Biological Process stringlengths 7 1.01k | Cellular Component stringlengths 6 867 | Molecular Function stringlengths 11 871 | Organism stringlengths 8 73 | Keywords stringlengths 1 810 | Sequence 10 stringlengths 5 10 | Sequence stringlengths 5 1.02k | Combined stringlengths 136 3.91k |
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fatty acid beta-oxidation fatty acid beta-oxidation using acyl-CoA oxidase medium-chain fatty acid metabolic process | extracellular region; peroxisome | acyl-CoA oxidase activity FAD binding | Arabidopsis thaliana | FAD Fatty acid metabolism Flavoprotein Lipid metabolism Oxidoreductase Peroxisome Reference proteome Transit peptide | MSDNRALRRA | MSDNRALRRAHVLANHILQSNPPSSNPSLSRELCLQYSPPELNESYGFDVKEMRKLLDGHNVVDRDWIYGLMMQSNLFNRKERGGKIFVSPDYNQTMEQQREITMKRIWYLLENGVFKGWLTETGPEAELRKLALLEVCGIYDHSVSIKVGVHFFLWGNAVKFFGTKRHHEKWLKNTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGTNQGVHAFIAQIRDQDGSICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNAVADVSSDGKYVSSIKDPDQRFGAFMAPLTSGRVTIASSAIYSAKVGLSIAIRYSLSRRAFSVTANGPEVLLLDYPSHQRRLLPLLAKTYAMSFAANELKMIYVKRTPETNKAIHVVSSGFKAVLTWHNMHTLQECREAVGGQGVKTENLVGQLKGEFDVQTTFEGDNNVLMQQVSKALFAEYVSCKKRNKPFKGLGLEHMNSPRPVLPTQLTSSTLRCSQFQTNVFCLRERDLLEQFTSEVAQLQGRGESREFSFLLSHQLAEDLGKAFTEKAILQTILDAEAKLPTGSVKDVLGLVRSMYALISLEEDPSLLRYGYLSQDNVGDVRREVSKLCGELRPHALALVTSFGIPDSFLSPIAFNWVEANAWSSV | fatty acid beta-oxidation fatty acid beta-oxidation using acyl-CoA oxidase medium-chain fatty acid metabolic process extracellular region; peroxisome acyl-CoA oxidase activity FAD binding Arabidopsis thaliana FAD Fatty acid metabolism Flavoprotein Lipid metabolism Oxidoreductase Peroxisome Reference proteome Transit peptide MSDNRALRRA MSDNRALRRAHVLANHILQSNPPSSNPSLSRELCLQYSPPELNESYGFDVKEMRKLLDGHNVVDRDWIYGLMMQSNLFNRKERGGKIFVSPDYNQTMEQQREITMKRIWYLLENGVFKGWLTETGPEAELRKLALLEVCGIYDHSVSIKVGVHFFLWGNAVKFFGTKRHHEKWLKNTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGTNQGVHAFIAQIRDQDGSICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNAVADVSSDGKYVSSIKDPDQRFGAFMAPLTSGRVTIASSAIYSAKVGLSIAIRYSLSRRAFSVTANGPEVLLLDYPSHQRRLLPLLAKTYAMSFAANELKMIYVKRTPETNKAIHVVSSGFKAVLTWHNMHTLQECREAVGGQGVKTENLVGQLKGEFDVQTTFEGDNNVLMQQVSKALFAEYVSCKKRNKPFKGLGLEHMNSPRPVLPTQLTSSTLRCSQFQTNVFCLRERDLLEQFTSEVAQLQGRGESREFSFLLSHQLAEDLGKAFTEKAILQTILDAEAKLPTGSVKDVLGLVRSMYALISLEEDPSLLRYGYLSQDNVGDVRREVSKLCGELRPHALALVTSFGIPDSFLSPIAFNWVEANAWSSV |
evasion of host immune response programmed cell death induced by symbiont proteolysis symbiont-mediated suppression of host autophagy | extracellular region; host cell cytosol; host extracellular space | cysteine-type endopeptidase activity toxin activity | Streptococcus pyogenes serotype M3 | Autocatalytic cleavage Host cytoplasm Hydrolase Methylation Protease Secreted Signal Thiol protease Toxin Virulence Zymogen | MNKKKLGIRL | MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP | evasion of host immune response programmed cell death induced by symbiont proteolysis symbiont-mediated suppression of host autophagy extracellular region; host cell cytosol; host extracellular space cysteine-type endopeptidase activity toxin activity Streptococcus pyogenes serotype M3 Autocatalytic cleavage Host cytoplasm Hydrolase Methylation Protease Secreted Signal Thiol protease Toxin Virulence Zymogen MNKKKLGIRL MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP |
de novo' pyrimidine nucleobase biosynthetic process 'de novo' UMP biosynthetic process | cytoplasm | dihydroorotate dehydrogenase (NADH) activity | Enterococcus faecalis | Cytoplasm Flavoprotein FMN NAD Oxidoreductase Pyrimidine biosynthesis Reference proteome | MMKNPLAVSI | MMKNPLAVSIPGLTLKNPIIPASGCFGFGEEYANYYDLDQLGSIMIKATTPQARYGNPTPRVAETPSGMLNAIGLQNPGLEVVMQEKLPKLEKYPNLPIIANVAGACEEDYVAVCAKIGQAPNVKAIELNISCPNVKHGGIAFGTDPEVAFQLTQAVKKVASVPIYVKLSPNVTDIVPIAQAIEAGGADGFSMINTLLGMRIDLKTRKPILANQTGGLSGPAIKPVAIRLIRQVASVSQLPIIGMGGVQTVDDVLEMFMAGASAVGVGTANFTDPYICPKLIDGLPKRMEELGIESLEQLIKEVREGQQNAR | de novo' pyrimidine nucleobase biosynthetic process 'de novo' UMP biosynthetic process cytoplasm dihydroorotate dehydrogenase (NADH) activity Enterococcus faecalis Cytoplasm Flavoprotein FMN NAD Oxidoreductase Pyrimidine biosynthesis Reference proteome MMKNPLAVSI MMKNPLAVSIPGLTLKNPIIPASGCFGFGEEYANYYDLDQLGSIMIKATTPQARYGNPTPRVAETPSGMLNAIGLQNPGLEVVMQEKLPKLEKYPNLPIIANVAGACEEDYVAVCAKIGQAPNVKAIELNISCPNVKHGGIAFGTDPEVAFQLTQAVKKVASVPIYVKLSPNVTDIVPIAQAIEAGGADGFSMINTLLGMRIDLKTRKPILANQTGGLSGPAIKPVAIRLIRQVASVSQLPIIGMGGVQTVDDVLEMFMAGASAVGVGTANFTDPYICPKLIDGLPKRMEELGIESLEQLIKEVREGQQNAR |
defense response to bacterium protein autophosphorylation recognition of pollen | plasma membrane | ATP binding calmodulin binding carbohydrate binding protein serine kinase activity protein serine/threonine kinase activity ubiquitin protein ligase binding | Arabidopsis thaliana | ATP-binding Cell membrane Disulfide bond Glycoprotein Kinase Lectin Membrane Nucleotide-binding Phosphoprotein Receptor Serine/threonine-protein kinase Signal Transferase Transmembrane Transmembrane helix | MRGELPNKHH | MRGELPNKHHSYTFFVFLFFFLILFPDLSISVNTLSATESLTISSNKTIVSPGGVFELGFFRILGDSWYLGIWYKKISQRTYVWVANRDTPLSNPIGILKISNANLVILDNSDTHVWSTNLTGAVRSSVVAELLDNGNFVLRGSKINESDEFLWQSFDFPTDTLLPQMKLGRDHKRGLNRFVTSWKSSFDPSSGSFMFKLETLGLPEFFGFTSFLEVYRSGPWDGLRFSGILEMQQWDDIIYNFTENREEVAYTFRVTDHNSYSRLTINTVGRLEGFMWEPTQQEWNMFWFMPKDTCDLYGICGPYAYCDMSTSPTCNCIKGFQPLSPQDWASGDVTGRCRRKTQLTCGEDRFFRLMNMKIPATTAAIVDKRIGLKECEEKCKTHCNCTAYANSDIRNGGSGCIIWIGEFRDIRNYAADGQDLFVRLAAAEFGERRTIRGKIIGLIIGISLMLVLSFIIYCFWKKKQKRARATAAPIGYRDRIQELIITNGVVMSSGRRLLGEEEDLELPLTEFETVVMATENFSDSNILGRGGFGIVYKGRLLDGQEIAVKRLSEMSSQGTNEFKNEVRLIARLQHINLVRLLSCCIYADEKILIYEYLENGSLDSHLFETTQSSNKLNWQTRFSIINGIARGLLYLHQDSRFKIIHRDLKASNVLLDKNMTPKISDFGMARIFERDETEANTRKVVGTYGYMSPEYAMEGIFSVKSDVFSFGVLVLEIVSGKRNRGFHNSGQDNNLLGYTWENWKEGKGLEIVDSIIVDSSSSMSLFQPHEVLRCIQIGLLCVQERAEDRPKMSSVVLMLGSEKGEIPQPKRPGYCVGRSSLDTADSSSSTKRDSESLTVNQITVSVINAR | defense response to bacterium protein autophosphorylation recognition of pollen plasma membrane ATP binding calmodulin binding carbohydrate binding protein serine kinase activity protein serine/threonine kinase activity ubiquitin protein ligase binding Arabidopsis thaliana ATP-binding Cell membrane Disulfide bond Glycoprotein Kinase Lectin Membrane Nucleotide-binding Phosphoprotein Receptor Serine/threonine-protein kinase Signal Transferase Transmembrane Transmembrane helix MRGELPNKHH MRGELPNKHHSYTFFVFLFFFLILFPDLSISVNTLSATESLTISSNKTIVSPGGVFELGFFRILGDSWYLGIWYKKISQRTYVWVANRDTPLSNPIGILKISNANLVILDNSDTHVWSTNLTGAVRSSVVAELLDNGNFVLRGSKINESDEFLWQSFDFPTDTLLPQMKLGRDHKRGLNRFVTSWKSSFDPSSGSFMFKLETLGLPEFFGFTSFLEVYRSGPWDGLRFSGILEMQQWDDIIYNFTENREEVAYTFRVTDHNSYSRLTINTVGRLEGFMWEPTQQEWNMFWFMPKDTCDLYGICGPYAYCDMSTSPTCNCIKGFQPLSPQDWASGDVTGRCRRKTQLTCGEDRFFRLMNMKIPATTAAIVDKRIGLKECEEKCKTHCNCTAYANSDIRNGGSGCIIWIGEFRDIRNYAADGQDLFVRLAAAEFGERRTIRGKIIGLIIGISLMLVLSFIIYCFWKKKQKRARATAAPIGYRDRIQELIITNGVVMSSGRRLLGEEEDLELPLTEFETVVMATENFSDSNILGRGGFGIVYKGRLLDGQEIAVKRLSEMSSQGTNEFKNEVRLIARLQHINLVRLLSCCIYADEKILIYEYLENGSLDSHLFETTQSSNKLNWQTRFSIINGIARGLLYLHQDSRFKIIHRDLKASNVLLDKNMTPKISDFGMARIFERDETEANTRKVVGTYGYMSPEYAMEGIFSVKSDVFSFGVLVLEIVSGKRNRGFHNSGQDNNLLGYTWENWKEGKGLEIVDSIIVDSSSSMSLFQPHEVLRCIQIGLLCVQERAEDRPKMSSVVLMLGSEKGEIPQPKRPGYCVGRSSLDTADSSSSTKRDSESLTVNQITVSVINAR |
protein transport vesicle-mediated transport | Golgi apparatus; mitochondrion; plant-type vacuole; plasma membrane | GTP binding GTPase activity mRNA binding phospholipase activator activity | Arabidopsis thaliana | ER-Golgi transport Golgi apparatus GTP-binding Lipoprotein Myristate Nucleotide-binding Protein transport Reference proteome Transport | MGLSFAKLFS | MGLSFAKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIAGKA | protein transport vesicle-mediated transport Golgi apparatus; mitochondrion; plant-type vacuole; plasma membrane GTP binding GTPase activity mRNA binding phospholipase activator activity Arabidopsis thaliana ER-Golgi transport Golgi apparatus GTP-binding Lipoprotein Myristate Nucleotide-binding Protein transport Reference proteome Transport MGLSFAKLFS MGLSFAKLFSRLFAKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRQRHWYIQSTCATSGEGLYEGLDWLSNNIAGKA |
hydrogen peroxide catabolic process response to oxidative stress | extracellular region; plant-type cell wall; plasmodesma | heme binding lactoperoxidase activity metal ion binding | Arabidopsis thaliana | Calcium Disulfide bond Glycoprotein Heme Hydrogen peroxide Iron Metal-binding Oxidoreductase Peroxidase Reference proteome Secreted Signal | MAIKNILALV | MAIKNILALVVLLSVVGVSVAIPQLLDLDYYRSKCPKAEEIVRGVTVQYVSRQKTLAAKLLRMHFHDCFVRGCDGSVLLKSAKNDAERDAVPNLTLKGYEVVDAAKTALERKCPNLISCADVLALVARDAVAVIGGPWWPVPLGRRDGRISKLNDALLNLPSPFADIKTLKKNFANKGLNAKDLVVLSGGHTIGISSCALVNSRLYNFTGKGDSDPSMNPSYVRELKRKCPPTDFRTSLNMDPGSALTFDTHYFKVVAQKKGLFTSDSTLLDDIETKNYVQTQAILPPVFSSFNKDFSDSMVKLGFVQILTGKNGEIRKRCAFPN | hydrogen peroxide catabolic process response to oxidative stress extracellular region; plant-type cell wall; plasmodesma heme binding lactoperoxidase activity metal ion binding Arabidopsis thaliana Calcium Disulfide bond Glycoprotein Heme Hydrogen peroxide Iron Metal-binding Oxidoreductase Peroxidase Reference proteome Secreted Signal MAIKNILALV MAIKNILALVVLLSVVGVSVAIPQLLDLDYYRSKCPKAEEIVRGVTVQYVSRQKTLAAKLLRMHFHDCFVRGCDGSVLLKSAKNDAERDAVPNLTLKGYEVVDAAKTALERKCPNLISCADVLALVARDAVAVIGGPWWPVPLGRRDGRISKLNDALLNLPSPFADIKTLKKNFANKGLNAKDLVVLSGGHTIGISSCALVNSRLYNFTGKGDSDPSMNPSYVRELKRKCPPTDFRTSLNMDPGSALTFDTHYFKVVAQKKGLFTSDSTLLDDIETKNYVQTQAILPPVFSSFNKDFSDSMVKLGFVQILTGKNGEIRKRCAFPN |
COPII vesicle coating endoplasmic reticulum to Golgi vesicle-mediated transport skeletal system development vesicle coating vesicle tethering | cytoplasm; cytosol; endoplasmic reticulum; endoplasmic reticulum-Golgi intermediate compartment; intracellular membrane-bounded organelle; nucleoplasm; nucleus; perinuclear region of cytoplasm; TRAPP complex; TRAPPII protein complex; TRAPPIII protein complex | transmembrane transporter binding | Homo sapiens | Alternative splicing Cytoplasm Disease variant ER-Golgi transport Nucleus Phosphoprotein Reference proteome Transcription Transport | MSGSFYFVIV | MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGHMRFIMLHDIRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS | COPII vesicle coating endoplasmic reticulum to Golgi vesicle-mediated transport skeletal system development vesicle coating vesicle tethering cytoplasm; cytosol; endoplasmic reticulum; endoplasmic reticulum-Golgi intermediate compartment; intracellular membrane-bounded organelle; nucleoplasm; nucleus; perinuclear region of cytoplasm; TRAPP complex; TRAPPII protein complex; TRAPPIII protein complex transmembrane transporter binding Homo sapiens Alternative splicing Cytoplasm Disease variant ER-Golgi transport Nucleus Phosphoprotein Reference proteome Transcription Transport MSGSFYFVIV MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGHMRFIMLHDIRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS |
COPII vesicle coating endoplasmic reticulum to Golgi vesicle-mediated transport positive regulation of gene expression vesicle coating vesicle tethering | cytoplasm; endoplasmic reticulum; endoplasmic reticulum-Golgi intermediate compartment; intracellular membrane-bounded organelle; nuclear outer membrane; nucleoplasm; nucleus; perinuclear region of cytoplasm; TRAPP complex; TRAPPII protein complex; TRAPPIII protein complex | transcription corepressor binding transcription regulator inhibitor activity | Homo sapiens | Cytoplasm ER-Golgi transport Nucleus Phosphoprotein Reference proteome Transcription Transport | MSGSFYFVIV | MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGHMRFIMLHDIRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS | COPII vesicle coating endoplasmic reticulum to Golgi vesicle-mediated transport positive regulation of gene expression vesicle coating vesicle tethering cytoplasm; endoplasmic reticulum; endoplasmic reticulum-Golgi intermediate compartment; intracellular membrane-bounded organelle; nuclear outer membrane; nucleoplasm; nucleus; perinuclear region of cytoplasm; TRAPP complex; TRAPPII protein complex; TRAPPIII protein complex transcription corepressor binding transcription regulator inhibitor activity Homo sapiens Cytoplasm ER-Golgi transport Nucleus Phosphoprotein Reference proteome Transcription Transport MSGSFYFVIV MSGSFYFVIVGHHDNPVFEMEFLPAGKAESKDDHRHLNQFIAHAALDLVDENMWLSNNMYLKTVDKFNEWFVSAFVTAGHMRFIMLHDIRQEDGIKNFFTDVYDLYIKFSMNPFYEPNSPIRSSAFDRKVQFLGKKHLLS |
apoptotic process defense response to bacterium killing of cells of another organism | extracellular region | L-phenylalaine oxidase activity toxin activity | Bothrops jararaca | Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Secreted Toxin | ADDKNPLEEC | ADDKNPLEECFRETDYEEFLEIARNGLKATSNPKRVV | apoptotic process defense response to bacterium killing of cells of another organism extracellular region L-phenylalaine oxidase activity toxin activity Bothrops jararaca Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Secreted Toxin ADDKNPLEEC ADDKNPLEECFRETDYEEFLEIARNGLKATSNPKRVV |
apoptotic process defense response to bacterium killing of cells of another organism | extracellular region | L-phenylalaine oxidase activity toxin activity | Bothrops leucurus | Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Platelet aggregation inhibiting toxin Secreted Toxin | ADDRNPLEEC | ADDRNPLEECFRETDYEEFLEIAKNGLSTT | apoptotic process defense response to bacterium killing of cells of another organism extracellular region L-phenylalaine oxidase activity toxin activity Bothrops leucurus Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Platelet aggregation inhibiting toxin Secreted Toxin ADDRNPLEEC ADDRNPLEECFRETDYEEFLEIAKNGLSTT |
apoptotic process defense response to bacterium killing of cells of another organism | extracellular region | L-phenylalaine oxidase activity toxin activity | Daboia russelii | Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Secreted Toxin | ADDKNPLEEC | ADDKNPLEECFCEDDDYCEG | apoptotic process defense response to bacterium killing of cells of another organism extracellular region L-phenylalaine oxidase activity toxin activity Daboia russelii Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Secreted Toxin ADDKNPLEEC ADDKNPLEECFCEDDDYCEG |
apoptotic process defense response to bacterium killing of cells of another organism | extracellular region | L-phenylalaine oxidase activity toxin activity | Naja oxiana | Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Platelet aggregation inhibiting toxin Secreted Toxin | DDRRSPLEEC | DDRRSPLEECFQQNDYEEFLEIARNSQLYQESLREDSSYHLSFIESLKSDALFSYEKKFWEADGIHGGKVINDLSLIHDLPKREIQALCYPSIKK | apoptotic process defense response to bacterium killing of cells of another organism extracellular region L-phenylalaine oxidase activity toxin activity Naja oxiana Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Platelet aggregation inhibiting toxin Secreted Toxin DDRRSPLEEC DDRRSPLEECFQQNDYEEFLEIARNSQLYQESLREDSSYHLSFIESLKSDALFSYEKKFWEADGIHGGKVINDLSLIHDLPKREIQALCYPSIKK |
adhesion of symbiont to host fungal-type cell wall organization induction by symbiont of defense-related host calcium ion flux induction by symbiont of host defense response nitrogen compound metabolic process protein catabolic process protein metabolic process proteolysis signal peptide processing transepithelial migration of symbiont in host | extracellular region; extracellular vesicle; fungal-type cell wall | aspartic-type endopeptidase activity metal ion binding | Candida albicans | Aspartyl protease Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Metal-binding Protease Reference proteome Secreted Signal Virulence Zinc Zymogen | MFLKNIFIAL | MFLKNIFIALAIALLVDATPTTTKRSAGFVALDFSVVKTPKAFPVTNGQEGKTSKRQAVPVTLHNEQVTYAADITVGSNNQKLNVIVDTGSSDLWVPDVNVDCQVTYSDQTADFCKQKGTYDPSGSSASQDLNTPFKIGYGDGSSSQGTLYKDTVGFGGVSIKNQVLADVDSTSIDQGILGVGYKTNEAGGSYDNVPVTLKKQGVIAKNAYSLYLNSPDAATGQIIFGGVDNAKYSGSLIALPVTSDRELRISLGSVEVSGKTINTDNVDVLVDSGTTITYLQQDLADQIIKAFNGKLTQDSNGNSFYEVDCNLSGDVVFNFSKNAKISVPASEFAASLQGDDGQPYDKCQLLFDVNDANILGDNFLRSAYIVYDLDDNEISLAQVKYTSASSISALT | adhesion of symbiont to host fungal-type cell wall organization induction by symbiont of defense-related host calcium ion flux induction by symbiont of host defense response nitrogen compound metabolic process protein catabolic process protein metabolic process proteolysis signal peptide processing transepithelial migration of symbiont in host extracellular region; extracellular vesicle; fungal-type cell wall aspartic-type endopeptidase activity metal ion binding Candida albicans Aspartyl protease Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Metal-binding Protease Reference proteome Secreted Signal Virulence Zinc Zymogen MFLKNIFIAL MFLKNIFIALAIALLVDATPTTTKRSAGFVALDFSVVKTPKAFPVTNGQEGKTSKRQAVPVTLHNEQVTYAADITVGSNNQKLNVIVDTGSSDLWVPDVNVDCQVTYSDQTADFCKQKGTYDPSGSSASQDLNTPFKIGYGDGSSSQGTLYKDTVGFGGVSIKNQVLADVDSTSIDQGILGVGYKTNEAGGSYDNVPVTLKKQGVIAKNAYSLYLNSPDAATGQIIFGGVDNAKYSGSLIALPVTSDRELRISLGSVEVSGKTINTDNVDVLVDSGTTITYLQQDLADQIIKAFNGKLTQDSNGNSFYEVDCNLSGDVVFNFSKNAKISVPASEFAASLQGDDGQPYDKCQLLFDVNDANILGDNFLRSAYIVYDLDDNEISLAQVKYTSASSISALT |
actin filament bundle assembly actin filament depolymerization actin filament severing cell motility hyperosmotic response response to bacterium | actin cytoskeleton; cytoplasm; intranuclear rod; nuclear matrix; nucleus; phagocytic vesicle; ruffle | actin filament binding actin monomer binding | Dictyostelium discoideum | Actin-binding Cytoplasm Cytoskeleton Nucleus Reference proteome | MSSGIALAPN | MSSGIALAPNCVSTFNDLKLGRKYGGIIYRISDDSKEIIVDSTLPAGCSFDEFTKCLPENECRYVVLDYQYKEEGAQKSKICFVAWCPDTANIKKKMMATSSKDSLRKACVGIQVEIQGTDASEVKDSCFYEKCTKI | actin filament bundle assembly actin filament depolymerization actin filament severing cell motility hyperosmotic response response to bacterium actin cytoskeleton; cytoplasm; intranuclear rod; nuclear matrix; nucleus; phagocytic vesicle; ruffle actin filament binding actin monomer binding Dictyostelium discoideum Actin-binding Cytoplasm Cytoskeleton Nucleus Reference proteome MSSGIALAPN MSSGIALAPNCVSTFNDLKLGRKYGGIIYRISDDSKEIIVDSTLPAGCSFDEFTKCLPENECRYVVLDYQYKEEGAQKSKICFVAWCPDTANIKKKMMATSSKDSLRKACVGIQVEIQGTDASEVKDSCFYEKCTKI |
envenomation resulting in fibrinogenolysis in another organism envenomation resulting in hemorrhagic damage in another organism envenomation resulting in negative regulation of platelet aggregation in another organism proteolysis | extracellular region; host extracellular space | metal ion binding metalloendopeptidase activity toxin activity | Crotalus atrox | Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Platelet aggregation inhibiting toxin Protease Secreted Toxin Zinc | LLRRKSHDHA | LLRRKSHDHAQNHDGDKCLRGASLGYYQSFLNQYKPQCILNKP | envenomation resulting in fibrinogenolysis in another organism envenomation resulting in hemorrhagic damage in another organism envenomation resulting in negative regulation of platelet aggregation in another organism proteolysis extracellular region; host extracellular space metal ion binding metalloendopeptidase activity toxin activity Crotalus atrox Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Platelet aggregation inhibiting toxin Protease Secreted Toxin Zinc LLRRKSHDHA LLRRKSHDHAQNHDGDKCLRGASLGYYQSFLNQYKPQCILNKP |
induction of blood coagulation in another organism proteolysis | extracellular region; host extracellular space | metal ion binding metalloendopeptidase activity peptidase activator activity toxin activity | Micropechis ikaheca | Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Prothrombin activator Secreted Toxin Zinc | TNTPEQDRYL | TNTPEQDRYLQVKKYLEYVVVDNNMYRNYGNAGPCVMSAEISFEPLQEFSSCDIQEPLSQDIVQPAVCGNYYVEVGGECDCGSPKPCRSACCNAATCKLQREHQCDSGECCEKKDDCDLPEICTGRSAKCSCVISQGDLGYGMVEPGTKCTDGMVCSNEQCVDVQTAAK | induction of blood coagulation in another organism proteolysis extracellular region; host extracellular space metal ion binding metalloendopeptidase activity peptidase activator activity toxin activity Micropechis ikaheca Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Prothrombin activator Secreted Toxin Zinc TNTPEQDRYL TNTPEQDRYLQVKKYLEYVVVDNNMYRNYGNAGPCVMSAEISFEPLQEFSSCDIQEPLSQDIVQPAVCGNYYVEVGGECDCGSPKPCRSACCNAATCKLQREHQCDSGECCEKKDDCDLPEICTGRSAKCSCVISQGDLGYGMVEPGTKCTDGMVCSNEQCVDVQTAAK |
envenomation resulting in fibrinogenolysis in another organism envenomation resulting in hemorrhagic damage in another organism proteolysis | extracellular region; host extracellular space | metal ion binding metallopeptidase activity toxin activity | Vipera ammodytes ammodytes | Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc | MVTKYSSIFM | MVTKYSSIFMSPILSNPPILYFSDCSREXYQKXLTN | envenomation resulting in fibrinogenolysis in another organism envenomation resulting in hemorrhagic damage in another organism proteolysis extracellular region; host extracellular space metal ion binding metallopeptidase activity toxin activity Vipera ammodytes ammodytes Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc MVTKYSSIFM MVTKYSSIFMSPILSNPPILYFSDCSREXYQKXLTN |
proteolysis | extracellular region | serine-type endopeptidase activity toxin activity | Bothrops leucurus | Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Toxin | VIGGDECDIN | VIGGDECDINEHPFLAFMYYSPRYFCGMTLINQEWVLTAAHCNRRFMRIXXXXHAGSVANYDEVVRXXXXXFICPNKKKNVITDKDIMLIRLDRPVKNSEHIAPLSLPSNPPSVGSVCRIMGWGAITTSEDTYPDVPHCANINLFNNTVCREAYNGLPAKTLCAGVLQGGIDTCGGDSGGPLICNGQFQGILSWGSDPCAEPRKPAFYTKVFDYLPWIQSIIAGNKTATCP | proteolysis extracellular region serine-type endopeptidase activity toxin activity Bothrops leucurus Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Toxin VIGGDECDIN VIGGDECDINEHPFLAFMYYSPRYFCGMTLINQEWVLTAAHCNRRFMRIXXXXHAGSVANYDEVVRXXXXXFICPNKKKNVITDKDIMLIRLDRPVKNSEHIAPLSLPSNPPSVGSVCRIMGWGAITTSEDTYPDVPHCANINLFNNTVCREAYNGLPAKTLCAGVLQGGIDTCGGDSGGPLICNGQFQGILSWGSDPCAEPRKPAFYTKVFDYLPWIQSIIAGNKTATCP |
carbohydrate utilization | extracellular region | levansucrase activity | Zymomonas mobilis subsp. mobilis | Direct protein sequencing Glycosyltransferase Reference proteome Secreted Transferase | MLNKAGIAEP | MLNKAGIAEPSLWTRADAMKVHTDDPTATMPTIDYDFPVMTDKYWVWDTWPLRDINGQVVSFQGWSVIFALVADRTKYGWHNRNDGARIGYFYSRGGSNWIFGGHLLKDGANPRSWEWSGCTIMAPGTANSVEVFFTSVNDTPSESVPAQCKGYIYADDKSVWFDGFDKVTDLFQADGLYYADYAENNFWDFRDPHVFINPEDGKTYALFEGNVAMERGTVAVGEEEIGPVPPKTETPDGARYCAAAIGIAQALNEARTEWKLLPPLVTAFGVNDQTERPHVVFQNGLTYLFTISHHSTYADGLSGPDGVYGFVSENGIFGPYEPLNGSGLVLGNPSSQPYQAYSHYVMTNGLVTSFIDTIPSSDPNVYRYGGTLAPTIKLELVGHRSFVTEVKGYGYIPPQIEWLAEDESSNSAAALSLLNK | carbohydrate utilization extracellular region levansucrase activity Zymomonas mobilis subsp. mobilis Direct protein sequencing Glycosyltransferase Reference proteome Secreted Transferase MLNKAGIAEP MLNKAGIAEPSLWTRADAMKVHTDDPTATMPTIDYDFPVMTDKYWVWDTWPLRDINGQVVSFQGWSVIFALVADRTKYGWHNRNDGARIGYFYSRGGSNWIFGGHLLKDGANPRSWEWSGCTIMAPGTANSVEVFFTSVNDTPSESVPAQCKGYIYADDKSVWFDGFDKVTDLFQADGLYYADYAENNFWDFRDPHVFINPEDGKTYALFEGNVAMERGTVAVGEEEIGPVPPKTETPDGARYCAAAIGIAQALNEARTEWKLLPPLVTAFGVNDQTERPHVVFQNGLTYLFTISHHSTYADGLSGPDGVYGFVSENGIFGPYEPLNGSGLVLGNPSSQPYQAYSHYVMTNGLVTSFIDTIPSSDPNVYRYGGTLAPTIKLELVGHRSFVTEVKGYGYIPPQIEWLAEDESSNSAAALSLLNK |
mRNA processing positive regulation of mRNA splicing, via spliceosome regulation of alternative mRNA splicing, via spliceosome RNA splicing | nucleolus; nucleoplasm; spliceosomal complex | mRNA binding RNA binding | Homo sapiens | 3D-structure Activator Alternative splicing mRNA processing mRNA splicing Nucleus Reference proteome RNA-binding | MVEADHPGKL | MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSHEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTSHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREACGSSSYVASIVDGGESRSEKGDSSRY | mRNA processing positive regulation of mRNA splicing, via spliceosome regulation of alternative mRNA splicing, via spliceosome RNA splicing nucleolus; nucleoplasm; spliceosomal complex mRNA binding RNA binding Homo sapiens 3D-structure Activator Alternative splicing mRNA processing mRNA splicing Nucleus Reference proteome RNA-binding MVEADHPGKL MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAKKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSHEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTSHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREACGSSSYVASIVDGGESRSEKGDSSRY |
mRNA processing positive regulation of mRNA splicing, via spliceosome regulation of RNA splicing RNA splicing | nucleus; protein-containing complex; spliceosomal complex | identical protein binding RNA binding | Homo sapiens | Activator mRNA processing mRNA splicing Nucleus Reference proteome RNA-binding | MVEADHPGKL | MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAQKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSHEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTSHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREACGSSSYVASIVDGGESRSEKGDSSRY | mRNA processing positive regulation of mRNA splicing, via spliceosome regulation of RNA splicing RNA splicing nucleus; protein-containing complex; spliceosomal complex identical protein binding RNA binding Homo sapiens Activator mRNA processing mRNA splicing Nucleus Reference proteome RNA-binding MVEADHPGKL MVEADHPGKLFIGGLNRETNEKMLKAVFGKHGPISEVLLIKDRTSKSRGFAFITFENPADAKNAAKDMNGKSLHGKAIKVEQAQKPSFQSGGRRRPPASSRNRSPSGSLRSARGSRGGTRGWLPSHEGHLDDGGYTPDLKMSYSRGLIPVKRGPSSRSGGPPPKKSAPSAVARSNSWMGSQGPMSQRRENYGVPPRRATISSWRNDRMSTRHDGYATNDGNHPSCQETRDYAPPSRGYAYRDNGHSNRDEHSSRGYRNHRSSRETRDYAPPSRGHAYRDYGHSRRDESYSRGYRNRRSSRETREYAPPSRGHGYRDYGHSRRHESYSRGYRNHPSSRETRDYAPPHRDYAYRDYGHSSWDEHSSRGYSYHDGYGEALGRDHSEHLSGSSYRDALQRYGTSHGAPPARGPRMSYGGSTCHAYSNTRDRYGRSWESYSSCGDFHYCDREHVCRKDQRNPPSLGRVLPDPREACGSSSYVASIVDGGESRSEKGDSSRY |
digestion proteolysis | extracellular exosome; multivesicular body lumen | aspartic-type endopeptidase activity | Homo sapiens | 3D-structure Aspartyl protease Digestion Direct protein sequencing Disulfide bond Hydrolase Phosphoprotein Protease Reference proteome Secreted Signal Zymogen | MKWLLLLGLV | MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWEAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNLPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA | digestion proteolysis extracellular exosome; multivesicular body lumen aspartic-type endopeptidase activity Homo sapiens 3D-structure Aspartyl protease Digestion Direct protein sequencing Disulfide bond Hydrolase Phosphoprotein Protease Reference proteome Secreted Signal Zymogen MKWLLLLGLV MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWEAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNLPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA |
digestion proteolysis | extracellular exosome; multivesicular body lumen | aspartic-type endopeptidase activity | Homo sapiens | Aspartyl protease Digestion Direct protein sequencing Disulfide bond Hydrolase Protease Reference proteome Secreted Signal Zymogen | MKWLLLLGLV | MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWKAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNLPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA | digestion proteolysis extracellular exosome; multivesicular body lumen aspartic-type endopeptidase activity Homo sapiens Aspartyl protease Digestion Direct protein sequencing Disulfide bond Hydrolase Protease Reference proteome Secreted Signal Zymogen MKWLLLLGLV MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWKAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDQSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGEAIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNLPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA |
digestion proteolysis | extracellular exosome; multivesicular body lumen | aspartic-type endopeptidase activity | Homo sapiens | Aspartyl protease Digestion Direct protein sequencing Disulfide bond Hydrolase Phosphoprotein Protease Reference proteome Secreted Signal Zymogen | MKWLLLLGLV | MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWEAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDKSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGETIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNVPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA | digestion proteolysis extracellular exosome; multivesicular body lumen aspartic-type endopeptidase activity Homo sapiens Aspartyl protease Digestion Direct protein sequencing Disulfide bond Hydrolase Phosphoprotein Protease Reference proteome Secreted Signal Zymogen MKWLLLLGLV MKWLLLLGLVALSECIMYKVPLIRKKSLRRTLSERGLLKDFLKKHNLNPARKYFPQWEAPTLVDEQPLENYLDMEYFGTIGIGTPAQDFTVVFDTGSSNLWVPSVYCSSLACTNHNRFNPEDSSTYQSTSETVSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISSSGATPVFDNIWNQGLVSQDLFSVYLSADDKSGSVVIFGGIDSSYYTGSLNWVPVTVEGYWQITVDSITMNGETIACAEGCQAIVDTGTSLLTGPTSPIANIQSDIGASENSDGDMVVSCSAISSLPDIVFTINGVQYPVPPSAYILQSEGSCISGFQGMNVPTESGELWILGDVFIRQYFTVFDRANNQVGLAPVA |
proteolysis | extracellular region | metal ion binding metallopeptidase activity toxin activity | Bothrops atrox | Calcium Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Myotoxin Protease Secreted Toxin Zinc | YIELAVVADH | YIELAVVADHGIFTKYNSNLNTIR | proteolysis extracellular region metal ion binding metallopeptidase activity toxin activity Bothrops atrox Calcium Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Myotoxin Protease Secreted Toxin Zinc YIELAVVADH YIELAVVADHGIFTKYNSNLNTIR |
proteolysis | extracellular region | metal ion binding metalloendopeptidase activity toxin activity | Vipera ammodytes ammodytes | Calcium Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc | KSAAXVTLDL | KSAAXVTLDLFGDWRAKRHDNAQLLTGINLNGQTLGIAFMSKXSVGLIQDYXKSYLLVASVMAHELGHNLGMEHDDGNCICPAKCIDNKPLRTDIVSPAVCGNYFVELTPGSQCADGVCCDQCRKAGVTVAPDLCFDYNQLGTEDKFTHSPDDPDYGMVDLGTKCADGKVCNSNRQCVDVNTAY | proteolysis extracellular region metal ion binding metalloendopeptidase activity toxin activity Vipera ammodytes ammodytes Calcium Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc KSAAXVTLDL KSAAXVTLDLFGDWRAKRHDNAQLLTGINLNGQTLGIAFMSKXSVGLIQDYXKSYLLVASVMAHELGHNLGMEHDDGNCICPAKCIDNKPLRTDIVSPAVCGNYFVELTPGSQCADGVCCDQCRKAGVTVAPDLCFDYNQLGTEDKFTHSPDDPDYGMVDLGTKCADGKVCNSNRQCVDVNTAY |
envenomation resulting in fibrinogenolysis in another organism envenomation resulting in positive regulation of platelet aggregation in another organism proteolysis | extracellular region | serine-type endopeptidase activity toxin activity | Bothrops marajoensis | Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Platelet aggregation activating toxin Protease Secreted Serine protease Toxin | VIGGDECNIN | VIGGDECNINESPFLAFLYSQLLSSRRYFCGMTLINQEWVLTAAHCNLYPDRKDMNWWLLIKLGKHSGSTRRWVANYDEQVRYWPKEKFIWWYCPNKKKDVINNYVWVWWDKDILLWELWMLIRLNRPVKYSEHIAPLSLPSSPPSAKWWHVGSVCRIMGWGQITETWWNSEDTLPDVPRCANINLFNYEVCRAYNQRWWRGLPAKTLCAGDLEGIIRGGWDTCVGDSGGPLICDGQYQGIAYWGSKPCAEPDEPAAYSKVFDHLDWSQSVIAGGTWWRGDDTCP | envenomation resulting in fibrinogenolysis in another organism envenomation resulting in positive regulation of platelet aggregation in another organism proteolysis extracellular region serine-type endopeptidase activity toxin activity Bothrops marajoensis Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Platelet aggregation activating toxin Protease Secreted Serine protease Toxin VIGGDECNIN VIGGDECNINESPFLAFLYSQLLSSRRYFCGMTLINQEWVLTAAHCNLYPDRKDMNWWLLIKLGKHSGSTRRWVANYDEQVRYWPKEKFIWWYCPNKKKDVINNYVWVWWDKDILLWELWMLIRLNRPVKYSEHIAPLSLPSSPPSAKWWHVGSVCRIMGWGQITETWWNSEDTLPDVPRCANINLFNYEVCRAYNQRWWRGLPAKTLCAGDLEGIIRGGWDTCVGDSGGPLICDGQYQGIAYWGSKPCAEPDEPAAYSKVFDHLDWSQSVIAGGTWWRGDDTCP |
proteolysis | extracellular region | serine-type peptidase activity toxin activity | Bothrops jararacussu | Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Sialic acid Toxin | VVGGDCIPQV | VVGGDCIPQVPFLAFLYSEYFC | proteolysis extracellular region serine-type peptidase activity toxin activity Bothrops jararacussu Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Sialic acid Toxin VVGGDCIPQV VVGGDCIPQVPFLAFLYSEYFC |
cholesterol metabolic process lipid transport lipoprotein metabolic process phosphatidylcholine metabolic process positive regulation of cholesterol efflux positive regulation of phagocytosis positive regulation of phospholipid efflux protein stabilization regulation of intestinal cholesterol absorption | high-density lipoprotein particle | high-density lipoprotein particle receptor binding lipid binding protein homodimerization activity | Pan troglodytes | Cholesterol metabolism Glycoprotein HDL Lipid metabolism Lipid transport Lipoprotein Oxidation Palmitate Phosphoprotein Reference proteome Repeat Secreted Signal Steroid metabolism Sterol metabolism Transport | MKAAVLTLAV | MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ | cholesterol metabolic process lipid transport lipoprotein metabolic process phosphatidylcholine metabolic process positive regulation of cholesterol efflux positive regulation of phagocytosis positive regulation of phospholipid efflux protein stabilization regulation of intestinal cholesterol absorption high-density lipoprotein particle high-density lipoprotein particle receptor binding lipid binding protein homodimerization activity Pan troglodytes Cholesterol metabolism Glycoprotein HDL Lipid metabolism Lipid transport Lipoprotein Oxidation Palmitate Phosphoprotein Reference proteome Repeat Secreted Signal Steroid metabolism Sterol metabolism Transport MKAAVLTLAV MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNLKLLDNWDSVTSTFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRARAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGLLPVLESFKVSFLSALEEYTKKLNTQ |
cholesterol homeostasis cholesterol metabolic process cholesterol transport high-density lipoprotein particle assembly high-density lipoprotein particle remodeling lipoprotein metabolic process low-density lipoprotein particle remodeling peptidyl-methionine modification positive regulation of phagocytosis protein oxidation protein stabilization triglyceride-rich lipoprotein particle remodeling | chylomicron; spherical high-density lipoprotein particle; very-low-density lipoprotein particle | apolipoprotein receptor binding cholesterol binding high-density lipoprotein particle binding high-density lipoprotein particle receptor binding lipase inhibitor activity phosphatidylcholine binding | Gorilla gorilla gorilla | Cleavage on pair of basic residues Disulfide bond HDL Lipid transport Oxidation Phosphoprotein Reference proteome Secreted Signal Transport | MKLLAATVLL | MKLLAATVLLLTICSLEGALVRRQAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ | cholesterol homeostasis cholesterol metabolic process cholesterol transport high-density lipoprotein particle assembly high-density lipoprotein particle remodeling lipoprotein metabolic process low-density lipoprotein particle remodeling peptidyl-methionine modification positive regulation of phagocytosis protein oxidation protein stabilization triglyceride-rich lipoprotein particle remodeling chylomicron; spherical high-density lipoprotein particle; very-low-density lipoprotein particle apolipoprotein receptor binding cholesterol binding high-density lipoprotein particle binding high-density lipoprotein particle receptor binding lipase inhibitor activity phosphatidylcholine binding Gorilla gorilla gorilla Cleavage on pair of basic residues Disulfide bond HDL Lipid transport Oxidation Phosphoprotein Reference proteome Secreted Signal Transport MKLLAATVLL MKLLAATVLLLTICSLEGALVRRQAKEPCVESLVSQYFQTVTDYGKDLMEKVKSPELQAEAKSYFEKSKEQLTPLIKKAGTELVNFLSYFVELGTQPATQ |
proteolysis | extracellular region | serine-type endopeptidase activity toxin activity | Bothrocophias andianus | Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Platelet aggregation activating toxin Protease Secreted Serine protease Sialic acid Toxin | VIGGDECNIN | VIGGDECNINEHPFLVALYYSTFFCGMTLINQEWVLTAAHESEKFPKEKYFIFCPNNKDIMLIRLDKPVSNSEHIAPLSLPSSPPSVGSVCRKPALYTKVFDYLLWIQSIIAGNTATCP | proteolysis extracellular region serine-type endopeptidase activity toxin activity Bothrocophias andianus Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Platelet aggregation activating toxin Protease Secreted Serine protease Sialic acid Toxin VIGGDECNIN VIGGDECNINEHPFLVALYYSTFFCGMTLINQEWVLTAAHESEKFPKEKYFIFCPNNKDIMLIRLDKPVSNSEHIAPLSLPSSPPSVGSVCRKPALYTKVFDYLLWIQSIIAGNTATCP |
proteolysis | extracellular region | serine-type peptidase activity toxin activity | Deinagkistrodon acutus | Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Toxin | VIGGVECDIN | VIGGVECDINEHRFL | proteolysis extracellular region serine-type peptidase activity toxin activity Deinagkistrodon acutus Blood coagulation cascade activating toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Protease Secreted Serine protease Toxin VIGGVECDIN VIGGVECDINEHRFL |
proteolysis | extracellular region | metal ion binding metallopeptidase activity toxin activity | Deinagkistrodon acutus | Calcium Cell adhesion impairing toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Platelet aggregation inhibiting toxin Protease Secreted Toxin Zinc Zymogen | DVVSPPVCGN | DVVSPPVCGN | proteolysis extracellular region metal ion binding metallopeptidase activity toxin activity Deinagkistrodon acutus Calcium Cell adhesion impairing toxin Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Platelet aggregation inhibiting toxin Protease Secreted Toxin Zinc Zymogen DVVSPPVCGN DVVSPPVCGN |
proteolysis | extracellular region | metal ion binding metallopeptidase activity toxin activity | Daboia siamensis | Calcium Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc Zymogen | VATSEPNRYF | VATSEPNRYFNPYSYVELIITVDHS | proteolysis extracellular region metal ion binding metallopeptidase activity toxin activity Daboia siamensis Calcium Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc Zymogen VATSEPNRYF VATSEPNRYFNPYSYVELIITVDHS |
cell division chromosome segregation kinetochore assembly mitotic cell cycle | kinetochore; nucleoplasm | DNA binding protein heterodimerization activity | Gallus gallus | 3D-structure Cell cycle Cell division Centromere Chromosome DNA-binding Kinetochore Mitosis Nucleus Reference proteome | MRRTVPRGTL | MRRTVPRGTLRKIIKKHKPHLRLAANTDLLVHLSFLLFLHRLAEEARTNAFENKSKIIKPEHTIAAAKVILKKSRG | cell division chromosome segregation kinetochore assembly mitotic cell cycle kinetochore; nucleoplasm DNA binding protein heterodimerization activity Gallus gallus 3D-structure Cell cycle Cell division Centromere Chromosome DNA-binding Kinetochore Mitosis Nucleus Reference proteome MRRTVPRGTL MRRTVPRGTLRKIIKKHKPHLRLAANTDLLVHLSFLLFLHRLAEEARTNAFENKSKIIKPEHTIAAAKVILKKSRG |
cellular response to cold cellular response to starvation energy homeostasis fat cell differentiation intracellular glucose homeostasis negative regulation of DNA-templated transcription protein acetylation temperature homeostasis | cytosol; mitochondrion; nucleus | acetyltransferase activity chromatin binding | Mus musculus | Cytoplasm Nucleus Phosphoprotein Reference proteome Repressor Transcription Transcription regulation Transferase | MGGPTRRHQE | MGGPTRRHQEEGSAECLGGPSTRAAPGPGLRDFHFTTAGPSKADRLGDAAQIHRERMRPVQCGDGSGERVFLQSPGSIGTLYIRLDLNSQRSTCCCLLNAGTKGMC | cellular response to cold cellular response to starvation energy homeostasis fat cell differentiation intracellular glucose homeostasis negative regulation of DNA-templated transcription protein acetylation temperature homeostasis cytosol; mitochondrion; nucleus acetyltransferase activity chromatin binding Mus musculus Cytoplasm Nucleus Phosphoprotein Reference proteome Repressor Transcription Transcription regulation Transferase MGGPTRRHQE MGGPTRRHQEEGSAECLGGPSTRAAPGPGLRDFHFTTAGPSKADRLGDAAQIHRERMRPVQCGDGSGERVFLQSPGSIGTLYIRLDLNSQRSTCCCLLNAGTKGMC |
acute-phase response lymphocyte chemotaxis macrophage chemotaxis negative regulation of inflammatory response neutrophil chemotaxis platelet activation positive regulation of cell adhesion positive regulation of cytokine production positive regulation of cytosolic calcium ion concentration positive regulation of interleukin-1 production regulation of protein secretion | cytoplasmic microtubule; endocytic vesicle lumen; extracellular exosome; extracellular region; high-density lipoprotein particle | G protein-coupled receptor binding heparin binding | Homo sapiens | 3D-structure Acute phase Amyloid Amyloidosis Direct protein sequencing HDL Heparin-binding Methylation Reference proteome Secreted Signal | MKLLTGLVFC | MKLLTGLVFCSLVLGVSSRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVITDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY | acute-phase response lymphocyte chemotaxis macrophage chemotaxis negative regulation of inflammatory response neutrophil chemotaxis platelet activation positive regulation of cell adhesion positive regulation of cytokine production positive regulation of cytosolic calcium ion concentration positive regulation of interleukin-1 production regulation of protein secretion cytoplasmic microtubule; endocytic vesicle lumen; extracellular exosome; extracellular region; high-density lipoprotein particle G protein-coupled receptor binding heparin binding Homo sapiens 3D-structure Acute phase Amyloid Amyloidosis Direct protein sequencing HDL Heparin-binding Methylation Reference proteome Secreted Signal MKLLTGLVFC MKLLTGLVFCSLVLGVSSRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGAWAAEVITDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY |
clathrin-dependent endocytosis energy homeostasis positive regulation of eating behavior positive regulation of feeding behavior positive regulation of multicellular organism growth positive regulation of receptor-mediated endocytosis response to dietary excess response to starvation | AP-2 adaptor complex; clathrin-coated pit; clathrin-coated vesicle; cytoplasm; plasma membrane; presynapse; terminal bouton | microtubule binding phospholipid binding SH3 domain binding tubulin binding | Rattus norvegicus | Coated pit Endocytosis Membrane Phosphoprotein Reference proteome | MMEGLKKRTR | MMEGLKKRTRKAFGIRKKEKDTDSTGSPDRDGMQPSPHEPPYHSKAECAREGGKKASKKSNGAPNGFYAEIDWERYNSPELDEEGYSIRPEEPGSTKGKHFYSSSESEEEEESHKKFNIKIKPLQSKDVLKNAATVDELKASIGNIALSPSPVRKSPRRSPGAIKRNLSSEEVARPRRSTPTPELTSKKPLDDTLALAPLFGPPLESAFDEQKTEVLLDQPEIWGSGQPINPSMESPKLARPFPTGTPPPLPPKAVPATPPRTGSPLTVATGNDQAATEAKIEKLPSISDLDSIFGPVLSPKSVAVNTEEKWVHFSDASPEHVTPELTPREKVVTPPAASDIPADSPAPGPPGPPGSAGPPGPPGPRHVPSPLNLEEVQKKVAEQTFIKDDYLETLSSPKECGLGQRATPPPPPPPTYRTVVSSPGPGSGSGTGTASGASSPARPATPLVPCSSTTPPPPPPRPPSRPKLPPGKPGVGDVSRPFSPPIHSSSPPPIAPLARAESTSSISSTNSLSAATTPTVENEQPSLVWFDRGKFYLTFEGSSRGPSPLTMGAQDTLPVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINSSRLEHVLPNPQLLCCDNTQNDANTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPGSTDLRIDYKYNTDAMTTAVALNNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSGCDIELVGAGYRFSLIKKRFAAGKYLADN | clathrin-dependent endocytosis energy homeostasis positive regulation of eating behavior positive regulation of feeding behavior positive regulation of multicellular organism growth positive regulation of receptor-mediated endocytosis response to dietary excess response to starvation AP-2 adaptor complex; clathrin-coated pit; clathrin-coated vesicle; cytoplasm; plasma membrane; presynapse; terminal bouton microtubule binding phospholipid binding SH3 domain binding tubulin binding Rattus norvegicus Coated pit Endocytosis Membrane Phosphoprotein Reference proteome MMEGLKKRTR MMEGLKKRTRKAFGIRKKEKDTDSTGSPDRDGMQPSPHEPPYHSKAECAREGGKKASKKSNGAPNGFYAEIDWERYNSPELDEEGYSIRPEEPGSTKGKHFYSSSESEEEEESHKKFNIKIKPLQSKDVLKNAATVDELKASIGNIALSPSPVRKSPRRSPGAIKRNLSSEEVARPRRSTPTPELTSKKPLDDTLALAPLFGPPLESAFDEQKTEVLLDQPEIWGSGQPINPSMESPKLARPFPTGTPPPLPPKAVPATPPRTGSPLTVATGNDQAATEAKIEKLPSISDLDSIFGPVLSPKSVAVNTEEKWVHFSDASPEHVTPELTPREKVVTPPAASDIPADSPAPGPPGPPGSAGPPGPPGPRHVPSPLNLEEVQKKVAEQTFIKDDYLETLSSPKECGLGQRATPPPPPPPTYRTVVSSPGPGSGSGTGTASGASSPARPATPLVPCSSTTPPPPPPRPPSRPKLPPGKPGVGDVSRPFSPPIHSSSPPPIAPLARAESTSSISSTNSLSAATTPTVENEQPSLVWFDRGKFYLTFEGSSRGPSPLTMGAQDTLPVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINSSRLEHVLPNPQLLCCDNTQNDANTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPGSTDLRIDYKYNTDAMTTAVALNNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSGCDIELVGAGYRFSLIKKRFAAGKYLADN |
envenomation resulting in fibrinogenolysis in another organism envenomation resulting in fibrinolysis in another organism envenomation resulting in induction of edema in another organism proteolysis | extracellular region; host extracellular space | metal ion binding metallopeptidase activity toxin activity | Bothrops leucurus | Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Fibrinolytic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc | TLTSFGEWR | TLTSFGEWR | envenomation resulting in fibrinogenolysis in another organism envenomation resulting in fibrinolysis in another organism envenomation resulting in induction of edema in another organism proteolysis extracellular region; host extracellular space metal ion binding metallopeptidase activity toxin activity Bothrops leucurus Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Fibrinolytic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc TLTSFGEWR TLTSFGEWR |
arachidonic acid secretion lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity toxin activity | Protobothrops flavoviridis | 3D-structure Blood coagulation cascade inhibiting toxin Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Metal-binding Myotoxin Secreted Signal Toxin | MRTLWIMAVL | MRTLWIMAVLLVGVDGSLVQLWKMIFQETGKEAAKNYGLYGCNCGVGRRGKPKDATDSCCYVHKCCYKKVTGCNPKMDSYSYSWKNKAIVCGEKNPPCLKQVCECDKAVAICLRENLGTYNKKYTIYPKPFCKKADTC | arachidonic acid secretion lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Protobothrops flavoviridis 3D-structure Blood coagulation cascade inhibiting toxin Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Metal-binding Myotoxin Secreted Signal Toxin MRTLWIMAVL MRTLWIMAVLLVGVDGSLVQLWKMIFQETGKEAAKNYGLYGCNCGVGRRGKPKDATDSCCYVHKCCYKKVTGCNPKMDSYSYSWKNKAIVCGEKNPPCLKQVCECDKAVAICLRENLGTYNKKYTIYPKPFCKKADTC |
arginine biosynthetic process clavulanic acid biosynthetic process | cytoplasm | acetyl-CoA:L-glutamate N-acetyltransferase activity glutamate N-acetyltransferase activity | Streptomyces clavuligerus | 3D-structure Acyltransferase Autocatalytic cleavage Cytoplasm Direct protein sequencing Transferase | MSDSTPKTPR | MSDSTPKTPRGFVVHTAPVGLADDGRDDFTVLASTAPATVSAVFTRSRFAGPSVVLCREAVADGQARGVVVLARNANVATGLEGEENAREVREAVARALGLPEGEMLIASTGVIGRQYPMESIREHLKTLEWPAGEGGFDRAARAIMTTDTRPKEVRVSVGGATLVGIAKGVGMLEPDMATLLTFFATDARLDPAEQDRLFRRVMDRTFNAVSIDTDTSTSDTAVLFANGLAGEVDAGEFEEALHTAALALVKDIASDGEGAAKLIEVQVTGARDDAQAKRVGKTVVNSPLVKTAVHGCDPNWGRVAMAIGKCSDDTDIDQERVTIRFGEVEVYPPKARGDQADDALRAAVAEHLRGDEVVIGIDLAIADGAFTVYGCDLTEGYVRLNSEYTT | arginine biosynthetic process clavulanic acid biosynthetic process cytoplasm acetyl-CoA:L-glutamate N-acetyltransferase activity glutamate N-acetyltransferase activity Streptomyces clavuligerus3D-structure Acyltransferase Autocatalytic cleavage Cytoplasm Direct protein sequencing Transferase MSDSTPKTPR MSDSTPKTPRGFVVHTAPVGLADDGRDDFTVLASTAPATVSAVFTRSRFAGPSVVLCREAVADGQARGVVVLARNANVATGLEGEENAREVREAVARALGLPEGEMLIASTGVIGRQYPMESIREHLKTLEWPAGEGGFDRAARAIMTTDTRPKEVRVSVGGATLVGIAKGVGMLEPDMATLLTFFATDARLDPAEQDRLFRRVMDRTFNAVSIDTDTSTSDTAVLFANGLAGEVDAGEFEEALHTAALALVKDIASDGEGAAKLIEVQVTGARDDAQAKRVGKTVVNSPLVKTAVHGCDPNWGRVAMAIGKCSDDTDIDQERVTIRFGEVEVYPPKARGDQADDALRAAVAEHLRGDEVVIGIDLAIADGAFTVYGCDLTEGYVRLNSEYTT |
clathrin-dependent endocytosis of virus by host cell fusion of virus membrane with host endosome membrane proteolysis suppression by virus of host toll-like receptor signaling pathway virion attachment to host cell | host cell cytoplasm; host cell nucleus; host cell plasma membrane; membrane; T=4 icosahedral viral capsid; viral envelope; virion membrane | serine-type endopeptidase activity structural molecule activity | Semliki forest virus | Autocatalytic cleavage Capsid protein Clathrin-mediated endocytosis of virus by host Cleavage on pair of basic residues Disulfide bond Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Glycoprotein Host cell membrane Host cytoplasm Host membrane Host nucleus Host-virus interaction Hydrolase Lipoprotein Membrane Palmitate Protease Ribosomal frameshifting Serine protease T=4 icosahedral capsid protein Transmembrane Transmembrane helix Viral attachment to host cell Viral envelope protein Viral penetration into host cytoplasm Virion Virus endocytosis by host Virus entry into host cell | MNYIPTQTFY | MNYIPTQTFYGRRWRPRPAARPWPLQATPVAPVVPDFQAQQMQQLISAVNALTMRQNAIAPARPPKPKKKKTTKPKPKTQPKKINGKTQQQKKKDKQADKKKKKPGKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEWSAPLITAMCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQAALTCRNGTRHRRSVSQHFNVYKATRPYIAYCADCGAGHSCHSPVAIEAVRSEATDGMLKIQFSAQIGIDKSDNHDYTKIRYADGHAIENAVRSSLKVATSGDCFVHGTMGHFILAKCPPGEFLQVSIQDTRNAVRACRIQYHHDPQPVGREKFTIRPHYGKEIPCTTYQQTTAETVEEIDMHMPPDTPDRTLLSQQSGNVKITVGGKKVKYNCTCGTGNVGTTNSDMTINTCLIEQCHVSVTDHKKWQFNSPFVPRADEPARKGKVHIPFPLDNITCRVPMAREPTVIHGKREVTLHLHPDHPTLFSYRTLGEDPQYHEEWVTAAVERTIPVPVDGMEYHWGNNDPVRLWSQLTTEGKPHGWPHQIVQYYYGLYPAATVSAVVGMSLLALISIFASCYMLVAARSKCLTPYALTPGAAVPWTLGILCCAPRAHAASVAETMAYLWDQNQALFWLEFAAPVACILIITYCLRNVLCCCKSLSFLSATEPRGHRQSLRTFDSNAERGGVPV | clathrin-dependent endocytosis of virus by host cell fusion of virus membrane with host endosome membrane proteolysis suppression by virus of host toll-like receptor signaling pathway virion attachment to host cell host cell cytoplasm; host cell nucleus; host cell plasma membrane; membrane; T=4 icosahedral viral capsid; viral envelope; virion membrane serine-type endopeptidase activity structural molecule activity Semliki forest virus Autocatalytic cleavage Capsid protein Clathrin-mediated endocytosis of virus by host Cleavage on pair of basic residues Disulfide bond Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Glycoprotein Host cell membrane Host cytoplasm Host membrane Host nucleus Host-virus interaction Hydrolase Lipoprotein Membrane Palmitate Protease Ribosomal frameshifting Serine protease T=4 icosahedral capsid protein Transmembrane Transmembrane helix Viral attachment to host cell Viral envelope protein Viral penetration into host cytoplasm Virion Virus endocytosis by host Virus entry into host cell MNYIPTQTFY MNYIPTQTFYGRRWRPRPAARPWPLQATPVAPVVPDFQAQQMQQLISAVNALTMRQNAIAPARPPKPKKKKTTKPKPKTQPKKINGKTQQQKKKDKQADKKKKKPGKRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGVIDNADLAKLAFKKSSKYDLECAQIPVHMRSDASKYTHEKPEGHYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGSRTALSVVTWNKDMVTRVTPEGSEEWSAPLITAMCVLANATFPCFQPPCVPCCYENNAEATLRMLEDNVDRPGYYDLLQAALTCRNGTRHRRSVSQHFNVYKATRPYIAYCADCGAGHSCHSPVAIEAVRSEATDGMLKIQFSAQIGIDKSDNHDYTKIRYADGHAIENAVRSSLKVATSGDCFVHGTMGHFILAKCPPGEFLQVSIQDTRNAVRACRIQYHHDPQPVGREKFTIRPHYGKEIPCTTYQQTTAETVEEIDMHMPPDTPDRTLLSQQSGNVKITVGGKKVKYNCTCGTGNVGTTNSDMTINTCLIEQCHVSVTDHKKWQFNSPFVPRADEPARKGKVHIPFPLDNITCRVPMAREPTVIHGKREVTLHLHPDHPTLFSYRTLGEDPQYHEEWVTAAVERTIPVPVDGMEYHWGNNDPVRLWSQLTTEGKPHGWPHQIVQYYYGLYPAATVSAVVGMSLLALISIFASCYMLVAARSKCLTPYALTPGAAVPWTLGILCCAPRAHAASVAETMAYLWDQNQALFWLEFAAPVACILIITYCLRNVLCCCKSLSFLSATEPRGHRQSLRTFDSNAERGGVPV |
steroid biosynthetic process steroid metabolic process | cytosol; lipid droplet; membrane | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity 17-beta-hydroxysteroid dehydrogenase (NADP+) activity cortisol dehydrogenase activity estradiol 17-beta-dehydrogenase activity | Arabidopsis thaliana | Lipid biosynthesis Lipid droplet Lipid metabolism Membrane NADP Oxidoreductase Reference proteome Signal-anchor Steroid biosynthesis Transmembrane Transmembrane helix | MELINDFLNL | MELINDFLNLTAPFFTFFGLCFFLPPFYFFKFLQSIFSTIFSENLYGKVVLITGASSGIGEQLAYEYACRGACLALTARRKNRLEEVAEIARELGSPNVVTVHADVSKPDDCRRIVDDTITHFGRLDHLVNNAGMTQISMFENIEDITRTKAVLDTNFWGSVYTTRAALPYLRQSNGKIVAMSSSAAWLTAPRMSFYNASKAALLSFFETMRIELGGDVHITIVTPGYIESELTQGKYFSGEGELIVNQDMRDVQVGPFPVASASGCAKSIVNGVCRKQRYVTEPSWFKVTYLWKVLCPELIEWGCRLLYMTGTGMSEDTALNKRIMDIPGVRSTLYPESIRTPEIKSD | steroid biosynthetic process steroid metabolic process cytosol; lipid droplet; membrane 11-beta-hydroxysteroid dehydrogenase (NADP+) activity 17-beta-hydroxysteroid dehydrogenase (NADP+) activity cortisol dehydrogenase activity estradiol 17-beta-dehydrogenase activity Arabidopsis thaliana Lipid biosynthesis Lipid droplet Lipid metabolism Membrane NADP Oxidoreductase Reference proteome Signal-anchor Steroid biosynthesis Transmembrane Transmembrane helix MELINDFLNL MELINDFLNLTAPFFTFFGLCFFLPPFYFFKFLQSIFSTIFSENLYGKVVLITGASSGIGEQLAYEYACRGACLALTARRKNRLEEVAEIARELGSPNVVTVHADVSKPDDCRRIVDDTITHFGRLDHLVNNAGMTQISMFENIEDITRTKAVLDTNFWGSVYTTRAALPYLRQSNGKIVAMSSSAAWLTAPRMSFYNASKAALLSFFETMRIELGGDVHITIVTPGYIESELTQGKYFSGEGELIVNQDMRDVQVGPFPVASASGCAKSIVNGVCRKQRYVTEPSWFKVTYLWKVLCPELIEWGCRLLYMTGTGMSEDTALNKRIMDIPGVRSTLYPESIRTPEIKSD |
morphine biosynthetic process | membrane | 1,2-dehydroreticulinium reductase (NADPH) activity heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor | Papaver somniferum | Alkaloid metabolism Heme Iron Membrane Metal-binding Multifunctional enzyme NADP Oxidoreductase Transmembrane Transmembrane helix | MELQYISYFQ | MELQYISYFQPTSSVVALLLALVSILSSVVVLRKTFLNNYSSSPASSTKTAVLSHQRQQSCALPISGLLHIFMNKNGLIHVTLGNMADKYGPIFSFPTGSHRTLVVSSWEMVKECFTGNNDTAFSNRPIPLAFKTIFYACGGIDSYGLSSVPYGKYWRELRKVCVHNLLSNQQLLKFRHLIISQVDTSFNKLYELCKNSEDNHGNYTTTTTTAAGMVRIDDWLAELSFNVIGRIVCGFQSGPKTGAPSRVEQFKEAINEASYFMSTSPVSDNVPMLGWIDQLTGLTRNMKHCGKKLDLVVESIINDHRQKRRFSRTKGGDEKDDEQDDFIDICLSIMEQPQLPGNNNPSQIPIKSIVLDMIGGGTDTTKLTTIWTLSLLLNNPHVLDKAKQEVDAHFRTKRRSTNDAAAAVVDFDDIRNLVYIQAIIKESMRLYPASPVVERLSGEDCVVGGFHVPAGTRLWANVWKMQRDPKVWDDPLVFRPDRFLSDEQKMVDVRGQNYELLPFGAGRRVCPGVSFSLDLMQLVLTRLILEFEMKSPSGKVDMTATPGLMSYKVIPLDILLTHRRIKPCVQSAASERDMESSGVPVITLGSGKVMPVLGMGTFEKVGKGSERERLAILKAIEVGYRYFDTAAAYETEEVLGEAIAEALQLGLVKSRDELFISSMLWCTDAHADRVLLALQNSLRNLKLEYVDLYMLPFPASLKPGKITMDIPEEDICRMDYRSVWAAMEECQNLGFTKSIGVSNFSCKKLQELMATANIPPAVNQVEMSPAFQQKKLREYCNANNILVSAISVLGSNGTPWGSNAVLGSEVLKKIAMAKGKSVAQVSMRWVYEQGASLVVKSFSEERLRENLNIFDWELTKEDHEKIGEIPQCRILSAYFLVSPNGPFKSQEELWDDEA | morphine biosynthetic process membrane 1,2-dehydroreticulinium reductase (NADPH) activity heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Papaver somniferum Alkaloid metabolism Heme Iron Membrane Metal-binding Multifunctional enzyme NADP Oxidoreductase Transmembrane Transmembrane helix MELQYISYFQ MELQYISYFQPTSSVVALLLALVSILSSVVVLRKTFLNNYSSSPASSTKTAVLSHQRQQSCALPISGLLHIFMNKNGLIHVTLGNMADKYGPIFSFPTGSHRTLVVSSWEMVKECFTGNNDTAFSNRPIPLAFKTIFYACGGIDSYGLSSVPYGKYWRELRKVCVHNLLSNQQLLKFRHLIISQVDTSFNKLYELCKNSEDNHGNYTTTTTTAAGMVRIDDWLAELSFNVIGRIVCGFQSGPKTGAPSRVEQFKEAINEASYFMSTSPVSDNVPMLGWIDQLTGLTRNMKHCGKKLDLVVESIINDHRQKRRFSRTKGGDEKDDEQDDFIDICLSIMEQPQLPGNNNPSQIPIKSIVLDMIGGGTDTTKLTTIWTLSLLLNNPHVLDKAKQEVDAHFRTKRRSTNDAAAAVVDFDDIRNLVYIQAIIKESMRLYPASPVVERLSGEDCVVGGFHVPAGTRLWANVWKMQRDPKVWDDPLVFRPDRFLSDEQKMVDVRGQNYELLPFGAGRRVCPGVSFSLDLMQLVLTRLILEFEMKSPSGKVDMTATPGLMSYKVIPLDILLTHRRIKPCVQSAASERDMESSGVPVITLGSGKVMPVLGMGTFEKVGKGSERERLAILKAIEVGYRYFDTAAAYETEEVLGEAIAEALQLGLVKSRDELFISSMLWCTDAHADRVLLALQNSLRNLKLEYVDLYMLPFPASLKPGKITMDIPEEDICRMDYRSVWAAMEECQNLGFTKSIGVSNFSCKKLQELMATANIPPAVNQVEMSPAFQQKKLREYCNANNILVSAISVLGSNGTPWGSNAVLGSEVLKKIAMAKGKSVAQVSMRWVYEQGASLVVKSFSEERLRENLNIFDWELTKEDHEKIGEIPQCRILSAYFLVSPNGPFKSQEELWDDEA |
arachidonic acid secretion lipid catabolic process phospholipid metabolic process | extracellular region | metal ion binding phospholipase A2 activity toxin activity | Pandinus imperator | Calcium Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Secreted Signal Toxin Zymogen | MVDLARRCSG | MVDLARRCSGSTEGRFLMWECTKWCGPGNNAKCESDLGPLEADKCCRTHDHCDYIASGETKYGITNYAFFTKLNCKCEEAFDRCLTEAYNKEEKESAKSSTKRLQNFYFGTYSPECYVVTCNSKRSGRDAGCENGVATWKKSYKD | arachidonic acid secretion lipid catabolic process phospholipid metabolic process extracellular region metal ion binding phospholipase A2 activity toxin activity Pandinus imperator Calcium Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Secreted Signal Toxin Zymogen MVDLARRCSG MVDLARRCSGSTEGRFLMWECTKWCGPGNNAKCESDLGPLEADKCCRTHDHCDYIASGETKYGITNYAFFTKLNCKCEEAFDRCLTEAYNKEEKESAKSSTKRLQNFYFGTYSPECYVVTCNSKRSGRDAGCENGVATWKKSYKD |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Colobus guereza | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKVLWAALLV | MKVLWAALLVTFLAGCQAKVEQPVESEPEPELRQQTEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTTLMDETMKELKAYKSDLEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRGEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Colobus guereza Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKVLWAALLV MKVLWAALLVTFLAGCQAKVEQPVESEPEPELRQQTEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTTLMDETMKELKAYKSDLEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRGEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Ateles geoffroyi | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKVLWAALLV | MKVLWAALLVAFLAGCQGKMEPELEREPELEREPELHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAXYRSEVQAMLGQSXDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLVPLVEQGRARAATVGSSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASAAPVPGDNH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Ateles geoffroyi Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKVLWAALLV MKVLWAALLVAFLAGCQGKMEPELEREPELEREPELHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAXYRSEVQAMLGQSXDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLVPLVEQGRARAATVGSSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASAAPVPGDNH |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Plecturocebus moloch | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKVLWAALLV | MKVLWAALLVAFLAGCQGKVEQVVEPELEPEPELHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRARAATVGSSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASAAPVPSDNH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Plecturocebus moloch Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKVLWAALLV MKVLWAALLVAFLAGCQGKVEQVVEPELEPEPELHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRARAATVGSSLAGQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASAAPVPSDNH |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Saimiri boliviensis boliviensis | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Reference proteome Repeat Secreted Signal Transport VLDL | MKVLWAAFLV | MKVLWAAFLVAFLAGCQGKVEQVVEPELGPEPELHPQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRARAATVGSSLASQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASATPVPSDNH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Saimiri boliviensis boliviensis Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Reference proteome Repeat Secreted Signal Transport VLDL MKVLWAAFLV MKVLWAAFLVAFLAGCQGKVEQVVEPELGPEPELHPQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRARAATVGSSLASQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASATPVPSDNH |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Papio hamadryas | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKVLWAALLV | MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Papio hamadryas Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKVLWAALLV MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH |
carbohydrate metabolic process | cytoplasm | cellobiose epimerase activity | Ruminococcus albus | 3D-structure Cytoplasm Direct protein sequencing Isomerase | MMISEIRQEL | MMISEIRQELTDHIIPFWNKLRDDENGGFYGYLSYGLGLDKKADKGVILHSRILWFYSNAYMTLGGDELLDNAKHAYEFIKNNCIDYEYGGVYWMMDFEGKPADTMKHTYNIAFAIYALSSYYRASGDKEALALAYRPFEDIEKNTLYEYGYREAFDRQWRLVDNEALSENGLKADKTMNAILHLIEAYTELYKADGNEKVADRLKFQLGQMRDIVYTPDTNALKVFFDTAFNLVGDIHSYGHDIEATWLMDRACDVLGDEDLKKQFAEMDLKISHNIQDIALEDGALNNERDKNEIDKTRVWWVQAEAVVGFINAYQHSGDEKFLESAKSVWENIKEYIIDKREGGEWYSEVTFDHTPHDYKETVGPWKCPYHNGRMCMEVITRGVDI | carbohydrate metabolic process cytoplasm cellobiose epimerase activity Ruminococcus albus3D-structure Cytoplasm Direct protein sequencing Isomerase MMISEIRQEL MMISEIRQELTDHIIPFWNKLRDDENGGFYGYLSYGLGLDKKADKGVILHSRILWFYSNAYMTLGGDELLDNAKHAYEFIKNNCIDYEYGGVYWMMDFEGKPADTMKHTYNIAFAIYALSSYYRASGDKEALALAYRPFEDIEKNTLYEYGYREAFDRQWRLVDNEALSENGLKADKTMNAILHLIEAYTELYKADGNEKVADRLKFQLGQMRDIVYTPDTNALKVFFDTAFNLVGDIHSYGHDIEATWLMDRACDVLGDEDLKKQFAEMDLKISHNIQDIALEDGALNNERDKNEIDKTRVWWVQAEAVVGFINAYQHSGDEKFLESAKSVWENIKEYIIDKREGGEWYSEVTFDHTPHDYKETVGPWKCPYHNGRMCMEVITRGVDI |
nucleotide metabolic process | cytoplasm; nucleolus; nucleoplasm | 5'-(N(7)-methylguanosine 5'-triphospho)- hydrolase activity dIDP phosphatase activity IDP phosphatase activity metal ion binding nucleotide binding RNA binding | Homalodisca vitripennis | Alternative splicing Cytoplasm Hydrolase Magnesium Manganese Metal-binding Nucleotide metabolism Nucleotide-binding Nucleus RNA-binding | MSSDTGDRTW | MSSDTGDRTWGHLAATEHYGRITDTTDYIQVDKENLKNDPYYNSSQASHCMIFARNNKKTFGVYNPRAAILMQMRFDGNLGFPGGLVDAGEDSIKALNRELTEEMNLDTSKHSVSESSYVVTHWSISKRLCLHFYALEVSLAELYEIEKRALLAKDYGSEVLGTIRMPLYTMGDGYRGFPTFLTTPS | nucleotide metabolic process cytoplasm; nucleolus; nucleoplasm 5'-(N(7)-methylguanosine 5'-triphospho)- hydrolase activity dIDP phosphatase activity IDP phosphatase activity metal ion binding nucleotide binding RNA binding Homalodisca vitripennis Alternative splicing Cytoplasm Hydrolase Magnesium Manganese Metal-binding Nucleotide metabolism Nucleotide-binding Nucleus RNA-binding MSSDTGDRTW MSSDTGDRTWGHLAATEHYGRITDTTDYIQVDKENLKNDPYYNSSQASHCMIFARNNKKTFGVYNPRAAILMQMRFDGNLGFPGGLVDAGEDSIKALNRELTEEMNLDTSKHSVSESSYVVTHWSISKRLCLHFYALEVSLAELYEIEKRALLAKDYGSEVLGTIRMPLYTMGDGYRGFPTFLTTPS |
cell differentiation phosphorylation regulation of floral meristem growth specification of floral organ number | membrane | ATP binding protein serine kinase activity protein serine/threonine kinase activity receptor serine/threonine kinase binding | Zea mays | ATP-binding Developmental protein Differentiation Kinase Leucine-rich repeat Membrane Nucleotide-binding Receptor Reference proteome Repeat Serine/threonine-protein kinase Signal Transferase Transmembrane Transmembrane helix | MPPPTFLLGL | MPPPTFLLGLLLLLLLAAAAPAPASATPERDAYALSRLKASLVPSATNSTSAPLSDWDPAATPPAHCAFTGVTCDAATSRVVAINLTAVPLHGGALPPEVALLDALASLTVANCYLRGRLPPALASMPALRHLNLSNNNLSGPFPPPPPAAYFPALEIVDVYNNNLSGPLPPLGAPHARSLRYLHLGGNYFNGSIPDTFGDLAALEYLGLNGNALSGRVPPSLSRLSRLREMYVGYYNQYSGGVPREFGALQSLVRLDMSSCTLTGPIPPELARLSRLDTLFLALNQLTGEIPPELGALTSLRSLDLSINDLAGEIPASFAALTNLKLLNLFRNHLRGEIPAFLGDFPFLEVLQVWDNNLTGPLPPALGRNGRLKTLDVTSNHLTGTIPPDLCAGRNLQLLVLMDNGFFGSIPESLGDCKTLTRVRLGKNFLTGPVPAGLFDLPQANMLELTDNMLTGELPDVIAGDKIGMLMLGNNRIGGRIPAAIGNLPALQTLSLESNNFSGPLPPEIGRLRNLTRLNASGNALTGGIPRELMGCASLGAVDLSRNGLTGEIPDTVTSLKILCTLNVSRNRLSGELPAAMANMTSLTTLDVSYNQLSGPVPMQGQFLVFNESSFVGNPGLCSACPPSSGGARSPFSLRRWDSKKLLVWLVVLLTLLVLAVLGARKAHEAWREAARRRSGAWKMTAFQKLDFSADDVVECLKEDNIIGKGGAGIVYHGVTRGGAELAIKRLVGRGCGDHDRGFTAEVTTLGRIRHRNIVRLLGFVSNREANLLLYEYMPNGSLGEMLHGGKGGHLGWEARARVAAEAARGLCYLHHDCAPRIIHRDVKSNNILLDSAFEAHVADFGLAKFLGGGGATSECMSAIAGSYGYIAPEYAYTLRVDEKSDVYSFGVVLLELITGRRPVGSFGDGVDIVHWVRKVTADAAAAEEPVLLVADRRLAPEPVPLLADLYRVAMACVEEASTARPTMREVVHMLSTSAAAQPDVPHALCKVVD | cell differentiation phosphorylation regulation of floral meristem growth specification of floral organ number membrane ATP binding protein serine kinase activity protein serine/threonine kinase activity receptor serine/threonine kinase binding Zea mays ATP-binding Developmental protein Differentiation Kinase Leucine-rich repeat Membrane Nucleotide-binding Receptor Reference proteome Repeat Serine/threonine-protein kinase Signal Transferase Transmembrane Transmembrane helix MPPPTFLLGL MPPPTFLLGLLLLLLLAAAAPAPASATPERDAYALSRLKASLVPSATNSTSAPLSDWDPAATPPAHCAFTGVTCDAATSRVVAINLTAVPLHGGALPPEVALLDALASLTVANCYLRGRLPPALASMPALRHLNLSNNNLSGPFPPPPPAAYFPALEIVDVYNNNLSGPLPPLGAPHARSLRYLHLGGNYFNGSIPDTFGDLAALEYLGLNGNALSGRVPPSLSRLSRLREMYVGYYNQYSGGVPREFGALQSLVRLDMSSCTLTGPIPPELARLSRLDTLFLALNQLTGEIPPELGALTSLRSLDLSINDLAGEIPASFAALTNLKLLNLFRNHLRGEIPAFLGDFPFLEVLQVWDNNLTGPLPPALGRNGRLKTLDVTSNHLTGTIPPDLCAGRNLQLLVLMDNGFFGSIPESLGDCKTLTRVRLGKNFLTGPVPAGLFDLPQANMLELTDNMLTGELPDVIAGDKIGMLMLGNNRIGGRIPAAIGNLPALQTLSLESNNFSGPLPPEIGRLRNLTRLNASGNALTGGIPRELMGCASLGAVDLSRNGLTGEIPDTVTSLKILCTLNVSRNRLSGELPAAMANMTSLTTLDVSYNQLSGPVPMQGQFLVFNESSFVGNPGLCSACPPSSGGARSPFSLRRWDSKKLLVWLVVLLTLLVLAVLGARKAHEAWREAARRRSGAWKMTAFQKLDFSADDVVECLKEDNIIGKGGAGIVYHGVTRGGAELAIKRLVGRGCGDHDRGFTAEVTTLGRIRHRNIVRLLGFVSNREANLLLYEYMPNGSLGEMLHGGKGGHLGWEARARVAAEAARGLCYLHHDCAPRIIHRDVKSNNILLDSAFEAHVADFGLAKFLGGGGATSECMSAIAGSYGYIAPEYAYTLRVDEKSDVYSFGVVLLELITGRRPVGSFGDGVDIVHWVRKVTADAAAAEEPVLLVADRRLAPEPVPLLADLYRVAMACVEEASTARPTMREVVHMLSTSAAAQPDVPHALCKVVD |
proteolysis | extracellular region | serine-type endopeptidase activity toxin activity | Bothrops pirajai | Blood coagulation cascade activating toxin Complement system impairing toxin Direct protein sequencing Disulfide bond Fibrinolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Platelet aggregation activating toxin Protease Secreted Serine protease Toxin | VVGGDECNIN | VVGGDECNINEHRSLVAIFNSTGFFCSGILLNQEWVLTASHCDSTNFQMK | proteolysis extracellular region serine-type endopeptidase activity toxin activity Bothrops pirajai Blood coagulation cascade activating toxin Complement system impairing toxin Direct protein sequencing Disulfide bond Fibrinolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Platelet aggregation activating toxin Protease Secreted Serine protease Toxin VVGGDECNIN VVGGDECNINEHRSLVAIFNSTGFFCSGILLNQEWVLTASHCDSTNFQMK |
proteolysis | extracellular region | serine-type endopeptidase activity toxin activity | Bothrops pirajai | Blood coagulation cascade activating toxin Complement system impairing toxin Direct protein sequencing Disulfide bond Fibrinolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Platelet aggregation activating toxin Protease Secreted Serine protease Toxin | VVGGDECDIN | VVGGDECDINEHPFLAFLYSHGYFCGLTLINQEWVLTAAHCDRRFMRIYL | proteolysis extracellular region serine-type endopeptidase activity toxin activity Bothrops pirajai Blood coagulation cascade activating toxin Complement system impairing toxin Direct protein sequencing Disulfide bond Fibrinolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Platelet aggregation activating toxin Protease Secreted Serine protease Toxin VVGGDECDIN VVGGDECDINEHPFLAFLYSHGYFCGLTLINQEWVLTAAHCDRRFMRIYL |
proteolysis | extracellular region | metal ion binding metalloendopeptidase activity toxin activity | Bothrops pirajai | Calcium Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Fibrinolytic toxin Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc | TYIEVAVVAD | TYIEVAVVADHRMFKKYNSNLNTIRKWVHEMVNSMNGVYRSMDVHLSLANLEVWSKKDLINVQKDSRETLKSFGEWRERDLLPRISHDNAQLLTAIVFDQQTIGRAYIGGMCDPRHSVGVVMDHSKINLQVAVTMAHELGHNLGMEHDENQCHCDAPSCVMXXXXXXXXXXXXXXCXXXXXXXXXTKHNPQCILNEPL | proteolysis extracellular region metal ion binding metalloendopeptidase activity toxin activity Bothrops pirajai Calcium Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Fibrinolytic toxin Hemorrhagic toxin Hemostasis impairing toxin Hydrolase Metal-binding Metalloprotease Protease Secreted Toxin Zinc TYIEVAVVAD TYIEVAVVADHRMFKKYNSNLNTIRKWVHEMVNSMNGVYRSMDVHLSLANLEVWSKKDLINVQKDSRETLKSFGEWRERDLLPRISHDNAQLLTAIVFDQQTIGRAYIGGMCDPRHSVGVVMDHSKINLQVAVTMAHELGHNLGMEHDENQCHCDAPSCVMXXXXXXXXXXXXXXCXXXXXXXXXTKHNPQCILNEPL |
arachidonic acid secretion defense response to bacterium lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity toxin activity | Bothrops pauloensis | Antibiotic Antimicrobial Blood coagulation cascade inhibiting toxin Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Lipid degradation Lipid metabolism Metal-binding Myotoxin Neurotoxin Secreted Toxin | DLWQFGKMIL | DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDRCCFVHDCC | arachidonic acid secretion defense response to bacterium lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Bothrops pauloensis Antibiotic Antimicrobial Blood coagulation cascade inhibiting toxin Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Lipid degradation Lipid metabolism Metal-binding Myotoxin Neurotoxin Secreted Toxin DLWQFGKMIL DLWQFGKMILKVAGKLPFPYYGAYGCYCGWGGRGKPKDPTDRCCFVHDCC |
cellular localization energy homeostasis energy reserve metabolic process positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway protein localization to plasma membrane regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway response to starvation | cytoplasm; endoplasmic reticulum; endoplasmic reticulum membrane; Golgi apparatus; perinuclear region of cytoplasm; plasma membrane | corticotropin hormone receptor binding signaling receptor regulator activity type 1 melanocortin receptor binding type 3 melanocortin receptor binding type 4 melanocortin receptor binding type 5 melanocortin receptor binding | Danio rerio | Cell membrane Endoplasmic reticulum Glycoprotein Membrane Reference proteome Transmembrane Transmembrane helix | MSEYSNRSQA | MSEYSNRSQAGADYEWHYEYYEDEEPVSFEGLRANRYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHPEMCDASMKPHVLIGCELEVGGSLAFSLPPLPDQSRSLFHFYIHKEERVKTHKDAVIGRGMHCGRGNAERADEDEHFMSSFNIPNFVNSEQSSSLGHDDFLLSEPPIITDGQSDELKTAEPAHLCYDIIRH | cellular localization energy homeostasis energy reserve metabolic process positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway protein localization to plasma membrane regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway response to starvation cytoplasm; endoplasmic reticulum; endoplasmic reticulum membrane; Golgi apparatus; perinuclear region of cytoplasm; plasma membrane corticotropin hormone receptor binding signaling receptor regulator activity type 1 melanocortin receptor binding type 3 melanocortin receptor binding type 4 melanocortin receptor binding type 5 melanocortin receptor binding Danio rerio Cell membrane Endoplasmic reticulum Glycoprotein Membrane Reference proteome Transmembrane Transmembrane helix MSEYSNRSQA MSEYSNRSQAGADYEWHYEYYEDEEPVSFEGLRANRYSIVIGFWVGLAVFVIFMFFVLTLLTKTGAPHPEMCDASMKPHVLIGCELEVGGSLAFSLPPLPDQSRSLFHFYIHKEERVKTHKDAVIGRGMHCGRGNAERADEDEHFMSSFNIPNFVNSEQSSSLGHDDFLLSEPPIITDGQSDELKTAEPAHLCYDIIRH |
autophagosome assembly autophagy cellular response to nitrogen starvation endosome to lysosome transport G protein-coupled receptor catabolic process glucose homeostasis late endosome to vacuole transport | phagophore assembly site; phosphatidylinositol 3-kinase complex, class III, type I; phosphatidylinositol 3-kinase complex, class III, type II | protein-containing complex binding | Mus musculus | Autophagy Coiled coil Cytoplasm Reference proteome | MSPALFLCQR | MSPALFLCQRCKEPLKLLQQQGGPLEVQHHANTPTEIPVSAESQVRTSGRPHSDGGRVSQGSALCTFTLLTSGGPDSEGGTTSQGNACCTFTLLGESASMRTMNTIQNTVLETFEILSDQKVVDHPLCVDCTDHLLMQLDDQLALLASDNQKYKSFQDRELLVSEEEREALHAELCAELSSLEQEEARLTQELEDLDGHHARVAAELRAAQAESKELYKQHEQHRVEYSVFKMEQLELMDQLSSVENQLTYALSQQYRLRQTNIFNATFTISDEGPLGVINNFRLGCLPGVRVGWTEISSAWGQTVLLLFSLSKIAGLQFQRYQLVPFGDHSYLKSLTGDGVLPLFSDGSHSVFLNNKFDCGMKAFLDCLQQFVEEIERDERCPCLPYRIHVKEGLMEDVWDSGECCSIRTHLNTEEEWSRALKFMLSDLKLILAWASLRFSRVQRP | autophagosome assembly autophagy cellular response to nitrogen starvation endosome to lysosome transport G protein-coupled receptor catabolic process glucose homeostasis late endosome to vacuole transport phagophore assembly site; phosphatidylinositol 3-kinase complex, class III, type I; phosphatidylinositol 3-kinase complex, class III, type II protein-containing complex binding Mus musculus Autophagy Coiled coil Cytoplasm Reference proteome MSPALFLCQR MSPALFLCQRCKEPLKLLQQQGGPLEVQHHANTPTEIPVSAESQVRTSGRPHSDGGRVSQGSALCTFTLLTSGGPDSEGGTTSQGNACCTFTLLGESASMRTMNTIQNTVLETFEILSDQKVVDHPLCVDCTDHLLMQLDDQLALLASDNQKYKSFQDRELLVSEEEREALHAELCAELSSLEQEEARLTQELEDLDGHHARVAAELRAAQAESKELYKQHEQHRVEYSVFKMEQLELMDQLSSVENQLTYALSQQYRLRQTNIFNATFTISDEGPLGVINNFRLGCLPGVRVGWTEISSAWGQTVLLLFSLSKIAGLQFQRYQLVPFGDHSYLKSLTGDGVLPLFSDGSHSVFLNNKFDCGMKAFLDCLQQFVEEIERDERCPCLPYRIHVKEGLMEDVWDSGECCSIRTHLNTEEEWSRALKFMLSDLKLILAWASLRFSRVQRP |
phosphorelay signal transduction system | plasma membrane | ATP binding metal ion binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity | Salmonella typhimurium | 3D-structure ATP-binding Cell inner membrane Cell membrane Growth regulation Hydrolase Kinase Magnesium Membrane Metal-binding Nucleotide-binding Phosphoprotein Protein phosphatase Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system Virulence | MNKFARHFLP | MNKFARHFLPLSLRVRFLLATAGVVLVLSLAYGIVALVGYSVSFDKTTFRLLRGESNLFYTLAKWENNKISVELPENLDMQSPTMTLIYDETGKLLWTQRNIPWLIKSIQPEWLKTNGFHEIETNVDATSTLLSEDHSAQEKLKEVREDDDDAEMTHSVAVNIYPATARMPQLTIVVVDTIPIELKRSYMVWSWFVYVLAANLLLVIPLLWIAAWWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGYYLHRASMRGSGVLLSRELHPVAPLLDNLISALNKVYQRKGVNISMDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDDHLHIFVEDDGPGIPHSKRSLVFDRGQRADTLRPGQGVGLAVAREITEQYAGQIIASDSLLGGARMEVVFGRQHPTQKEE | phosphorelay signal transduction system plasma membrane ATP binding metal ion binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity Salmonella typhimurium 3D-structure ATP-binding Cell inner membrane Cell membrane Growth regulation Hydrolase Kinase Magnesium Membrane Metal-binding Nucleotide-binding Phosphoprotein Protein phosphatase Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system Virulence MNKFARHFLP MNKFARHFLPLSLRVRFLLATAGVVLVLSLAYGIVALVGYSVSFDKTTFRLLRGESNLFYTLAKWENNKISVELPENLDMQSPTMTLIYDETGKLLWTQRNIPWLIKSIQPEWLKTNGFHEIETNVDATSTLLSEDHSAQEKLKEVREDDDDAEMTHSVAVNIYPATARMPQLTIVVVDTIPIELKRSYMVWSWFVYVLAANLLLVIPLLWIAAWWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGYYLHRASMRGSGVLLSRELHPVAPLLDNLISALNKVYQRKGVNISMDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDDHLHIFVEDDGPGIPHSKRSLVFDRGQRADTLRPGQGVGLAVAREITEQYAGQIIASDSLLGGARMEVVFGRQHPTQKEE |
chromosome segregation DNA replication regulation of single-species biofilm formation on inanimate substrate | bacterial nucleoid; cytoplasm | GTP binding GTPase activity ribosome binding | Escherichia coli | Chromosome partition Coiled coil Cytoplasm DNA replication Reference proteome | MYTQTLYELS | MYTQTLYELSQEAERLLQLSRQQLQLLEKMPLSVPGDDAPQLALPWSQPNIAERHAMLNNELRKISRLEMVLAIVGTMKAGKSTTINAIVGTEVLPNRNRPMTALPTLIRHTPGQKEPVLHFSHVAPIDCLIQQLQQRLRDCDIKHLTDVLEIDKDMRALMQRIENGVAFEKYYLGAQPIFHCLKSLNDLVRLAKALDVDFPFSAYAAIEHIPVIEVEFVHLAGLESYPGQLTLLDTPGPNEAGQPHLQKMLNQQLARASAVLAVLDYTQLKSISDEEVREAILAVGQSVPLYVLVNKFDQQDRNSDDADQVRALISGTLMKGCITPQQIFPVSSMWGYLANRARYELANNGKLPPPEQQRWVEDFAHAALGRRWRHADLADLEHIRHAADQLWEDSLFAQPIQALLHAAYANASLYALRSAAHKLLNYAQQAREYLDFRAHGLNVACEQLRQNIHQIEESLQLLQLNQAQVSGEIKHEIELALTSANHFLRQQQDALKVQLAALFQDDSEPLSEIRTRCETLLQTAQNTISRDFTLRFAELESTLCRVLTDVIRPIEQQVKMELSESGFRPGFHFPVFHGVVPHFNTRQLFSEVISRQEATDEQSTRLGVVRETFSRWLNQPDWGRGNEKSPTETVDYSVLQRALSAEVDLYCQQMAKVLAEQVDESVTAGMNTFFAEFASCLTELQTRLRESLALRQQNESVVRLMQQQLQQTVMTHGWIYTDAQLLRDDIQTLFTAERY | chromosome segregation DNA replication regulation of single-species biofilm formation on inanimate substrate bacterial nucleoid; cytoplasm GTP binding GTPase activity ribosome binding Escherichia coli Chromosome partition Coiled coil Cytoplasm DNA replication Reference proteome MYTQTLYELS MYTQTLYELSQEAERLLQLSRQQLQLLEKMPLSVPGDDAPQLALPWSQPNIAERHAMLNNELRKISRLEMVLAIVGTMKAGKSTTINAIVGTEVLPNRNRPMTALPTLIRHTPGQKEPVLHFSHVAPIDCLIQQLQQRLRDCDIKHLTDVLEIDKDMRALMQRIENGVAFEKYYLGAQPIFHCLKSLNDLVRLAKALDVDFPFSAYAAIEHIPVIEVEFVHLAGLESYPGQLTLLDTPGPNEAGQPHLQKMLNQQLARASAVLAVLDYTQLKSISDEEVREAILAVGQSVPLYVLVNKFDQQDRNSDDADQVRALISGTLMKGCITPQQIFPVSSMWGYLANRARYELANNGKLPPPEQQRWVEDFAHAALGRRWRHADLADLEHIRHAADQLWEDSLFAQPIQALLHAAYANASLYALRSAAHKLLNYAQQAREYLDFRAHGLNVACEQLRQNIHQIEESLQLLQLNQAQVSGEIKHEIELALTSANHFLRQQQDALKVQLAALFQDDSEPLSEIRTRCETLLQTAQNTISRDFTLRFAELESTLCRVLTDVIRPIEQQVKMELSESGFRPGFHFPVFHGVVPHFNTRQLFSEVISRQEATDEQSTRLGVVRETFSRWLNQPDWGRGNEKSPTETVDYSVLQRALSAEVDLYCQQMAKVLAEQVDESVTAGMNTFFAEFASCLTELQTRLRESLALRQQNESVVRLMQQQLQQTVMTHGWIYTDAQLLRDDIQTLFTAERY |
proteolysis | extracellular region | metal ion binding metalloendopeptidase activity toxin activity | Gloydius brevicaudus | Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Metal-binding Pyrrolidone carboxylic acid Secreted Toxin Zinc | QQRYLNAKRY | QQRYLNAKRYVKLAIVADRSMVTKHNGKLKKLRKWIYRIVNTINEVYRSLNILVALVYLEIWSKEDLINVTSAAKDTLASFGNWRATDLLKRRSHDAAHLLTNIKFDGTTVGKAYVASMCQQDSSVGINQDHSKINLLVALTMAHELGHNLGMSHDVVNTEKQCNCGTCVMAPTISDQISKLFSNCSKNDYENFLTLYKPQCILNEPSKTDIVSPPVCGNELLEVGEECDCGSPETCQNPCCDAATCKLTSGSQCAKGLCCDQCKFSKSGTECRAAKDDCDIAESCTGQSADCPTDDLQRNGKPCQNNAGYCYNGKCPIMLNQCISFYGSNATVAPDICFNYNLKGEGNFYCRKEQATIFPCAQKDKKCGRLFCVLGPTGKRISCKNTYSEDDPNYGMVDLGTKCEDGKVCNSNRECVDVNTAY | proteolysis extracellular region metal ion binding metalloendopeptidase activity toxin activity Gloydius brevicaudus Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Metal-binding Pyrrolidone carboxylic acid Secreted Toxin Zinc QQRYLNAKRY QQRYLNAKRYVKLAIVADRSMVTKHNGKLKKLRKWIYRIVNTINEVYRSLNILVALVYLEIWSKEDLINVTSAAKDTLASFGNWRATDLLKRRSHDAAHLLTNIKFDGTTVGKAYVASMCQQDSSVGINQDHSKINLLVALTMAHELGHNLGMSHDVVNTEKQCNCGTCVMAPTISDQISKLFSNCSKNDYENFLTLYKPQCILNEPSKTDIVSPPVCGNELLEVGEECDCGSPETCQNPCCDAATCKLTSGSQCAKGLCCDQCKFSKSGTECRAAKDDCDIAESCTGQSADCPTDDLQRNGKPCQNNAGYCYNGKCPIMLNQCISFYGSNATVAPDICFNYNLKGEGNFYCRKEQATIFPCAQKDKKCGRLFCVLGPTGKRISCKNTYSEDDPNYGMVDLGTKCEDGKVCNSNRECVDVNTAY |
proteolysis | extracellular region | metal ion binding metalloendopeptidase activity toxin activity | Gloydius brevicaudus | Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Metal-binding Pyrrolidone carboxylic acid Secreted Toxin Zinc | QQRYLNAKRY | QQRYLNAKRYVKLAIVADRSMVTKHNGKLKKLRKWIYRIVNTINEVYRSLNILVALVYLEIWSKEDLINVTSAAKDTLASFGNWRATDLLKRRSHDAAHLLTNIKFDGTTVGKAYVASMCQQDSSVGINQDHSKINLLVALTMAHELGHNLGMSHDVVNTEKQCNCGTCVMAPTISDQISKLFSNCSKNDYENFLTLYKPQCILNEPSKTDIVSPPVCGNELLEVGEECDCGSPETCQNPCCDAATCKLTSGSQCAKGLCCDQCKFSKSGTECRAAKDDCDIAESCTGQSADCPTDDLQRNGQPCGNNAQYCRKGKCPIMTNQCISFYGPNAAVAPDACFDYNLKGEGNFYCRKEQATIFPCAQKDKKCGRLFCVLGPTGKRISCEHTYSQDDPDIGMVLPGTKCADGKVCNSNRECVDVNTAY | proteolysis extracellular region metal ion binding metalloendopeptidase activity toxin activity Gloydius brevicaudus Direct protein sequencing Disulfide bond Fibrinogenolytic toxin Glycoprotein Hemostasis impairing toxin Hydrolase Metal-binding Pyrrolidone carboxylic acid Secreted Toxin Zinc QQRYLNAKRY QQRYLNAKRYVKLAIVADRSMVTKHNGKLKKLRKWIYRIVNTINEVYRSLNILVALVYLEIWSKEDLINVTSAAKDTLASFGNWRATDLLKRRSHDAAHLLTNIKFDGTTVGKAYVASMCQQDSSVGINQDHSKINLLVALTMAHELGHNLGMSHDVVNTEKQCNCGTCVMAPTISDQISKLFSNCSKNDYENFLTLYKPQCILNEPSKTDIVSPPVCGNELLEVGEECDCGSPETCQNPCCDAATCKLTSGSQCAKGLCCDQCKFSKSGTECRAAKDDCDIAESCTGQSADCPTDDLQRNGQPCGNNAQYCRKGKCPIMTNQCISFYGPNAAVAPDACFDYNLKGEGNFYCRKEQATIFPCAQKDKKCGRLFCVLGPTGKRISCEHTYSQDDPDIGMVLPGTKCADGKVCNSNRECVDVNTAY |
killing of cells of another organism lipid catabolic process | extracellular region | 1-acyl-2-lysophosphatidylserine acylhydrolase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity toxin activity | Vespa affinis | Allergen Cytolysis Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Neurotoxin Secreted Signal Toxin | MMNLKYLLFF | MMNLKYLLFFCLVQALHYCYAYGDPSLSNELDRFNPCPYSDDTVKMIILTRENKKHDFYTLNTIKNHNEFKKSTIKHQVVFITHGFTSTATAENFLAMAEALLDKGNYLVILIDWRVAACTNEMAGVKLAYYSYAASNTRLVGNYIATVTKMLVQQYNVPMANIRLIGHSLGAHTSGFAGKKVQELRLGKYSEIIGLDPAGPSFKSQECSQRICETDANYVQIIHTSNHLGTLVTLGTVDFYMNNGYNQPGCGLPIIGETCSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRNECVCVGLNAKTYPKTGSFYVPVESKAPYCNNKGKII | killing of cells of another organism lipid catabolic process extracellular region 1-acyl-2-lysophosphatidylserine acylhydrolase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity toxin activity Vespa affinis Allergen Cytolysis Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Neurotoxin Secreted Signal Toxin MMNLKYLLFF MMNLKYLLFFCLVQALHYCYAYGDPSLSNELDRFNPCPYSDDTVKMIILTRENKKHDFYTLNTIKNHNEFKKSTIKHQVVFITHGFTSTATAENFLAMAEALLDKGNYLVILIDWRVAACTNEMAGVKLAYYSYAASNTRLVGNYIATVTKMLVQQYNVPMANIRLIGHSLGAHTSGFAGKKVQELRLGKYSEIIGLDPAGPSFKSQECSQRICETDANYVQIIHTSNHLGTLVTLGTVDFYMNNGYNQPGCGLPIIGETCSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRNECVCVGLNAKTYPKTGSFYVPVESKAPYCNNKGKII |
killing of cells of another organism lipid catabolic process | extracellular region | 1-acyl-2-lysophosphatidylserine acylhydrolase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity | Vespa affinis | Allergen Cytolysis Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Secreted Signal | MMNLKYLLFF | MMNLKYLLFFCLVQALHYCYAYGDPSLSNELDRFNPCPYSDDTVKMIILTRENKKHDFYTLNTIKNHNEFKKSTIKHQVVFITHGFTSTATAENFLAMAEALLDKGNYLVILIDWRVAACTNEMAGVKLAYYSYAASNTRLVGNYIATVTKMLVQQYNVPMANIRLVGHSLGAHTSGFAGKKVQELRLGKYSEIIGLDPAGPSFKSQECSQRICETDANYVQIIHTSNHLGTLVTLGTVDFYMNNGYNQPGCGLPIIGETCSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRNQCVCVGLNAKTYPKTGSFYVPVESKAPYCNNKGKII | killing of cells of another organism lipid catabolic process extracellular region 1-acyl-2-lysophosphatidylserine acylhydrolase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity Vespa affinis Allergen Cytolysis Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Secreted Signal MMNLKYLLFF MMNLKYLLFFCLVQALHYCYAYGDPSLSNELDRFNPCPYSDDTVKMIILTRENKKHDFYTLNTIKNHNEFKKSTIKHQVVFITHGFTSTATAENFLAMAEALLDKGNYLVILIDWRVAACTNEMAGVKLAYYSYAASNTRLVGNYIATVTKMLVQQYNVPMANIRLVGHSLGAHTSGFAGKKVQELRLGKYSEIIGLDPAGPSFKSQECSQRICETDANYVQIIHTSNHLGTLVTLGTVDFYMNNGYNQPGCGLPIIGETCSHTRAVKYFTECIRHECCLIGVPQSKNPQPVSKCTRNQCVCVGLNAKTYPKTGSFYVPVESKAPYCNNKGKII |
killing of cells of another organism lipid catabolic process | extracellular region | 1-acyl-2-lysophosphatidylserine acylhydrolase activity lysophospholipase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity | Vespa velutina | Allergen Cytolysis Direct protein sequencing Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Secreted | GLLPKVKLVP | GLLPKVKLVPEQISFILSTRENR | killing of cells of another organism lipid catabolic process extracellular region 1-acyl-2-lysophosphatidylserine acylhydrolase activity lysophospholipase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity Vespa velutina Allergen Cytolysis Direct protein sequencing Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Secreted GLLPKVKLVP GLLPKVKLVPEQISFILSTRENR |
killing of cells of another organism lipid catabolic process | extracellular region | 1-acyl-2-lysophosphatidylserine acylhydrolase activity lysophospholipase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity | Vespa velutina | Allergen Cytolysis Direct protein sequencing Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Secreted | FNPCPYSDDT | FNPCPYSDDTVKMIILTRENKKHDF | killing of cells of another organism lipid catabolic process extracellular region 1-acyl-2-lysophosphatidylserine acylhydrolase activity lysophospholipase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity Vespa velutina Allergen Cytolysis Direct protein sequencing Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Secreted FNPCPYSDDT FNPCPYSDDTVKMIILTRENKKHDF |
killing of cells of another organism lipid catabolic process | extracellular region | 1-acyl-2-lysophosphatidylserine acylhydrolase activity lysophospholipase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity | Vespa velutina | Allergen Cytolysis Direct protein sequencing Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Secreted | FNPCPYSDDT | FNPCPYSDDTVKMIILTRENKKHDF | killing of cells of another organism lipid catabolic process extracellular region 1-acyl-2-lysophosphatidylserine acylhydrolase activity lysophospholipase activity phosphatidylserine 1-acylhydrolase activity phospholipase A1 activity Vespa velutina Allergen Cytolysis Direct protein sequencing Disulfide bond Hemolysis Hydrolase Lipid degradation Lipid metabolism Secreted FNPCPYSDDT FNPCPYSDDTVKMIILTRENKKHDF |
adult heart development angioblast cell migration from lateral mesoderm to midline apelin receptor signaling pathway cell migration involved in gastrulation cell migration involved in mesendoderm migration chordate embryonic development coronary vasculature development determination of heart left/right asymmetry determination of left/right symmetry determination of liver left/right asymmetry embryonic heart tube development endoderm development endodermal cell differentiation heart development Kupffer's vesicle development mesendoderm migration mesoderm migration involved in gastrulation positive regulation of angiogenesis positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade positive regulation of heart contraction positive regulation of trophoblast cell migration sprouting angiogenesis vasculogenesis | extracellular region; extracellular space | apelin receptor binding hormone activity receptor ligand activity | Danio rerio | Angiogenesis Developmental protein Differentiation Gastrulation Hormone Reference proteome Secreted Signal | MRFFHPLYLL | MRFFHPLYLLLLLLTVLVLISADKHGTKHDFLNLRRKYRRHNCPKKRCLPLHSRVPFP | adult heart development angioblast cell migration from lateral mesoderm to midline apelin receptor signaling pathway cell migration involved in gastrulation cell migration involved in mesendoderm migration chordate embryonic development coronary vasculature development determination of heart left/right asymmetry determination of left/right symmetry determination of liver left/right asymmetry embryonic heart tube development endoderm development endodermal cell differentiation heart development Kupffer's vesicle development mesendoderm migration mesoderm migration involved in gastrulation positive regulation of angiogenesis positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade positive regulation of heart contraction positive regulation of trophoblast cell migration sprouting angiogenesis vasculogenesis extracellular region; extracellular space apelin receptor binding hormone activity receptor ligand activity Danio rerio Angiogenesis Developmental protein Differentiation Gastrulation Hormone Reference proteome Secreted Signal MRFFHPLYLL MRFFHPLYLLLLLLTVLVLISADKHGTKHDFLNLRRKYRRHNCPKKRCLPLHSRVPFP |
adult heart development angiogenesis apelin receptor signaling pathway cell migration involved in mesendoderm migration coronary vasculature development embryonic heart tube development endoderm development heart development mesendoderm migration mesoderm migration involved in gastrulation placenta blood vessel development positive regulation of angiogenesis positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade positive regulation of G protein-coupled receptor internalization positive regulation of heart contraction positive regulation of trophoblast cell migration vasculogenesis | extracellular region; extracellular space | apelin receptor binding hormone activity | Homo sapiens | 3D-structure Angiogenesis Developmental protein Differentiation Gastrulation Glycoprotein Hormone Reference proteome Secreted Signal | MRFQQFLFAF | MRFQQFLFAFFIFIMSLLLISGQRPVNLTMRRKLRKHNCLQRRCMPLHSRVPFP | adult heart development angiogenesis apelin receptor signaling pathway cell migration involved in mesendoderm migration coronary vasculature development embryonic heart tube development endoderm development heart development mesendoderm migration mesoderm migration involved in gastrulation placenta blood vessel development positive regulation of angiogenesis positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade positive regulation of G protein-coupled receptor internalization positive regulation of heart contraction positive regulation of trophoblast cell migration vasculogenesis extracellular region; extracellular space apelin receptor binding hormone activity Homo sapiens 3D-structure Angiogenesis Developmental protein Differentiation Gastrulation Glycoprotein Hormone Reference proteome Secreted Signal MRFQQFLFAF MRFQQFLFAFFIFIMSLLLISGQRPVNLTMRRKLRKHNCLQRRCMPLHSRVPFP |
angiogenesis apelin receptor signaling pathway cell migration involved in mesendoderm migration coronary vasculature development embryonic heart tube development endoderm development heart development mesendoderm migration mesoderm migration involved in gastrulation placenta blood vessel development positive regulation of angiogenesis positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade positive regulation of G protein-coupled receptor internalization positive regulation of heart contraction positive regulation of trophoblast cell migration regulation of blood pressure vasculogenesis | extracellular region; extracellular space | apelin receptor binding hormone activity | Mus musculus | Angiogenesis Developmental protein Differentiation Gastrulation Hormone Reference proteome Secreted Signal | MRFQPLFWVF | MRFQPLFWVFFIFAMSLLFISEQKPVNFPRRRKLYRHNCFRRRCIPLHSRVPFP | angiogenesis apelin receptor signaling pathway cell migration involved in mesendoderm migration coronary vasculature development embryonic heart tube development endoderm development heart development mesendoderm migration mesoderm migration involved in gastrulation placenta blood vessel development positive regulation of angiogenesis positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade positive regulation of G protein-coupled receptor internalization positive regulation of heart contraction positive regulation of trophoblast cell migration regulation of blood pressure vasculogenesis extracellular region; extracellular space apelin receptor binding hormone activity Mus musculus Angiogenesis Developmental protein Differentiation Gastrulation Hormone Reference proteome Secreted Signal MRFQPLFWVF MRFQPLFWVFFIFAMSLLFISEQKPVNFPRRRKLYRHNCFRRRCIPLHSRVPFP |
cellular response to osmotic stress phosphorelay signal transduction system regulation of DNA-templated transcription single-species biofilm formation | cytosol; outer membrane-bounded periplasmic space; plasma membrane | ATP binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity protein histidine kinase activity | Escherichia coli | 3D-structure ATP-binding Capsule biogenesis/degradation Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system | MKYLASFRTT | MKYLASFRTTLKASRYMFRALALVLWLLIAFSSVFYIVNALHQRESEIRQEFNLSSDQAQRFIQRTSDVMKELKYIAENRLSAENGVLSPRGRETQADVPAFEPLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRDMPVERDTALKALHERINKYRNAPQDDSGSNLYWISEGPRPGVGYFYALTPVYLANRLQALLGVEQTIRMENFFLPGTLPMGVTILDENGHTLISLTGPESKIKGDPRWMQERSWFGYTEGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLAGAALFTLARMYERRIFIPAESDALRLEEHEQFNRKIVASAPVGICILRTADGVNILSNELAHTYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSRYRNENVAICVLVDVSSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLYGAQYPQKKGVEGLSGKRCWLAVRNASLCQFLETSLQRSGIVVTTYEGQEPTPEDVLITDEVVSKKWQGRAVVTFCRRHIGIPLEKAPGEWVHSVAAPHELPALLARIYLIEMESDDPANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRKSRDS | cellular response to osmotic stress phosphorelay signal transduction system regulation of DNA-templated transcription single-species biofilm formation cytosol; outer membrane-bounded periplasmic space; plasma membrane ATP binding phosphoprotein phosphatase activity phosphorelay sensor kinase activity protein histidine kinase activity Escherichia coli 3D-structure ATP-binding Capsule biogenesis/degradation Cell inner membrane Cell membrane Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system MKYLASFRTT MKYLASFRTTLKASRYMFRALALVLWLLIAFSSVFYIVNALHQRESEIRQEFNLSSDQAQRFIQRTSDVMKELKYIAENRLSAENGVLSPRGRETQADVPAFEPLFADSDCSAMSNTWRGSLESLAWFMRYWRDNFSAAYDLNRVFLIGSDNLCMANFGLRDMPVERDTALKALHERINKYRNAPQDDSGSNLYWISEGPRPGVGYFYALTPVYLANRLQALLGVEQTIRMENFFLPGTLPMGVTILDENGHTLISLTGPESKIKGDPRWMQERSWFGYTEGFRELVLKKNLPPSSLSIVYSVPVDKVLERIRMLILNAILLNVLAGAALFTLARMYERRIFIPAESDALRLEEHEQFNRKIVASAPVGICILRTADGVNILSNELAHTYLNMLTHEDRQRLTQIICGQQVNFVDVLTSNNTNLQISFVHSRYRNENVAICVLVDVSSRVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPREFSPREVMNHITANYLPLVVRKQLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRADGDYLSIRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLISMMDGDISVDSEPGMGSQFTVRIPLYGAQYPQKKGVEGLSGKRCWLAVRNASLCQFLETSLQRSGIVVTTYEGQEPTPEDVLITDEVVSKKWQGRAVVTFCRRHIGIPLEKAPGEWVHSVAAPHELPALLARIYLIEMESDDPANALPSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLSDVNMPNMDGYRLTQRIRQLGLTLPVIGVTANALAEEKQRCLESGMDSCLSKPVTLDVIKQTLTLYAERVRKSRDS |
cellular stress response to acidic pH DNA-templated transcription negative regulation of DNA-templated transcription phosphorelay signal transduction system positive regulation of cell projection organization positive regulation of DNA-templated transcription regulation of bacterial-type flagellum-dependent cell motility regulation of capsule organization regulation of carbohydrate catabolic process regulation of DNA-templated transcription response to antibiotic single-species biofilm formation on inanimate substrate | cytosol; transcription regulator complex | DNA binding DNA-binding transcription activator activity DNA-binding transcription repressor activity identical protein binding | Escherichia coli | 3D-structure Activator Capsule biogenesis/degradation DNA-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system | MNNMNVIIAD | MNNMNVIIADDHPIVLFGIRKSLEQIEWVNVVGEFEDSTALINNLPKLDAHVLITDLSMPGDKYGDGITLIKYIKRHFPSLSIIVLTMNNNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQKGKKFTPESVSRLLEKISAGGYGDKRLSPKESEVLRLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGVENDIALLNYLSSVTLSPADKD | cellular stress response to acidic pH DNA-templated transcription negative regulation of DNA-templated transcription phosphorelay signal transduction system positive regulation of cell projection organization positive regulation of DNA-templated transcription regulation of bacterial-type flagellum-dependent cell motility regulation of capsule organization regulation of carbohydrate catabolic process regulation of DNA-templated transcription response to antibiotic single-species biofilm formation on inanimate substrate cytosol; transcription regulator complex DNA binding DNA-binding transcription activator activity DNA-binding transcription repressor activity identical protein binding Escherichia coli 3D-structure Activator Capsule biogenesis/degradation DNA-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system MNNMNVIIAD MNNMNVIIADDHPIVLFGIRKSLEQIEWVNVVGEFEDSTALINNLPKLDAHVLITDLSMPGDKYGDGITLIKYIKRHFPSLSIIVLTMNNNPAILSAVLDLDIEGIVLKQGAPTDLPKALAALQKGKKFTPESVSRLLEKISAGGYGDKRLSPKESEVLRLFAEGFLVTEIAKKLNRSIKTISSQKKSAMMKLGVENDIALLNYLSSVTLSPADKD |
DNA-templated transcription negative regulation of DNA-templated transcription positive regulation of DNA-templated transcription regulation of bacterial-type flagellum-dependent cell motility regulation of capsule organization response to stimulus | transcription regulator complex | DNA binding | Escherichia coli | Activator Capsule biogenesis/degradation Direct protein sequencing DNA-binding Reference proteome Sensory transduction Transcription Transcription regulation | MSTIIMDLCS | MSTIIMDLCSYTRLGLTGYLLSRGVKKREINDIETVDDLAIACDSQRPSVVFINEDCFIHDASNSQRIKLIINQHPNTLFIVFMAIANVHFDEYLLVRKNLLISSKSIKPESLDDILGDILKKETTITSFLNMPTLSLSRTESSMLRMWMAGQGTIQISDQMNIKAKTVSSHKGNIKRKIKTHNKQVIYHVVRLTDNVTNGIFVNMR | DNA-templated transcription negative regulation of DNA-templated transcription positive regulation of DNA-templated transcription regulation of bacterial-type flagellum-dependent cell motility regulation of capsule organization response to stimulus transcription regulator complex DNA binding Escherichia coli Activator Capsule biogenesis/degradation Direct protein sequencing DNA-binding Reference proteome Sensory transduction Transcription Transcription regulation MSTIIMDLCS MSTIIMDLCSYTRLGLTGYLLSRGVKKREINDIETVDDLAIACDSQRPSVVFINEDCFIHDASNSQRIKLIINQHPNTLFIVFMAIANVHFDEYLLVRKNLLISSKSIKPESLDDILGDILKKETTITSFLNMPTLSLSRTESSMLRMWMAGQGTIQISDQMNIKAKTVSSHKGNIKRKIKTHNKQVIYHVVRLTDNVTNGIFVNMR |
endothelial cell differentiation nucleosome assembly positive regulation of transcription by RNA polymerase II | chromatin; cytoplasm; lipid droplet; nucleoplasm; nucleus | chromatin binding histone binding | Homo sapiens | Activator Coiled coil Cytoplasm Differentiation Nucleus Reference proteome Transcription Transcription regulation | MVWFLDFPNS | MVWFLDFPNSMAPKRQSPLPLQKKKPRPPPALGLEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNEQDSEEILKVEQKYNKLRQPFFQKRSELIAKIPNFGVTTFVNHPQVSSLLGEEDEEALHYLTKVEVTEFEDIKSGYRIDFYFDENPYFENKVFSKEFHLNESGDPSSKSTKIKWKSGKDVTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELEEVIKDDIWPNPLQYYLVPDMDDEEGGEDDDDDDDDGDEGEEELEDIDEGDEDEGEEDEDDDEGEEGEEDEGEDD | endothelial cell differentiation nucleosome assembly positive regulation of transcription by RNA polymerase II chromatin; cytoplasm; lipid droplet; nucleoplasm; nucleus chromatin binding histone binding Homo sapiens Activator Coiled coil Cytoplasm Differentiation Nucleus Reference proteome Transcription Transcription regulation MVWFLDFPNS MVWFLDFPNSMAPKRQSPLPLQKKKPRPPPALGLEETSASAGLPKKGEKEQQEAIEHIDEVQNEIDRLNEQDSEEILKVEQKYNKLRQPFFQKRSELIAKIPNFGVTTFVNHPQVSSLLGEEDEEALHYLTKVEVTEFEDIKSGYRIDFYFDENPYFENKVFSKEFHLNESGDPSSKSTKIKWKSGKDVTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELEEVIKDDIWPNPLQYYLVPDMDDEEGGEDDDDDDDDGDEGEEELEDIDEGDEDEGEEDEDDDEGEEGEEDEGEDD |
animal organ development growth hormone receptor signaling pathway positive regulation of growth positive regulation of receptor signaling pathway via JAK-STAT positive regulation of tyrosine phosphorylation of STAT protein response to nutrient levels | endoplasmic reticulum; endosome lumen; extracellular region; extracellular space; vesicle | growth factor activity growth hormone receptor binding hormone activity metal ion binding | Homo sapiens | 3D-structure Direct protein sequencing Disulfide bond Hormone Metal-binding Reference proteome Secreted Signal Zinc | MAPGSRTSLL | MAPGSRTSLLLAFALLCLPWLQEAGAVQTVPLSRLFDHAMLQAHRAHQLAIDTYQEFEETYIPKDQKYSFLHDSQTSFCFSDSIPTPSNMEETQQKSNLELLRISLLLIESWLEPVRFLRSMFANNLVYDTSDSDDYHLLKDLEEGIQTLMGRLEDGSRRTGQILKQTYSKFDTNSHNHDALLKNYGLLYCFRKDMDKVETFLRMVQCRSVEGSCGF | animal organ development growth hormone receptor signaling pathway positive regulation of growth positive regulation of receptor signaling pathway via JAK-STAT positive regulation of tyrosine phosphorylation of STAT protein response to nutrient levels endoplasmic reticulum; endosome lumen; extracellular region; extracellular space; vesicle growth factor activity growth hormone receptor binding hormone activity metal ion binding Homo sapiens 3D-structure Direct protein sequencing Disulfide bond Hormone Metal-binding Reference proteome Secreted Signal Zinc MAPGSRTSLL MAPGSRTSLLLAFALLCLPWLQEAGAVQTVPLSRLFDHAMLQAHRAHQLAIDTYQEFEETYIPKDQKYSFLHDSQTSFCFSDSIPTPSNMEETQQKSNLELLRISLLLIESWLEPVRFLRSMFANNLVYDTSDSDDYHLLKDLEEGIQTLMGRLEDGSRRTGQILKQTYSKFDTNSHNHDALLKNYGLLYCFRKDMDKVETFLRMVQCRSVEGSCGF |
animal organ development growth hormone receptor signaling pathway positive regulation of growth positive regulation of receptor signaling pathway via JAK-STAT positive regulation of tyrosine phosphorylation of STAT protein response to nutrient levels | endoplasmic reticulum; extracellular space; vesicle | growth factor activity growth hormone receptor binding hormone activity metal ion binding | Homo sapiens | Alternative promoter usage Direct protein sequencing Disulfide bond Hormone Metal-binding Reference proteome Secreted Signal Zinc | MAAGSRTSLL | MAAGSRTSLLLAFALLCLPWLQEAGAVQTVPLSRLFDHAMLQAHRAHQLAIDTYQEFEETYIPKDQKYSFLHDSQTSFCFSDSIPTPSNMEETQQKSNLELLRISLLLIESWLEPVRFLRSMFANNLVYDTSDSDDYHLLKDLEEGIQTLMGRLEDGSRRTGQILKQTYSKFDTNSHNHDALLKNYGLLYCFRKDMDKVETFLRMVQCRSVEGSCGF | animal organ development growth hormone receptor signaling pathway positive regulation of growth positive regulation of receptor signaling pathway via JAK-STAT positive regulation of tyrosine phosphorylation of STAT protein response to nutrient levels endoplasmic reticulum; extracellular space; vesicle growth factor activity growth hormone receptor binding hormone activity metal ion binding Homo sapiens Alternative promoter usage Direct protein sequencing Disulfide bond Hormone Metal-binding Reference proteome Secreted Signal Zinc MAAGSRTSLL MAAGSRTSLLLAFALLCLPWLQEAGAVQTVPLSRLFDHAMLQAHRAHQLAIDTYQEFEETYIPKDQKYSFLHDSQTSFCFSDSIPTPSNMEETQQKSNLELLRISLLLIESWLEPVRFLRSMFANNLVYDTSDSDDYHLLKDLEEGIQTLMGRLEDGSRRTGQILKQTYSKFDTNSHNHDALLKNYGLLYCFRKDMDKVETFLRMVQCRSVEGSCGF |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Balaenoptera acutorostrata scammoni | Chylomicron Endosome Extracellular matrix HDL Heparin-binding Lipid transport Lipid-binding Phosphoprotein Reference proteome Repeat Secreted Signal Transport VLDL | MKVLWVALVI | MKVLWVALVITLLAGCQAEVEPEPEPEVQLGREWPGWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEEQLGPIAQETQARVSKELQAAQARLASDMEDVRSRLAQYRSEVQAVMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGAVEGSERSVSAIRERLGPLMEKGRGRAGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEIREQLEEVRAKVEEQGSQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Balaenoptera acutorostrata scammoni Chylomicron Endosome Extracellular matrix HDL Heparin-binding Lipid transport Lipid-binding Phosphoprotein Reference proteome Repeat Secreted Signal Transport VLDL MKVLWVALVI MKVLWVALVITLLAGCQAEVEPEPEPEVQLGREWPGWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEEQLGPIAQETQARVSKELQAAQARLASDMEDVRSRLAQYRSEVQAVMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGAVEGSERSVSAIRERLGPLMEKGRGRAGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEIREQLEEVRAKVEEQGSQIRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Lipotes vexillifer | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Reference proteome Repeat Secreted Signal Transport VLDL | MKVLWVALVI | MKVLWVALVITLLAGCQAEVEPEPEPEVQLGQEWPGWQDSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEGQLAPIAQETQARVSKELQAAQARLASDMEDVRSRLAQYRSEVQAMMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRARAATVGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEMREQLEEVRAKVEEQGSQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Lipotes vexillifer Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Reference proteome Repeat Secreted Signal Transport VLDL MKVLWVALVI MKVLWVALVITLLAGCQAEVEPEPEPEVQLGQEWPGWQDSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEGQLAPIAQETQARVSKELQAAQARLASDMEDVRSRLAQYRSEVQAMMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRARAATVGTLASQTLRERAEAWHQKLRGRVEEMGTQARDHLEEMREQLEEVRAKVEEQGSQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSSTSAPSENH |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Orcinus orca | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKVLWVALVI | MKVLWVALVITLLAGCQAEVEPEPEPEVQLGREWPRWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEGQLGPIAQETQARVSKELQAAQARLASDMEDVRSRVAQYRSEVQAMMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRVRAATVGTLASQTLRERAEAWHQKLRGRMEEMGTQARDHLEEMREQLEEVRAKVEEQGSQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSPTSAPIENS | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Orcinus orca Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKVLWVALVI MKVLWVALVITLLAGCQAEVEPEPEPEVQLGREWPRWQGSQPWEQALGRFWDYLRWVQTLSDQVQEELLSTQVIQELTVLMDETMKEVKAYREELEGQLGPIAQETQARVSKELQAAQARLASDMEDVRSRVAQYRSEVQAMMGQTTDELRGRLASHLRKLRKRLLRDAEDLQKRLAVYRAGALEGSERSVSAIRERLGPLVEQGRVRAATVGTLASQTLRERAEAWHQKLRGRMEEMGTQARDHLEEMREQLEEVRAKVEEQGSQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQLAMATSPTSAPIENS |
3'-phosphoadenosine 5'-phosphosulfate metabolic process cellular response to dopamine dopamine catabolic process dopamine metabolic process ethanol catabolic process flavonoid metabolic process steroid metabolic process sulfation xenobiotic metabolic process | cytoplasm; cytosol | amine sulfotransferase activity aryl sulfotransferase activity sulfate binding sulfotransferase activity | Homo sapiens | 3D-structure Alternative splicing Catecholamine metabolism Cytoplasm Direct protein sequencing Lipid metabolism Reference proteome Steroid metabolism Transferase | MELIQDTSRP | MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL | 3'-phosphoadenosine 5'-phosphosulfate metabolic process cellular response to dopamine dopamine catabolic process dopamine metabolic process ethanol catabolic process flavonoid metabolic process steroid metabolic process sulfation xenobiotic metabolic process cytoplasm; cytosol amine sulfotransferase activity aryl sulfotransferase activity sulfate binding sulfotransferase activity Homo sapiens 3D-structure Alternative splicing Catecholamine metabolism Cytoplasm Direct protein sequencing Lipid metabolism Reference proteome Steroid metabolism Transferase MELIQDTSRP MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL |
catecholamine metabolic process steroid metabolic process sulfation | cytoplasm; cytosol | aryl sulfotransferase activity | Homo sapiens | Catecholamine metabolism Cytoplasm Lipid metabolism Reference proteome Steroid metabolism Transferase | MELIQDTSRP | MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL | catecholamine metabolic process steroid metabolic process sulfation cytoplasm; cytosol aryl sulfotransferase activity Homo sapiens Catecholamine metabolism Cytoplasm Lipid metabolism Reference proteome Steroid metabolism Transferase MELIQDTSRP MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL |
polyamine metabolic process S-adenosylmethionine metabolic process spermidine biosynthetic process spermine biosynthetic process | cytosol | adenosylmethionine decarboxylase activity identical protein binding putrescine binding | Mus musculus | Autocatalytic cleavage Decarboxylase Lyase Phosphoprotein Polyamine biosynthesis Pyruvate Reference proteome S-adenosyl-L-methionine Schiff base Spermidine biosynthesis Zymogen | MEAAHFFEGT | MEAAHFFEGTEKLLEVWFSRQQSDASQGSGDLRTIPRSEWDVLLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATLFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLSSPQKIDGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS | polyamine metabolic process S-adenosylmethionine metabolic process spermidine biosynthetic process spermine biosynthetic process cytosol adenosylmethionine decarboxylase activity identical protein binding putrescine binding Mus musculus Autocatalytic cleavage Decarboxylase Lyase Phosphoprotein Polyamine biosynthesis Pyruvate Reference proteome S-adenosyl-L-methionine Schiff base Spermidine biosynthesis Zymogen MEAAHFFEGT MEAAHFFEGTEKLLEVWFSRQQSDASQGSGDLRTIPRSEWDVLLKDVQCSIISVTKTDKQEAYVLSESSMFVSKRRFILKTCGTTLLLKALVPLLKLARDYSGFDSIQSFFYSRKNFMKPSHQGYPHRNFQEEIEFLNAIFPNGAAYCMGRMNSDCWYLYTLDFPESRVISQPDQTLEILMSELDPAVMDQFYMKDGVTAKDVTRESGIRDLIPGSVIDATLFNPCGYSMNGMKSDGTYWTIHITPEPEFSYVSFETNLSQTSYDDLIRKVVEVFKPGKFVTTLFVNQSSKCRTVLSSPQKIDGFKRLDCQSAMFNDYNFVFTSFAKKQQQQQS |
cholesterol efflux cholesterol homeostasis chylomicron remnant clearance G protein-coupled receptor signaling pathway high-density lipoprotein particle remodeling lipoprotein metabolic process negative regulation of cholesterol import negative regulation of fatty acid biosynthetic process negative regulation of high-density lipoprotein particle clearance negative regulation of low-density lipoprotein particle clearance negative regulation of receptor-mediated endocytosis negative regulation of triglyceride catabolic process negative regulation of very-low-density lipoprotein particle clearance negative regulation of very-low-density lipoprotein particle remodeling phospholipid efflux regulation of Cdc42 protein signal transduction triglyceride catabolic process triglyceride homeostasis | chylomicron; intermediate-density lipoprotein particle; spherical high-density lipoprotein particle; very-low-density lipoprotein particle | high-density lipoprotein particle receptor binding lipase inhibitor activity phospholipid binding | Panthera tigris altaica | Chylomicron Glycoprotein Lipid degradation Lipid metabolism Lipid transport Reference proteome Secreted Sialic acid Signal Transport VLDL | MQSRVLLVTA | MQSRVLLVTALLVLLASARATEGEDPSLLGLMQGYVQHATKTAQDTLTTMREFPVAQQARDWVTGRFSSLKDYWSTLTGKFSGFWDSTFAVTPTPASEAK | cholesterol efflux cholesterol homeostasis chylomicron remnant clearance G protein-coupled receptor signaling pathway high-density lipoprotein particle remodeling lipoprotein metabolic process negative regulation of cholesterol import negative regulation of fatty acid biosynthetic process negative regulation of high-density lipoprotein particle clearance negative regulation of low-density lipoprotein particle clearance negative regulation of receptor-mediated endocytosis negative regulation of triglyceride catabolic process negative regulation of very-low-density lipoprotein particle clearance negative regulation of very-low-density lipoprotein particle remodeling phospholipid efflux regulation of Cdc42 protein signal transduction triglyceride catabolic process triglyceride homeostasis chylomicron; intermediate-density lipoprotein particle; spherical high-density lipoprotein particle; very-low-density lipoprotein particle high-density lipoprotein particle receptor binding lipase inhibitor activity phospholipid binding Panthera tigris altaica Chylomicron Glycoprotein Lipid degradation Lipid metabolism Lipid transport Reference proteome Secreted Sialic acid Signal Transport VLDL MQSRVLLVTA MQSRVLLVTALLVLLASARATEGEDPSLLGLMQGYVQHATKTAQDTLTTMREFPVAQQARDWVTGRFSSLKDYWSTLTGKFSGFWDSTFAVTPTPASEAK |
fructose biosynthetic process fructose metabolic process NADH oxidation NADH regeneration sorbitol biosynthetic process sorbitol catabolic process | mitochondrial membrane; motile cilium; protein-containing complex | L-iditol 2-dehydrogenase activity NAD binding zinc ion binding | Gallus gallus | Acetylation Cell projection Cilium Flagellum Membrane Metal-binding Mitochondrion NAD Oxidoreductase Reference proteome Zinc | MAATGQNLAV | MAATGQNLAVVVHRAGDLRLENRPIPEPGPNEVLLRMHSVGICGSDVHYWQHGRIGDFVVKDPMVLGHEASGTVIKVGAGVTHLKPGDRVAIEPGVPRETDEFCKTGRYNLSPTIFFCATPPDDGNLCRYYKHSASYCYKLPDSVTFEEGALIEPLSVGIHACKRAGVTLGSRVFVSGSGPIGLVNVIIAKMMGAAAVVVTDLSASRLQTAKELGADFTIQIKNETPQEVAAKVESLLGCMPEITVECTGVQACIQASIYATRSGGTLVLVGLGPEMVTVPIVNAAVREVDIRGIFRYCNTWPVAISLLASKRINIKPLVTHRFPLEKALEAFETTKRGEGVKIMLKCDPTDQNP | fructose biosynthetic process fructose metabolic process NADH oxidation NADH regeneration sorbitol biosynthetic process sorbitol catabolic process mitochondrial membrane; motile cilium; protein-containing complex L-iditol 2-dehydrogenase activity NAD binding zinc ion binding Gallus gallus Acetylation Cell projection Cilium Flagellum Membrane Metal-binding Mitochondrion NAD Oxidoreductase Reference proteome Zinc MAATGQNLAV MAATGQNLAVVVHRAGDLRLENRPIPEPGPNEVLLRMHSVGICGSDVHYWQHGRIGDFVVKDPMVLGHEASGTVIKVGAGVTHLKPGDRVAIEPGVPRETDEFCKTGRYNLSPTIFFCATPPDDGNLCRYYKHSASYCYKLPDSVTFEEGALIEPLSVGIHACKRAGVTLGSRVFVSGSGPIGLVNVIIAKMMGAAAVVVTDLSASRLQTAKELGADFTIQIKNETPQEVAAKVESLLGCMPEITVECTGVQACIQASIYATRSGGTLVLVGLGPEMVTVPIVNAAVREVDIRGIFRYCNTWPVAISLLASKRINIKPLVTHRFPLEKALEAFETTKRGEGVKIMLKCDPTDQNP |
defense response to virus positive regulation of gene expression positive regulation of protein phosphorylation type I interferon-mediated signaling pathway | cytosol; extracellular space; perinuclear region of cytoplasm | cytokine activity cytokine receptor binding | Oncorhynchus mykiss | Alternative splicing Antiviral defense Cytokine Cytoplasm Disulfide bond Secreted Signal | MYTMQSWSCI | MYTMQSWSCIFLIICSMQSVCHCCDWIRHHYGHLSAEYLSLLDQMGGDITKQNAPVLFPTSLYRHIDDAEFEDKVIFLKETIYQITKLFDGNMKSVTWDKKNLDDFLNILERQLENLNSCVSPAMKPERRLKRYFKKLNSKVLRKMNYSAQAWELIRKEIKRHLQRLDILAAQMY | defense response to virus positive regulation of gene expression positive regulation of protein phosphorylation type I interferon-mediated signaling pathway cytosol; extracellular space; perinuclear region of cytoplasm cytokine activity cytokine receptor binding Oncorhynchus mykiss Alternative splicing Antiviral defense Cytokine Cytoplasm Disulfide bond Secreted Signal MYTMQSWSCI MYTMQSWSCIFLIICSMQSVCHCCDWIRHHYGHLSAEYLSLLDQMGGDITKQNAPVLFPTSLYRHIDDAEFEDKVIFLKETIYQITKLFDGNMKSVTWDKKNLDDFLNILERQLENLNSCVSPAMKPERRLKRYFKKLNSKVLRKMNYSAQAWELIRKEIKRHLQRLDILAAQMY |
activation of adenylate cyclase activity G protein-coupled adenosine receptor signaling pathway inflammatory response negative regulation of cell migration negative regulation of cell population proliferation negative regulation of NF-kappaB transcription factor activity presynaptic modulation of chemical synaptic transmission regulation of heart contraction regulation of norepinephrine secretion response to wounding signal transduction | dendrite; plasma membrane; presynaptic membrane; Schaffer collateral - CA1 synapse; synapse | G protein-coupled adenosine receptor activity | Homo sapiens | Alternative splicing Cell membrane Disulfide bond G-protein coupled receptor Glycoprotein Lipoprotein Membrane Palmitate Receptor Reference proteome Transducer Transmembrane Transmembrane helix | MPNNSTALSL | MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIAVGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKRVTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYFSFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFALSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKACVVCHPSDSLDTSIEKNSE | activation of adenylate cyclase activity G protein-coupled adenosine receptor signaling pathway inflammatory response negative regulation of cell migration negative regulation of cell population proliferation negative regulation of NF-kappaB transcription factor activity presynaptic modulation of chemical synaptic transmission regulation of heart contraction regulation of norepinephrine secretion response to wounding signal transduction dendrite; plasma membrane; presynaptic membrane; Schaffer collateral - CA1 synapse; synapse G protein-coupled adenosine receptor activity Homo sapiens Alternative splicing Cell membrane Disulfide bond G-protein coupled receptor Glycoprotein Lipoprotein Membrane Palmitate Receptor Reference proteome Transducer Transmembrane Transmembrane helix MPNNSTALSL MPNNSTALSLANVTYITMEIFIGLCAIVGNVLVICVVKLNPSLQTTTFYFIVSLALADIAVGVLVMPLAIVVSLGITIHFYSCLFMTCLLLIFTHASIMSLLAIAVDRYLRVKLTVRYKRVTTHRRIWLALGLCWLVSFLVGLTPMFGWNMKLTSEYHRNVTFLSCQFVSVMRMDYMVYFSFLTWIFIPLVVMCAIYLDIFYIIRNKLSLNLSNSKETGAFYGREFKTAKSLFLVLFLFALSWLPLSIINCIIYFNGEVPQLVLYMGILLSHANSMMNPIVYAYKIKKFKETYLLILKACVVCHPSDSLDTSIEKNSE |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Capra hircus aegagrus | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKVLWVALVV | MKVLWVALVVALLAGCQADMEGELGSEEPLPPEQPRGQDSQPWEQVLGRLWDYLRWVQTLSDQVQEELLNTQVIQELTVLMEETMKEVKAYREELEGQLAPMAQETQARVSKELQAAQARLGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGASEGAERSVSAIRERLRPLVEQGQSRAATLSTQAAQPLLDRAEAWRQKLHGRLEEVGVRAQDRLDKMRQQLEEVRAKVEEQGSQIRLQAEAFQARLRSWFEPLVGDMQRQWAGLVEKVQLALHLSPTSPPSENH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Capra hircus aegagrus Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKVLWVALVV MKVLWVALVVALLAGCQADMEGELGSEEPLPPEQPRGQDSQPWEQVLGRLWDYLRWVQTLSDQVQEELLNTQVIQELTVLMEETMKEVKAYREELEGQLAPMAQETQARVSKELQAAQARLGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGASEGAERSVSAIRERLRPLVEQGQSRAATLSTQAAQPLLDRAEAWRQKLHGRLEEVGVRAQDRLDKMRQQLEEVRAKVEEQGSQIRLQAEAFQARLRSWFEPLVGDMQRQWAGLVEKVQLALHLSPTSPPSENH |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Ovis aries musimon | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKVLWVALVV | MKVLWVALVVALLAGCQADMEGELGSEEPLPPEQPRGQDSQPWEQVLGRLWDYLRWVQTLSDQVQEELLNTQVIQELTVLMEETMKEVKAYREELEGQLAPMAQETQARVSKELQAAQARLGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGASEGAERSVSAIRERLRPLVEQSQSRAATLSTQVGQPLLDRAEAWRQKLHGRLEEVGVRAQDRLDKMRQQLEEVRAKVEEQGSQIRLQAEAFQARLRSWFEPLVEDMQRQWAGLVEKVQLALHLSPTSPPSENH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Ovis aries musimon Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKVLWVALVV MKVLWVALVVALLAGCQADMEGELGSEEPLPPEQPRGQDSQPWEQVLGRLWDYLRWVQTLSDQVQEELLNTQVIQELTVLMEETMKEVKAYREELEGQLAPMAQETQARVSKELQAAQARLGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGASEGAERSVSAIRERLRPLVEQSQSRAATLSTQVGQPLLDRAEAWRQKLHGRLEEVGVRAQDRLDKMRQQLEEVRAKVEEQGSQIRLQAEAFQARLRSWFEPLVEDMQRQWAGLVEKVQLALHLSPTSPPSENH |
positive regulation of ATPase-coupled calcium transmembrane transporter activity positive regulation of calcium ion import positive regulation of calcium ion import into sarcoplasmic reticulum positive regulation of cardiac muscle cell contraction regulation of ATPase-coupled calcium transmembrane transporter activity regulation of slow-twitch skeletal muscle fiber contraction | sarcoplasmic reticulum membrane | enzyme activator activity | Mus musculus | Membrane Reference proteome Sarcoplasmic reticulum Transmembrane Transmembrane helix | MAEKESTSPH | MAEKESTSPHLIVPILLLVGWIVGCIIVIYIVFF | positive regulation of ATPase-coupled calcium transmembrane transporter activity positive regulation of calcium ion import positive regulation of calcium ion import into sarcoplasmic reticulum positive regulation of cardiac muscle cell contraction regulation of ATPase-coupled calcium transmembrane transporter activity regulation of slow-twitch skeletal muscle fiber contraction sarcoplasmic reticulum membrane enzyme activator activity Mus musculus Membrane Reference proteome Sarcoplasmic reticulum Transmembrane Transmembrane helix MAEKESTSPH MAEKESTSPHLIVPILLLVGWIVGCIIVIYIVFF |
positive regulation of calcium ion import into sarcoplasmic reticulum regulation of ATPase-coupled calcium transmembrane transporter activity regulation of slow-twitch skeletal muscle fiber contraction | sarcoplasmic reticulum membrane | enzyme activator activity | Homo sapiens | 3D-structure Membrane Reference proteome Sarcoplasmic reticulum Transmembrane Transmembrane helix | MAEKAGSTFS | MAEKAGSTFSHLLVPILLLIGWIVGCIIMIYVVFS | positive regulation of calcium ion import into sarcoplasmic reticulum regulation of ATPase-coupled calcium transmembrane transporter activity regulation of slow-twitch skeletal muscle fiber contraction sarcoplasmic reticulum membrane enzyme activator activity Homo sapiens 3D-structure Membrane Reference proteome Sarcoplasmic reticulum Transmembrane Transmembrane helix MAEKAGSTFS MAEKAGSTFSHLLVPILLLIGWIVGCIIMIYVVFS |
apoptotic process cell-cell signaling female gamete generation G protein-coupled receptor signaling pathway hormone-mediated signaling pathway signal transduction | cytoplasm; extracellular region; extracellular space; pituitary gonadotropin complex | hormone activity | Homo sapiens | 3D-structure Alternative splicing Direct protein sequencing Disulfide bond Glycoprotein Hormone Pharmaceutical Reference proteome Secreted Signal | MEMFQGLLLL | MEMFQGLLLLLLLSMGGTWASKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ | apoptotic process cell-cell signaling female gamete generation G protein-coupled receptor signaling pathway hormone-mediated signaling pathway signal transduction cytoplasm; extracellular region; extracellular space; pituitary gonadotropin complex hormone activity Homo sapiens 3D-structure Alternative splicing Direct protein sequencing Disulfide bond Glycoprotein Hormone Pharmaceutical Reference proteome Secreted Signal MEMFQGLLLL MEMFQGLLLLLLLSMGGTWASKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ |
chaperone cofactor-dependent protein refolding protein refolding response to heat | chloroplast; cytoplasm; endoplasmic reticulum | ATP binding heat shock protein binding metal ion binding unfolded protein binding | Oryza sativa subsp. japonica | Chloroplast Metal-binding Plastid Reference proteome Repeat Transit peptide Zinc Zinc-finger | MALLQFGGTL | MALLQFGGTLAPKLGEKPQLLPRSPALTRVIYADPRFLVSKSGSGGRLKHLVSPTASLQSRTSSRLFNHAPSPRFRHRRSSRFIVRADADFYSTLGVSRNASKSEIKSAYRKLARSYHPDVNKDPGAEQKFKDISNAYEVLSDDEKRSIYDKYGEAGLKGAGMGTGDYSNPFDLFESLFEGFGGMGGMGGRAARNRPMQGDDEAYNLVLNFKEAVFGVEKEIEITRLEGCNTCDGTGAKPGTKPTTCKTCGGQGQVVSSTRTPLGIFQQVSTCNTCGGTGEFSTPCNTCGGDGRVRKTKRISLKVPAGVDSGSRLRVRSEGNAGRRGGPPGDLYVFIDVLSDPVLKRDGTNILYTCKVSYIDAILGTTVKVPTVDGMVDLKIPSGTQPGTTLVMSKKGVPLLGKSNARGDQLVRVQVEIPKRLSSDERKLIEELANLNKAQTANSRR | chaperone cofactor-dependent protein refolding protein refolding response to heat chloroplast; cytoplasm; endoplasmic reticulum ATP binding heat shock protein binding metal ion binding unfolded protein binding Oryza sativa subsp. japonica Chloroplast Metal-binding Plastid Reference proteome Repeat Transit peptide Zinc Zinc-finger MALLQFGGTL MALLQFGGTLAPKLGEKPQLLPRSPALTRVIYADPRFLVSKSGSGGRLKHLVSPTASLQSRTSSRLFNHAPSPRFRHRRSSRFIVRADADFYSTLGVSRNASKSEIKSAYRKLARSYHPDVNKDPGAEQKFKDISNAYEVLSDDEKRSIYDKYGEAGLKGAGMGTGDYSNPFDLFESLFEGFGGMGGMGGRAARNRPMQGDDEAYNLVLNFKEAVFGVEKEIEITRLEGCNTCDGTGAKPGTKPTTCKTCGGQGQVVSSTRTPLGIFQQVSTCNTCGGTGEFSTPCNTCGGDGRVRKTKRISLKVPAGVDSGSRLRVRSEGNAGRRGGPPGDLYVFIDVLSDPVLKRDGTNILYTCKVSYIDAILGTTVKVPTVDGMVDLKIPSGTQPGTTLVMSKKGVPLLGKSNARGDQLVRVQVEIPKRLSSDERKLIEELANLNKAQTANSRR |
protein folding response to heat | chloroplast; endoplasmic reticulum | ATP binding heat shock protein binding metal ion binding unfolded protein binding | Oryza sativa subsp. japonica | Chloroplast Metal-binding Plastid Reference proteome Repeat Transit peptide Zinc Zinc-finger | MALLQFGGTL | MALLQFGGTLAPKLGEKPQLLPRSPALTRVIYADPRFLVSKSGSGGRLKHLVSPTASLQSRTSSRLFNHAPSPRFRHRRSSRFIVRADADFYSTLGVSRNASKSEIKSAYRKLARSYHPDVNKDPGAEQKFKDISNAYEVLSDDEKRSIYDKYGEAGLKGAGMGTGDYSNPFDLFESLFEGFGGMGGMGGRAARNRPMQGDDEAYNLVLNFKEAVFGVEKEIEITRLEGCNTCDGTGAKPGTKPTTCKTCGGQGQVVSSTRTPLGIFQQVSTCNTCGGTGEFSTPCNTCGGDGRVRKTKRISLKVPAGVDSGSRLRVRSEGNAGRRGGPPGDLYVFIDVLSDPVLKRDGTNILYTCKVSYIDAILGTTVKVPTVDGMVDLKIPSGTQPGTTLVMSKKGVPLLGKSNARGDQLVRVQVEIPKRLSSDERKLIEELANLNKAQTANSRR | protein folding response to heat chloroplast; endoplasmic reticulum ATP binding heat shock protein binding metal ion binding unfolded protein binding Oryza sativa subsp. japonica Chloroplast Metal-binding Plastid Reference proteome Repeat Transit peptide Zinc Zinc-finger MALLQFGGTL MALLQFGGTLAPKLGEKPQLLPRSPALTRVIYADPRFLVSKSGSGGRLKHLVSPTASLQSRTSSRLFNHAPSPRFRHRRSSRFIVRADADFYSTLGVSRNASKSEIKSAYRKLARSYHPDVNKDPGAEQKFKDISNAYEVLSDDEKRSIYDKYGEAGLKGAGMGTGDYSNPFDLFESLFEGFGGMGGMGGRAARNRPMQGDDEAYNLVLNFKEAVFGVEKEIEITRLEGCNTCDGTGAKPGTKPTTCKTCGGQGQVVSSTRTPLGIFQQVSTCNTCGGTGEFSTPCNTCGGDGRVRKTKRISLKVPAGVDSGSRLRVRSEGNAGRRGGPPGDLYVFIDVLSDPVLKRDGTNILYTCKVSYIDAILGTTVKVPTVDGMVDLKIPSGTQPGTTLVMSKKGVPLLGKSNARGDQLVRVQVEIPKRLSSDERKLIEELANLNKAQTANSRR |
response to abscisic acid response to cytokine response to glucose response to mannose response to salt response to starvation response to sucrose | cytoplasm; cytosol; nucleus | metal ion binding | Arabidopsis thaliana | Cytoplasm Metal-binding Nucleus Reference proteome Zinc Zinc-finger | MTKISVGLQL | MTKISVGLQLVTRDSREKLNNIVIKSSLRLNRSNPNISELCFLKTCHLCNKQLHQDKDVYMYRGDLGFCSRECRESQMLIDDRKELEASTKMMLASYRRCNNGAGKSESRNLFDDLRRRRQLFIVP | response to abscisic acid response to cytokine response to glucose response to mannose response to salt response to starvation response to sucrose cytoplasm; cytosol; nucleus metal ion binding Arabidopsis thaliana Cytoplasm Metal-binding Nucleus Reference proteome Zinc Zinc-finger MTKISVGLQL MTKISVGLQLVTRDSREKLNNIVIKSSLRLNRSNPNISELCFLKTCHLCNKQLHQDKDVYMYRGDLGFCSRECRESQMLIDDRKELEASTKMMLASYRRCNNGAGKSESRNLFDDLRRRRQLFIVP |
intracellular manganese ion homeostasis intracellular sequestering of iron ion iron ion transport | vacuolar membrane | manganese ion transmembrane transporter activity metal ion binding protein homodimerization activity | Eucalyptus grandis | 3D-structure Ion transport Iron Iron transport Membrane Metal-binding Transmembrane Transmembrane helix Transport Vacuole | MADGANDGGN | MADGANDGGNPGAEEQQRLLDQHKEAHFTAGEIVRDIIIGVSDGLTVPFALAAGLSGANASSSIVLTAGIAEVAAGAISMGLGGYLAAKSEADNYARELKREQEEIIRVPDTEAAEVAEILARYGIEPHEYGPVVNALRKKPQAWLDFMMKFELGLEKPDPKRALQSAFTIAIAYVLGGLVPLIPYMFIPVARKAVVASVILTLMALLIFGYAKGYFTDNKPFKSALQTALIGAIASAAAFGMAKAVQS | intracellular manganese ion homeostasis intracellular sequestering of iron ion iron ion transport vacuolar membrane manganese ion transmembrane transporter activity metal ion binding protein homodimerization activity Eucalyptus grandis 3D-structure Ion transport Iron Iron transport Membrane Metal-binding Transmembrane Transmembrane helix Transport Vacuole MADGANDGGN MADGANDGGNPGAEEQQRLLDQHKEAHFTAGEIVRDIIIGVSDGLTVPFALAAGLSGANASSSIVLTAGIAEVAAGAISMGLGGYLAAKSEADNYARELKREQEEIIRVPDTEAAEVAEILARYGIEPHEYGPVVNALRKKPQAWLDFMMKFELGLEKPDPKRALQSAFTIAIAYVLGGLVPLIPYMFIPVARKAVVASVILTLMALLIFGYAKGYFTDNKPFKSALQTALIGAIASAAAFGMAKAVQS |
nonphotochemical quenching photosynthesis, light harvesting in photosystem I response to high light intensity response to light stimulus response to photooxidative stress | chloroplast thylakoid membrane; photosystem I; photosystem II | chlorophyll binding metal ion binding | Chlamydomonas reinhardtii | Chlorophyll Chloroplast Chromophore Magnesium Membrane Metal-binding Photosynthesis Photosystem I Photosystem II Plastid Reference proteome Stress response Thylakoid Transit peptide Transmembrane Transmembrane helix | MLANVVSRKA | MLANVVSRKASGLRQTPARATVAVKSVSGRRTTAAEPQTAAPVAAEDVFAYTKNLPGVTAPFEGVFDPAGFLATASIKDVRRWRESEITHGRVAMLAALGFVVGEQLQDFPLFFNWDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKVMQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLALRFEKEAILELDDIERDLGLPVTPLPDNLKSL | nonphotochemical quenching photosynthesis, light harvesting in photosystem I response to high light intensity response to light stimulus response to photooxidative stress chloroplast thylakoid membrane; photosystem I; photosystem II chlorophyll binding metal ion binding Chlamydomonas reinhardtii Chlorophyll Chloroplast Chromophore Magnesium Membrane Metal-binding Photosynthesis Photosystem I Photosystem II Plastid Reference proteome Stress response Thylakoid Transit peptide Transmembrane Transmembrane helix MLANVVSRKA MLANVVSRKASGLRQTPARATVAVKSVSGRRTTAAEPQTAAPVAAEDVFAYTKNLPGVTAPFEGVFDPAGFLATASIKDVRRWRESEITHGRVAMLAALGFVVGEQLQDFPLFFNWDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKVMQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLALRFEKEAILELDDIERDLGLPVTPLPDNLKSL |
nonphotochemical quenching photosynthesis, light harvesting in photosystem I response to high light intensity response to light stimulus response to photooxidative stress | chloroplast thylakoid membrane; photosystem I; photosystem II | chlorophyll binding metal ion binding | Chlamydomonas reinhardtii | Chlorophyll Chloroplast Chromophore Magnesium Membrane Metal-binding Photosynthesis Photosystem I Photosystem II Plastid Reference proteome Stress response Thylakoid Transit peptide Transmembrane Transmembrane helix | MLANVVSRKA | MLANVVSRKASGLRQTPARATVAVKSVSGRRTTAAEPQTAAPVAAEDVFAYTKNLPGVTAPFEGVFDPAGFLATASIKDVRRWRESEITHGRVAMLAALGFVVGEQLQDFPLFFNWDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKVMQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLALRFEKEAILELDDIERDLGLPVTPLPDNLKSL | nonphotochemical quenching photosynthesis, light harvesting in photosystem I response to high light intensity response to light stimulus response to photooxidative stress chloroplast thylakoid membrane; photosystem I; photosystem II chlorophyll binding metal ion binding Chlamydomonas reinhardtii Chlorophyll Chloroplast Chromophore Magnesium Membrane Metal-binding Photosynthesis Photosystem I Photosystem II Plastid Reference proteome Stress response Thylakoid Transit peptide Transmembrane Transmembrane helix MLANVVSRKA MLANVVSRKASGLRQTPARATVAVKSVSGRRTTAAEPQTAAPVAAEDVFAYTKNLPGVTAPFEGVFDPAGFLATASIKDVRRWRESEITHGRVAMLAALGFVVGEQLQDFPLFFNWDGRVSGPAIYHFQQIGQGFWEPLLIAIGVAESYRVAVGWATPTGTGFNSLKDDYEPGDLGFDPLGLKPTDPEELKVMQTKELNNGRLAMIAIAAFVAQELVEQTEIFEHLALRFEKEAILELDDIERDLGLPVTPLPDNLKSL |
indole alkaloid biosynthetic process | endoplasmic reticulum membrane | heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Catharanthus roseus | Alkaloid metabolism Endoplasmic reticulum Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Transmembrane Transmembrane helix | MELDECSPSI | MELDECSPSIFIISFIFIAISIAILRRIRPKKTKALPPGPWKLPLIGNLHQFISRDSLPYKILRDLAQKHGPLMHLQLGEVSAVVASSPEMAKVITRTKDLEFADKPAIRAIRIVTYDYLDIAFNSYGKYWREMRKIFVQELLTPKRVRSFWSAREDVFSNLVKTINSANGKSINLTKLISSTTNSIINRVALGNVPYEREIFMELIKQLLTAAGGFKLVDLFPSYKIIHVLEGTERKLWKILGKIDKILDKVIDEHRENLLRTGKGSGENGQEDIVDILLKIEDGGELDHDIPFGNNNIKALLFDIISGGSDTSSTTIDWAMSEMMKNPQVMSKAQKEIREAFNGKKKIDENDVQNLKYLKSVIQETLRLHPPAAFLMRQCREECEIGGYHIPVGTKVFINIWAMGRDPEHWPNPESFIPERFENIPYDFTGSEHQLATFPFGSGRRICPGISFGLANVELSLALLLYHFNWQLPDSSTDLDMTEAIGIAARRKYDLHLIPTSYM | indole alkaloid biosynthetic process endoplasmic reticulum membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Catharanthus roseus Alkaloid metabolism Endoplasmic reticulum Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Transmembrane Transmembrane helix MELDECSPSI MELDECSPSIFIISFIFIAISIAILRRIRPKKTKALPPGPWKLPLIGNLHQFISRDSLPYKILRDLAQKHGPLMHLQLGEVSAVVASSPEMAKVITRTKDLEFADKPAIRAIRIVTYDYLDIAFNSYGKYWREMRKIFVQELLTPKRVRSFWSAREDVFSNLVKTINSANGKSINLTKLISSTTNSIINRVALGNVPYEREIFMELIKQLLTAAGGFKLVDLFPSYKIIHVLEGTERKLWKILGKIDKILDKVIDEHRENLLRTGKGSGENGQEDIVDILLKIEDGGELDHDIPFGNNNIKALLFDIISGGSDTSSTTIDWAMSEMMKNPQVMSKAQKEIREAFNGKKKIDENDVQNLKYLKSVIQETLRLHPPAAFLMRQCREECEIGGYHIPVGTKVFINIWAMGRDPEHWPNPESFIPERFENIPYDFTGSEHQLATFPFGSGRRICPGISFGLANVELSLALLLYHFNWQLPDSSTDLDMTEAIGIAARRKYDLHLIPTSYM |
defense response to insect response to insect response to jasmonic acid response to salicylic acid response to UV-C terpenoid biosynthetic process | membrane | heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Origanum vulgare | Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix | MDISISWVVI | MDISISWVVIILLVLSYLILMEKWRAAKLPKNLPPGPPKLPVIGHLHLLGGGLPQHVLRGITQKYGPVAHVQLGEVSSVVLSSTEAARQAMKVLDPAFADRFVNIGSRIMWYDSEDIIFSRYNDHWRQIRKICVSELLSPKNVKSFGYIRQDEMARLIRLFESSEGAAINVSEEISKTVCTIVSRVAFGSVVKDQSLLLNLVKESLRMASGFELADLFPSSWLLNLLCFNKYRLWGMRRRLDNFLDGFLEEHRVKKSGEYGGEDIIDVLYRMQKDSQMKVPITNNGIKGFIYDVFSAGTDTSAATILWALSELMRNPEKMAKAQAEVREILKGKTNVDMAEVHELKYLRSVVKEALRLHPPFPIIPRLCIQESEVTGYTIPANTRILINVWSIGRDPLYWNEPDTFNPDRYDEVPRDIIGNDFELIPFGSGRRICPGLHFGLANIEVPLAQLLYHFDWKLPQGMTAADIDMTEKPGLSGPRKNPLILVPTIHNPTS | defense response to insect response to insect response to jasmonic acid response to salicylic acid response to UV-C terpenoid biosynthetic process membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Origanum vulgare Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix MDISISWVVI MDISISWVVIILLVLSYLILMEKWRAAKLPKNLPPGPPKLPVIGHLHLLGGGLPQHVLRGITQKYGPVAHVQLGEVSSVVLSSTEAARQAMKVLDPAFADRFVNIGSRIMWYDSEDIIFSRYNDHWRQIRKICVSELLSPKNVKSFGYIRQDEMARLIRLFESSEGAAINVSEEISKTVCTIVSRVAFGSVVKDQSLLLNLVKESLRMASGFELADLFPSSWLLNLLCFNKYRLWGMRRRLDNFLDGFLEEHRVKKSGEYGGEDIIDVLYRMQKDSQMKVPITNNGIKGFIYDVFSAGTDTSAATILWALSELMRNPEKMAKAQAEVREILKGKTNVDMAEVHELKYLRSVVKEALRLHPPFPIIPRLCIQESEVTGYTIPANTRILINVWSIGRDPLYWNEPDTFNPDRYDEVPRDIIGNDFELIPFGSGRRICPGLHFGLANIEVPLAQLLYHFDWKLPQGMTAADIDMTEKPGLSGPRKNPLILVPTIHNPTS |
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