.287.2480;6.10.250.1160;6.20.370.50; | Paramyxoviruses fusion glycoprotein family | PTM: [Fusion glycoprotein F0]: The F glycoprotein is synthesized as a F0 inactive precursor that is heavily N-glycosylated and processed at two sites by a host furin-like protease probably in the Golgi. The cleavage site between p27 and F1 may occur after endocytosis to yield the mature F1 and F2 proteins. Both cleavag... | SUBCELLULAR LOCATION: [Fusion glycoprotein F0]: Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P03420}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03420}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane {ECO:0000250|UniProtKB:P03420}; Single-pass type I membrane protein {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: [Fusion glycoprotein F0]: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins. {ECO:0000250|UniProtKB:P03420}.; FUNCTION: [Fusion glycoprotein F1]: Class I viral fusion protein. Under the current model, the protein has at least 3 c... | Human respiratory syncytial virus |
P12576 | L_MEASE | MDSLSVNQILYPEVHLDSPIVTNKIVAILEYARVPHAYSLEDPTLCQNIKHRLKNGFSNQMIINNVEVGNVIKSKLRSYPAHSHIPYPNCNQDLFNIEDKESTRKIRELLKKGNSLYSKVSDKVFQCLRDTNSRLGLGSELREDIKEKVINLGVYMHSSQWFEPFLFWFTVKTEMRSVIKSQTHTCHRRRHTPVFFTGSSVELLISRDLVAIISKESQHVYYLTFELVLMYCDVIEGRLMTETAMTIDARYTELLGRVRYMWKLIDGFFPALGNPTYQIVAMLEPLSLAYLQLRDITVELRGAFLNHCFTEIHDVLDQNG... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | null | host cell cytoplasm [GO:0030430]; viral nucleocapsid [GO:0019013] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF14318;PF00946; | 3.40.50.150; | Paramyxovirus L protein family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm {ECO:0000250}. | 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=a 5'-end... | null | null | null | null | FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all vir... | Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis virus) |
P12606 | ITB1A_XENLA | MAHYPVFTVGLLTCLVLCINAQQGGTECLKANAKSCGECIQAGPNCGWCTKVDFLQEGEPTSARCDDLAALKSKGCPEDDIQNPRGRKQKLKDIPITSKGKGERMDPANITQLRPQQMVFELRSGEPQTFNLTFRRAEDYPIDLYYLMDLSFSMKDDLENVKSLGTALMTEMEKITSDFRIGFGSFVEKTVMPYISTTPAKLINPCTSDQNCTSPFSYKNVLNLTKDGKLFNDLVGKQQISGNLDSPEGGFDAIMQVAVCGEQIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGKCHLHENMYTMSHYYDYPSIAH... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520] | cell surface [GO:0009986]; cleavage furrow [GO:0032154]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; ruffle membrane [GO:0032587] | C-X3-C chemokine binding [GO:0019960]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; laminin binding [GO:0043236]; metal ion binding [GO:0046872] | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass ty... | null | null | null | null | null | FUNCTION: Beta integrins associate with alpha subunits to form receptor complexes that recognize the sequence R-G-D in a wide array of ligands. May be involved in osteoblast compaction (By similarity). May play role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). {ECO:0000250|UniProtK... | Xenopus laevis (African clawed frog) |
P12607 | ITB1B_XENLA | MARYPVFTFVFLICLVLCTNAQQGGTECLKANAKSCGECIQAGPNCGWCTKVDFLQEGEPTSARCDDLAALKTKGCPEDDIQNPRGRKQKLKDIPITSKGKGERMDPANITQLRPQQLVFELRSGEPQTFNLTFRRAEDYPIDLYYLMDLSFSMKDDLENVKSLGTALMTEMEKITSDFRIGFGSFVEKTVMPYISTTPAKLLNPCTNDQNCTSPFSYKNVLNLTKDGKLFNDLVGKQQISGNLDSPEGGFDAIMQVAVCGEQIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGRCHLHGNMYTMSHYYDYPSIAH... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520] | cell surface [GO:0009986]; cleavage furrow [GO:0032154]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; ruffle membrane [GO:0032587] | C-X3-C chemokine binding [GO:0019960]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; laminin binding [GO:0043236]; metal ion binding [GO:0046872] | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass ty... | null | null | null | null | null | FUNCTION: Beta integrins associate with alpha subunits to form receptor complexes that recognize the sequence R-G-D in a wide array of ligands. May be involved in osteoblast compaction (By similarity). May play role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). {ECO:0000250|UniProtK... | Xenopus laevis (African clawed frog) |
P12611 | WHI2_YEAST | MDDIITQVSPDNAESAPILQEQQQQQNSQYEGNEEDYGDSLIHLNIQENHYFITRDQLMSLPESLLLCLFPSGVFLDRCGQVITNLTRDDEVYIVNFPPDCFEYIMEIYTKAHDDLYNHPVEKFFDRPSSSFVSNAKGFFGLSSNNSISSNNEQDILHQKPAIIVLREDLDYYCVPQEEFQFDSTNEENNEDLLRHFMAQVKMAAGSYLTSKTSIFQGLYSSNRLKQQQQQQKIEKGSNSSSNTKSTSKKLGPAEQHLMDMLCSSGFTKETCWGNRTQETGKTVISSLSLCRLANETTEGFRQKFNEAKAKWEAEHKPSQ... | null | null | actin filament organization [GO:0007015]; cell cycle [GO:0007049]; endocytosis [GO:0006897]; mitophagy [GO:0000423]; negative regulation of TORC1 signaling [GO:1904262]; positive regulation of G1 to G0 transition [GO:1903452]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by ... | cell periphery [GO:0071944]; nucleus [GO:0005634]; phosphatase complex [GO:1903293] | protein phosphatase binding [GO:0019903]; RNA binding [GO:0003723] | null | null | WHI2 family | null | null | null | null | null | null | null | FUNCTION: Plays a role in the coordination of growth and proliferation. Required for entry into G0 phase under conditions of carbon limitation. Involved in the general stress response; acts together with PSR1 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12624 | MARCS_BOVIN | MGAQFSKTAAKGEATAERPGEAAVASSPSKANGQENGHVKVNGDASPAAAEPGAKEELQANGSAPAADKEEPAAAGSGAASPAAAEKDEPAAAAPDAGASPVEKEAPVEGEAAEPGSPTAAEGEAASAASSTSSPKAEDGATPSPSNETPKKKKKRFSFKKSFKLSGFSFKKNKKEAGEGGEAEGAAGASAEGGKDEASGGAAAAAGEAGAAPGEPTAAPGEEAAAGEEGAAGGDPQEAKPEEAAVAPEKPPASEEAKAVEEPSKAEEKAEEAGVSAAGCEAPSAAGPGVPPEQEAAPAEEAAAAPASSACAAPSQEAQP... | null | null | actin crosslink formation [GO:0051764]; actin filament bundle assembly [GO:0051017]; actin filament organization [GO:0007015]; apoptotic process [GO:0006915]; central nervous system development [GO:0007417]; mitochondrion organization [GO:0007005]; neural tube development [GO:0021915]; neurogenesis [GO:0022008]; respon... | actin filament bundle [GO:0032432]; cell cortex [GO:0005938]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; germinal vesicle [GO:0042585]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; calmodulin binding [GO:0005516]; identical protein binding [GO:0042802]; protein kinase C binding [GO:0005080] | PF02063; | null | MARCKS family | PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It also inhibits the F-actin cross-linking activity. {ECO:0000269|PubMed:2473066, ECO:0000269|PubMed:8034575}.; PTM: Myristoylated. A proper myristoylation is essential for the proper distribution to the plasma membrane. {ECO:0000269|PubMed:8034575}.; PTM:... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8463217}; Lipid-anchor {ECO:0000269|PubMed:8463217}. Cytoplasm {ECO:0000269|PubMed:8463217}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P29966}. Note=PKC-dependent phosphorylation displaces MARCKS from the cell membrane and subsequent dephosphorylation is acco... | null | null | null | null | null | FUNCTION: Membrane-associated protein that plays a role in the structural modulation of the actin cytoskeleton, chemotaxis, motility, cell adhesion, phagocytosis, and exocytosis through lipid sequestering and/or protein docking to membranes. Thus, exerts an influence on a plethora of physiological processes, such as em... | Bos taurus (Bovine) |
P12630 | BAR1_YEAST | MSAINHLCLKLILASFAIINTITALTNDGTGHLEFLLQHEEEMYYATTLDIGTPSQSLTVLFDTGSADFWVMDSSNPFCLPNSNTSSYSNATYNGEEVKPSIDCRSMSTYNEHRSSTYQYLENGRFYITYADGTFADGSWGTETVSINGIDIPNIQFGVAKYATTPVSGVLGIGFPRRESVKGYEGAPNEYYPNFPQILKSEKIIDVVAYSLFLNSPDSGTGSIVFGAIDESKFSGDLFTFPMVNEYPTIVDAPATLAMTIQGLGAQNKSSCEHETFTTTKYPVLLDSGTSLLNAPKVIADKMASFVNASYSEEEGIYIL... | 3.4.23.35 | null | cellular response to pheromone [GO:0071444]; fungal-type cell wall organization [GO:0031505]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cell periphery [GO:0071944]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277] | aspartic-type endopeptidase activity [GO:0004190] | PF00026; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of 6-Leu-|-Lys-7 bond in the pheromone alpha-mating factor.; EC=3.4.23.35; | null | null | null | null | FUNCTION: This protein called 'barrier activity' is excreted by yeast cells mating type a. It is probably a protease that cleaves alpha-factor and thus acts as an antagonist of this mating pheromone and establishes optimal pheromone concentration for conjugation. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12635 | MBHS_BRADU | MGAATETFYSVIRRQGITRRSFHKFCSLTATSLGLGPLAASRIANALETKPRVPVIWMHGLECTCCSESFIRSAHPLVKDAVLSMISLDYDDTIMAAAGHQAEAILEETRAKHKGQYILAVEGNPPLNEGGMFCIDGGKPFVEKLKMMAEDAMAIIAWGACASWGCVQAAKPNPTQATPIDKVITNKPIIKVPGCPPIAEVMTGVVTFITTFGKLPELDRQGRPKMFYSQRIHDKCYRRPHFDAGQFVEEWDDEAARKGYCLYKMGCKGPTTYNACSTVRWNGGVSFPIQSGHGCIGCSEDGFWDKGSFYDRLTNIKQFG... | 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]; membrane [GO:0016020]; 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. | Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) |
P12637 | CASQ2_CANLF | MKRTHLFIAGLYLLASCRAEEGLNFPTYDGKDRVVSLTEKNFKQVLKKYDVLCLYYHESVSSDKVAQKQFQLKEIVLELVAQVLEHKDIGFVMVDAKKEAKLAKKLGFDEEGSLYVLKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIINSKLEVQAFERIEDQIKLIGFFKSEESEYYKAFEEAAEHFQPYIKFFATFDKGVAKKLSLKMNEVDFYEPFMDEPIAIPDKPYTEEELVEFVKEHQRPTLRRLRPEDMFETWEDDLNGIHIVAFAERSDPDGYEFLEILKQVARDNTDNPDLSIVWIDPDDFPLLVAYWEK... | null | null | negative regulation of ryanodine-sensitive calcium-release channel activity [GO:0060315]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]; regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0010880] | sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018]; Z disc [GO:0030018] | calcium ion binding [GO:0005509] | PF01216; | 3.40.30.10; | Calsequestrin family | PTM: Phosphorylation in the C-terminus, probably by CK2, moderately increases calcium buffering capacity. {ECO:0000250|UniProtKB:O14958}.; PTM: N-glycosylated. {ECO:0000269|PubMed:20302875, ECO:0000269|PubMed:21431367}. | SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:O09161}. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells. {ECO:0000250|UniProtKB:O09161}. | null | null | null | null | null | FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle (PubMed:3427023). Calcium ions are bound by clusters of acidic residues at the protein surface, especially at the interface between subunits. Can bind around 60 Ca(2+) ions. Regula... | Canis lupus familiaris (Dog) (Canis familiaris) |
P12643 | BMP2_HUMAN | MVAGTRCLLALLLPQVLLGGAAGLVPELGRRKFAAASSGRPSSQPSDEVLSEFELRLLSMFGLKQRPTPSRDAVVPPYMLDLYRRHSGQPGSPAPDHRLERAASRANTVRSFHHEESLEELPETSGKTTRRFFFNLSSIPTEEFITSAELQVFREQMQDALGNNSSFHHRINIYEIIKPATANSKFPVTRLLDTRLVNQNASRWESFDVTPAVMRWTAQGHANHGFVVEVAHLEEKQGVSKRHVRISRSLHQDEHSWSQIRPLLVTFGHDGKGHPLHKREKRQAKHKQRKRLKSSCKRHPLYVDFSDVGWNDWIVAPPGY... | null | null | ameloblast differentiation [GO:0036305]; animal organ morphogenesis [GO:0009887]; aortic valve development [GO:0003176]; astrocyte differentiation [GO:0048708]; atrioventricular canal morphogenesis [GO:1905222]; atrioventricular valve morphogenesis [GO:0003181]; BMP signaling pathway [GO:0030509]; bone development [GO:... | BMP receptor complex [GO:0070724]; cell surface [GO:0009986]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231] | BMP receptor binding [GO:0070700]; co-receptor binding [GO:0039706]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; phosphatase activator activity [GO:0019211]; protein serine/threonine kinase activator activity [GO:0043539]; signaling receptor binding [GO:0005102] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis (PubMed:18436533, PubMed:24362451, PubMed:31019025). Induces cartilage and bone formation (PubMed:3201241). Initiates the canonical BMP signaling cascad... | Homo sapiens (Human) |
P12644 | BMP4_HUMAN | MIPGNRMLMVVLLCQVLLGGASHASLIPETGKKKVAEIQGHAGGRRSGQSHELLRDFEATLLQMFGLRRRPQPSKSAVIPDYMRDLYRLQSGEEEEEQIHSTGLEYPERPASRANTVRSFHHEEHLENIPGTSENSAFRFLFNLSSIPENEVISSAELRLFREQVDQGPDWERGFHRINIYEVMKPPAEVVPGHLITRLLDTRLVHHNVTRWETFDVSPAVLRWTREKQPNYGLAIEVTHLHQTRTHQGQHVRISRSLPQGSGNWAQLRPLLVTFGHDGRGHALTRRRRAKRSPKHHSQRARKKNKNCRRHSLYVDFSDV... | null | null | ameloblast differentiation [GO:0036305]; anterior/posterior axis specification [GO:0009948]; aortic valve morphogenesis [GO:0003180]; blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; BMP signaling pathway [GO:0030509]; branching involved in prostate gland morphogenesis [GO:00... | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | BMP receptor binding [GO:0070700]; chemoattractant activity [GO:0042056]; co-receptor binding [GO:0039706]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix. | null | null | null | null | null | FUNCTION: Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including neurogenesis, vascular development, angiogenesis and osteogenesis (PubMed:31363885). Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibi... | Homo sapiens (Human) |
P12645 | BMP3_HUMAN | MAGASRLLFLWLGCFCVSLAQGERPKPPFPELRKAVPGDRTAGGGPDSELQPQDKVSEHMLRLYDRYSTVQAARTPGSLEGGSQPWRPRLLREGNTVRSFRAAAAETLERKGLYIFNLTSLTKSENILSATLYFCIGELGNISLSCPVSGGCSHHAQRKHIQIDLSAWTLKFSRNQSQLLGHLSVDMAKSHRDIMSWLSKDITQLLRKAKENEEFLIGFNITSKGRQLPKRRLPFPEPYILVYANDAAISEPESVVSSLQGHRNFPTGTVPKWDSHIRAALSIERRKKRSTGVLLPLQNNELPGAEYQYKKDEVWEERKP... | null | null | cartilage development [GO:0051216]; cell-cell signaling [GO:0007267]; osteoblast differentiation [GO:0001649]; skeletal system development [GO:0001501] | extracellular exosome [GO:0070062]; extracellular space [GO:0005615] | BMP receptor binding [GO:0070700]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; signaling receptor binding [GO:0005102] | PF00019; | 2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Growth factor of the TGF-beta superfamily that plays an essential role in developmental process by inducing and patterning early skeletal formation and by negatively regulating bone density. Antagonizes the ability of certain osteogenic BMPs to induce osteoprogenitor differentiation and ossification (PubMed:1... | Homo sapiens (Human) |
P12646 | G6PD_DROME | MATQKEDHTALDLIIKSLKSPTMVCEGTHFDGKIPHTFVIFGASGDLAKKKIYPTLWWLYRDDLLPKPTKFCGYARSMLTVDSIKEQCLPYMKVQPHEQKKYEEFWALNEYVSGRYDGRTGFELLNQQLEIMENKNKANRIFYLALPPSVFEEVTVNIKQICMSVCGWNRVIIEKPFGRDDASSQALSDHLAGLFQEDQLYRIDHYLGKEMVQNLMTIRFGNKILSSTWNRENIASVLITFKEPFGTQGRGGYFDEFGIIRDVMQNHLLQILSLVAMEKPVSCHPDDIRDEKVKVLKSIEALTLDDMVLGQYLGNPQGTN... | 1.1.1.49 | null | glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; NADP metabolic process [GO:0006739]; pentose-phosphate shunt [GO:0006098]; pentose-phosphate shunt, oxidative branch [GO:0009051] | cytosol [GO:0005829] | glucose-6-phosphate dehydrogenase activity [GO:0004345]; NADP binding [GO:0050661] | PF02781;PF00479; | 3.40.50.720; | Glucose-6-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11413}. | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; PhysiologicalDirection=left-to-right; ... | null | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000250|UniProtKB:P11413}. | null | null | FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty a... | Drosophila melanogaster (Fruit fly) |
P12651 | SPIKE_IBVM | MLVTPLLLVTLLCVLCSAALYDSSSYVYYYQSAFRPPNGWHLHGGAYAVVNISSESNNAGSSPGCIVGTIHGGRVVNASSIAMTAPSSGMAWSSSQFCTAHCNFSDTTVFVTHCYKYDGCPITGMLQKNFLRVSAMKNGQLFYNLTVSVAKYPTFKSFQCVNNLTSVYLNGDLVYTSNETTDVTSAGVYFKAGGPITYKVMRKVKALAYFVNGTAQDVILCDGSPRGLLACQYNTGNFSDGFYPFINSSLVKQKFIVYRENSVNTTFTLHNFTFHNETGANPNPSGVQNILTYQTQTAQSGYYNFNFSFLSSFVYKESNF... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF19209;PF01601;PF19214; | 1.20.5.300; | Gammacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or furin-like protease to yield the mature S1 and S2 proteins. The cleavage site between S1 and S2 requires the optimal sequence [KR]-X-[KR]-R. Additionally, a second cleavage leads to the relea... | SUBCELLULAR LOCATION: [Spike protein S2]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04098}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04098}; Single-pass type I membrane protein {ECO:0000255|HAMAP... | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the host cell membrane by interacting with sialic acids, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04098}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current mo... | Avian infectious bronchitis virus (strain M41) (IBV) |
P12653 | GSTF1_MAIZE | MAPMKLYGAVMSWNLTRCATALEEAGSDYEIVPINFATAEHKSPEHLVRNPFGQVPALQDGDLYLFESRAICKYAARKNKPELLREGNLEEAAMVDVWIEVEANQYTAALNPILFQVLISPMLGGTTDQKVVDENLEKLKKVLEVYEARLTKCKYLAGDFLSLADLNHVSVTLCLFATPYASVLDAYPHVKAWWSGLMERPSVQKVAALMKPSA | 2.5.1.18 | null | glutathione metabolic process [GO:0006749]; response to herbicide [GO:0009635]; response to hydrogen peroxide [GO:0042542]; response to reactive oxygen species [GO:0000302]; response to salicylic acid [GO:0009751]; response to xenobiotic stimulus [GO:0009410] | cytoplasm [GO:0005737]; protein-containing complex [GO:0032991] | glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Phi family | null | null | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides. | Zea mays (Maize) |
P12657 | ACM1_MOUSE | MNTSVPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPESPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDPEAQAPTKQPPK... | null | null | adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway [GO:0007197]; chemical synaptic transmission [GO:0007268]; cognition [GO:0050890]; G protein-coupled acetylcholine receptor signaling pathway [GO:0007213]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide s... | asymmetric synapse [GO:0032279]; axon terminus [GO:0043679]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; glutamatergic synapse [GO:0098978]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; Schaffer collateral - CA1 synapse [GO:0098685]; syn... | G protein-coupled acetylcholine receptor activity [GO:0016907]; G protein-coupled serotonin receptor activity [GO:0004993] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Muscarinic acetylcholine receptor subfamily, CHRM1 sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. | Mus musculus (Mouse) |
P12658 | CALB1_MOUSE | MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKSFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNITTYKKNIMALSDGGKLYRTDLALILSAGDN | null | null | cellular response to organic substance [GO:0071310]; cochlea development [GO:0090102]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; metanephric collecting duct development [GO:0072205]; metanephric connecting tubule development [GO:0072286]; metanephric distal convoluted tubule development [GO:00722... | axon [GO:0030424]; calyx of Held [GO:0044305]; cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuron projection [GO:... | calcium ion binding [GO:0005509]; calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration [GO:0099567]; calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration [GO:0099534]; vitamin D binding [GO:0005499]; zinc ion binding [GO:0008270] | PF00036;PF13499; | 1.10.238.10; | Calbindin family | null | null | null | null | null | null | null | FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. | Mus musculus (Mouse) |
P12670 | NP24_SOLLC | MGYLTSSFVLFFLLCVTYTYAATIEVRNNCPYTVWAASTPIGGGRRLNRGQTWVINAPRGTKMARIWGRTGCNFNAAGRGTCQTGDCGGVLQCTGWGKPPNTLAEYALDQFSNLDFWDISLVDGFNIPMTFAPTKPSGGKCHAIHCTANINGECPRALKVPGGCNNPCTTFGGQQYCCTQGPCGPTELSKFFKKRCPDAYSYPQDDPTSTFTCPGGSTNYRVVFCPNGVADPNFPLEMPASTDEVAK | 3.2.1.6 | null | antifungal innate immune response [GO:0061760]; defense response [GO:0006952]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152]; response to salt stress [GO:0009651]; response to virus [GO:0009615] | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; vacuole [GO:0005773] | beta-glucanase activity [GO:0052736] | PF00314; | 2.60.110.10; | Thaumatin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|Ref.3}. Vacuole {ECO:0000303|PubMed:10504569}. Note=Or soluble fractions of cytoplasmic organelles, except mitochondria and plastids. {ECO:0000269|Ref.3}. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6; Evidence={ECO:0000269|PubMed:10504569}; | null | null | null | null | FUNCTION: Has antifungal activity against P.betae and F.dahliae (PubMed:9115696). May be involved in disease resistance in tomatoes and/or have a possible role in fruit development and ripening (PubMed:9115696). Binds to beta-glucans and exhibits beta-1,3-D-glucanase activity (Probable) (PubMed:10504569). {ECO:0000269|... | Solanum lycopersicum (Tomato) (Lycopersicon esculentum) |
P12672 | RAPSN_MOUSE | MGQDQTKQQIEKGLQLYQSNQTEKALQVWMKVLEKGSDLVGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARGLEDADFLLESYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLGGQVSLSMGNAFLGLSLFQKALESFEKALRYAHNNDDTMLECRVCCSLGSFYAQVKDYEKALFFPCKAAELVNDYGKGWSLKYRAMSQYHMAVAYRLLGHLGSAMECCEESMKIALQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVHVLLGVAKCWMARKVQDKALDAIEKAQDLAEEVG... | null | null | establishment of protein localization to postsynaptic membrane [GO:1903540]; motor neuron apoptotic process [GO:0097049]; neuromuscular junction development [GO:0007528]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; positive regulation of motor neuron apoptotic process [G... | centrosome [GO:0005813]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; postsynaptic specialization membrane [GO:0099634]; synapse [GO:0045202] | acetylcholine receptor binding [GO:0033130]; ionotropic glutamate receptor binding [GO:0035255]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]; protein-membrane adaptor activity [GO:0043495]; structural constituent of postsynaptic specialization [GO:0098879] | PF10579;PF17874;PF13639; | 1.25.40.10;3.30.40.10; | RAPsyn family | PTM: Ubiquitinated by the BCR(KLHL8) complex, leading to its degradation. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Postsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Cytoplasmic surface of postsynaptic membranes. | null | null | null | null | null | FUNCTION: Postsynaptic protein required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction. It may link the receptor to the underlying postsynaptic cytoskeleton, possibly by direct association with actin or spectrin (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P12676 | CHOD_STRS0 | MTAQQHLSRRRMLGMAAFGAAALAGGTTIAAPRAAAAAKSAADNGGYVPAVVIGTGYGAAVSALRLGEAGVQTLMLEMGQLWNQPGPDGNIFCGMLNPDKRSSWFKNRTEAPLGSFLWLDVVNRNIDPYAGVLDRVNYDQMSVYVGRGVGGGSLVNGGMAVEPKRSYFEEILPRVDSSEMYDRYFPRANSMLRVNHIDTKWFEDTEWYKFARVSREQAGKAGLGTVFVPNVYDFGYMQREAAGEVPKSALATEVIYGNNHGKQSLDKTYLAAALGTGKVTIQTLHQVKTIRQTKDGGYALTVEQKDTDGKLLATKEISCR... | 1.1.3.6; 5.3.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10194345}; | cholesterol catabolic process [GO:0006707] | extracellular region [GO:0005576] | cholesterol oxidase activity [GO:0016995]; flavin adenine dinucleotide binding [GO:0050660]; steroid delta-isomerase activity [GO:0004769] | PF05199;PF00732; | 3.50.50.60; | GMC oxidoreductase family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=cholesterol + O2 = cholest-5-en-3-one + H2O2; Xref=Rhea:RHEA:32183, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:CHEBI:16240, ChEBI:CHEBI:63906; EC=1.1.3.6; Evidence={ECO:0000269|PubMed:9922167}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32184; Evidence={ECO:0000305|PubMed:9922167... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for cholesterol {ECO:0000269|PubMed:9922167}; KM=6.2 uM for cholest-5-en-3-one {ECO:0000269|PubMed:9922167}; Note=kcat is 44 sec(-1) for the oxidation of cholesterol. kcat is 64 sec(-1) for the isomerization of cholest-5-en-3-one. {ECO:0000269|PubMed:9922167}; | PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:9922167}. | null | null | FUNCTION: Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product, producing cholest-4-en-3-one. These reactions are part of a cholesterol degradation pathway that allows the bacterium to utilize cholesterol as its sol... | Streptomyces sp. (strain SA-COO) |
P12682 | HMGB1_PIG | MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDASVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKHPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEEEEEDDDDE | null | null | adaptive immune response [GO:0002250]; apoptotic cell clearance [GO:0043277]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA geometric change [GO:0032392]; DNA recombination [GO:0006310]; double-strand break repair via nonhomologous end joining [GO:0006303]; inflammatory response [GO:0006954]; innate immune respo... | chromatin [GO:0000785]; condensed chromosome [GO:0000793]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | bubble DNA binding [GO:0000405]; DNA binding, bending [GO:0008301]; four-way junction DNA binding [GO:0000400]; non-sequence-specific DNA binding, bending [GO:0044378]; supercoiled DNA binding [GO:0097100] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion (By similarity). Phosphorylation at Thr-51 within the NLS is crucial for secretion induced by porcine reproductive and respiratory syndrome virus (PRRSV) (PubMed:35632744). {ECO:00... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32321806, ECO:0000269|PubMed:35632744}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000269|PubMed:35632744}. Secreted {ECO:0000269|PubMed:32321806, ECO:0000269|PubMed:35632744}. Cell membrane {ECO:0000250|UniProtKB:P09429, EC... | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... | Sus scrofa (Pig) |
P12683 | HMDH1_YEAST | MPPLFKGLKQMAKPIAYVSRFSAKRPIHIILFSLIISAFAYLSVIQYYFNGWQLDSNSVFETAPNKDSNTLFQECSHYYRDSSLDGWVSITAHEASELPAPHHYYLLNLNFNSPNETDSIPELANTVFEKDNTKYILQEDLSVSKEISSTDGTKWRLRSDRKSLFDVKTLAYSLYDVFSENVTQADPFDVLIMVTAYLMMFYTIFGLFNDMRKTGSNFWLSASTVVNSASSLFLALYVTQCILGKEVSALTLFEGLPFIVVVVGFKHKIKIAQYALEKFERVGLSKRITTDEIVFESVSEEGGRLIQDHLLCIFAFIGCS... | 1.1.1.34 | null | coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; isoprenoid biosynthetic process [GO:0008299] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; peroxisomal membrane [GO:0005778] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420] | PF00368;PF13323;PF12349; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003, ECO:0... | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000269|PubMed:3526336}. | null | null | FUNCTION: HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway constitutes by the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:3065625, PubMed:3526336). HMG1 and HMG2 catalyze the reduc... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12684 | HMDH2_YEAST | MSLPLKTIVHLVKPFACTARFSARYPIHVIVVAVLLSAAAYLSVTQSYLNEWKLDSNQYSTYLSIKPDELFEKCTHYYRSPVSDTWKLLSSKEAADIYTPFHYYLSTISFQSKDNSTTLPSLDDVIYSVDHTRYLLSEEPKIPTELVSENGTKWRLRNNSNFILDLHNIYRNMVKQFSNKTSEFDQFDLFIILAAYLTLFYTLCCLFNDMRKIGSKFWLSFSALSNSACALYLSLYTTHSLLKKPASLLSLVIGLPFIVVIIGFKHKVRLAAFSLQKFHRISIDKKITVSNIIYEAMFQEGAYLIRDYLFYISSFIGCAI... | 1.1.1.34 | null | coenzyme A metabolic process [GO:0015936]; ergosterol biosynthetic process [GO:0006696]; isoprenoid biosynthetic process [GO:0008299] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; peroxisomal membrane [GO:0005778]; proteasome complex [GO:0000502] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420] | PF00368;PF13323;PF12349; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass membrane protein {ECO:0000255}. Nucleus envelope {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003, ECO:0... | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. {ECO:0000269|PubMed:3065625, ECO:0000269|PubMed:3526336}. | null | null | FUNCTION: HMG-CoA reductase; part of the first module of ergosterol biosynthesis pathway constitutes by the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:3065625, PubMed:3526336). HMG1 and HMG2 catalyze the reduc... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12688 | YPK1_YEAST | MYSWKSKFKFGKSKEEKEAKHSGFFHSSKKEEQQNNQATAGEHDASITRSSLDRKGTINPSNSSVVPVRVSYDASSSTSTVRDSNGGNSENTNSSQNLDETANIGSTGTPNDATSSSGMMTIKVYNGDDFILPFPITSSEQILNKLLASGVPPPHKEISKEVDALIAQLSRVQIKNQGPADEDLISSESAAKFIPSTIMLPGSSTLNPLLYFTIEFDNTVATIEAEYGTIAKPGFNKISTFDVTRKLPYLKIDVFARIPSILLPSKTWQQEMGLQDEKLQTIFDKINSNQDIHLDSFHLPINLSFDSAASIRLYNHHWIT... | 2.7.11.1 | null | cell wall organization [GO:0071555]; cellular response to acetate [GO:0071311]; eisosome assembly [GO:0070941]; endocytosis [GO:0006897]; glycerophospholipid metabolic process [GO:0006650]; intracellular signal transduction [GO:0035556]; negative regulation of phospholipid translocation [GO:0061093]; negative regulatio... | cellular bud neck [GO:0005935]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein kinase regulator activity [GO:0019887]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069;PF00433; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, RAC subfamily | PTM: Autophosphorylated. Autophosphorylation is stimulated by PHS. Phosphorylated by PKH1. PHS stimulates phosphorylation by PKH1. The N-terminal half is phosphorylated by FPK1. {ECO:0000269|PubMed:10074427, ECO:0000269|PubMed:15470109, ECO:0000269|PubMed:15840588, ECO:0000269|PubMed:19966303}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10825204, ECO:0000269|PubMed:12221112, ECO:0000269|PubMed:14562095}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Intracellular localization is regulated by the intracellular sphingolipid levels. During t... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Plays an essential role in the proliferation of yeast cells. Involved in a signaling pathway, required for optimal cell wall integrity, that acts in parallel with the PKC1-SLT2-dependent pathway. Downstream kinase in the sphingolipid-mediated signaling pathway. Its phosphorylation is regulated by the intracel... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12689 | REV1_YEAST | MGEHGGLVDLLDSDLEYSINRETPDKNNCLSQQSVNDSHLTAKTGGLNARSFLSTLSDDSLIEYVNQLSQTNKNNSNPTAGTLRFTTKNISCDELHADLGGGEDSPIARSVIEIQESDSNGDDVKKNTVYTREAYFHEKAHGQTLQDQILKDQYKDQISSQSSKIFKNCVIYINGYTKPGRLQLHEMIVLHGGKFLHYLSSKKTVTHIVASNLPLKKRIEFANYKVVSPDWIVDSVKEARLLPWQNYSLTSKLDEQQKKLDNCKTVNSIPLPSETSLHKGSKCVGSALLPVEQQSPVNLNNLEAKRIVACDDPDFLTSYF... | 2.7.7.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16195463, ECO:0000269|PubMed:18275815}; Note=Binds 2 magnesium ions. {ECO:0000269|PubMed:16195463, ECO:0000269|PubMed:18275815}; | error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; replication fork [GO:0005657] | damaged DNA binding [GO:0003684]; deoxycytidyl transferase activity [GO:0017125]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872] | PF16589;PF00817;PF11799; | 3.30.70.270;3.40.1170.60;6.10.250.1490;1.10.150.20;3.40.50.10190;3.30.1490.100; | DNA polymerase type-Y family | null | SUBCELLULAR LOCATION: Nucleus. Mitochondrion. | null | null | null | null | null | FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by p... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12691 | ALKB_PSEOL | MLEKHRVLDSAPEYVDKKKYLWILSTLWPATPMIGIWLANETGWGIFYGLVLLVWYGALPLLDAMFGEDFNNPPEEVVPKLEKERYYRVLTYLTVPMHYAALIVSAWWVGTQPMSWLEIGALALSLGIVNGLALNTGHELGHKKETFDRWMAKIVLAVVGYGHFFIEHNKGHHRDVATPMDPATSRMGESIYKFSIREIPGAFIRAWGLEEQRLSRRGQSVWSFDNEILQPMIITVILYAVLLALFGPKMLVFLPIQMAFGWWQLTSANYIEHYGLLRQKMEDGRYEHQKPHHSWNSNHIVSNLVLFHLQRHSDHHAHPT... | 1.14.15.3 | COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000269|PubMed:9096332, ECO:0000269|PubMed:921275}; Note=Binds 2 Fe(3+) ions per subunit. {ECO:0000269|PubMed:9096332, ECO:0000269|PubMed:921275}; | alkane catabolic process [GO:0043448]; lipid metabolic process [GO:0006629] | plasma membrane [GO:0005886] | alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid omega-hydroxylase activity [GO:0052869]; metal ion binding [GO:0046872] | PF00487; | null | Fatty acid desaturase type 1 family, AlkB subfamily | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + O2 + octane + 2 reduced [rubredoxin] = H2O + octan-1-ol + 2 oxidized [rubredoxin]; Xref=Rhea:RHEA:19341, Rhea:RHEA-COMP:10302, Rhea:RHEA-COMP:10303, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16188, ChEBI:CHEBI:17590, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; ... | null | PATHWAY: Hydrocarbon metabolism; alkane degradation. | null | null | FUNCTION: Catalyzes the hydroxylation of n-alkanes and fatty acids in the presence of a NADH-rubredoxin reductase and rubredoxin. {ECO:0000269|PubMed:921275}. | Pseudomonas oleovorans |
P12694 | ODBA_HUMAN | MAVAIAAARVWRLNRGLSQAALLLLRQPGARGLARSHPPRQQQQFSSLDDKPQFPGASAEFIDKLEFIQPNVISGIPIYRVMDRQGQIINPSEDPHLPKEKVLKLYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLVFGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVTISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAATLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVFAVYNATKEARRRAVAE... | 1.2.4.4 | COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000269|PubMed:10745006}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10745006}; | branched-chain amino acid catabolic process [GO:0009083] | mitochondrial branched-chain alpha-keto acid dehydrogenase complex [GO:0160120]; mitochondrial matrix [GO:0005759]; mitochondrial oxoglutarate dehydrogenase complex [GO:0009353]; mitochondrion [GO:0005739] | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity [GO:0003863]; carboxy-lyase activity [GO:0016831]; metal ion binding [GO:0046872] | PF00676; | 3.40.50.970; | BCKDHA family | PTM: Phosphorylated at Ser-337 by BCKDK and dephosphorylated by protein phosphatase PPM1K. {ECO:0000269|PubMed:19411760, ECO:0000269|PubMed:22589535}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:10745006}. | CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]; Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rh... | null | null | null | null | FUNCTION: Together with BCKDHB forms the heterotetrameric E1 subunit of the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) complex. The BCKD complex catalyzes the multi-step oxidative decarboxylation of alpha-ketoacids derived from the branched-chain amino-acids valine, leucine and isoleucine producin... | Homo sapiens (Human) |
P12695 | ODP2_YEAST | MSAFVRVVPRISRSSVLTRSLRLQLRCYASYPEHTIIGMPALSPTMTQGNLAAWTKKEGDQLSPGEVIAEIETDKAQMDFEFQEDGYLAKILVPEGTKDIPVNKPIAVYVEDKADVPAFKDFKLEDSGSDSKTSTKAQPAEPQAEKKQEAPAEETKTSAPEAKKSDVAAPQGRIFASPLAKTIALEKGISLKDVHGTGPRGRITKADIESYLEKSSKQSSQTSGAAAATPAAATSSTTAGSAPSPSSTASYEDVPISTMRSIIGERLLQSTQGIPSYIVSSKISISKLLKLRQSLNATANDKYKLSINDLLVKAITVAAK... | 2.3.1.12 | COFACTOR: Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Note=Binds 1 lipoyl cofactor covalently. {ECO:0000269|PubMed:3050999}; | acetyl-CoA biosynthetic process from pyruvate [GO:0006086] | mitochondrial pyruvate dehydrogenase complex [GO:0005967]; mitochondrion [GO:0005739] | dihydrolipoyllysine-residue acetyltransferase activity [GO:0004742] | PF00198;PF00364;PF02817; | 2.40.50.100;3.30.559.10;4.10.320.10; | 2-oxoacid dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein]; Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12; Evidence={ECO:000... | null | null | null | null | FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). {ECO:0000269|PubMed:7030741}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12709 | G6PI_YEAST | MSNNSFTNFKLATELPAWSKLQKIYESQGKTLSVKQEFQKDAKRFEKLNKTFTNYDGSKILFDYSKNLVNDEIIAALIELAKEANVTGLRDAMFKGEHINSTEDRAVYHVALRNRANKPMYVDGVNVAPEVDSVLKHMKEFSEQVRSGEWKGYTGKKITDVVNIGIGGSDLGPVMVTEALKHYAGVLDVHFVSNIDGTHIAETLKVVDPETTLFLIASKTFTTAETITNANTAKNWFLSKTGNDPSHIAKHFAALSTNETEVAKFGIDTKNMFGFESWVGGRYSVWSAIGLSVALYIGYDNFEAFLKGAEAVDNHFTQTP... | 5.3.1.9 | null | gluconeogenesis [GO:0006094]; glucose 6-phosphate metabolic process [GO:0051156]; glycolytic process [GO:0006096] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | carbohydrate derivative binding [GO:0097367]; glucose-6-phosphate isomerase activity [GO:0004347]; monosaccharide binding [GO:0048029] | PF00342; | 1.10.1390.10; | GPI family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P78917}. | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225; EC=5.3.1.9; Evidence={ECO:0000250|UniProtKB:P06744}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. {ECO:0000305}. | null | null | FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis. {ECO:0000250|UniProtKB:P06744}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12710 | FABPL_MOUSE | MNFSGKYQLQSQENFEPFMKAIGLPEDLIQKGKDIKGVSEIVHEGKKIKLTITYGPKVVRNEFTLGEECELETMTGEKVKAVVKLEGDNKMVTTFKGIKSVTELNGDTITNTMTLGDIVYKRVSKRI | null | null | cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; fatty acid transport [GO:0015908]; intestinal absorption [GO:0050892]; long-chain fatty acid transport [GO:0015909]; negative regulation of apoptotic process [GO:0043066]; positive regulation of fatty acid beta-oxidation [GO... | apical cortex [GO:0045179]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal matrix [GO:0005782]; protein-containing complex [GO:0032991] | antioxidant activity [GO:0016209]; bile acid binding [GO:0032052]; chromatin binding [GO:0003682]; fatty acid binding [GO:0005504]; heterocyclic compound binding [GO:1901363]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538]; phospholipid binding [GO:0005543] | PF14651; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes. Binds cholesterol. Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. {ECO:0000250|UniProtKB:P07148, ECO:0000250|UniProtKB... | Mus musculus (Mouse) |
P12711 | ADHX_RAT | MANQVIRCKAAVAWEAGKPLSIEEIEVAPPQAHEVRIKIIATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTKLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKPILHFMGTSTFSEYTVVADISVAKIDPSAPLDKVCLLGCGISTGYGAAVNTAKVEPGSTCAVFGLGGVGLAVIMGCKVAGASRIIGIDINKDKFAKAKEFGATECINPQDFSKSIQEVLIEMTDGGVDFSFECIGNVKVMRSALEAAHKGWGVSVVVGVAASGEEISTRPFQLVTGRTWKGTAFG... | 1.1.1.-; 1.1.1.1; 1.1.1.284 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P11766}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766}; | ethanol catabolic process [GO:0006068]; ethanol oxidation [GO:0006069]; fatty acid omega-oxidation [GO:0010430]; formaldehyde catabolic process [GO:0046294]; positive regulation of blood pressure [GO:0045777]; respiratory system process [GO:0003016]; response to lipopolysaccharide [GO:0032496]; response to nitrosative ... | cytosol [GO:0005829]; mitochondrion [GO:0005739] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; fatty acid binding [GO:0005504]; formaldehyde dehydrogenase activity [GO:0018467]; identical protein binding [GO:0042802]; S-(hydroxymethyl)glutathione dehydrogenase activity [GO:0051903]; S-(hydroxymethyl)g... | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Class-III subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000250|UniProtKB:P11766}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ket... | null | null | null | null | FUNCTION: Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraened... | Rattus norvegicus (Rat) |
P12724 | ECP_HUMAN | MVPKLFTSQICLLLLLGLMGVEGSLHARPPQFTRAQWFAIQHISLNPPRCTIAMRAINNYRWRCKNQNTFLRTTFANVVNVCGNQSIRCPHNRTLNNCHRSRFRVPLLHCDLINPGAQNISNCTYADRPGRRFYVVACDNRDPRDSPRYPVVPVHLDTTI | 3.1.27.- | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; chemotaxis [GO:0006935]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; induction of bacterial agglutination [GO:0043152... | azurophil granule lumen [GO:0035578]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | endonuclease activity [GO:0004519]; lipopolysaccharide binding [GO:0001530]; nucleic acid binding [GO:0003676]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Secreted. Note=Located in the matrix of eosinophil large specific granule, which are released following activation by an immune stimulus. | null | null | null | null | null | FUNCTION: Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, ... | Homo sapiens (Human) |
P12729 | PSA_DICDI | MKFQHTFIALLSLLTYANAYDYFTTTLANQNPVCASVDVIQNVCTEVCGRFVRYIPDATNTNQFTFAEYTTNQCTVQVTPAVTNTFTCADQTSSHALGSDWSGVCKITATPAPTVTPTVTPTVTPTVTPTPTNTPNPTPSQTSTTTGSASTVVASLSLIIFSMILSLC | null | null | adenylate cyclase-activating G protein-coupled cAMP receptor signaling pathway [GO:0140582]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; GPI anchor biosynthetic process [GO:0006506]; mannosyl-inositol phosphorylceramide biosynthetic process [GO:0051999]; response to catechin [GO:1902168]; sl... | asexual spore wall [GO:0097515]; cell surface [GO:0009986]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | actin binding [GO:0003779] | null | null | Ponticulin family | PTM: O-glycosylated in the repeat region. The oligosaccharides contain N-acetylglucosamine and fucose as the major constituents. {ECO:0000269|PubMed:8404891, ECO:0000269|PubMed:8681966}.; PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | null | null | FUNCTION: May bind F-actin and nucleates actin assembly. {ECO:0000305|PubMed:18522444}. | Dictyostelium discoideum (Social amoeba) |
P12749 | RL26_RAT | MKFNPFVTSDRSKNRKRHFNAPSHIRRKIMSSPLSKELRQKYNVRSMPIRKDDEVQVVRGHYKGQQIGKVVQVYRKKYVIYIERVQREKANGTTVHVGIRPSKVVITRLKLDKDRKKILERKAKSRQVGKEKGKYKEETIEKMQE | null | null | cellular response to gamma radiation [GO:0071480]; cellular response to ionizing radiation [GO:0071479]; cellular response to UV [GO:0034644]; cytoplasmic translation [GO:0002181]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; positive regulation of DNA dama... | cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:1990904]; synapse [GO:0045202]; terminal bouton [GO:0043195] | mRNA 5'-UTR binding [GO:0048027]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00467;PF16906; | 2.30.30.30; | Universal ribosomal protein uL24 family | PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress, promoting reticulophagy of endoplasmic reticulum sheets. {ECO:0000250|UniProtKB:P61254}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P61254}. | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. {ECO:0000250|UniProtKB:P61254}. | Rattus norvegicus (Rat) |
P12753 | RAD50_YEAST | MSAIYKLSIQGIRSFDSNDRETIEFGKPLTLIVGMNGSGKTTIIECLKYATTGDLPPNSKGGVFIHDPKITGEKDIRAQVKLAFTSANGLNMIVTRNIQLLMKKTTTTFKTLEGQLVAINNSGDRSTLSTRSLELDAQVPLYLGVPKAILEYVIFCHQEDSLWPLSEPSNLKKKFDEIFQAMKFTKALDNLKSIKKDMSVDIKLLKQSVEHLKLDKDRSKAMKLNIHQLQTKIDQYNEEVSEIESQLNEITEKSDKLFKSNQDFQKILSKVENLKNTKLSISDQVKRLSNSIDILDLSKPDLQNLLANFSKVLMDKNNQL... | 3.6.-.- | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q92878}; Note=Binds 1 zinc ion per homodimer. {ECO:0000250|UniProtKB:Q92878}; | base-excision repair [GO:0006284]; chromosome organization involved in meiotic cell cycle [GO:0070192]; DNA duplex unwinding [GO:0032508]; double-strand break repair [GO:0006302]; double-strand break repair via nonhomologous end joining [GO:0006303]; homologous chromosome pairing at meiosis [GO:0007129]; maintenance of... | condensed nuclear chromosome [GO:0000794]; mitochondrion [GO:0005739]; Mre11 complex [GO:0030870]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded DNA binding [GO:0003690]; double-stranded telomeric DNA binding [GO:0003691]; G-quadruplex DNA binding [GO:0051880]; metal ion binding [GO:0046872]; single-stranded telomeric DNA binding [GO:0043047];... | PF13476;PF04423;PF13558; | 3.40.50.300; | SMC family, RAD50 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9845372}. Chromosome {ECO:0000250|UniProtKB:Q92878}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:Q92878}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q92878}; | null | null | null | null | FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:26896444, PubMed:28134932). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12754 | EI2BD_YEAST | MSESEAKSRSATPPSKAKQATPTTTAAANGEKKLTNKELKELKKQEKAAKRAAMKQANGISIEQQQQQAQMKKEKKQLQREQQQKREQKQKNANKKKQNERNVKKSTLFGHLETTEERRATILALTSAVSSPKTSRITAAGLMVPVVASALSGSNVLTASSLMPVGPNASSTVSASAPASTTTTLPASSAALSAGTSSASTNTPTAIQQEIASSNASDVAKTLASISLEAGEFNVIPGISSVIPTVLEQSFDNSSLISSVKELLLNKDLIHPSILLLTSHLAHYKIVGSIPRCIAMLEVFQIVIKDYQTPKGTTLSRNLT... | null | null | cytoplasmic translational initiation [GO:0002183]; regulation of translational initiation [GO:0006446] | cytosol [GO:0005829]; eukaryotic translation initiation factor 2B complex [GO:0005851]; guanyl-nucleotide exchange factor complex [GO:0032045] | enzyme regulator activity [GO:0030234]; translation initiation factor activity [GO:0003743] | PF01008; | null | EIF-2B alpha/beta/delta subunits family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09924}. | null | null | null | null | null | FUNCTION: Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on the eukaryotic initiation factor 2 (eIF2) complex gamma subunit. Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subun... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12755 | SKI_HUMAN | MEAAAGGRGCFQPHPGLQKTLEQFHLSSMSSLGGPAAFSARWAQEAYKKESAKEAGAAAVPAPVPAATEPPPVLHLPAIQPPPPVLPGPFFMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAERLCNALLYGGAYPPPCKKELAASLALGLELSERSVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYTGKEEQARLGRCLDDVKEKFDYGNKYKRR... | null | null | anterior/posterior axis specification [GO:0009948]; bone morphogenesis [GO:0060349]; camera-type eye development [GO:0043010]; camera-type eye morphogenesis [GO:0048593]; cardiac muscle cell proliferation [GO:0060038]; cell motility [GO:0048870]; embryonic limb morphogenesis [GO:0030326]; face morphogenesis [GO:0060325... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone deacetylase inhibitor activity [GO:0046811]; identical protein binding [GO:0042802]; p... | PF08782;PF02437; | 3.10.390.10;3.10.260.20; | SKI family | PTM: Ubiquitinated by ARK2C, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling. {ECO:0000250|UniProtKB:Q60698}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling. {ECO:0000269|PubMed:19049980}. | Homo sapiens (Human) |
P12757 | SKIL_HUMAN | MENLQTNFSLVQGSTKKLNGMGDDGSPPAKKMITDIHANGKTINKVPTVKKEHLDDYGEAPVETDGEHVKRTCTSVPETLHLNPSLKHTLAQFHLSSQSSLGGPAAFSARHSQESMSPTVFLPLPSPQVLPGPLLIPSDSSTELTQTVLEGESISCFQVGGEKRLCLPQVLNSVLREFTLQQINTVCDELYIYCSRCTSDQLHILKVLGILPFNAPSCGLITLTDAQRLCNALLRPRTFPQNGSVLPAKSSLAQLKETGSAFEVEHECLGKCQGLFAPQFYVQPDAPCIQCLECCGMFAPQTFVMHSHRSPDKRTCHWGF... | null | null | blastocyst formation [GO:0001825]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; lens fiber cell differentiation [GO:0070306]; lymphocyte homeostasis [GO:0002260]; negative regulation of BMP signaling pathway ... | acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; protein-containing complex bind... | PF08782;PF02437; | 3.10.390.10;3.10.260.20; | SKI family | PTM: Ubiquitinated by RNF111 and ARK2C, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling. {ECO:0000269|PubMed:17591695}. | null | null | null | null | null | null | FUNCTION: May have regulatory role in cell division or differentiation in response to extracellular signals. | Homo sapiens (Human) |
P12758 | UDP_ECOLI | MSKSDVFHLGLTKNDLQGATLAIVPGDPDRVEKIAALMDKPVKLASHREFTTWRAELDGKPVIVCSTGIGGPSTSIAVEELAQLGIRTFLRIGTTGAIQPHINVGDVLVTTASVRLDGASLHFAPLEFPAVADFECTTALVEAAKSIGATTHVGVTASSDTFYPGQERYDTYSGRVVRHFKGSMEEWQAMGVMNYEMESATLLTMCASQGLRAGMVAGVIVNRTQQEIPNAETMKQTESHAVKIVVEAARRLL | 2.4.2.3 | null | DNA damage response [GO:0006974]; nucleotide catabolic process [GO:0009166]; purine nucleoside catabolic process [GO:0006152]; UMP salvage [GO:0044206]; uridine catabolic process [GO:0006218] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; potassium ion binding [GO:0030955]; purine-nucleoside phosphorylase activity [GO:0004731]; uridine phosphorylase activity [GO:0004850] | PF01048; | 3.40.50.1580; | PNP/UDP phosphorylase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3; Evidence={ECO:0000269|PubMed:16751}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for uridine {ECO:0000269|PubMed:16751}; KM=7.3 mM for phosphate {ECO:0000269|PubMed:16751}; KM=0.24 mM for uracyl {ECO:0000269|PubMed:16751}; KM=1.4 mM for ribose-1-phosphate {ECO:0000269|PubMed:16751}; | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; uracil from uridine (phosphorylase route): step 1/1. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.3. {ECO:0000269|PubMed:16751}; | null | FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate (PubMed:16751). Shows weak activity towards deoxyuridine and thymidine (PubMed:16751). The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesi... | Escherichia coli (strain K12) |
P12760 | NMU_RAT | MSRAANRRPGLSAGQLAAATASPLLSLLLLLACCADACRGTPISPQRLPPEQELQLWNEIPEACASFLSVDSQPQASVALRKLCRVLMEIFQKPQEQTEKDNAKRFLFHYSKTQKLGNSNVVSSVVHPLLQLVPQLHERRMKRYKVNEYQGPVAPSGGFFLFRPRNGKRSTSFI | null | null | eating behavior [GO:0042755]; energy homeostasis [GO:0097009]; gastric acid secretion [GO:0001696]; negative regulation of eating behavior [GO:1903999]; negative regulation of feeding behavior [GO:2000252]; negative regulation of gastric acid secretion [GO:0060455]; negative regulation of gastric emptying [GO:0120061];... | extracellular region [GO:0005576]; terminal bouton [GO:0043195] | neuromedin U receptor binding [GO:0042922]; type 1 neuromedin U receptor binding [GO:0031839]; type 2 neuromedin U receptor binding [GO:0031840] | PF02070; | null | NmU family | null | SUBCELLULAR LOCATION: [Neuromedin-U-23]: Secreted {ECO:0000305|PubMed:28874765}. | null | null | null | null | null | FUNCTION: [Neuromedin-U-23]: Ligand for receptors NMUR1 and NMUR2 (PubMed:28874765). Receptor-binding is very tight if not irreversible and triggers an increase in the cytosolic Ca(2+) concentration (PubMed:28874765). Stimulates muscle contractions of specific regions of the gastrointestinal tract. In rat, NMU stimulat... | Rattus norvegicus (Rat) |
P12762 | ALDH2_HORSE | AAAATQAVPAPNQQPEVFYNQIFINNEWHDAVSKKTFPTVNPSTGEVICQVAAGDKEDVDRAVKAARAAFQLGSPWRRMDASDRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAAKLGPALATGNVVVMKVAEQTPLTALYVANLTKEAGFPPGVVNVVPGFGPTAGAAIASHEDVDKVAFTGSTEVGHLIQVAAGRSNLKKVTLELGGKSPNIIVSDADMDWAVEQAHFALFFNQGQCCGAGSRTFVQEDVYAEFVE... | 1.2.1.3 | null | aldehyde catabolic process [GO:0046185]; ethanol catabolic process [GO:0006068]; regulation of dopamine biosynthetic process [GO:1903179]; regulation of serotonin biosynthetic process [GO:1905627] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | aldehyde dehydrogenase (NAD+) activity [GO:0004029]; carboxylesterase activity [GO:0106435]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; NAD binding [GO:0051287]; nitroglycerin reductase activity [GO:0018547]; phenylacetaldehyde dehydrogenase activity [GO:0008957] | PF00171; | null | Aldehyde dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; | null | PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2. | null | null | FUNCTION: Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage. {ECO:0000250|UniProtKB:P05091}. | Equus caballus (Horse) |
P12763 | FETUA_BOVIN | MKSFVLLFCLAQLWGCHSIPLDPVAGYKEPACDDPDTEQAALAAVDYINKHLPRGYKHTLNQIDSVKVWPRRPTGEVYDIEIDTLETTCHVLDPTPLANCSVRQQTQHAVEGDCDIHVLKQDGQFSVLFTKCDSSPDSAEDVRKLCPDCPLLAPLNDSRVVHAVEVALATFNAESNGSYLQLVEISRAQFVPLPVSVSVEFAVAATDCIAKEVVDPTKCNLLAEKQYGFCKGSVIQKALGGEDVRVTCTLFQTQPVIPQPQPDGAEAEAPSAVPDAAGPTPSAAGPPVASVVVGPSVVAVPLPLHRAHYDLRHTFSGVAS... | null | null | acute-phase response [GO:0006953]; negative regulation of bone mineralization [GO:0030502]; positive regulation of phagocytosis [GO:0050766]; regulation of inflammatory response [GO:0050727] | blood microparticle [GO:0072562]; extracellular matrix [GO:0031012]; extracellular membrane-bounded organelle [GO:0065010]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; endopeptidase inhibitor activity [GO:0004866] | PF00031; | 3.10.450.10; | Fetuin family | PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P02765}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Suggested to have lymphocyte stimulating properties, lipid binding capability and to bind thyroid hormone. | Bos taurus (Bovine) |
P12785 | FAS_RAT | MEEVVIAGMSGKLPESENLQEFWANLIGGVDMVTDDDRRWKAGLYGLPKRSGKLKDLSKFDASFFGVHPKQAHTMDPQLRLLLEVSYEAIVDGGINPASLRGTNTGVWVGVSGSEASEALSRDPETLLGYSMVGCQRAMMANRLSFFFDFKGPSIALDTACSSSLLALQNAYQAIRSGECPAAIVGGINLLLKPNTSVQFMKLGMLSPDGTCRSFDDSGNGYCRAEAVVAVLLTKKSLARRVYATILNAGTNTDGCKEQGVTFPSGEAQEQLIRSLYQPGGVAPESLEYIEAHGTGTKVGDPQELNGITRSLCAFRQSPL... | 1.1.1.100; 1.3.1.39; 2.3.1.38; 2.3.1.39; 2.3.1.41; 2.3.1.85; 3.1.2.14; 4.2.1.59 | null | acetyl-CoA metabolic process [GO:0006084]; cellular response to interleukin-4 [GO:0071353]; establishment of endothelial intestinal barrier [GO:0090557]; ether lipid biosynthetic process [GO:0008611]; fatty acid biosynthetic process [GO:0006633]; glandular epithelial cell development [GO:0002068]; inflammatory response... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; glycogen granule [GO:0042587]; melanosome [GO:0042470] | (3R)-3-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity [GO:0047450]; (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity [GO:0008693]; (3R)-3-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity [GO:0008659]; (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity [GO:0047451... | PF00698;PF13602;PF21149;PF16197;PF00109;PF02801;PF08659;PF08242;PF21089;PF00550;PF00975; | 3.30.70.3290;3.40.47.10;1.10.1200.10;3.40.50.1820;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150; | null | PTM: S-nitrosylation of Fatty acid synthase at cysteine residues Cys-1464 or Cys-2085 is important for the enzyme dimerization. In adipocytes, S-nitrosylation of Fatty acid synthase occurs under physiological conditions and gradually increases during adipogenesis. {ECO:0000250|UniProtKB:P49327}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=300 nmol/min/mg enzyme for the overall fatty acid synthase reaction {ECO:0000269|PubMed:15715522}; Vmax=900 nmol/min/mg enzyme for the beta-ketoacyl reductase reaction of acetoacetyl-CoA {ECO:0000269|PubMed:15715522}; Vmax=25 nmol/min/mg enzyme for the enoyl redu... | PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000269|PubMed:15715522, ECO:0000269|PubMed:8250834, ECO:0000269|PubMed:8756713}. | null | null | FUNCTION: Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-ph... | Rattus norvegicus (Rat) |
P12791 | CP2BA_MOUSE | MEPSVLLLLALLVGFLLLLARGHPKSRGNFPPGPRPLPLLGNLLQMDRGGLLKSLIQLREKYGDVFTVHLGPRPVVMLCGTDTIREALVGQAEAFSGRGTVAVVEPTFKEYGVIFANGERWKTLRRFSLATMRDFGMGKRSVEERIQEEAQCLVEELRKSQGAPLDPTFLFQCITANVICSIVFGERFEYTDRQFLRLLELFYQTFSLISSFSSQMFELFSGFLKYFPGAHRQISKNLQELLDYIGHSVERHKATLDPSVPRDFIDIYLLRMEKEKSNQNAEFHHQNLMMSVLSLFFVGTETSSTTLHYGFLLMLKYPHV... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | epoxygenase P450 pathway [GO:0019373]; response to bacterium [GO:0009617]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporatio... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Mus musculus (Mouse) |
P12798 | KPBB_RABIT | MAGATGLMAEVSWKVLERRARTKRSGSVYEPLKSINLPRPDNETLWDKLDYYYKIVKSTLLLYQSPTTGLFPTKTCGGDQTAKIHDSLYCAAGAWALALAYRRIDDDKGRTHELEHSAIKCMRGILYCYMRQADKVQQFKQDPRPTTCLHSLFNVHTGDELLSYEEYGHLQINAVSLYLLYLVEMISSGLQIIYNTDEVSFIQNLVFCVERVYRVPDFGVWERGSKYNNGSTELHSSSVGLAKAALEAINGFNLFGNQGCSWSVIFVDLDAHNRNRQTLCSLLPRESRSHNTDAALLPCISYPAFALDDDVLYNQTLDKV... | null | null | glycogen metabolic process [GO:0005977] | phosphorylase kinase complex [GO:0005964]; plasma membrane [GO:0005886] | calmodulin binding [GO:0005516] | PF00723;PF19292; | null | Phosphorylase b kinase regulatory chain family | PTM: Cys-1090 is farnesylated, but the C-terminal tripeptide is not removed and the cysteine carboxyl is not methylated. {ECO:0000269|PubMed:1409665}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | null | null | PATHWAY: Glycan biosynthesis; glycogen metabolism. | null | null | FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I. The beta chain acts as a regulatory unit and modulates the activity of the holoenzyme in response to phosphorylation. | Oryctolagus cuniculus (Rabbit) |
P12799 | FIBG_BOVIN | MSWSSHPPSVIFYILSLLSSACLAYVATRDNCCILDERFGSYCPTTCGIADFLNNYQTSVDKDLRTLEGILYQVENKTSEARELVKAIQISYNPDQPSKPNNIESATKNSKSMMEEIMKYETLISTHESTIRFLQEVYNSNSQKIVNLRDKVVQLEANCQEPCQDTVKIHDVTGRDCQDVANKGAKESGLYFIRPLKAKQFLVYCEIDGSGNGWTVFQKRLDGSLDFKKNWIQYKEGFGHLSPTGTGNTEFWLGNEKIHLISTQSSIPYVLRIQLEDWNGRTSTADYASFKVTGENDKYRLTYAYFIGGDAGDAFDGYDF... | null | null | cell-matrix adhesion [GO:0007160]; platelet aggregation [GO:0070527]; protein polymerization [GO:0051258] | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577] | metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102] | PF08702;PF00147; | 1.20.5.50;3.90.215.10;4.10.530.10; | null | PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsil... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11593005}. | null | null | null | null | null | FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration du... | Bos taurus (Bovine) |
P12804 | FGL2_MOUSE | MRLPGWLWLSSAVLAACRAVEEHNLTEGLEDASAQAACPARLEGSGRCEGSQCPFQLTLPTLTIQLPRQLGSMEEVLKEVRTLKEAVDSLKKSCQDCKLQADDHRDPGGNGGNGAETAEDSRVQELESQVNKLSSELKNAKDQIQGLQGRLETLHLVNMNNIENYVDNKVANLTVVVNSLDGKCSKCPSQEHMQSQPVQHLIYKDCSDHYVLGRRSSGAYRVTPDHRNSSFEVYCDMETMGGGWTVLQARLDGSTNFTREWKDYKAGFGNLEREFWLGNDKIHLLTKSKEMILRIDLEDFNGLTLYALYDQFYVANEFLK... | null | null | killing of cells of another organism [GO:0031640]; negative regulation of defense response to virus [GO:0050687]; negative regulation of dendritic cell antigen processing and presentation [GO:0002605]; negative regulation of macrophage antigen processing and presentation [GO:0002617]; negative regulation of memory T ce... | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | null | PF00147; | 3.90.215.10; | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Converts prothrombin to thrombin. | Mus musculus (Mouse) |
P12807 | AMO_PICAN | MERLRQIASQATAASAAPARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPILTVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGTGKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSKHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKFHIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKHALDI... | 1.4.3.21 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000269|PubMed:7556609, ECO:0000269|PubMed:9551552}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10933787}; Note=Binds 1 copper ion per subunit. Can also use zinc ion as cofactor (PubMed:10933787). {ECO:0000269|PubMed:10933787, ECO:00... | amine metabolic process [GO:0009308] | peroxisome [GO:0005777] | aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; primary amine oxidase activity [GO:0008131]; quinone binding [GO:0048038] | PF01179;PF02727;PF02728; | 3.10.450.40;2.70.98.20; | Copper/topaquinone oxidase family | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000269|PubMed:10933787, ECO:0000269|PubMed:9551552}. | SUBCELLULAR LOCATION: Peroxisome {ECO:0000305|PubMed:9551552}. | CATALYTIC ACTIVITY: Reaction=a primary methyl amine + H2O + O2 = an aldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938, ChEBI:CHEBI:228804; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:7556609, ECO:0000269|PubMed:9551552}; | null | null | null | null | null | Pichia angusta (Yeast) (Hansenula polymorpha) |
P12813 | NR4A1_MOUSE | MPCIQAQYGTPATSPGPRDHLTGDPLALEFGKPTMDLASPETAPAAPATLPSFSTFMDGYTGEFDTFLYQLPGTTQPCSSACSSASSTSSSSSSATSPASASFKFEDFQVYGCYPGTLSGPLDETLSSSGSEYYGSPCSAPSPSTPNFQPSQLSPWDGSFGHFSPSQTYEGLWAWTEQLPKASSGPPPPPTFFSFSPPTGPSPSLAQSSLKLFPPPATHQLGEGESYSMPAAFPGLAPTSPNRDTSGILDAPVTSTKSRSGASGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKSAKYICLANKDCPVDKRRRN... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P22829}; Note=Binds 2 zinc ions. {ECO:0000250|UniProtKB:P22829}; | apoptotic process [GO:0006915]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to corticotropin-releasing hormone stimulus [GO:0071376]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to organic substance [GO:0071310]; cellular response to vascu... | chromatin [GO:0000785]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; presynapse [GO:0098793]; transcription regulator complex [GO:0005667] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; identical protein binding [GO:0042802]; lipopolysaccharide binding [GO:0001530]; ... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR4 subfamily | PTM: Phosphorylated at Ser-354 by RPS6KA1 and RPS6KA3 in response to mitogenic or stress stimuli. {ECO:0000250}.; PTM: Acetylated by p300/CBP, acetylation increases stability. Deacetylated by HDAC1 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2555161, ECO:0000269|PubMed:30134173}. Cytoplasm, cytosol {ECO:0000269|PubMed:37001519}. Mitochondrion {ECO:0000250|UniProtKB:P22736}. Note=Nuclear export to the cytosol is XPO1-mediated and positively regulated by IFI27. Translocation to the mitochondrion upon interact... | null | null | null | null | null | FUNCTION: Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAGGTCA-3' (PubMed:37001519). Binds 9-cis-retinoic acid outside of its ligand-binding (NR LBD) domain (By similarity). Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK... | Mus musculus (Mouse) |
P12814 | ACTN1_HUMAN | MDHYDSQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMHAMQQKLEDFRDYR... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; actin filament network formation [GO:0051639]; actin filament organization [GO:0007015]; focal adhesion assembly [GO:0048041]; muscle cell development [GO:0055001]; platelet formation [GO:0030220]; platelet morphogenesis [GO:0036... | brush border [GO:0005903]; cell junction [GO:0030054]; cell projection [GO:0042995]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fascia ad... | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; double-stranded RNA binding [GO:0003725]; integrin binding [GO:0005178]; nuclear receptor coactivator activity [GO:0030374]; protein homodimerization activity [GO:0042803]; structural constituent of postsynapse [GO:0099186]; transmembrane transporte... | PF00307;PF13405;PF08726;PF00435; | 1.20.58.60;1.10.418.10;1.10.238.10; | Alpha-actinin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24069336, ECO:0000269|PubMed:7750553}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:7750553}. Cell membrane {ECO:0000250|UniProtKB:Q9Z1P2}. Cell junction {ECO:0000250|UniProtKB:Q9Z1P2}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q7TPR4... | null | null | null | null | null | FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. | Homo sapiens (Human) |
P12815 | PDCD6_MOUSE | MAAYSYRPGPGGGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDNELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cellular response to heat [GO:0034605]; COPII vesicle coating [GO:0048208]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; negative regulation of phosphatidylinositol 3-kinase/protein kinase... | COPII vesicle coat [GO:0030127]; Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; magnesium ion binding [GO:0000287]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein-macromolecule adaptor activity [GO:0030674]; protein-membrane adaptor activity [GO:0043495]; ubiquitin... | PF13499; | 1.10.238.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75340}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75340}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:O75340}. Cytoplasm {ECO:0000250|UniProtKB:O75340}. Nucleus {ECO:0000250|UniProtKB:O75340}. Endosome {... | null | null | null | null | null | FUNCTION: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (PubMed:10744743, PubMed:11525164, PubMed:27541325). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in respon... | Mus musculus (Mouse) |
P12820 | ACE_BOVIN | MGAASGRRSPPLLLPLLLLLLPPPPVILELDPALQPGNFPADEAGAQIFAASFNSSAEQVLFQSTAASWAHDTNITEENARLQEEAALLSQEFSEAWGQKAKDLFDPVWQNFTDPTLLRIIGAVRTLGPANLDLEKRQKYNSLLSNMSRIYSTAKVCFPNKTAPCWSLDPELTNILASSRSYTLLLYAWEGWHNAAGIPLKPLYQDFTALSNEAYKQDGFSDTGAYWRSWYDSPTFTEDLERLYQQLEPLYLNLHAYVRRALHRRYGDRYINLRGPIPAHLLGNMWAQSWENIYDTVVPFPDKPNLDVTDVMVQKGWNAT... | 3.4.15.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12821}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P12821}; COFACTOR: Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P12821}; Note=Binds 3 chloride ions per subunit. {ECO:0000250|UniProtKB:P12821}; | angiotensin maturation [GO:0002003]; bradykinin catabolic process [GO:0010815]; hormone catabolic process [GO:0042447]; hormone metabolic process [GO:0042445]; kidney development [GO:0001822]; positive regulation of systemic arterial blood pressure [GO:0003084]; regulation of blood pressure [GO:0008217]; regulation of ... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | calmodulin binding [GO:0005516]; carboxypeptidase activity [GO:0004180]; chloride ion binding [GO:0031404]; metal ion binding [GO:0046872]; metallodipeptidase activity [GO:0070573]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; peptidyl-dipeptidase activity [GO:0008241] | PF01401; | 1.10.1370.30; | Peptidase M2 family | PTM: [Angiotensin-converting enzyme, soluble form]: Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region. Cleavage can take place at different sites of the juxtamembrane stalk region. {ECO:0000250|UniProtKB... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12821}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P09470}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:P09470}.; SUBCELLULAR LOCATION: [Angiotensin-converting enzyme, soluble fo... | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.; EC=3.4.15.1; Evidence={ECO:0000250|UniProtKB:P128... | null | null | null | null | FUNCTION: Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity. Composed of two similar catalytic doma... | Bos taurus (Bovine) |
P12821 | ACE_HUMAN | MGAASGRRGPGLLLPLPLLLLLPPQPALALDPGLQPGNFSADEAGAQLFAQSYNSSAEQVLFQSVAASWAHDTNITAENARRQEEAALLSQEFAEAWGQKAKELYEPIWQNFTDPQLRRIIGAVRTLGSANLPLAKRQQYNALLSNMSRIYSTAKVCLPNKTATCWSLDPDLTNILASSRSYAMLLFAWEGWHNAAGIPLKPLYEDFTALSNEAYKQDGFTDTGAYWRSWYNSPTFEDDLEHLYQQLEPLYLNLHAFVRRALHRRYGDRYINLRGPIPAHLLGDMWAQSWENIYDMVVPFPDKPNLDVTSTMLQQGWNAT... | 3.4.15.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12540854, ECO:0000269|PubMed:16476442, ECO:0000269|PubMed:1649623, ECO:0000269|PubMed:20826823, ECO:0000269|PubMed:23056909, ECO:0000269|PubMed:26403559, ECO:0000269|PubMed:7961923}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:125... | amyloid-beta metabolic process [GO:0050435]; angiogenesis involved in coronary vascular morphogenesis [GO:0060978]; angiotensin maturation [GO:0002003]; angiotensin-activated signaling pathway [GO:0038166]; animal organ regeneration [GO:0031100]; antigen processing and presentation of peptide antigen via MHC class I [G... | basal plasma membrane [GO:0009925]; brush border membrane [GO:0031526]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; sperm midpiece [GO:0... | actin binding [GO:0003779]; bradykinin receptor binding [GO:0031711]; calmodulin binding [GO:0005516]; carboxypeptidase activity [GO:0004180]; chloride ion binding [GO:0031404]; endopeptidase activity [GO:0004175]; exopeptidase activity [GO:0008238]; heterocyclic compound binding [GO:1901363]; metallodipeptidase activi... | PF01401; | null | Peptidase M2 family | PTM: [Angiotensin-converting enzyme, soluble form]: Produced following proteolytic cleavage by secretase enzymes that cleave the transmembrane form in the juxtamembrane stalk region upstream of the transmembrane region (PubMed:10769174, PubMed:11274151, PubMed:7499427, PubMed:8253769). Cleavage can take place at differ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12386153}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P09470}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:P09470}.; SUBCELLULAR LOCATION: [Angiotensin-converting enzyme, soluble for... | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.; EC=3.4.15.1; Evidence={ECO:0000269|PubMed:1091325... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.51 mM for Hip-His-Leu {ECO:0000269|PubMed:11076943, ECO:0000269|PubMed:12542396}; KM=30 uM for angiotensin I {ECO:0000305|PubMed:6270633}; KM=16 uM for angiotensin I {ECO:0000269|PubMed:1851160}; KM=1 uM for bradykinin {ECO:0000305|PubMed:6270633}; KM=0.18 uM for... | null | null | null | FUNCTION: Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:15615692, PubMed:20826823, PubM... | Homo sapiens (Human) |
P12822 | ACE_RABIT | MGAAPGRRGPRLLRPPPPLLLLLLLLRPPPAALTLDPGLLPGDFAADEAGARLFASSYNSSAEQVLFRSTAASWAHDTNITAENARRQEEEALLSQEFAEAWGKKAKELYDPVWQNFTDPELRRIIGAVRTLGPANLPLAKRQQYNSLLSNMSQIYSTGKVCFPNKTASCWSLDPDLNNILASSRSYAMLLFAWEGWHNAVGIPLKPLYQEFTALSNEAYRQDGFSDTGAYWRSWYDSPTFEEDLERIYHQLEPLYLNLHAYVRRVLHRRYGDRYINLRGPIPAHLLGNMWAQSWESIYDMVVPFPDKPNLDVTSTMVQK... | 3.4.15.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12821}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P12821}; COFACTOR: [Isoform Testis-specific]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P12821}; Note=Isoform Testis-specific only binds 1 Zn(2+... | angiotensin maturation [GO:0002003]; bradykinin catabolic process [GO:0010815]; hormone catabolic process [GO:0042447]; hormone metabolic process [GO:0042445]; kidney development [GO:0001822]; positive regulation of systemic arterial blood pressure [GO:0003084]; regulation of blood pressure [GO:0008217]; regulation of ... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | calmodulin binding [GO:0005516]; carboxypeptidase activity [GO:0004180]; chloride ion binding [GO:0031404]; metal ion binding [GO:0046872]; metallodipeptidase activity [GO:0070573]; metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; peptidyl-dipeptidase activity [GO:0008241] | PF01401; | 1.10.1370.30; | Peptidase M2 family | PTM: N-glycosylated. {ECO:0000269|PubMed:1654880}.; PTM: Phosphorylated by CK2 on Ser-1303; which allows membrane retention (By similarity). Phosphorylated on tyrosine residues on its extracellular part, promoting cleavage by secretase enzymes and formation of the soluble form (Angiotensin-converting enzyme, soluble fo... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12821}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P09470}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000250|UniProtKB:P09470}.; SUBCELLULAR LOCATION: [Angiotensin-converting enzyme, soluble fo... | CATALYTIC ACTIVITY: Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.; EC=3.4.15.1; Evidence={ECO:0000269|PubMed:7902354... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.6 mM for Hip-His-Leu {ECO:0000269|PubMed:7902354}; KM=0.09 mM for angiotensin I {ECO:0000269|PubMed:7902354}; | null | null | null | FUNCTION: Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:7902354, PubMed:8171037). Compo... | Oryctolagus cuniculus (Rabbit) |
P12823 | POLG_DEN2P | MNDQRKKARNTPFNMLKRERNRVSTVQQLTKRFSLGMLQGRGPLKLFMALVAFLRFLTIPPTAGILKRWGTIKKSKAINVLRGFRKEIGRMLNILNRRRRTAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTKDGTNMCTLMAMDLGELCEDTITYKCPFLKQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIETWILRHPGFTIMAAILAYTIGTTHFQRVLIFILLTAIAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPT... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont-mediated suppression of host cytoplasmic pattern recog... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell mitochondrion [GO:0033650]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:00550... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; prot... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;2.40.10.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P17763}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969) (DENV-2) |
P12825 | RASN_CAVPO | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMKKLNSNDDGTQGCMGLPCVVM | 3.6.5.2 | null | positive regulation of endothelial cell proliferation [GO:0001938]; Ras protein signal transduction [GO:0007265] | Golgi membrane [GO:0000139]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. Depalmitoylated by ABHD17A, ABHD17B and ABHD17C. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi. {ECO:0000250|UniProtKB:P01111}.; PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01111}; Lipid-anchor {ECO:0000250|UniProtKB:P01111}; Cytoplasmic side {ECO:0000250|UniProtKB:P01111}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P01111}; Lipid-anchor {ECO:0000250|UniProtKB:P01111}. Note=Shuttles between the plasma membrane and the Golgi ... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01116}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. {ECO:0000250|UniProtKB:P01111}. | Cavia porcellus (Guinea pig) |
P12829 | MYL4_HUMAN | MAPKKPEPKKEAAKPAPAPAPAPAPAPAPAPEAPKEPAFDPKSVKIDFTADQIEEFKEAFSLFDRTPTGEMKITYGQCGDVLRALGQNPTNAEVLRVLGKPKPEEMNVKMLDFETFLPILQHISRNKEQGTYEDFVEGLRVFDKESNGTVMGAELRHVLATLGEKMTEAEVEQLLAGQEDANGCINYEAFVKHIMSG | null | null | cardiac muscle contraction [GO:0060048]; positive regulation of ATP-dependent activity [GO:0032781]; regulation of the force of heart contraction [GO:0002026] | A band [GO:0031672]; cytosol [GO:0005829]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; calcium ion binding [GO:0005509]; myosin II heavy chain binding [GO:0032038] | null | 1.10.238.10; | null | null | null | null | null | null | null | null | FUNCTION: Regulatory light chain of myosin. Does not bind calcium. | Homo sapiens (Human) |
P12830 | CADH1_HUMAN | MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTIN... | null | null | adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; cellular response ... | actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; apical junction complex [GO:0043296]; catenin complex [GO:0016342]; cell junction [GO:0030054]; cytoplasmic side of plasma membrane [GO:0009898]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; flotillin compl... | ankyrin binding [GO:0030506]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; cell adhesion molecule binding [GO:0050839]; gamma-catenin binding [GO:0045295]; GTPase activating protein binding [GO:0032794]; identical protein binding [GO:0042802]; protein tyrosine kina... | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | PTM: During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (PubMed:10597309, PubMed:11076937, PubMed:11953314). Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release ... | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000269|PubMed:27760340, ECO:0000269|PubMed:28169360}. Cell membrane {ECO:0000269|PubMed:19403558, ECO:0000269|PubMed:28301459}; Single-pass type I membrane protein. Endosome {ECO:0000269|PubMed:15689490}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubM... | null | null | null | null | null | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility a... | Homo sapiens (Human) |
P12838 | DEF4_HUMAN | MRIIALLAAILLVALQVRAGPLQARGDEAPGQEQRGPEDQDISISFAWDKSSALQVSGSTRGMVCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRVD | null | null | antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; antimicrobial humoral response [GO:0019730]; cellular response to lipopolysaccharide [GO:0071222]; defense response to fungus [GO:0050832]; defense... | azurophil granule [GO:0042582]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; specific granule lumen [GO:0035580]; transport vesicle [GO:0030133] | protein homodimerization activity [GO:0042803] | PF00323;PF00879; | null | Alpha-defensin family | PTM: The three-dimensional structure formed by the three intramolecular disulfide bridges is indispensable for effective bacterial killing. {ECO:0000269|PubMed:17088326, ECO:0000269|PubMed:30658057}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01523}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:2500436, ECO:0000269|PubMed:2501794}. Note=Stored as mature peptide in neutrophil granules. {ECO:0000269|PubMed:2500436}. | null | null | null | null | null | FUNCTION: Host-defense peptide that has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi (PubMed:15317502, PubMed:15616305, PubMed:2500436, PubMed:2501794, PubMed:30658057). Exhibits antimicrobial activity against Gram-negative E.coli and E.aero... | Homo sapiens (Human) |
P12839 | NFM_RAT | MSYTLDSLGNPSAYRRVPTETRSSFSRVSGSPSSGFRSQSWSRGSPSTVSSSYKRSALAPRLAYSSAMLSSAESSLDFSQSSSLLNGGSGGDYKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIHALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRAVRKDIEESSMVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYR... | null | null | axo-dendritic transport [GO:0008088]; axon regeneration [GO:0031103]; cellular response to estradiol stimulus [GO:0071392]; cellular response to oxidative stress [GO:0034599]; cerebral cortex development [GO:0021987]; hippocampus development [GO:0021766]; intermediate filament bundle assembly [GO:0045110]; intermediate... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intermediate filament [GO:0005882]; neurofibrillary tangle [GO:0097418]; neurofilament [GO:0005883]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; perikaryon [GO:0043204]; postsynaptic density [GO:0014069]; postsynaptic interme... | protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; structural constituent of cytoskeleton [GO:0005200]; toxic substance binding [GO:0015643] | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: There are a number of repeats of the tripeptide K-S-P, NFM is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFM results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber. {ECO:0000269|PubMed:1537832}.; PTM: Phosp... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08553}. Cell projection, axon {ECO:0000250|UniProtKB:P08553}. | null | null | null | null | null | FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniP... | Rattus norvegicus (Rat) |
P12841 | FOS_RAT | MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNTQDFCADLSVSSANFIPTVTAISTSPDLQWLVQPTLVSSVAPSQTRAPHPYGLPTPSTGAYARAGVVKTMSGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPNDLGFPEEMSVTSLDLTGGLPEATTPESEEAFTLPLLNDPEPKPSLEPVKNISNMELKAEPFDDFLFPASSRPSGSETARSVPDVDLSGSFYAADWEPLHSSSLGMGPMVTEL... | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to calcium ion [GO:0071277]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to extracellular stimulus [GO:0031668]; cellular response to hormone stimulus [GO:0032870]; cellular response to hypoxia [GO:0071456]; cellu... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:000... | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | PTM: Phosphorylated in the C-terminal upon stimulation by nerve growth factor (NGF) and epidermal growth factor (EGF) (By similarity). Phosphorylated, in vitro, by MAPK and RSK1. Phosphorylation on both Ser-362 and Ser-374 by MAPK1/2 and RSK1/2 leads to protein stabilization with phosphorylation on Ser-374 being the ma... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucle... | null | null | null | null | null | FUNCTION: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling (By similarity). Has a critical function in regulati... | Rattus norvegicus (Rat) |
P12843 | IBP2_RAT | MLPRLGGPALPLLLPSLLLLLLLGAGGCGPGVRAEVLFRCPPCTPERLAACGPPPDAPCAELVREPGCGCCSVCARQEGEACGVYIPRCAQTLRCYPNPGSELPLKALVTGAGTCEKRRVGATPQQVADSEDDHSEGGLVENHVDGTMNMLGGSSAGRKPPKSGMKELAVFREKVNEQHRQMGKGAKHLSLEEPKKLRPPPARTPCQQELDQVLERISTMRLPDDRGPLEHLYSLHIPNCDKHGLYNLKQCKMSLNGQRGECWCVNPNTGKPIQGAPTIRGDPECHLFYNEQQENDGAHAQRVQ | null | null | cellular response to hormone stimulus [GO:0032870]; female pregnancy [GO:0007565]; positive regulation of activated T cell proliferation [GO:0042104]; regulation of insulin-like growth factor receptor signaling pathway [GO:0043567]; response to estradiol [GO:0032355]; response to estrogen [GO:0043627]; response to gluc... | apical plasma membrane [GO:0016324]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | insulin-like growth factor binding [GO:0005520]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995] | PF00219;PF00086; | 4.10.40.20;4.10.800.10; | null | PTM: O-glycosylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2426267, ECO:0000269|PubMed:2480123, ECO:0000269|PubMed:2538475}. | null | null | null | null | null | FUNCTION: Inhibits IGF-mediated growth and developmental rates (By similarity). IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. {ECO:0... | Rattus norvegicus (Rat) |
P12844 | MYO3_CAEEL | MSGNPDAFENDPGFPFLGISREARAATAARPFDSKKNCWIPDPEDGFVAAEIQSTTGEQVTVVTVKGNQITVKKDQCQEMNPPKFDKTEDMANLTFLNEASVLGNLKDRYKDLMIYTYSGLFCVVINPYKRLPIYSESVIKHFMGKRRNEMPPHLFAVSDEAYRNMVQDKENQSMLITGESGAGKTENTKKVISYFAIVGATQAASGKEAKDGKKGGTLEEQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRTHFSGSGKLAGGDIEHYLLEKSRVVRQAPGERCYHIFYQIMSGNDPSLRGKLKLSNDITYYHFCSQAE... | null | null | locomotory behavior [GO:0007626]; muscle contraction [GO:0006936]; positive regulation of ovulation [GO:0060279]; sarcomere organization [GO:0045214] | A band [GO:0031672]; cytoplasm [GO:0005737]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; striated muscle myosin thick filament [GO:0005863] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; cytoskeletal motor activity [GO:0003774]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:6352051}. Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:6352051}. Note=In myoepithelial sheath cells, forms filaments assembled in a nonstriated meshwork. Colocalizes with unc-15/paramy... | null | null | null | null | null | FUNCTION: Essential for muscle contraction (PubMed:2583106). Involved in ovulation likely by regulating the contraction of gonadal myoepithelial sheath cells (PubMed:17326220). {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:2583106}. | Caenorhabditis elegans |
P12845 | MYO2_CAEEL | MDYENDPGWKYLRRSREEMLQDQSRAYDSKKNVWIPDSEDGYIEGVITKTAGDNVTVSIGQGAEKTVKKDVVQEMNPPKFEKTEDMSNLTFLNDASVLYNLKARYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDEAYRNMLQNHENQSMLITGESGAGKTENTKKVISYFAAVGAAQQETFGAKKAATEEDKNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFSKQGRVASCDIEHYLLEKSRVIRQAPGERCYHIFYQVFSDYLPNLKKDLLLNKPVKDYWFIAQA... | null | null | muscle contraction [GO:0006936]; sarcomere organization [GO:0045214] | cytoplasm [GO:0005737]; muscle myosin complex [GO:0005859]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; sarcomere [GO:0030017] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Caenorhabditis elegans |
P12847 | MYH3_RAT | MSSDTEMEVFGIAAPFLRKSEKERIEAQNQPFDAKTYCFVVDSKEEYAKGKIKSSQDGKVTVETEDNRTLVVKPEDVYAMNPPKFDKIEDMAMLTHLNEPAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYTPEVVDGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYDYPFISQGEIL... | null | null | ATP metabolic process [GO:0046034]; muscle contraction [GO:0006936]; skeletal muscle contraction [GO:0003009] | contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Rattus norvegicus (Rat) |
P12849 | KAP1_MOUSE | MASPSCFHSEDEDSLKGCEMYVQKHGIQQVLKECIVHLCVAKPDRPLRFLREHFEKLEKEENRQILARQKSNSQCDSHDEEISPTPPNPVVKARRRRGGVSAEVYTEEDAVSYVRKVIPKDYKTMTALAKAISKNVLFSHLDDNERSDIFDAMFPVTHIGGETVIQQGNEGDNFYVIDQGEVDVYVNGEWVTNISEGGSFGELALIYGTPRAATVKAKTDLKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLEKWERLTVADALEPVQFEDGEKIVVQGEPGDDFYIITEGTASVLQRRSPNEEYVEVGRLGP... | null | null | animal organ morphogenesis [GO:0009887]; learning or memory [GO:0007611]; modulation of chemical synaptic transmission [GO:0050804]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of fear response [GO:1903367]; positive regulation of long-term synaptic potentiation [GO:190027... | cAMP-dependent protein kinase complex [GO:0005952]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; multivesicular body [GO:0005771]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; Schaffer collateral - CA1 synapse [GO:00986... | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; cAMP-dependent protein kinase regulator activity [GO:0008603]; protein kinase A catalytic subunit binding [GO:0034236] | PF00027;PF02197; | 1.20.890.10;2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. {ECO:0000250}. | Mus musculus (Mouse) |
P12850 | GROA_MOUSE | MIPATRSLLCAALLLLATSRLATGAPIANELRCQCLQTMAGIHLKNIQSLKVLPSGPHCTQTEVIATLKNGREACLDPEAPLVQKIVQKMLKGVPK | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to interleukin-17 [GO:0097398]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; inflammatory response [GO:0006954]; neutrophil chemotaxis [GO:0030593]; positiv... | extracellular space [GO:0005615] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; growth factor activity [GO:0008083] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | PTM: The N-terminal processed form KC(5-72) is produced by proteolytic cleavage after secretion from bone marrow stromal cells. {ECO:0000269|PubMed:10725737}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Has chemotactic activity for neutrophils. Contributes to neutrophil activation during inflammation (By similarity). Hematoregulatory chemokine, which, in vitro, suppresses hematopoietic progenitor cell proliferation. KC(5-72) shows a highly enhanced hematopoietic activity. {ECO:0000250, ECO:0000269|PubMed:107... | Mus musculus (Mouse) |
P12866 | STE6_YEAST | MNFLSFKTTKHYHIFRYVNIRNDYRLLMIMIIGTVATGLVPAITSILTGRVFDLLSVFVANGSHQGLYSQLVQRSMAVMALGAASVPVMWLSLTSWMHIGERQGFRIRSQILEAYLEEKPMEWYDNNEKLLGDFTQINRCVEELRSSSAEASAITFQNLVAICALLGTSFYYSWSLTLIILCSSPIITFFAVVFSRMIHVYSEKENSETSKAAQLLTWSMNAAQLVRLYCTQRLERKKFKEIILNCNTFFIKSCFFVAANAGILRFLTLTMFVQGFWFGSAMIKKGKLNINDVITCFHSCIMLGSTLNNTLHQIVVLQKG... | 7.4.2.7 | null | peptide pheromone export [GO:0000770]; response to pheromone [GO:0019236] | fungal-type vacuole [GO:0000324]; Golgi apparatus [GO:0005794]; mating projection tip [GO:0043332]; plasma membrane [GO:0005886] | ABC-type oligopeptide transporter activity [GO:0015421]; ABC-type peptide transporter activity [GO:0015440]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily, Alpha-factor sex pheromone exporter (TC 3.A.1.206) family | PTM: Degraded via the ubiquitin system. {ECO:0000269|PubMed:8045256}. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=an [alpha-factor](in) + ATP + H2O = ADP + an [alpha-factor](out) + H(+) + phosphate; Xref=Rhea:RHEA:10848, Rhea:RHEA-COMP:11611, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83228, ChEBI:CHEBI:456216; EC=7.4.2.7; | null | null | null | null | FUNCTION: STE6 is required in yeast MATA cells for production of A-factor pheromone. STE6 is involved in the transport of the farnesyl-derivation of the A-factor pheromone. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12868 | PEP5_YEAST | MSLSSWRQFQLFENIPIRDPNFGGDSLLYSDPTLCAATIVDPQTLIIAVNSNIIKVVKLNQSQVIHEFQSFPHDFQITFLKVINGEFLVALAESIGKPSLIRVYKLEKLPNREQLYHSQVELKNGNNTYPISVVSISNDLSCIVVGFINGKIILIRGDISRDRGSQQRIIYEDPSKEPITALFLNNDATACFAATTSRILLFNTTGRNRGRPSLVLNSKNGLDLNCGSFNPATNEFICCLSNFIEFFSSSGKKHQFAFDLSLRKRIFCVDKDHILIVTEETGVPTTSISVNELSPTIINRIFIIDAKNKIISLNFVVSSA... | 2.3.2.27 | null | endosome organization [GO:0007032]; Golgi to endosome transport [GO:0006895]; histone catabolic process [GO:0036205]; intracellular protein transport [GO:0006886]; late endosome to vacuole transport [GO:0045324]; organelle fusion [GO:0048284]; regulation of SNARE complex assembly [GO:0035542]; regulation of vacuole fus... | CORVET complex [GO:0033263]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; fungal-type vacuole membrane [GO:0000329]; HOPS complex [GO:0030897] | metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin protein ligase activity [GO:0061630] | PF12451; | 2.130.10.10;3.30.40.10; | VPS11 family | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10944212}; Peripheral membrane protein {ECO:0000269|PubMed:10944212}; Cytoplasmic side {ECO:0000269|PubMed:10944212}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:22570702}; | null | null | null | null | FUNCTION: Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. It is required for gluconeogenic growth of yeast. Acts as a component of the HOPS compl... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12870 | CAPSD_FHV | MVNNNRPRRQRAQRVVVTTTQTAPVPQQNVPRNGRRRRNRTRRNRRRVRGMNMAALTRLSQPGLAFLKCAFAPPDFNTDPGKGIPDRFEGKVVSRKDVLNQSISFTAGQDTFILIAPTPGVAYWSASVPAGTFPTSATTFNPVNYPGFTSMFGTTSTSRSDQVSSFRYASMNVGIYPTSNLMQFAGSITVWKCPVKLSTVQFPVATDPATSSLVHTLVGLDGVLAVGPDNFSESFIKGVFSQSACNEPDFEFNDILEGIQTLPPANVSLGSTGQPFTMDSGAEATSGVVGWGNMDTIVIRVSAPEGAVNSAILKAWSCIE... | 3.4.23.44 | null | permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; proteolysis [GO:0006508]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008] | T=3 icosahedral viral capsid [GO:0039617] | aspartic-type endopeptidase activity [GO:0004190]; metal ion binding [GO:0046872] | PF01829; | 2.60.120.20; | Peptidase A6 family | PTM: [Capsid protein alpha]: Capsid protein alpha autocatalytically maturates into capsid protein beta and peptide gamma. {ECO:0000269|PubMed:1404613, ECO:0000269|PubMed:19553341}. | SUBCELLULAR LOCATION: [Capsid protein beta]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Membrane-lytic peptide gamma]: Virion {ECO:0000305}. Note=Located inside the capsid and probably externalized in early endosomes. {ECO:0000305}. | CATALYTIC ACTIVITY: [Capsid protein beta]: Reaction=Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-.; EC=3.4.23.44; Evidence={ECO:0000269|PubMed:1404613}; | null | null | null | null | FUNCTION: [Capsid protein alpha]: Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, 240 calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Caps... | Flock house virus (FHV) |
P12881 | PSA1_DROME | MFRNQYDSDVTVWSPQGRLHQVEYAMEAVKLGTATVGLKNKDYAVLVALCKPTSELSDTQRKIIPIDDHLGISIAGLTADARVLSRYLRSECLNYKHSYDTTYPVSRLITNLGNKMQTTTQRYDRRPYGVGLLVAGYDERGPHIYQVTPSATFFNCKANSIGSRSQSARTYLEKNLNKFLDSSKDEIIRHGIRAILGTLPTDEQGKDAGQYDITVAIVGKDQPFTILSNKDSAKHVAIAKENDNDTPRNDDDDDRPSPPEEPAAGPRDPEVLVATEQRP | null | null | determination of adult lifespan [GO:0008340]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; ventral furrow formation [GO:0007370] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex, alpha-subunit complex [GO:0019773] | null | PF00227;PF10584; | 3.60.20.10; | Peptidase T1A family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. | Drosophila melanogaster (Fruit fly) |
P12882 | MYH1_HUMAN | MSSDSEMAIFGEAAPFLRKSERERIEAQNKPFDAKTSVFVVDPKESFVKATVQSREGGKVTAKTEAGATVTVKDDQVFPMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGEKKKEEVTSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFVSQGE... | null | null | muscle contraction [GO:0006936] | A band [GO:0031672]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; intercalated disc [GO:0014704]; muscle myosin complex [GO:0005859]; myosin filament [GO:0032982]; myosin II complex [GO:0016460] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Homo sapiens (Human) |
P12883 | MYH7_HUMAN | MGDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTV... | null | null | adult heart development [GO:0007512]; ATP metabolic process [GO:0046034]; cardiac muscle contraction [GO:0060048]; cardiac muscle hypertrophy in response to stress [GO:0014898]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; regulation of heart rate [GO:0002027]; regulation of slow-twitch skelet... | cytoplasm [GO:0005737]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; sarcomere [GO:0030017]; stress fiber [GO:0001725]; Z disc [GO:0030018] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000250|UniProtKB:P02564}. Cytoplasm, myofibril, sarcomere {ECO:0000250|UniProtKB:P02564}. Note=Thick filaments of the myofibrils. {ECO:0000250|UniProtKB:P02564}. | null | null | null | null | null | FUNCTION: Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305|PubMed:26150528, ECO:0000305|PubMed:26246073}. | Homo sapiens (Human) |
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