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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epithelial cell differentiation fructose 1,6-bisphosphate metabolic process gluconeogenesis glycolytic process | axon; cytosol; mitochondrion; postsynaptic cytosol | cytoskeletal protein binding fructose-bisphosphate aldolase activity identical protein binding protein-containing complex binding | Mus musculus | Acetylation Direct protein sequencing Glycolysis Lyase Phosphoprotein Reference proteome Schiff base | MPHSYPALSA | MPHSYPALSAEQKKELSDIALRIVTPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY | epithelial cell differentiation fructose 1,6-bisphosphate metabolic process gluconeogenesis glycolytic process axon; cytosol; mitochondrion; postsynaptic cytosol cytoskeletal protein binding fructose-bisphosphate aldolase activity identical protein binding protein-containing complex binding Mus musculus Acetylation Direct protein sequencing Glycolysis Lyase Phosphoprotein Reference proteome Schiff base MPHSYPALSA MPHSYPALSAEQKKELSDIALRIVTPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY |
ATP biosynthetic process binding of sperm to zona pellucida canonical glycolysis fructose 1,6-bisphosphate metabolic process fructose metabolic process glycolytic process glycolytic process through fructose-6-phosphate methylglyoxal biosynthetic process muscle cell cellular homeostasis positive regulation of cell migration protein homotetramerization regulation of cell shape striated muscle contraction | actin cytoskeleton; cytoplasm; cytosol; extracellular exosome; extracellular space; heterochromatin; M band; membrane; myelin sheath; plasma membrane; protein-containing complex; sperm fibrous sheath; sperm head; Z disc | cytoskeletal protein binding fructose binding fructose-bisphosphate aldolase activity identical protein binding protease binding | Mus musculus | Acetylation Cytoplasm Direct protein sequencing Glycolysis Hydroxylation Isopeptide bond Lyase Phosphoprotein Reference proteome Schiff base Ubl conjugation | MPHPYPALTP | MPHPYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYIKRALANSLACQGKYTPSGQSGAAASESLFISNHAY | ATP biosynthetic process binding of sperm to zona pellucida canonical glycolysis fructose 1,6-bisphosphate metabolic process fructose metabolic process glycolytic process glycolytic process through fructose-6-phosphate methylglyoxal biosynthetic process muscle cell cellular homeostasis positive regulation of cell migration protein homotetramerization regulation of cell shape striated muscle contraction actin cytoskeleton; cytoplasm; cytosol; extracellular exosome; extracellular space; heterochromatin; M band; membrane; myelin sheath; plasma membrane; protein-containing complex; sperm fibrous sheath; sperm head; Z disc cytoskeletal protein binding fructose binding fructose-bisphosphate aldolase activity identical protein binding protease binding Mus musculus Acetylation Cytoplasm Direct protein sequencing Glycolysis Hydroxylation Isopeptide bond Lyase Phosphoprotein Reference proteome Schiff base Ubl conjugation MPHPYPALTP MPHPYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYIKRALANSLACQGKYTPSGQSGAAASESLFISNHAY |
ATP biosynthetic process binding of sperm to zona pellucida fructose 1,6-bisphosphate metabolic process fructose metabolic process glycolytic process methylglyoxal biosynthetic process muscle cell cellular homeostasis protein homotetramerization regulation of cell shape response to estrogen response to hypoxia response to lipopolysaccharide response to nicotine striated muscle contraction | actin cytoskeleton; cytoplasm; cytosol; extracellular exosome; heterochromatin; I band; M band; sperm head | cytoskeletal protein binding fructose binding fructose-bisphosphate aldolase activity identical protein binding | Rattus norvegicus | Acetylation Cytoplasm Direct protein sequencing Glycolysis Hydroxylation Isopeptide bond Lyase Phosphoprotein Reference proteome Schiff base Ubl conjugation | MPHPYPALTP | MPHPYPALTPEQKKELADIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSSLAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYIKRALANSLACQGKYTPSGQSGAAASESLFISNHAY | ATP biosynthetic process binding of sperm to zona pellucida fructose 1,6-bisphosphate metabolic process fructose metabolic process glycolytic process methylglyoxal biosynthetic process muscle cell cellular homeostasis protein homotetramerization regulation of cell shape response to estrogen response to hypoxia response to lipopolysaccharide response to nicotine striated muscle contraction actin cytoskeleton; cytoplasm; cytosol; extracellular exosome; heterochromatin; I band; M band; sperm head cytoskeletal protein binding fructose binding fructose-bisphosphate aldolase activity identical protein binding Rattus norvegicus Acetylation Cytoplasm Direct protein sequencing Glycolysis Hydroxylation Isopeptide bond Lyase Phosphoprotein Reference proteome Schiff base Ubl conjugation MPHPYPALTP MPHPYPALTPEQKKELADIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSSLAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYIKRALANSLACQGKYTPSGQSGAAASESLFISNHAY |
circadian regulation of gene expression entrainment of circadian clock by photoperiod photoreactive repair | cytoplasm; mitochondrion; nucleus | deoxyribodipyrimidine photo-lyase activity DNA binding FAD binding mRNA binding | Saccharomyces cerevisiae | Chromophore DNA damage DNA repair DNA-binding FAD Flavoprotein Lyase Mitochondrion Nucleotide-binding Nucleus Reference proteome Transit peptide | MKRTVISSSN | MKRTVISSSNAYASKRSRLDIEHDFEQYHSLNKKYYPRPITRTGANQFNNKSRAKPMEIVEKLQKKQKTSFENVSTVMHWFRNDLRLYDNVGLYKSVALFQQLRQKNAKAKLYAVYVINEDDWRAHMDSGWKLMFIMGALKNLQQSLAELHIPLLLWEFHTPKSTLSNSKEFVEFFKEKCMNVSSGTGTIITANIEYQTDELYRDIRLLENEDHRLQLKYYHDSCIVAPGLITTDRGTNYSVFTPWYKKWVLYVNNYKKSTSEICHLHIIEPLKYNETFELKPFQYSLPDEFLQYIPKSKWCLPDVSEEAALSRLKDFLGTKSSKYNNEKDMLYLGGTSGLSVYITTGRISTRLIVNQAFQSCNGQIMSKALKDNSSTQNFIKEVAWRDFYRHCMCNWPYTSMGMPYRLDTLDIKWENNPVAFEKWCTGNTGIPIVDAIMRKLLYTGYINNRSRMITASFLSKNLLIDWRWGERWFMKHLIDGDSSSNVGGWGFCSSTGIDAQPYFRVFNMDIQAKKYDPQMIFVKQWVPELISSENKRPENYPKPLVDLKHSRERALKVYKDAM | circadian regulation of gene expression entrainment of circadian clock by photoperiod photoreactive repair cytoplasm; mitochondrion; nucleus deoxyribodipyrimidine photo-lyase activity DNA binding FAD binding mRNA binding Saccharomyces cerevisiae Chromophore DNA damage DNA repair DNA-binding FAD Flavoprotein Lyase Mitochondrion Nucleotide-binding Nucleus Reference proteome Transit peptide MKRTVISSSN MKRTVISSSNAYASKRSRLDIEHDFEQYHSLNKKYYPRPITRTGANQFNNKSRAKPMEIVEKLQKKQKTSFENVSTVMHWFRNDLRLYDNVGLYKSVALFQQLRQKNAKAKLYAVYVINEDDWRAHMDSGWKLMFIMGALKNLQQSLAELHIPLLLWEFHTPKSTLSNSKEFVEFFKEKCMNVSSGTGTIITANIEYQTDELYRDIRLLENEDHRLQLKYYHDSCIVAPGLITTDRGTNYSVFTPWYKKWVLYVNNYKKSTSEICHLHIIEPLKYNETFELKPFQYSLPDEFLQYIPKSKWCLPDVSEEAALSRLKDFLGTKSSKYNNEKDMLYLGGTSGLSVYITTGRISTRLIVNQAFQSCNGQIMSKALKDNSSTQNFIKEVAWRDFYRHCMCNWPYTSMGMPYRLDTLDIKWENNPVAFEKWCTGNTGIPIVDAIMRKLLYTGYINNRSRMITASFLSKNLLIDWRWGERWFMKHLIDGDSSSNVGGWGFCSSTGIDAQPYFRVFNMDIQAKKYDPQMIFVKQWVPELISSENKRPENYPKPLVDLKHSRERALKVYKDAM |
ADP biosynthetic process AMP metabolic process ATP metabolic process nucleoside triphosphate biosynthetic process phosphorylation | cytoplasm; cytosol | adenylate kinase activity ATP binding magnesium ion binding nucleoside diphosphate kinase activity nucleoside triphosphate adenylate kinase activity | Gallus gallus | ATP-binding Cytoplasm Kinase Nucleotide-binding Reference proteome Transferase | MSTEKLKHHK | MSTEKLKHHKIIFVVGGPGSGKGTQCEKIVHKYGYTHLSTGDLLRAEVSSGSERGKKLQAIMEKGELVPLDTVLDMLRDAMLAKADTSKGFLIDGYPREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYKGRGIVRQLNAEGTVDEVFQQVCSYLDKL | ADP biosynthetic process AMP metabolic process ATP metabolic process nucleoside triphosphate biosynthetic process phosphorylation cytoplasm; cytosol adenylate kinase activity ATP binding magnesium ion binding nucleoside diphosphate kinase activity nucleoside triphosphate adenylate kinase activity Gallus gallus ATP-binding Cytoplasm Kinase Nucleotide-binding Reference proteome Transferase MSTEKLKHHK MSTEKLKHHKIIFVVGGPGSGKGTQCEKIVHKYGYTHLSTGDLLRAEVSSGSERGKKLQAIMEKGELVPLDTVLDMLRDAMLAKADTSKGFLIDGYPREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYKGRGIVRQLNAEGTVDEVFQQVCSYLDKL |
anterior/posterior axis specification ganglion mother cell fate determination generation of neurons negative regulation of transcription by RNA polymerase II neuroblast fate determination positive regulation of transcription by RNA polymerase II posterior head segmentation regulation of development, heterochronic regulation of neural precursor cell proliferation regulation of neurogenesis regulation of transcription by RNA polymerase II salivary gland development trunk segmentation ventral cord development zygotic determination of anterior/posterior axis, embryo | nucleus | DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific metal ion binding RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding sequence-specific DNA binding | Drosophila melanogaster | Developmental protein DNA-binding Gap protein Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Zinc Zinc-finger | MQNWETTATT | MQNWETTATTNYEQHNAWYNSMFAANIKQEPGHHLDGNSVASSPRQSPIPSTNHLEQFLKQQQQQLQQQPMDTLCAMTPSPSQNDQNSLQHYDANLQQQLLQQQQYQQHFQAAQQQHHHHHHLMGGFNPLTPPGLPNPMQHFYGGNLRPSPQPTPTSASTIAPVAVATGSSEKLQALTPPMDVTPPKSPAKSSQSNIEPEKEHDQMSNSSEDMKYMAESEDDDTNIRMPIYNSHGKMKNYKCKTCGVVAITKVDFWAHTRTHMKPDKILQCPKCPFVTEFKHHLEYHIRKHKNQKPFQCDKCSYTCVNKSMLNSHRKSHSSVYQYRCADCDYATKYCHSFKLHLRKYGHKPGMVLDEDGTPNPSLVIDVYGTRRGPKSKNGGPIASGGSGSGSRKSNVAAVAPQQQQSQPAQPVATSQLSAALQGFPLVQGNSAPPAASPVLPLPASPAKSVASVEQTPSLPSPANLLPPLASLLQQNRNMAFFPYWNLNLQMLAAQQQAAVLAQLSPRMREQLQQQNQQQSDNEEEEQDDEYERKSVDSAMDLSQGTPVKEDEQQQQPQQPLAMNLKVEEEATPLMSSSNASRRKGRVLKLDTLLQLRSEAMTSPEQLKVPSTPMPTASSPIAGRKPMPEEHCSGTSSADESMETAHVPQANTSASSTASSSGNSSNASSNSNGNSSSNSSSNGTTSAVAAPPSGTPAAAGAIYECKYCDIFFKDAVLYTIHMGYHSCDDVFKCNMCGEKCDGPVGLFVHMARNAHS | anterior/posterior axis specification ganglion mother cell fate determination generation of neurons negative regulation of transcription by RNA polymerase II neuroblast fate determination positive regulation of transcription by RNA polymerase II posterior head segmentation regulation of development, heterochronic regulation of neural precursor cell proliferation regulation of neurogenesis regulation of transcription by RNA polymerase II salivary gland development trunk segmentation ventral cord development zygotic determination of anterior/posterior axis, embryo nucleus DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific metal ion binding RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II transcription regulatory region sequence-specific DNA binding sequence-specific DNA binding Drosophila melanogaster Developmental protein DNA-binding Gap protein Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Zinc Zinc-finger MQNWETTATT MQNWETTATTNYEQHNAWYNSMFAANIKQEPGHHLDGNSVASSPRQSPIPSTNHLEQFLKQQQQQLQQQPMDTLCAMTPSPSQNDQNSLQHYDANLQQQLLQQQQYQQHFQAAQQQHHHHHHLMGGFNPLTPPGLPNPMQHFYGGNLRPSPQPTPTSASTIAPVAVATGSSEKLQALTPPMDVTPPKSPAKSSQSNIEPEKEHDQMSNSSEDMKYMAESEDDDTNIRMPIYNSHGKMKNYKCKTCGVVAITKVDFWAHTRTHMKPDKILQCPKCPFVTEFKHHLEYHIRKHKNQKPFQCDKCSYTCVNKSMLNSHRKSHSSVYQYRCADCDYATKYCHSFKLHLRKYGHKPGMVLDEDGTPNPSLVIDVYGTRRGPKSKNGGPIASGGSGSGSRKSNVAAVAPQQQQSQPAQPVATSQLSAALQGFPLVQGNSAPPAASPVLPLPASPAKSVASVEQTPSLPSPANLLPPLASLLQQNRNMAFFPYWNLNLQMLAAQQQAAVLAQLSPRMREQLQQQNQQQSDNEEEEQDDEYERKSVDSAMDLSQGTPVKEDEQQQQPQQPLAMNLKVEEEATPLMSSSNASRRKGRVLKLDTLLQLRSEAMTSPEQLKVPSTPMPTASSPIAGRKPMPEEHCSGTSSADESMETAHVPQANTSASSTASSSGNSSNASSNSNGNSSSNSSSNGTTSAVAAPPSGTPAAAGAIYECKYCDIFFKDAVLYTIHMGYHSCDDVFKCNMCGEKCDGPVGLFVHMARNAHS |
adaptive immune response arginine catabolic process arginine catabolic process to ornithine defense response to protozoan innate immune response negative regulation of activated T cell proliferation negative regulation of T cell proliferation negative regulation of T-helper 2 cell cytokine production negative regulation of type II interferon-mediated signaling pathway positive regulation of neutrophil mediated killing of fungus urea cycle | azurophil granule lumen; cytoplasm; cytosol; extracellular region; extracellular space; nucleus; specific granule lumen | arginase activity manganese ion binding | Homo sapiens | 3D-structure Adaptive immunity Alternative splicing Arginine metabolism Cytoplasm Disease variant Hydrolase Immunity Innate immunity Manganese Metal-binding Phosphoprotein Reference proteome Urea cycle | MSAKSRTIGI | MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK | adaptive immune response arginine catabolic process arginine catabolic process to ornithine defense response to protozoan innate immune response negative regulation of activated T cell proliferation negative regulation of T cell proliferation negative regulation of T-helper 2 cell cytokine production negative regulation of type II interferon-mediated signaling pathway positive regulation of neutrophil mediated killing of fungus urea cycle azurophil granule lumen; cytoplasm; cytosol; extracellular region; extracellular space; nucleus; specific granule lumen arginase activity manganese ion binding Homo sapiens 3D-structure Adaptive immunity Alternative splicing Arginine metabolism Cytoplasm Disease variant Hydrolase Immunity Innate immunity Manganese Metal-binding Phosphoprotein Reference proteome Urea cycle MSAKSRTIGI MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPNDSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGVIWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSFTPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAITLACFGLAREGNHKPIDYLNPPK |
angiogenesis brain development glucose metabolic process lipid metabolic process negative regulation of cytokine production involved in inflammatory response negative regulation of focal adhesion assembly negative regulation of lipoprotein lipid oxidation negative regulation of monocyte chemotactic protein-1 production negative regulation of platelet-derived growth factor receptor signaling pathway negative regulation of protein import into nucleus negative regulation of smooth muscle cell proliferation negative regulation of smooth muscle cell-matrix adhesion negative regulation of T cell migration peripheral nervous system axon regeneration response to axon injury response to reactive oxygen species tissue regeneration | cytoplasm; cytosolic ribosome; dendrite; endoplasmic reticulum; extracellular exosome; extracellular region; extracellular space; neuronal cell body; perinuclear region of cytoplasm | cholesterol binding lipid transporter activity | Homo sapiens | 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Lipid-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal Transport | MVMLLLLLSA | MVMLLLLLSALAGLFGAAEGQAFHLGKCPNPPVQENFDVNKYLGRWYEIEKIPTTFENGRCIQANYSLMENGKIKVLNQELRADGTVNQIEGEATPVNLTEPAKLEVKFSWFMPSAPYWILATDYENYALVYSCTCIIQLFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQVNCPKLS | angiogenesis brain development glucose metabolic process lipid metabolic process negative regulation of cytokine production involved in inflammatory response negative regulation of focal adhesion assembly negative regulation of lipoprotein lipid oxidation negative regulation of monocyte chemotactic protein-1 production negative regulation of platelet-derived growth factor receptor signaling pathway negative regulation of protein import into nucleus negative regulation of smooth muscle cell proliferation negative regulation of smooth muscle cell-matrix adhesion negative regulation of T cell migration peripheral nervous system axon regeneration response to axon injury response to reactive oxygen species tissue regeneration cytoplasm; cytosolic ribosome; dendrite; endoplasmic reticulum; extracellular exosome; extracellular region; extracellular space; neuronal cell body; perinuclear region of cytoplasm cholesterol binding lipid transporter activity Homo sapiens 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Lipid-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal Transport MVMLLLLLSA MVMLLLLLSALAGLFGAAEGQAFHLGKCPNPPVQENFDVNKYLGRWYEIEKIPTTFENGRCIQANYSLMENGKIKVLNQELRADGTVNQIEGEATPVNLTEPAKLEVKFSWFMPSAPYWILATDYENYALVYSCTCIIQLFHVDFAWILARNPNLPPETVDSLKNILTSNNIDVKKMTVTDQVNCPKLS |
alcohol metabolic process aldehyde catabolic process carbohydrate metabolic process ethanol catabolic process regulation of dopamine biosynthetic process regulation of serotonin biosynthetic process | extracellular exosome; mitochondrial matrix; mitochondrion | aldehyde dehydrogenase (NAD+) activity aldehyde dehydrogenase activity carboxylesterase activity electron transfer activity glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity NAD binding nitroglycerin reductase activity phenylacetaldehyde dehydrogenase activity | Homo sapiens | 3D-structure Acetylation Alternative splicing Direct protein sequencing Disease variant Dwarfism Intellectual disability Mitochondrion NAD Oxidoreductase Reference proteome Transit peptide | MLRAAARFGP | MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS | alcohol metabolic process aldehyde catabolic process carbohydrate metabolic process ethanol catabolic process regulation of dopamine biosynthetic process regulation of serotonin biosynthetic process extracellular exosome; mitochondrial matrix; mitochondrion aldehyde dehydrogenase (NAD+) activity aldehyde dehydrogenase activity carboxylesterase activity electron transfer activity glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity NAD binding nitroglycerin reductase activity phenylacetaldehyde dehydrogenase activity Homo sapiens 3D-structure Acetylation Alternative splicing Direct protein sequencing Disease variant Dwarfism Intellectual disability Mitochondrion NAD Oxidoreductase Reference proteome Transit peptide MLRAAARFGP MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS |
androgen biosynthetic process glucocorticoid biosynthetic process hormone biosynthetic process progesterone metabolic process sex differentiation steroid biosynthetic process steroid metabolic process | axon; endoplasmic reticulum; endoplasmic reticulum membrane; neuronal cell body | 17-alpha-hydroxyprogesterone aldolase activity heme binding iron ion binding oxygen binding steroid 17-alpha-monooxygenase activity | Homo sapiens | 3D-structure Congenital adrenal hyperplasia Disease variant Endoplasmic reticulum Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Phosphoprotein Reference proteome Steroidogenesis | MWELVALLLL | MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVISLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVVFLIDSFKVKIKVRQAWREAQAEGST | androgen biosynthetic process glucocorticoid biosynthetic process hormone biosynthetic process progesterone metabolic process sex differentiation steroid biosynthetic process steroid metabolic process axon; endoplasmic reticulum; endoplasmic reticulum membrane; neuronal cell body 17-alpha-hydroxyprogesterone aldolase activity heme binding iron ion binding oxygen binding steroid 17-alpha-monooxygenase activity Homo sapiens 3D-structure Congenital adrenal hyperplasia Disease variant Endoplasmic reticulum Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Phosphoprotein Reference proteome Steroidogenesis MWELVALLLL MWELVALLLLTLAYLFWPKRRCPGAKYPKSLLSLPLVGSLPFLPRHGHMHNNFFKLQKKYGPIYSVRMGTKTTVIVGHHQLAKEVLIKKGKDFSGRPQMATLDIASNNRKGIAFADSGAHWQLHRRLAMATFALFKDGDQKLEKIICQEISTLCDMLATHNGQSIDISFPVFVAVTNVISLICFNTSYKNGDPELNVIQNYNEGIIDNLSKDSLVDLVPWLKIFPNKTLEKLKSHVKIRNDLLNKILENYKEKFRSDSITNMLDTLMQAKMNSDNGNAGPDQDSELLSDNHILTTIGDIFGAGVETTTSVVKWTLAFLLHNPQVKKKLYEEIDQNVGFSRTPTISDRNRLLLLEATIREVLRLRPVAPMLIPHKANVDSSIGEFAVDKGTEVIINLWALHHNEKEWHQPDQFMPERFLNPAGTQLISPSVSYLPFGAGPRSCIGEILARQELFLIMAWLLQRFDLEVPDDGQLPSLEGIPKVVFLIDSFKVKIKVRQAWREAQAEGST |
actin cytoskeleton organization muscle cell development sarcomere organization skeletal muscle fiber development | bicellular tight junction; cell junction; cell leading edge; cell projection; cortical actin cytoskeleton; dense body; focal adhesion; inner dense plaque of desmosome; lamellipodium; lateral plasma membrane; outer dense plaque of desmosome; plasma membrane; ruffle; sarcolemma; smooth muscle dense body; stress fiber; terminal web; Z disc; zonula adherens | actin filament binding alpha-actinin binding calcium ion binding LIM domain binding phosphoprotein binding protein homodimerization activity vinculin binding | Gallus gallus | 3D-structure Actin-binding Alternative splicing Calcium Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Metal-binding Phosphoprotein Reference proteome Repeat | MDHHYDPQQT | MDHHYDPQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRAPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNAWGGLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHESWTDGKEAMLQQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERQAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWEHVRQLVPRRDQALMEEHARQQQNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLNHLRQYEKSIVNYKPKIDQLEGDHQQIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDAQGEAEFARIMSIVDPNRMGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITVDELRRELPPDQAEYCIARMAPYNGRDAVPGALDYMSFSTALYGESDL | actin cytoskeleton organization muscle cell development sarcomere organization skeletal muscle fiber development bicellular tight junction; cell junction; cell leading edge; cell projection; cortical actin cytoskeleton; dense body; focal adhesion; inner dense plaque of desmosome; lamellipodium; lateral plasma membrane; outer dense plaque of desmosome; plasma membrane; ruffle; sarcolemma; smooth muscle dense body; stress fiber; terminal web; Z disc; zonula adherens actin filament binding alpha-actinin binding calcium ion binding LIM domain binding phosphoprotein binding protein homodimerization activity vinculin binding Gallus gallus 3D-structure Actin-binding Alternative splicing Calcium Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Metal-binding Phosphoprotein Reference proteome Repeat MDHHYDPQQT MDHHYDPQQTNDYMQPEEDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRAPENTMQAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNAWGGLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHESWTDGKEAMLQQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERQAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWEHVRQLVPRRDQALMEEHARQQQNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLNHLRQYEKSIVNYKPKIDQLEGDHQQIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRDHSGTLGPEEFKACLISLGYDIGNDAQGEAEFARIMSIVDPNRMGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITVDELRRELPPDQAEYCIARMAPYNGRDAVPGALDYMSFSTALYGESDL |
actin crosslink formation actin cytoskeleton organization actin filament bundle assembly cell motility cellular response to starvation hyperosmotic response phagocytosis sorocarp development | actin filament; cell cortex; cell junction; cell leading edge; cell projection; contractile vacuole; cortical actin cytoskeleton; cytosol; extracellular matrix; macropinocytic cup; phagocytic vesicle; pseudopodium | actin filament binding calcium ion binding protein-macromolecule adaptor activity structural constituent of cytoskeleton | Dictyostelium discoideum | 3D-structure Actin-binding Calcium Cytoplasm Cytoplasmic vesicle Developmental protein Direct protein sequencing Metal-binding Reference proteome Repeat Vacuole | MSEEPTPVSG | MSEEPTPVSGNDKQLLNKAWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKLVGIGAEELVDKNLKMTLGMIWTIILRFAIQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFSASRKAETAGKQVGKVLDTFMLLEQTKSDYLKRANELVQWINDKQASLESRDFGDSIESVQSFMNAHKEYKKTEKPPKGQEVSELEAIYNSLQTKLRLIKREPFVAPAGLTPNEIDSTWSALEKAEQEHAEALRIELKRQKKIAVLLQKYNRILKKLENWATTKSVYLGSNETGDSITAVQAKLKNLEAFDGECQSLEGQSNSDLLSILAQLTELNYNGVPELTERKDTFFAQQWTGVKSSAETYKNTLLAELERLQKIEDSLVEFAKRAAQLNVWIEAADDHVFDPINVDSVQGVQEIQEKFDAFLHDQSQQFAELEALAALTQQLRELGRSENDYSVISYDELSAKWNNLLAGIEERKVQLANELTTQTNNDVLCQSFSVKANEISDYVRVTLDAISQNTSSDPQEQLNNIRAIITAHAEKKPELDELYTIASQLEEAQVVDNKHTQHSLESIKLKWDKLNTLAKKNEQVVEGEILAKQLTGVTAEELSEFKACFSHFDKDNDNKLNRLEFSSCLKSIGDELTEEQLNQVISKIDTDGNGTISFEEFIDYMVSSRKGTDSVESTKAAFKVMAEDKDFITEAQIRAAISDSKQIDYLLASMPAVEGGFDYNSFAEKLYQ | actin crosslink formation actin cytoskeleton organization actin filament bundle assembly cell motility cellular response to starvation hyperosmotic response phagocytosis sorocarp development actin filament; cell cortex; cell junction; cell leading edge; cell projection; contractile vacuole; cortical actin cytoskeleton; cytosol; extracellular matrix; macropinocytic cup; phagocytic vesicle; pseudopodium actin filament binding calcium ion binding protein-macromolecule adaptor activity structural constituent of cytoskeleton Dictyostelium discoideum 3D-structure Actin-binding Calcium Cytoplasm Cytoplasmic vesicle Developmental protein Direct protein sequencing Metal-binding Reference proteome Repeat Vacuole MSEEPTPVSG MSEEPTPVSGNDKQLLNKAWEITQKKTFTAWCNSHLRKLGSSIEQIDTDFTDGIKLAQLLEVISNDPVFKVNKTPKLRIHNIQNVGLCLKHIESHGVKLVGIGAEELVDKNLKMTLGMIWTIILRFAIQDISIEELSAKEALLLWCQRKTEGYDRVKVGNFHTSFQDGLAFCALIHKHRPDLINFDSLNKDDKAGNLQLAFDIAEKELDIPKMLDVSDMLDVVRPDERSVMTYVAQYYHHFSASRKAETAGKQVGKVLDTFMLLEQTKSDYLKRANELVQWINDKQASLESRDFGDSIESVQSFMNAHKEYKKTEKPPKGQEVSELEAIYNSLQTKLRLIKREPFVAPAGLTPNEIDSTWSALEKAEQEHAEALRIELKRQKKIAVLLQKYNRILKKLENWATTKSVYLGSNETGDSITAVQAKLKNLEAFDGECQSLEGQSNSDLLSILAQLTELNYNGVPELTERKDTFFAQQWTGVKSSAETYKNTLLAELERLQKIEDSLVEFAKRAAQLNVWIEAADDHVFDPINVDSVQGVQEIQEKFDAFLHDQSQQFAELEALAALTQQLRELGRSENDYSVISYDELSAKWNNLLAGIEERKVQLANELTTQTNNDVLCQSFSVKANEISDYVRVTLDAISQNTSSDPQEQLNNIRAIITAHAEKKPELDELYTIASQLEEAQVVDNKHTQHSLESIKLKWDKLNTLAKKNEQVVEGEILAKQLTGVTAEELSEFKACFSHFDKDNDNKLNRLEFSSCLKSIGDELTEEQLNQVISKIDTDGNGTISFEEFIDYMVSSRKGTDSVESTKAAFKVMAEDKDFITEAQIRAAISDSKQIDYLLASMPAVEGGFDYNSFAEKLYQ |
amyloid-beta clearance apoptotic process cell adhesion cell-cell adhesion cell-cell adhesion via plasma-membrane adhesion molecules cell-cell signaling cell-matrix adhesion cellular response to low-density lipoprotein particle stimulus endodermal cell differentiation heterotypic cell-cell adhesion inflammatory response integrin-mediated signaling pathway leukocyte cell-cell adhesion microglial cell activation negative regulation of dopamine metabolic process neutrophil chemotaxis neutrophil migration phagocytosis, engulfment positive regulation of leukocyte adhesion to vascular endothelial cell positive regulation of neutrophil degranulation positive regulation of prostaglandin-E synthase activity positive regulation of protein targeting to membrane positive regulation of superoxide anion generation receptor clustering receptor internalization receptor-mediated endocytosis regulation of cell shape regulation of peptidyl-tyrosine phosphorylation | cell surface; external side of plasma membrane; extracellular exosome; extracellular vesicle; ficolin-1-rich granule membrane; focal adhesion; integrin alphaL-beta2 complex; integrin alphaM-beta2 complex; integrin alphaX-beta2 complex; integrin complex; membrane; plasma membrane; plasma membrane raft; receptor complex; specific granule membrane; tertiary granule membrane | amyloid-beta binding cell adhesion molecule binding complement component C3b binding heat shock protein binding ICAM-3 receptor activity integrin binding metal ion binding protein kinase binding | Homo sapiens | 3D-structure Calcium Cell adhesion Cell membrane Direct protein sequencing Disease variant Disulfide bond EGF-like domain Glycoprotein Integrin Magnesium Membrane Metal-binding Phagocytosis Phosphoprotein Pyrrolidone carboxylic acid Receptor Reference proteome Repeat Signal Transmembrane Transmembrane helix | MLGLRPPLLA | MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVHLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES | amyloid-beta clearance apoptotic process cell adhesion cell-cell adhesion cell-cell adhesion via plasma-membrane adhesion molecules cell-cell signaling cell-matrix adhesion cellular response to low-density lipoprotein particle stimulus endodermal cell differentiation heterotypic cell-cell adhesion inflammatory response integrin-mediated signaling pathway leukocyte cell-cell adhesion microglial cell activation negative regulation of dopamine metabolic process neutrophil chemotaxis neutrophil migration phagocytosis, engulfment positive regulation of leukocyte adhesion to vascular endothelial cell positive regulation of neutrophil degranulation positive regulation of prostaglandin-E synthase activity positive regulation of protein targeting to membrane positive regulation of superoxide anion generation receptor clustering receptor internalization receptor-mediated endocytosis regulation of cell shape regulation of peptidyl-tyrosine phosphorylation cell surface; external side of plasma membrane; extracellular exosome; extracellular vesicle; ficolin-1-rich granule membrane; focal adhesion; integrin alphaL-beta2 complex; integrin alphaM-beta2 complex; integrin alphaX-beta2 complex; integrin complex; membrane; plasma membrane; plasma membrane raft; receptor complex; specific granule membrane; tertiary granule membrane amyloid-beta binding cell adhesion molecule binding complement component C3b binding heat shock protein binding ICAM-3 receptor activity integrin binding metal ion binding protein kinase binding Homo sapiens 3D-structure Calcium Cell adhesion Cell membrane Direct protein sequencing Disease variant Disulfide bond EGF-like domain Glycoprotein Integrin Magnesium Membrane Metal-binding Phagocytosis Phosphoprotein Pyrrolidone carboxylic acid Receptor Reference proteome Repeat Signal Transmembrane Transmembrane helix MLGLRPPLLA MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVHLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES |
C21-steroid hormone biosynthetic process cellular response to peptide hormone stimulus cholesterol metabolic process cortisol metabolic process glucocorticoid biosynthetic process sterol metabolic process vitamin D metabolic process | mitochondrial inner membrane; mitochondrial matrix; mitochondrion | cholesterol monooxygenase (side-chain-cleaving) activity heme binding iron ion binding | Homo sapiens | 3D-structure Alternative splicing Cholesterol metabolism Direct protein sequencing Disease variant Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Mitochondrion Mitochondrion inner membrane Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis Steroid metabolism Steroidogenesis Sterol metabolism Transit peptide | MLAKGLPPRS | MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRGILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAARHQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIYALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINMLENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ | C21-steroid hormone biosynthetic process cellular response to peptide hormone stimulus cholesterol metabolic process cortisol metabolic process glucocorticoid biosynthetic process sterol metabolic process vitamin D metabolic process mitochondrial inner membrane; mitochondrial matrix; mitochondrion cholesterol monooxygenase (side-chain-cleaving) activity heme binding iron ion binding Homo sapiens 3D-structure Alternative splicing Cholesterol metabolism Direct protein sequencing Disease variant Heme Iron Lipid biosynthesis Lipid metabolism Membrane Metal-binding Mitochondrion Mitochondrion inner membrane Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis Steroid metabolism Steroidogenesis Sterol metabolism Transit peptide MLAKGLPPRS MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNEIPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVYVIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKSAAWKKDRVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNYSGDISDDLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTSVPMLNLPPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRGILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQDMLRAEVLAARHQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVNDLVLRDYMIPAKTLVQVAIYALGREPTFFFDPENFDPTRWLSKDKNITYFRNLGFGWGVRQCLGRRIAELEMTIFLINMLENFRVEIQHLSDVGTTFNLILMPEKPISFTFWPFNQEATQQ |
activation of cysteine-type endopeptidase activity involved in apoptotic process apoptotic process astrocyte development autocrine signaling autophagy chronic inflammatory response defense response to bacterium defense response to fungus inflammatory response innate immune response leukocyte migration involved in inflammatory response neutrophil aggregation neutrophil chemotaxis peptide secretion peptidyl-cysteine S-nitrosylation positive regulation of cell growth positive regulation of inflammatory response positive regulation of intrinsic apoptotic signaling pathway positive regulation of NF-kappaB transcription factor activity positive regulation of peptide secretion regulation of cytoskeleton organization regulation of toll-like receptor signaling pathway response to ethanol response to lipopolysaccharide response to zinc ion sequestering of zinc ion | calprotectin complex; collagen-containing extracellular matrix; cytoskeleton; cytosol; extracellular exosome; extracellular region; extracellular space; intermediate filament cytoskeleton; nucleus; plasma membrane; secretory granule lumen | arachidonic acid binding calcium ion binding calcium-dependent protein binding microtubule binding RAGE receptor binding Toll-like receptor 4 binding zinc ion binding | Homo sapiens | 3D-structure Antimicrobial Apoptosis Autophagy Calcium Cell membrane Chemotaxis Cytoplasm Cytoskeleton Direct protein sequencing Immunity Inflammatory response Innate immunity Membrane Metal-binding Reference proteome Repeat S-nitrosylation Secreted Zinc | MLTELEKALN | MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE | activation of cysteine-type endopeptidase activity involved in apoptotic process apoptotic process astrocyte development autocrine signaling autophagy chronic inflammatory response defense response to bacterium defense response to fungus inflammatory response innate immune response leukocyte migration involved in inflammatory response neutrophil aggregation neutrophil chemotaxis peptide secretion peptidyl-cysteine S-nitrosylation positive regulation of cell growth positive regulation of inflammatory response positive regulation of intrinsic apoptotic signaling pathway positive regulation of NF-kappaB transcription factor activity positive regulation of peptide secretion regulation of cytoskeleton organization regulation of toll-like receptor signaling pathway response to ethanol response to lipopolysaccharide response to zinc ion sequestering of zinc ion calprotectin complex; collagen-containing extracellular matrix; cytoskeleton; cytosol; extracellular exosome; extracellular region; extracellular space; intermediate filament cytoskeleton; nucleus; plasma membrane; secretory granule lumen arachidonic acid binding calcium ion binding calcium-dependent protein binding microtubule binding RAGE receptor binding Toll-like receptor 4 binding zinc ion binding Homo sapiens 3D-structure Antimicrobial Apoptosis Autophagy Calcium Cell membrane Chemotaxis Cytoplasm Cytoskeleton Direct protein sequencing Immunity Inflammatory response Innate immunity Membrane Metal-binding Reference proteome Repeat S-nitrosylation Secreted Zinc MLTELEKALN MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLLETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILVIKMGVAAHKKSHEESHKE |
adenylate cyclase-activating G protein-coupled receptor signaling pathway cellular response to glucagon stimulus gluconeogenesis glucose homeostasis negative regulation of execution phase of apoptosis positive regulation of calcium ion import positive regulation of ERK1 and ERK2 cascade positive regulation of gluconeogenesis positive regulation of histone H3-K4 methylation positive regulation of insulin secretion involved in cellular response to glucose stimulus positive regulation of peptidyl-serine phosphorylation positive regulation of peptidyl-threonine phosphorylation protein kinase A signaling regulation of insulin secretion response to activity | cytoplasm; extracellular space; plasma membrane | hormone activity identical protein binding | Cavia porcellus | Amidation Cleavage on pair of basic residues Direct protein sequencing Hormone Phosphoprotein Reference proteome Secreted Signal | MKSVYFVAGL | MKSVYFVAGLFIMLAQGSWQRSLQDTEEKPRSVSASQTDMLDDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQQFLKWLLNVKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLATRDFINWLIQTKITDRK | adenylate cyclase-activating G protein-coupled receptor signaling pathway cellular response to glucagon stimulus gluconeogenesis glucose homeostasis negative regulation of execution phase of apoptosis positive regulation of calcium ion import positive regulation of ERK1 and ERK2 cascade positive regulation of gluconeogenesis positive regulation of histone H3-K4 methylation positive regulation of insulin secretion involved in cellular response to glucose stimulus positive regulation of peptidyl-serine phosphorylation positive regulation of peptidyl-threonine phosphorylation protein kinase A signaling regulation of insulin secretion response to activity cytoplasm; extracellular space; plasma membrane hormone activity identical protein binding Cavia porcellus Amidation Cleavage on pair of basic residues Direct protein sequencing Hormone Phosphoprotein Reference proteome Secreted Signal MKSVYFVAGL MKSVYFVAGLFIMLAQGSWQRSLQDTEEKPRSVSASQTDMLDDPDQMNEDKRHSQGTFTSDYSKYLDSRRAQQFLKWLLNVKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIVEELGRRHADGSFSDEMNTILDNLATRDFINWLIQTKITDRK |
cell differentiation cell surface receptor signaling pathway cell-cell signaling erythrocyte differentiation hemoglobin biosynthetic process male gonad development negative regulation of B cell differentiation negative regulation of cell cycle negative regulation of follicle-stimulating hormone secretion negative regulation of macrophage differentiation negative regulation of phosphorylation negative regulation of type II interferon production ovarian follicle development positive regulation of follicle-stimulating hormone secretion regulation of cell cycle regulation of cell population proliferation signal transduction skeletal system development | extracellular region; extracellular space; inhibin A complex; inhibin B complex; inhibin-betaglycan-ActRII complex; neuronal cell body; photoreceptor inner segment; photoreceptor outer segment | cytokine activity growth factor activity hormone activity inhibin binding protein-containing complex binding signaling receptor binding | Homo sapiens | Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Glycoprotein Growth factor Hormone Reference proteome Secreted Signal | MVLHLLLFLL | MVLHLLLFLLLTPQGGHSCQGLELARELVLAKVRALFLDALGPPAVTREGGDPGVRRLPRRHALGGFTHRGSEPEEEEDVSQAILFPATDASCEDKSAARGLAQEAEEGLFRYMFRPSQHTRSRQVTSAQLWFHTGLDRQGTAASNSSEPLLGLLALSPGGPVAVPMSLGHAPPHWAVLHLATSALSLLTHPVLVLLLRCPLCTCSARPEATPFLVAHTRTRPPSGGERARRSTPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIPPNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI | cell differentiation cell surface receptor signaling pathway cell-cell signaling erythrocyte differentiation hemoglobin biosynthetic process male gonad development negative regulation of B cell differentiation negative regulation of cell cycle negative regulation of follicle-stimulating hormone secretion negative regulation of macrophage differentiation negative regulation of phosphorylation negative regulation of type II interferon production ovarian follicle development positive regulation of follicle-stimulating hormone secretion regulation of cell cycle regulation of cell population proliferation signal transduction skeletal system development extracellular region; extracellular space; inhibin A complex; inhibin B complex; inhibin-betaglycan-ActRII complex; neuronal cell body; photoreceptor inner segment; photoreceptor outer segment cytokine activity growth factor activity hormone activity inhibin binding protein-containing complex binding signaling receptor binding Homo sapiens Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Glycoprotein Growth factor Hormone Reference proteome Secreted Signal MVLHLLLFLL MVLHLLLFLLLTPQGGHSCQGLELARELVLAKVRALFLDALGPPAVTREGGDPGVRRLPRRHALGGFTHRGSEPEEEEDVSQAILFPATDASCEDKSAARGLAQEAEEGLFRYMFRPSQHTRSRQVTSAQLWFHTGLDRQGTAASNSSEPLLGLLALSPGGPVAVPMSLGHAPPHWAVLHLATSALSLLTHPVLVLLLRCPLCTCSARPEATPFLVAHTRTRPPSGGERARRSTPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIPPNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI |
immune response inflammatory response interleukin-5-mediated signaling pathway positive regulation of B cell proliferation positive regulation of DNA-templated transcription positive regulation of eosinophil differentiation positive regulation of immunoglobulin production positive regulation of peptidyl-tyrosine phosphorylation positive regulation of podosome assembly positive regulation of receptor signaling pathway via JAK-STAT | extracellular region; extracellular space | cytokine activity growth factor activity interleukin-5 receptor binding | Homo sapiens | 3D-structure Cytokine Direct protein sequencing Disulfide bond Glycoprotein Growth factor Reference proteome Secreted Signal | MRMLLHLSLL | MRMLLHLSLLALGAAYVYAIPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES | immune response inflammatory response interleukin-5-mediated signaling pathway positive regulation of B cell proliferation positive regulation of DNA-templated transcription positive regulation of eosinophil differentiation positive regulation of immunoglobulin production positive regulation of peptidyl-tyrosine phosphorylation positive regulation of podosome assembly positive regulation of receptor signaling pathway via JAK-STAT extracellular region; extracellular space cytokine activity growth factor activity interleukin-5 receptor binding Homo sapiens 3D-structure Cytokine Direct protein sequencing Disulfide bond Glycoprotein Growth factor Reference proteome Secreted Signal MRMLLHLSLL MRMLLHLSLLALGAAYVYAIPTEIPTSALVKETLALLSTHRTLLIANETLRIPVPVHKNHQLCTEEIFQGIGTLESQTVQGGTVERLFKNLSLIKKYIDGQKKKCGEERRRVNQFLDYLQEFLGVMNTEWIIES |
chromatin organization positive regulation of DNA-templated transcription, elongation | chromatin; cytoplasm; nucleoplasm; nucleus | chromatin binding DNA binding nucleosomal DNA binding | Homo sapiens | Acetylation ADP-ribosylation Cytoplasm Direct protein sequencing DNA-binding Nucleus Phosphoprotein Reference proteome RNA editing | MPKRKVSSAE | MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD | chromatin organization positive regulation of DNA-templated transcription, elongation chromatin; cytoplasm; nucleoplasm; nucleus chromatin binding DNA binding nucleosomal DNA binding Homo sapiens Acetylation ADP-ribosylation Cytoplasm Direct protein sequencing DNA-binding Nucleus Phosphoprotein Reference proteome RNA editing MPKRKVSSAE MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD |
anther dehiscence cell wall organization fruit dehiscence fruit ripening pectin catabolic process | apoplast | polygalacturonase activity | Solanum lycopersicum | Apoplast Cell wall Cell wall biogenesis/degradation Direct protein sequencing Fruit ripening Genetically modified food Glycoprotein Glycosidase Hydrolase Reference proteome Repeat Secreted Signal | MVIQRNSILL | MVIQRNSILLLIIIFASSISTCRSNVIDDNLFKQVYDNILEQEFAHDFQAYLSYLSKNIESNNNIDKVDKNGIKVINVLSFGAKGDGKTYDNIAFEQAWNEACSSRTPVQFVVPKNKNYLLKQITFSGPCRSSISVKIFGSLEASSKISDYKDRRLWIAFDSVQNLVVGGGGTINGNGQVWWPSSCKINKSLPCRDAPTALTFWNCKNLKVNNLKSKNAQQIHIKFESCTNVVASNLMINASAKSPNTDGVHVSNTQYIQISDTIIGTGDDCISIVSGSQNVQATNITCGPGHGISIGSLGSGNSEAYVSNVTVNEAKIIGAENGVRIKTWQGGSGQASNIKFLNVEMQDVKYPIIIDQNYCDRVEPCIQQFSAVQVKNVVYENIKGTSATKVAIKFDCSTNFPCEGIIMENINLVGESGKPSEATCKNVHFNNAEHVTPHCTSLEISEDEALLYNY | anther dehiscence cell wall organization fruit dehiscence fruit ripening pectin catabolic process apoplast polygalacturonase activity Solanum lycopersicum Apoplast Cell wall Cell wall biogenesis/degradation Direct protein sequencing Fruit ripening Genetically modified food Glycoprotein Glycosidase Hydrolase Reference proteome Repeat Secreted Signal MVIQRNSILL MVIQRNSILLLIIIFASSISTCRSNVIDDNLFKQVYDNILEQEFAHDFQAYLSYLSKNIESNNNIDKVDKNGIKVINVLSFGAKGDGKTYDNIAFEQAWNEACSSRTPVQFVVPKNKNYLLKQITFSGPCRSSISVKIFGSLEASSKISDYKDRRLWIAFDSVQNLVVGGGGTINGNGQVWWPSSCKINKSLPCRDAPTALTFWNCKNLKVNNLKSKNAQQIHIKFESCTNVVASNLMINASAKSPNTDGVHVSNTQYIQISDTIIGTGDDCISIVSGSQNVQATNITCGPGHGISIGSLGSGNSEAYVSNVTVNEAKIIGAENGVRIKTWQGGSGQASNIKFLNVEMQDVKYPIIIDQNYCDRVEPCIQQFSAVQVKNVVYENIKGTSATKVAIKFDCSTNFPCEGIIMENINLVGESGKPSEATCKNVHFNNAEHVTPHCTSLEISEDEALLYNY |
fibrinolysis negative regulation of apoptotic process | cornified envelope; cytoplasm; extracellular region; extracellular space; plasma membrane | serine-type endopeptidase inhibitor activity | Homo sapiens | 3D-structure Cytoplasm Direct protein sequencing Disulfide bond Glycoprotein Plasminogen activation Protease inhibitor Reference proteome Secreted Serine protease inhibitor Signal | MEDLCVANTL | MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGFMQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCILFFGRFSSP | fibrinolysis negative regulation of apoptotic process cornified envelope; cytoplasm; extracellular region; extracellular space; plasma membrane serine-type endopeptidase inhibitor activity Homo sapiens 3D-structure Cytoplasm Direct protein sequencing Disulfide bond Glycoprotein Plasminogen activation Protease inhibitor Reference proteome Secreted Serine protease inhibitor Signal MEDLCVANTL MEDLCVANTLFALNLFKHLAKASPTQNLFLSPWSISSTMAMVYMGSRGSTEDQMAKVLQFNEVGANAVTPMTPENFTSCGFMQQIQKGSYPDAILQAQAADKIHSSFRSLSSAINASTGNYLLESVNKLFGEKSASFREEYIRLCQKYYSSEPQAVDFLECAEEARKKINSWVKTQTKGKIPNLLPEGSVDGDTRMVLVNAVYFKGKWKTPFEKKLNGLYPFRVNSAQRTPVQMMYLREKLNIGYIEDLKAQILELPYAGDVSMFLLLPDEIADVSTGLELLESEITYDKLNKWTSKDKMAEDEVEVYIPQFKLEEHYELRSILRSMGMEDAFNKGRANFSGMSERNDLFLSEVFHQAMVDVNEEGTEAAAGTGGVMTGRTGHGGPQFVADHPFLFLIMHKITNCILFFGRFSSP |
ATP biosynthetic process phosphocreatine biosynthetic process phosphorylation | cytosol; extracellular membrane-bounded organelle; extracellular space; mitochondrion; plasma membrane | ATP binding creatine kinase activity | Gallus gallus | 3D-structure Alternative splicing ATP-binding Cell membrane Cytoplasm Direct protein sequencing Kinase Membrane Mitochondrion Nucleotide-binding Phosphoprotein Reference proteome Transferase | MPFSNSHNLL | MPFSNSHNLLKMKYSVDDEYPDLSVHNNHMAKVLTLDLYKKLRDRQTSSGFTLDDVIQTGVDNPGHPFIMTVGCVAGDEESYEVFKELFDPVIEDRHGGYKPTDEHKTDLNADNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLSVEALGSLGGDLKGKYYALRNMTDAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFGEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEKRLEKGQSIDDLMPAQK | ATP biosynthetic process phosphocreatine biosynthetic process phosphorylation cytosol; extracellular membrane-bounded organelle; extracellular space; mitochondrion; plasma membrane ATP binding creatine kinase activity Gallus gallus 3D-structure Alternative splicing ATP-binding Cell membrane Cytoplasm Direct protein sequencing Kinase Membrane Mitochondrion Nucleotide-binding Phosphoprotein Reference proteome Transferase MPFSNSHNLL MPFSNSHNLLKMKYSVDDEYPDLSVHNNHMAKVLTLDLYKKLRDRQTSSGFTLDDVIQTGVDNPGHPFIMTVGCVAGDEESYEVFKELFDPVIEDRHGGYKPTDEHKTDLNADNLQGGDDLDPNYVLSSRVRTGRSIRGFCLPPHCSRGERRAIEKLSVEALGSLGGDLKGKYYALRNMTDAEQQQLIDDHFLFDKPVSPLLLASGMARDWPDARGIWHNDNKTFLVWINEEDHLRVISMQKGGNMKEVFTRFCTGLTQIETLFKSKNYEFMWNPHLGYILTCPSNLGTGLRAGVHIKLPNLGKHEKFGEVLKRLRLQKRGTGGVDTAAVGGVFDVSNADRLGFSEVELVQMVVDGVKLLIEMEKRLEKGQSIDDLMPAQK |
adaptive immune response apoptotic process B cell activation B cell receptor signaling pathway intracellular signal transduction negative regulation of glucose transmembrane transport negative regulation of insulin receptor signaling pathway phosphorylation positive regulation of angiogenesis positive regulation of B cell receptor signaling pathway positive regulation of canonical NF-kappaB signal transduction positive regulation of vascular endothelial growth factor receptor signaling pathway post-translational protein modification regulation of glucose transmembrane transport regulation of transcription by RNA polymerase II | cytoplasm; membrane; nucleus | ATP binding chromatin binding diacylglycerol-dependent serine/threonine kinase activity histone binding histone H3T6 kinase activity nuclear androgen receptor binding nuclear receptor coactivator activity protein serine kinase activity protein serine/threonine kinase activity zinc ion binding | Bos taurus | Acetylation Adaptive immunity Alternative splicing Apoptosis ATP-binding Calcium Chromatin regulator Cytoplasm Immunity Kinase Membrane Metal-binding Nucleotide-binding Nucleus Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Transcription Transcription regulation Transferase Zinc Zinc-finger | MADPAAGPPP | MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIEREVLIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFKLLSQEEGEYFNVPVPPEGSEGNEELRQKFERAKIGPGPKTPEEKTTNTISKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV | adaptive immune response apoptotic process B cell activation B cell receptor signaling pathway intracellular signal transduction negative regulation of glucose transmembrane transport negative regulation of insulin receptor signaling pathway phosphorylation positive regulation of angiogenesis positive regulation of B cell receptor signaling pathway positive regulation of canonical NF-kappaB signal transduction positive regulation of vascular endothelial growth factor receptor signaling pathway post-translational protein modification regulation of glucose transmembrane transport regulation of transcription by RNA polymerase II cytoplasm; membrane; nucleus ATP binding chromatin binding diacylglycerol-dependent serine/threonine kinase activity histone binding histone H3T6 kinase activity nuclear androgen receptor binding nuclear receptor coactivator activity protein serine kinase activity protein serine/threonine kinase activity zinc ion binding Bos taurus Acetylation Adaptive immunity Alternative splicing Apoptosis ATP-binding Calcium Chromatin regulator Cytoplasm Immunity Kinase Membrane Metal-binding Nucleotide-binding Nucleus Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Transcription Transcription regulation Transferase Zinc Zinc-finger MADPAAGPPP MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIEREVLIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFKLLSQEEGEYFNVPVPPEGSEGNEELRQKFERAKIGPGPKTPEEKTTNTISKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV |
intracellular signal transduction negative regulation of neuron apoptotic process negative regulation of proteasomal protein catabolic process negative regulation of protein ubiquitination phosphorylation regulation of circadian rhythm regulation of response to food response to morphine response to pain rhythmic process | cytosol; dendrite; perinuclear region of cytoplasm; plasma membrane; synapse | ATP binding diacylglycerol-dependent serine/threonine kinase activity protein serine kinase activity protein serine/threonine kinase activity zinc ion binding | Bos taurus | ATP-binding Biological rhythms Calcium Cell membrane Cell projection Cytoplasm Kinase Membrane Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Synapse Synaptosome Transferase Ubl conjugation Zinc Zinc-finger | RPLFCRKGAL | RPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTSDEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCNLLQKFEACNYPLELYERVRTGPSSSPIPSPSPSPTDSKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGSTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPAKRLGSGPDGEPTIRAHGFFRWIDWDRLERLEIAPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQAEFQGFTYVNPDFVHPDARSPISPTPVPVM | intracellular signal transduction negative regulation of neuron apoptotic process negative regulation of proteasomal protein catabolic process negative regulation of protein ubiquitination phosphorylation regulation of circadian rhythm regulation of response to food response to morphine response to pain rhythmic process cytosol; dendrite; perinuclear region of cytoplasm; plasma membrane; synapse ATP binding diacylglycerol-dependent serine/threonine kinase activity protein serine kinase activity protein serine/threonine kinase activity zinc ion binding Bos taurus ATP-binding Biological rhythms Calcium Cell membrane Cell projection Cytoplasm Kinase Membrane Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Synapse Synaptosome Transferase Ubl conjugation Zinc Zinc-finger RPLFCRKGAL RPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTSDEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCNLLQKFEACNYPLELYERVRTGPSSSPIPSPSPSPTDSKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGSTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPAKRLGSGPDGEPTIRAHGFFRWIDWDRLERLEIAPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQAEFQGFTYVNPDFVHPDARSPISPTPVPVM |
chemical synaptic transmission chemosensory behavior innervation intracellular signal transduction learning or memory long-term synaptic potentiation negative regulation of neuron apoptotic process negative regulation of proteasomal protein catabolic process negative regulation of protein catabolic process negative regulation of protein ubiquitination phosphorylation positive regulation of mismatch repair presynaptic modulation of chemical synaptic transmission protein phosphorylation regulation of circadian rhythm regulation of phagocytosis regulation of response to food regulation of synaptic vesicle exocytosis response to morphine response to pain response to psychosocial stress response to toxic substance rhythmic process | calyx of Held; cell-cell junction; cytosol; dendrite; nucleus; perinuclear region of cytoplasm; plasma membrane; postsynaptic cytosol; postsynaptic density; presynaptic cytosol; synaptic membrane | ATP binding calcium,diacylglycerol-dependent serine/threonine kinase activity diacylglycerol-dependent serine/threonine kinase activity protein kinase activity protein serine kinase activity protein serine/threonine kinase activity protein serine/threonine/tyrosine kinase activity zinc ion binding | Homo sapiens | 3D-structure Alternative splicing ATP-binding Biological rhythms Calcium Cell membrane Cell projection Cytoplasm Disease variant Kinase Membrane Metal-binding Neurodegeneration Nucleotide-binding Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Spinocerebellar ataxia Synapse Synaptosome Transferase Ubl conjugation Zinc Zinc-finger | MAGLGPGVGD | MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM | chemical synaptic transmission chemosensory behavior innervation intracellular signal transduction learning or memory long-term synaptic potentiation negative regulation of neuron apoptotic process negative regulation of proteasomal protein catabolic process negative regulation of protein catabolic process negative regulation of protein ubiquitination phosphorylation positive regulation of mismatch repair presynaptic modulation of chemical synaptic transmission protein phosphorylation regulation of circadian rhythm regulation of phagocytosis regulation of response to food regulation of synaptic vesicle exocytosis response to morphine response to pain response to psychosocial stress response to toxic substance rhythmic process calyx of Held; cell-cell junction; cytosol; dendrite; nucleus; perinuclear region of cytoplasm; plasma membrane; postsynaptic cytosol; postsynaptic density; presynaptic cytosol; synaptic membrane ATP binding calcium,diacylglycerol-dependent serine/threonine kinase activity diacylglycerol-dependent serine/threonine kinase activity protein kinase activity protein serine kinase activity protein serine/threonine kinase activity protein serine/threonine/tyrosine kinase activity zinc ion binding Homo sapiens 3D-structure Alternative splicing ATP-binding Biological rhythms Calcium Cell membrane Cell projection Cytoplasm Disease variant Kinase Membrane Metal-binding Neurodegeneration Nucleotide-binding Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Spinocerebellar ataxia Synapse Synaptosome Transferase Ubl conjugation Zinc Zinc-finger MAGLGPGVGD MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM |
intracellular signal transduction positive regulation of clathrin-dependent endocytosis protein phosphorylation regulation of hemocyte proliferation | plasma membrane | ATP binding diacylglycerol-dependent serine/threonine kinase activity protein serine kinase activity protein serine/threonine kinase activity zinc ion binding | Drosophila melanogaster | Alternative splicing ATP-binding Calcium Kinase Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Transferase Zinc Zinc-finger | MSEGSDNNGD | MSEGSDNNGDPQQQGAEGEAVGENKMKSRLRKGALKKKNVFNVKDHCFIARFFKQPTFCSHCKDFICGYQSGYAWMGFGKQGFQCQVCSYVVHKRCHEYVTFICPGKDKGIDSDSPKTQHNFEPFTYAGPTFCDHCGSLLYGIYHQGLKCSACDMNVHARCKENVPSLCGCDHTERRGRIYLEINVKENLLTVQIKEGRNLIPMDPNGLSDPYVKVKLIPDDKDQSKKKTRTIKACLNPVWNETLTYDLKPEDKDRRILIEVWDWDRTSRNDFMGALSFGISEIIKNPTNGWFKLLTQDEGEYYNVPCADDEQDLLKLKQKPSQKKPMVMRSDTNTHTSSKKDMIRATDFNFIKVLGKGSFGKVLLAERKGSEELYAIKILKKDVIIQDDDVECTMIEKRVLALGEKPPFLVQLHSCFQTMDRLFFVMEYVNGGDLMFQIQQFGKFKEPVAVFYAAEIAAGLFFLHTKGILYRDLKLDNVLLDADGHVKIADFGMCKENIVGDKTTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLYEMLVGQPPFDGEDEEELFAAITDHNVSYPKSLSKEAKEACKGFLTKQPNKRLGCGSSGEEDVRLHPFFRRIDWEKIENREVQPPFKPKIKHRKDVSNFDKQFTSEKTDLTPTDKVFMMNLDQSEFVGFSYMNPEYVFSP | intracellular signal transduction positive regulation of clathrin-dependent endocytosis protein phosphorylation regulation of hemocyte proliferation plasma membrane ATP binding diacylglycerol-dependent serine/threonine kinase activity protein serine kinase activity protein serine/threonine kinase activity zinc ion binding Drosophila melanogaster Alternative splicing ATP-binding Calcium Kinase Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Repeat Serine/threonine-protein kinase Transferase Zinc Zinc-finger MSEGSDNNGD MSEGSDNNGDPQQQGAEGEAVGENKMKSRLRKGALKKKNVFNVKDHCFIARFFKQPTFCSHCKDFICGYQSGYAWMGFGKQGFQCQVCSYVVHKRCHEYVTFICPGKDKGIDSDSPKTQHNFEPFTYAGPTFCDHCGSLLYGIYHQGLKCSACDMNVHARCKENVPSLCGCDHTERRGRIYLEINVKENLLTVQIKEGRNLIPMDPNGLSDPYVKVKLIPDDKDQSKKKTRTIKACLNPVWNETLTYDLKPEDKDRRILIEVWDWDRTSRNDFMGALSFGISEIIKNPTNGWFKLLTQDEGEYYNVPCADDEQDLLKLKQKPSQKKPMVMRSDTNTHTSSKKDMIRATDFNFIKVLGKGSFGKVLLAERKGSEELYAIKILKKDVIIQDDDVECTMIEKRVLALGEKPPFLVQLHSCFQTMDRLFFVMEYVNGGDLMFQIQQFGKFKEPVAVFYAAEIAAGLFFLHTKGILYRDLKLDNVLLDADGHVKIADFGMCKENIVGDKTTKTFCGTPDYIAPEIILYQPYGKSVDWWAYGVLLYEMLVGQPPFDGEDEEELFAAITDHNVSYPKSLSKEAKEACKGFLTKQPNKRLGCGSSGEEDVRLHPFFRRIDWEKIENREVQPPFKPKIKHRKDVSNFDKQFTSEKTDLTPTDKVFMMNLDQSEFVGFSYMNPEYVFSP |
negative regulation of TORC1 signaling protein kinase A signaling protein phosphorylation | cAMP-dependent protein kinase complex; cytosol; nucleus; plasma membrane | AMP-activated protein kinase activity ATP binding cAMP-dependent protein kinase activity protein serine kinase activity | Bos taurus | Alternative splicing ATP-binding cAMP Cell membrane Cytoplasm Direct protein sequencing Kinase Lipoprotein Membrane Myristate Nucleotide-binding Nucleus Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase | MGNAATAKKG | MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPAPNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEYAFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCGKEFCEF | negative regulation of TORC1 signaling protein kinase A signaling protein phosphorylation cAMP-dependent protein kinase complex; cytosol; nucleus; plasma membrane AMP-activated protein kinase activity ATP binding cAMP-dependent protein kinase activity protein serine kinase activity Bos taurus Alternative splicing ATP-binding cAMP Cell membrane Cytoplasm Direct protein sequencing Kinase Lipoprotein Membrane Myristate Nucleotide-binding Nucleus Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase MGNAATAKKG MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPAPNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEYAFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCGKEFCEF |
perturbation by virus of host apoptosis suppression by virus of host apoptotic process | helical viral capsid; host cell Golgi apparatus; host cell perinuclear region of cytoplasm; ribonucleoprotein complex; viral nucleocapsid | endonuclease activity RNA binding | Hantaan virus | 3D-structure Capsid protein Chaperone Coiled coil Endonuclease Helical capsid protein Host cytoplasm Host Golgi apparatus Host-virus interaction Hydrolase Modulation of host cell apoptosis by virus Nuclease Reference proteome Ribonucleoprotein RNA-binding Viral nucleoprotein Virion | MATMEELQRE | MATMEELQREINAHEGQLVIARQKVRDAEKQYEKDPDELNKRTLTDREGVAVSIQAKIDELKRQLADRIATGKNLGKEQDPTGVEPGDHLKERSMLSYGNVLDLNHLDIDEPTGQTADWLSIIVYLTSFVVPILLKALYMLTTRGRQTTKDNKGTRIRFKDDSSFEDVNGIRKPKHLYVSLPNAQSSMKAEEITPGRYRTAVCGLYPAQIKARQMISPVMSVIGFLALAKDWSDRIEQWLIEPCKLLPDTAAVSLLGGPATNRDYLRQRQVALGNMETKESKAIRQHAEAAGCSMIEDIESPSSIWVFAGAPDRCPPTCLFIAGIAELGAFFSILQDMRNTIMASKTVGTSEEKLRKKSSFYQSYLRRTQSMGIQLGQRIIVLFMVAWGKEAVDNFHLGDDMDPELRTLAQSLIDVKVKEISNQEPLKL | perturbation by virus of host apoptosis suppression by virus of host apoptotic process helical viral capsid; host cell Golgi apparatus; host cell perinuclear region of cytoplasm; ribonucleoprotein complex; viral nucleocapsid endonuclease activity RNA binding Hantaan virus 3D-structure Capsid protein Chaperone Coiled coil Endonuclease Helical capsid protein Host cytoplasm Host Golgi apparatus Host-virus interaction Hydrolase Modulation of host cell apoptosis by virus Nuclease Reference proteome Ribonucleoprotein RNA-binding Viral nucleoprotein Virion MATMEELQRE MATMEELQREINAHEGQLVIARQKVRDAEKQYEKDPDELNKRTLTDREGVAVSIQAKIDELKRQLADRIATGKNLGKEQDPTGVEPGDHLKERSMLSYGNVLDLNHLDIDEPTGQTADWLSIIVYLTSFVVPILLKALYMLTTRGRQTTKDNKGTRIRFKDDSSFEDVNGIRKPKHLYVSLPNAQSSMKAEEITPGRYRTAVCGLYPAQIKARQMISPVMSVIGFLALAKDWSDRIEQWLIEPCKLLPDTAAVSLLGGPATNRDYLRQRQVALGNMETKESKAIRQHAEAAGCSMIEDIESPSSIWVFAGAPDRCPPTCLFIAGIAELGAFFSILQDMRNTIMASKTVGTSEEKLRKKSSFYQSYLRRTQSMGIQLGQRIIVLFMVAWGKEAVDNFHLGDDMDPELRTLAQSLIDVKVKEISNQEPLKL |
adaptive thermogenesis adenine nucleotide transport B cell differentiation cellular response to leukemia inhibitory factor chromosome segregation erythrocyte differentiation mitochondrial ADP transmembrane transport mitochondrial ATP transmembrane transport negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway positive regulation of cell population proliferation positive regulation of mitophagy regulation of mitochondrial membrane permeability | membrane; mitochondrial inner membrane; mitochondrial nucleoid; mitochondrial permeability transition pore complex; mitochondrion; MMXD complex; nucleus; plasma membrane | adenine nucleotide transmembrane transporter activity adenine transmembrane transporter activity ATP:ADP antiporter activity oxidative phosphorylation uncoupler activity proton transmembrane transporter activity RNA binding ubiquitin protein ligase binding | Homo sapiens | Acetylation Antiport Chromosome partition Direct protein sequencing Host-virus interaction Membrane Methylation Mitochondrion Mitochondrion inner membrane Phosphoprotein Reference proteome Repeat Transmembrane Transmembrane helix Transport | MTDAAVSFAK | MTDAAVSFAKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQITADKQYKGIIDCVVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKRTQFWLYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKAGAEREFRGLGDCLVKIYKSDGIKGLYQGFNVSVQGIIIYRAAYFGIYDTAKGMLPDPKNTHIVISWMIAQTVTAVAGLTSYPFDTVRRRMMMQSGRKGTDIMYTGTLDCWRKIARDEGGKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYT | adaptive thermogenesis adenine nucleotide transport B cell differentiation cellular response to leukemia inhibitory factor chromosome segregation erythrocyte differentiation mitochondrial ADP transmembrane transport mitochondrial ATP transmembrane transport negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway positive regulation of cell population proliferation positive regulation of mitophagy regulation of mitochondrial membrane permeability membrane; mitochondrial inner membrane; mitochondrial nucleoid; mitochondrial permeability transition pore complex; mitochondrion; MMXD complex; nucleus; plasma membrane adenine nucleotide transmembrane transporter activity adenine transmembrane transporter activity ATP:ADP antiporter activity oxidative phosphorylation uncoupler activity proton transmembrane transporter activity RNA binding ubiquitin protein ligase binding Homo sapiens Acetylation Antiport Chromosome partition Direct protein sequencing Host-virus interaction Membrane Methylation Mitochondrion Mitochondrion inner membrane Phosphoprotein Reference proteome Repeat Transmembrane Transmembrane helix Transport MTDAAVSFAK MTDAAVSFAKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQITADKQYKGIIDCVVRIPKEQGVLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDKRTQFWLYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKAGAEREFRGLGDCLVKIYKSDGIKGLYQGFNVSVQGIIIYRAAYFGIYDTAKGMLPDPKNTHIVISWMIAQTVTAVAGLTSYPFDTVRRRMMMQSGRKGTDIMYTGTLDCWRKIARDEGGKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYT |
arginine biosynthetic process arginine biosynthetic process via ornithine citrulline biosynthetic process | cytosol; mitochondrion; ornithine carbamoyltransferase inhibitor complex | amino acid binding ornithine carbamoyltransferase activity | Saccharomyces cerevisiae | Acetylation Amino-acid biosynthesis Arginine biosynthesis Cytoplasm Reference proteome Transferase | MSTTASTPSS | MSTTASTPSSLRHLISIKDLSDEEFRILVQRAQHFKNVFKANKTNDFQSNHLKLLGRTIALIFTKRSTRTRISTEGAATFFGAQPMFLGKEDIQLGVNESFYDTTKVVSSMVSCIFARVNKHEDILAFCKDSSVPIINSLCDKFHPLQAICDLLTIIENFNISLDEVNKGINSKLKMAWIGDANNVINDMCIACLKFGISVSISTPPGIEMDSDIVDEAKKVAERNGATFELTHDSLKASTNANILVTDTFVSMGEEFAKQAKLKQFKGFQINQELVSVADPNYKFMHCLPRHQEEVSDDVFYGEHSIVFEEAENRLYAAMSAIDIFVNNKGNFKDLK | arginine biosynthetic process arginine biosynthetic process via ornithine citrulline biosynthetic process cytosol; mitochondrion; ornithine carbamoyltransferase inhibitor complex amino acid binding ornithine carbamoyltransferase activity Saccharomyces cerevisiae Acetylation Amino-acid biosynthesis Arginine biosynthesis Cytoplasm Reference proteome Transferase MSTTASTPSS MSTTASTPSSLRHLISIKDLSDEEFRILVQRAQHFKNVFKANKTNDFQSNHLKLLGRTIALIFTKRSTRTRISTEGAATFFGAQPMFLGKEDIQLGVNESFYDTTKVVSSMVSCIFARVNKHEDILAFCKDSSVPIINSLCDKFHPLQAICDLLTIIENFNISLDEVNKGINSKLKMAWIGDANNVINDMCIACLKFGISVSISTPPGIEMDSDIVDEAKKVAERNGATFELTHDSLKASTNANILVTDTFVSMGEEFAKQAKLKQFKGFQINQELVSVADPNYKFMHCLPRHQEEVSDDVFYGEHSIVFEEAENRLYAAMSAIDIFVNNKGNFKDLK |
fusion of sperm to egg plasma membrane involved in single fertilization lipid transport negative regulation of hydrolase activity negative regulation of proteolysis seminal vesicle development spermatogenesis | acrosomal membrane; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; membrane; platelet alpha granule; platelet dense tubular network; protein C inhibitor-coagulation factor V complex; protein C inhibitor-coagulation factor Xa complex; protein C inhibitor-coagulation factor XI complex; protein C inhibitor-KLK3 complex; protein C inhibitor-plasma kallikrein complex; protein C inhibitor-PLAT complex; protein C inhibitor-PLAU complex; protein C inhibitor-thrombin complex; protein C inhibitor-TMPRSS11E complex; protein C inhibitor-TMPRSS7 complex; protein-containing complex | acrosin binding glycosaminoglycan binding heparin binding phosphatidylcholine binding protease binding retinoic acid binding serine-type endopeptidase inhibitor activity | Homo sapiens | 3D-structure Direct protein sequencing Fertilization Glycoprotein Heparin-binding Lipid transport Protease inhibitor Reference proteome Secreted Serine protease inhibitor Signal Transport | MQLFLLLCLV | MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP | fusion of sperm to egg plasma membrane involved in single fertilization lipid transport negative regulation of hydrolase activity negative regulation of proteolysis seminal vesicle development spermatogenesis acrosomal membrane; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; membrane; platelet alpha granule; platelet dense tubular network; protein C inhibitor-coagulation factor V complex; protein C inhibitor-coagulation factor Xa complex; protein C inhibitor-coagulation factor XI complex; protein C inhibitor-KLK3 complex; protein C inhibitor-plasma kallikrein complex; protein C inhibitor-PLAT complex; protein C inhibitor-PLAU complex; protein C inhibitor-thrombin complex; protein C inhibitor-TMPRSS11E complex; protein C inhibitor-TMPRSS7 complex; protein-containing complex acrosin binding glycosaminoglycan binding heparin binding phosphatidylcholine binding protease binding retinoic acid binding serine-type endopeptidase inhibitor activity Homo sapiens 3D-structure Direct protein sequencing Fertilization Glycoprotein Heparin-binding Lipid transport Protease inhibitor Reference proteome Secreted Serine protease inhibitor Signal Transport MQLFLLLCLV MQLFLLLCLVLLSPQGASLHRHHPREMKKRVEDLHVGATVAPSSRRDFTFDLYRALASAAPSQSIFFSPVSISMSLAMLSLGAGSSTKMQILEGLGLNLQKSSEKELHRGFQQLLQELNQPRDGFQLSLGNALFTDLVVDLQDTFVSAMKTLYLADTFPTNFRDSAGAMKQINDYVAKQTKGKIVDLLKNLDSNAVVIMVNYIFFKAKWETSFNHKGTQEQDFYVTSETVVRVPMMSREDQYHYLLDRNLSCRVVGVPYQGNATALFILPSEGKMQQVENGLSEKTLRKWLKMFKKRQLELYLPKFSIEGSYQLEKVLPSLGISNVFTSHADLSGISNHSNIQVSEMVHKAVVEVDESGTRAAAATGTIFTFRSARLNSQRLVFNRPFLMFIVDNNILFLGKVNRP |
blood circulation blood coagulation complement activation, classical pathway fibrinolysis innate immune response negative regulation of complement activation, lectin pathway | blood microparticle; collagen-containing extracellular matrix; endoplasmic reticulum lumen; extracellular exosome; extracellular region; extracellular space; platelet alpha granule lumen | serine-type endopeptidase inhibitor activity | Homo sapiens | 3D-structure Alternative splicing Blood coagulation Complement pathway Direct protein sequencing Disease variant Disulfide bond Fibrinolysis Glycoprotein Hemostasis Immunity Innate immunity Protease inhibitor Reference proteome Repeat Secreted Serine protease inhibitor Signal | MASRLTLLTL | MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFVLWDQQHKFPVFMGRVYDPRA | blood circulation blood coagulation complement activation, classical pathway fibrinolysis innate immune response negative regulation of complement activation, lectin pathway blood microparticle; collagen-containing extracellular matrix; endoplasmic reticulum lumen; extracellular exosome; extracellular region; extracellular space; platelet alpha granule lumen serine-type endopeptidase inhibitor activity Homo sapiens 3D-structure Alternative splicing Blood coagulation Complement pathway Direct protein sequencing Disease variant Disulfide bond Fibrinolysis Glycoprotein Hemostasis Immunity Innate immunity Protease inhibitor Reference proteome Repeat Secreted Serine protease inhibitor Signal MASRLTLLTL MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFVLWDQQHKFPVFMGRVYDPRA |
complement activation, classical pathway innate immune response proteolysis | extracellular exosome; extracellular region; extracellular space; membrane | metal ion binding serine-type endopeptidase activity | Homo sapiens | 3D-structure Age-related macular degeneration Calcium Cleavage on pair of basic residues Complement pathway Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemolytic uremic syndrome Host-virus interaction Hydrolase Immunity Innate immunity Metal-binding Protease Reference proteome Repeat Secreted Serine protease Signal | MKLLHVFLLF | MKLLHVFLLFLCFHLRFCKVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHIRRKRIVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV | complement activation, classical pathway innate immune response proteolysis extracellular exosome; extracellular region; extracellular space; membrane metal ion binding serine-type endopeptidase activity Homo sapiens 3D-structure Age-related macular degeneration Calcium Cleavage on pair of basic residues Complement pathway Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemolytic uremic syndrome Host-virus interaction Hydrolase Immunity Innate immunity Metal-binding Protease Reference proteome Repeat Secreted Serine protease Signal MKLLHVFLLF MKLLHVFLLFLCFHLRFCKVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHIRRKRIVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV |
defense response to bacterium defense response to virus innate immune response integrin-mediated signaling pathway ISG15-protein conjugation modification-dependent protein catabolic process negative regulation of protein ubiquitination negative regulation of type I interferon-mediated signaling pathway negative regulation of viral genome replication positive regulation of bone mineralization positive regulation of erythrocyte differentiation positive regulation of interferon-beta production positive regulation of interleukin-10 production positive regulation of protein oligomerization positive regulation of type II interferon production protein localization to mitochondrion regulation of type II interferon production response to type I interferon response to virus | cytoplasm; cytosol; extracellular region; nucleoplasm | integrin binding protein tag activity ubiquitin protein ligase binding | Homo sapiens | 3D-structure Antiviral defense Cytoplasm Direct protein sequencing Disulfide bond Host-virus interaction Immunity Innate immunity Isopeptide bond Reference proteome Repeat S-nitrosylation Secreted Ubl conjugation pathway | MGWDLTVKML | MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPLASQGLGPGSTVLLVVDKCDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGGGTEPGGRS | defense response to bacterium defense response to virus innate immune response integrin-mediated signaling pathway ISG15-protein conjugation modification-dependent protein catabolic process negative regulation of protein ubiquitination negative regulation of type I interferon-mediated signaling pathway negative regulation of viral genome replication positive regulation of bone mineralization positive regulation of erythrocyte differentiation positive regulation of interferon-beta production positive regulation of interleukin-10 production positive regulation of protein oligomerization positive regulation of type II interferon production protein localization to mitochondrion regulation of type II interferon production response to type I interferon response to virus cytoplasm; cytosol; extracellular region; nucleoplasm integrin binding protein tag activity ubiquitin protein ligase binding Homo sapiens 3D-structure Antiviral defense Cytoplasm Direct protein sequencing Disulfide bond Host-virus interaction Immunity Innate immunity Isopeptide bond Reference proteome Repeat S-nitrosylation Secreted Ubl conjugation pathway MGWDLTVKML MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPLASQGLGPGSTVLLVVDKCDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGGGTEPGGRS |
cell-cell adhesion positive regulation of apoptotic process positive regulation of inflammatory response T cell homeostasis | galectin complex | carbohydrate binding galactoside binding | Homo sapiens | 3D-structure Lectin Reference proteome | MTGELEVKNM | MTGELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE | cell-cell adhesion positive regulation of apoptotic process positive regulation of inflammatory response T cell homeostasis galectin complex carbohydrate binding galactoside binding Homo sapiens 3D-structure Lectin Reference proteome MTGELEVKNM MTGELEVKNMDMKPGSTLKITGSIADGTDGFVINLGQGTDKLNLHFNPRFSESTIVCNSLDGSNWGQEQREDHLCFSPGSEVKFTVTFESDKFKVKLPDGHELTFPNRLGHSHLSYLSVRGGFNMSSFKLKE |
defense response defense response to bacterium defense response to fungus hydrogen peroxide catabolic process hypochlorous acid biosynthetic process low-density lipoprotein particle remodeling negative regulation of apoptotic process removal of superoxide radicals respiratory burst involved in defense response response to food response to gold nanoparticle response to lipopolysaccharide response to mechanical stimulus response to oxidative stress response to yeast | azurophil granule; azurophil granule lumen; extracellular exosome; extracellular region; extracellular space; intracellular membrane-bounded organelle; lysosome; nucleoplasm; nucleus; phagocytic vesicle lumen; secretory granule | chromatin binding heme binding heparin binding metal ion binding peroxidase activity | Homo sapiens | 3D-structure Alternative splicing Calcium Direct protein sequencing Disease variant Disulfide bond Glycoprotein Heme Hydrogen peroxide Iron Lysosome Metal-binding Oxidation Oxidoreductase Peroxidase Reference proteome Signal | MGVPFFSSLR | MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTSLVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLHVALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREAS | defense response defense response to bacterium defense response to fungus hydrogen peroxide catabolic process hypochlorous acid biosynthetic process low-density lipoprotein particle remodeling negative regulation of apoptotic process removal of superoxide radicals respiratory burst involved in defense response response to food response to gold nanoparticle response to lipopolysaccharide response to mechanical stimulus response to oxidative stress response to yeast azurophil granule; azurophil granule lumen; extracellular exosome; extracellular region; extracellular space; intracellular membrane-bounded organelle; lysosome; nucleoplasm; nucleus; phagocytic vesicle lumen; secretory granule chromatin binding heme binding heparin binding metal ion binding peroxidase activity Homo sapiens 3D-structure Alternative splicing Calcium Direct protein sequencing Disease variant Disulfide bond Glycoprotein Heme Hydrogen peroxide Iron Lysosome Metal-binding Oxidation Oxidoreductase Peroxidase Reference proteome Signal MGVPFFSSLR MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTSLVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLHVALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMSNSYPRDFVNCSTLPALNLASWREAS |
branched-chain amino acid metabolic process fatty acid metabolic process short-chain fatty acid catabolic process | catalytic complex; cytosol; mitochondrial matrix; mitochondrion | ATP binding biotin binding enzyme binding metal ion binding propionyl-CoA carboxylase activity | Homo sapiens | 3D-structure Acetylation Alternative splicing ATP-binding Biotin Direct protein sequencing Disease variant Ligase Lipid degradation Lipid metabolism Magnesium Manganese Metal-binding Mitochondrion Nucleotide-binding Phosphoprotein Reference proteome Transit peptide | MAGFWVGTAP | MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNEKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRAQHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE | branched-chain amino acid metabolic process fatty acid metabolic process short-chain fatty acid catabolic process catalytic complex; cytosol; mitochondrial matrix; mitochondrion ATP binding biotin binding enzyme binding metal ion binding propionyl-CoA carboxylase activity Homo sapiens 3D-structure Acetylation Alternative splicing ATP-binding Biotin Direct protein sequencing Disease variant Ligase Lipid degradation Lipid metabolism Magnesium Manganese Metal-binding Mitochondrion Nucleotide-binding Phosphoprotein Reference proteome Transit peptide MAGFWVGTAP MAGFWVGTAPLVAAGRRGRWPPQQLMLSAALRTLKHVLYYSRQCLMVSRNLGSVGYDPNEKTFDKILVANRGEIACRVIRTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFARCLAAEDVVFIGPDTHAIQAMGDKIESKLLAKKAEVNTIPGFDGVVKDAEEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRLSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDAETRRAMGEQAVALARAVKYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHKQADIRINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPLHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSDRTEALKRMADALDNYVIRGVTHNIALLREVIINSRFVKGDISTKFLSDVYPDGFKGHMLTKSEKNQLLAIASSLFVAFQLRAQHFQENSRMPVIKPDIANWELSVKLHDKVHTVVASNNGSVFSVEVDGSKLNVTSTWNLASPLLSVSVDGTQRTVQCLSREAGGNMSIQFLGTVYKVNILTRLAAELNKFMLEKVTEDTSSVLRSPMPGVVVAVSVKPGDAVAEGQEICVIEAMKMQNSMTAGKTGTVKSVHCQAGDTVGEGDLLVELE |
branched-chain amino acid metabolic process fatty acid metabolic process short-chain fatty acid catabolic process | catalytic complex; cytosol; mitochondrial matrix; mitochondrion | ATP binding propionyl-CoA carboxylase activity | Homo sapiens | 3D-structure Acetylation Alternative splicing ATP-binding Direct protein sequencing Disease variant Ligase Mitochondrion Nucleotide-binding Phosphoprotein Reference proteome Transit peptide | MAAALRVAAV | MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL | branched-chain amino acid metabolic process fatty acid metabolic process short-chain fatty acid catabolic process catalytic complex; cytosol; mitochondrial matrix; mitochondrion ATP binding propionyl-CoA carboxylase activity Homo sapiens 3D-structure Acetylation Alternative splicing ATP-binding Direct protein sequencing Disease variant Ligase Mitochondrion Nucleotide-binding Phosphoprotein Reference proteome Transit peptide MAAALRVAAV MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL |
amine metabolic process cellular response to organic cyclic compound estrogen metabolic process heterocycle metabolic process hydrogen peroxide biosynthetic process lipid hydroxylation long-chain fatty acid metabolic process response to toxic substance retinol metabolic process steroid biosynthetic process toxin metabolic process xenobiotic metabolic process | endoplasmic reticulum membrane; mitochondrial inner membrane | arachidonic acid monooxygenase activity aromatase activity estrogen 16-alpha-hydroxylase activity estrogen 2-hydroxylase activity heme binding Hsp70 protein binding Hsp90 protein binding hydroperoxy icosatetraenoate dehydratase activity iron ion binding long-chain fatty acid omega-1 hydroxylase activity long-chain fatty acid omega-hydroxylase activity vitamin D 24-hydroxylase activity | Oryctolagus cuniculus | Cytoplasm Endoplasmic reticulum Glycoprotein Heme Iron Lipid biosynthesis Lipid metabolism Lyase Membrane Metal-binding Microsome Mitochondrion Mitochondrion inner membrane Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis | MVSDFGLPTF | MVSDFGLPTFISATELLLASAVFCLVFWVAGASKPRVPKGLKRLPGPWGWPLLGHVLTLGKNPHVALARLSRRYGDVFQIRLGSTPVVVLSGLDTIKQALVRQGDDFKGRPDLYSFSFVTKGQSMIFGSDSGPVWAARRRLAQNALNSFSVASDPASSSSCYLEEHVSQEAENLISKFQELMAAVGHFDPYRYVVMSVANVICAMCFGRRYDHDDQELLSLVNLNDEFGKVAASGSPADFFLILRYLPNPALDTFKDLNERFYSFTQERVKEHCRSFEKGHIRDITDSLIKHYRVDRLDENANVQVSDEKTVGIVLDLFGAGFDTVTTAISWSLMYLVTKPRIQRKIQEELDAVVGRARRPRFSDRPQLPYLEAVIMETFRHTSFLPFTIPHSTTRDTSLGGFYIPKGRCVFVNQWQNNHDPELWGDPEAFRPERFLTPSGAVDKALTEKVLLFGLGKRKCIGETIGRLEVFLFLATLLQQVEFSVSPGTTVDMTPIYGLTMKHARCEHFQAKLRFEA | amine metabolic process cellular response to organic cyclic compound estrogen metabolic process heterocycle metabolic process hydrogen peroxide biosynthetic process lipid hydroxylation long-chain fatty acid metabolic process response to toxic substance retinol metabolic process steroid biosynthetic process toxin metabolic process xenobiotic metabolic process endoplasmic reticulum membrane; mitochondrial inner membrane arachidonic acid monooxygenase activity aromatase activity estrogen 16-alpha-hydroxylase activity estrogen 2-hydroxylase activity heme binding Hsp70 protein binding Hsp90 protein binding hydroperoxy icosatetraenoate dehydratase activity iron ion binding long-chain fatty acid omega-1 hydroxylase activity long-chain fatty acid omega-hydroxylase activity vitamin D 24-hydroxylase activity Oryctolagus cuniculus Cytoplasm Endoplasmic reticulum Glycoprotein Heme Iron Lipid biosynthesis Lipid metabolism Lyase Membrane Metal-binding Microsome Mitochondrion Mitochondrion inner membrane Monooxygenase Oxidoreductase Reference proteome Steroid biosynthesis MVSDFGLPTF MVSDFGLPTFISATELLLASAVFCLVFWVAGASKPRVPKGLKRLPGPWGWPLLGHVLTLGKNPHVALARLSRRYGDVFQIRLGSTPVVVLSGLDTIKQALVRQGDDFKGRPDLYSFSFVTKGQSMIFGSDSGPVWAARRRLAQNALNSFSVASDPASSSSCYLEEHVSQEAENLISKFQELMAAVGHFDPYRYVVMSVANVICAMCFGRRYDHDDQELLSLVNLNDEFGKVAASGSPADFFLILRYLPNPALDTFKDLNERFYSFTQERVKEHCRSFEKGHIRDITDSLIKHYRVDRLDENANVQVSDEKTVGIVLDLFGAGFDTVTTAISWSLMYLVTKPRIQRKIQEELDAVVGRARRPRFSDRPQLPYLEAVIMETFRHTSFLPFTIPHSTTRDTSLGGFYIPKGRCVFVNQWQNNHDPELWGDPEAFRPERFLTPSGAVDKALTEKVLLFGLGKRKCIGETIGRLEVFLFLATLLQQVEFSVSPGTTVDMTPIYGLTMKHARCEHFQAKLRFEA |
aflatoxin metabolic process alkaloid metabolic process cellular respiration cellular response to cadmium ion cholesterol metabolic process dibenzo-p-dioxin metabolic process epoxygenase P450 pathway estrogen metabolic process heterocycle metabolic process hydrogen peroxide biosynthetic process long-chain fatty acid biosynthetic process lung development methylation monocarboxylic acid metabolic process monoterpenoid metabolic process omega-hydroxylase P450 pathway oxidative demethylation porphyrin-containing compound metabolic process post-embryonic development regulation of gene expression retinol metabolic process steroid catabolic process toxin biosynthetic process xenobiotic catabolic process xenobiotic metabolic process | endoplasmic reticulum membrane; intracellular membrane-bounded organelle | aromatase activity caffeine oxidase activity demethylase activity electron transfer activity enzyme binding estrogen 16-alpha-hydroxylase activity estrogen 2-hydroxylase activity heme binding hydroperoxy icosatetraenoate dehydratase activity iron ion binding monooxygenase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | Homo sapiens | 3D-structure Direct protein sequencing Endoplasmic reticulum Fatty acid metabolism Glycoprotein Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome Steroid metabolism Sterol metabolism | MALSQSVPFS | MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLSDRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPELWEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHVQARLRFSIN | aflatoxin metabolic process alkaloid metabolic process cellular respiration cellular response to cadmium ion cholesterol metabolic process dibenzo-p-dioxin metabolic process epoxygenase P450 pathway estrogen metabolic process heterocycle metabolic process hydrogen peroxide biosynthetic process long-chain fatty acid biosynthetic process lung development methylation monocarboxylic acid metabolic process monoterpenoid metabolic process omega-hydroxylase P450 pathway oxidative demethylation porphyrin-containing compound metabolic process post-embryonic development regulation of gene expression retinol metabolic process steroid catabolic process toxin biosynthetic process xenobiotic catabolic process xenobiotic metabolic process endoplasmic reticulum membrane; intracellular membrane-bounded organelle aromatase activity caffeine oxidase activity demethylase activity electron transfer activity enzyme binding estrogen 16-alpha-hydroxylase activity estrogen 2-hydroxylase activity heme binding hydroperoxy icosatetraenoate dehydratase activity iron ion binding monooxygenase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Homo sapiens 3D-structure Direct protein sequencing Endoplasmic reticulum Fatty acid metabolism Glycoprotein Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome Steroid metabolism Sterol metabolism MALSQSVPFS MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKNPHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDGQSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELMAGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFPILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGNLIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLSDRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPELWEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLEFSVPPGVKVDLTPIYGLTMKHARCEHVQARLRFSIN |
arachidonic acid metabolic process epoxygenase P450 pathway heterocycle metabolic process long-chain fatty acid metabolic process monoterpenoid metabolic process response to xenobiotic stimulus steroid metabolic process xenobiotic catabolic process xenobiotic metabolic process | cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bounded organelle | arachidonic acid 11,12-epoxygenase activity arachidonic acid 14,15-epoxygenase activity arachidonic acid epoxygenase activity aromatase activity enzyme binding heme binding iron ion binding long-chain fatty acid omega-1 hydroxylase activity monooxygenase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen steroid hydroxylase activity | Rattus norvegicus | Acetylation Endoplasmic reticulum Heme Iron Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome | MDLVMLLVLT | MDLVMLLVLTLTCLILLSIWRQSSGRGKLPPGPIPLPIIGNIFQLNVKNITQSLTSFSKVYGPVFTLYFGTKPTVILHGYEAVKEALIDHGEEFAERGSFPVAEKINKDLGIVFSHGNRWKEIRRFTLTTLRNLGMGKRNIEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENMKILSSPWTQFCSFFPVLIDYCPGSHTTLAKNVYHIRNYLLKKIKEHQESLDVTNPRDFIDYYLIKWKQENHNPHSEFTLENLSITVTDLFGAGTETTSTTLRYALLLLLKCPEVTAKVQEEIDRVVGKHRSPCMQDRSRMPYTDAHDHEVQRFIDLIPTNLPHAVTCDIKFRNYLIPKGTTIITSLSSVLHDSKEFPDPEIFDPGHFLDGNGKFKKSDYFMPFSAGKRMCAGEGLARMELFLFLTTILQNFKLKSVLHPKDIDTTPVFNGFASLPPFYELCFIPL | arachidonic acid metabolic process epoxygenase P450 pathway heterocycle metabolic process long-chain fatty acid metabolic process monoterpenoid metabolic process response to xenobiotic stimulus steroid metabolic process xenobiotic catabolic process xenobiotic metabolic process cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bounded organelle arachidonic acid 11,12-epoxygenase activity arachidonic acid 14,15-epoxygenase activity arachidonic acid epoxygenase activity aromatase activity enzyme binding heme binding iron ion binding long-chain fatty acid omega-1 hydroxylase activity monooxygenase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen steroid hydroxylase activity Rattus norvegicus Acetylation Endoplasmic reticulum Heme Iron Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome MDLVMLLVLT MDLVMLLVLTLTCLILLSIWRQSSGRGKLPPGPIPLPIIGNIFQLNVKNITQSLTSFSKVYGPVFTLYFGTKPTVILHGYEAVKEALIDHGEEFAERGSFPVAEKINKDLGIVFSHGNRWKEIRRFTLTTLRNLGMGKRNIEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENMKILSSPWTQFCSFFPVLIDYCPGSHTTLAKNVYHIRNYLLKKIKEHQESLDVTNPRDFIDYYLIKWKQENHNPHSEFTLENLSITVTDLFGAGTETTSTTLRYALLLLLKCPEVTAKVQEEIDRVVGKHRSPCMQDRSRMPYTDAHDHEVQRFIDLIPTNLPHAVTCDIKFRNYLIPKGTTIITSLSSVLHDSKEFPDPEIFDPGHFLDGNGKFKKSDYFMPFSAGKRMCAGEGLARMELFLFLTTILQNFKLKSVLHPKDIDTTPVFNGFASLPPFYELCFIPL |
epoxygenase P450 pathway response to ethanol response to lipopolysaccharide response to nutrient response to organic cyclic compound response to organonitrogen compound response to peptide hormone response to retinoic acid response to xenobiotic stimulus xenobiotic metabolic process | cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bounded organelle | arachidonic acid epoxygenase activity aromatase activity heme binding iron ion binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | Rattus norvegicus | Direct protein sequencing Endoplasmic reticulum Heme Iron Membrane Metal-binding Methylation Microsome Monooxygenase Oxidoreductase Reference proteome | MDLVTFLVLT | MDLVTFLVLTLSSLILLSLWRQSSRRRKLPPGPTPLPIIGNFLQIDVKNISQSLTKFSKTYGPVFTLYLGSQPTVILHGYEAIKEALIDNGEKFSGRGSYPMNENVTKGFGIVFSNGNRWKEMRRFTIMNFRNLGIGKRNIEDRVQEEAQCLVEELRKTKGSPCDPSLILNCAPCNVICSITFQNHFDYKDKEMLTFMEKVNENLKIMSSPWMQVCNSFPSLIDYFPGTHHKIAKNINYMKSYLLKKIEEHQESLDVTNPRDFVDYYLIKQKQANNIEQSEYSHENLTCSIMDLIGAGTETMSTTLRYALLLLMKYPHVTAKVQEEIDRVIGRHRSPCMQDRKHMPYTDAMIHEVQRFINFVPTNLPHAVTCDIKFRNYLIPKGTKVLTSLTSVLHDSKEFPNPEMFDPGHFLDENGNFKKSDYFLPFSAGKRACVGEGLARMQLFLFLTTILQNFNLKSLVHPKDIDTMPVLNGFASLPPTYQLCFIPS | epoxygenase P450 pathway response to ethanol response to lipopolysaccharide response to nutrient response to organic cyclic compound response to organonitrogen compound response to peptide hormone response to retinoic acid response to xenobiotic stimulus xenobiotic metabolic process cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bounded organelle arachidonic acid epoxygenase activity aromatase activity heme binding iron ion binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Rattus norvegicus Direct protein sequencing Endoplasmic reticulum Heme Iron Membrane Metal-binding Methylation Microsome Monooxygenase Oxidoreductase Reference proteome MDLVTFLVLT MDLVTFLVLTLSSLILLSLWRQSSRRRKLPPGPTPLPIIGNFLQIDVKNISQSLTKFSKTYGPVFTLYLGSQPTVILHGYEAIKEALIDNGEKFSGRGSYPMNENVTKGFGIVFSNGNRWKEMRRFTIMNFRNLGIGKRNIEDRVQEEAQCLVEELRKTKGSPCDPSLILNCAPCNVICSITFQNHFDYKDKEMLTFMEKVNENLKIMSSPWMQVCNSFPSLIDYFPGTHHKIAKNINYMKSYLLKKIEEHQESLDVTNPRDFVDYYLIKQKQANNIEQSEYSHENLTCSIMDLIGAGTETMSTTLRYALLLLMKYPHVTAKVQEEIDRVIGRHRSPCMQDRKHMPYTDAMIHEVQRFINFVPTNLPHAVTCDIKFRNYLIPKGTKVLTSLTSVLHDSKEFPNPEMFDPGHFLDENGNFKKSDYFLPFSAGKRACVGEGLARMQLFLFLTTILQNFNLKSLVHPKDIDTMPVLNGFASLPPTYQLCFIPS |
epoxygenase P450 pathway response to xenobiotic stimulus xenobiotic metabolic process | cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bounded organelle | arachidonic acid epoxygenase activity aromatase activity heme binding iron ion binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | Gallus gallus | Endoplasmic reticulum Heme Iron Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome | MDFLGLPTIL | MDFLGLPTILLLVCISCLLIAAWRSTSQRGKEPPGPTPIPIIGNVFQLNPWDLMGSFKELSKKYGPIFTIHLGPKKIVVLYGYDIVKEALIDNGEAFSGRGILPLIEKLFKGTGIVTSNGETWRQLRRFALTTLRDFGMGKKGIEERIQEEAHFLVERIRKTHEEPFNPGKFLIHAVANIICSIVFGDRFDYEDKKFLDLIEMLEENNKYQNRIQTLLYNFFPTILDSLPGPHKTLIKNTETVDDFIKEIVIAHQESFDASCPRDFIDAFINKMEQEKENSYFTVESLTRTTLDLFLAGTGTTSTTLRYGLLILLKHPEIEEKMHKEIDRVVGRDRSPCMADRSQLPYTDAVIHEIQRFIDFLPLNVPHAVIKDTKLRDYFIPKDTMIFPLLSPILQDCKEFPNPEKFDPGHFLNANGTFRRSDYFMPFSAGKRICAGEGLARMEIFLFLTSILQNFSLKPVKDRKDIDISPIITSLANMPRPYEVSFIPR | epoxygenase P450 pathway response to xenobiotic stimulus xenobiotic metabolic process cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bounded organelle arachidonic acid epoxygenase activity aromatase activity heme binding iron ion binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Gallus gallus Endoplasmic reticulum Heme Iron Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome MDFLGLPTIL MDFLGLPTILLLVCISCLLIAAWRSTSQRGKEPPGPTPIPIIGNVFQLNPWDLMGSFKELSKKYGPIFTIHLGPKKIVVLYGYDIVKEALIDNGEAFSGRGILPLIEKLFKGTGIVTSNGETWRQLRRFALTTLRDFGMGKKGIEERIQEEAHFLVERIRKTHEEPFNPGKFLIHAVANIICSIVFGDRFDYEDKKFLDLIEMLEENNKYQNRIQTLLYNFFPTILDSLPGPHKTLIKNTETVDDFIKEIVIAHQESFDASCPRDFIDAFINKMEQEKENSYFTVESLTRTTLDLFLAGTGTTSTTLRYGLLILLKHPEIEEKMHKEIDRVVGRDRSPCMADRSQLPYTDAVIHEIQRFIDFLPLNVPHAVIKDTKLRDYFIPKDTMIFPLLSPILQDCKEFPNPEKFDPGHFLNANGTFRRSDYFMPFSAGKRICAGEGLARMEIFLFLTSILQNFSLKPVKDRKDIDISPIITSLANMPRPYEVSFIPR |
4-nitrophenol metabolic process benzene metabolic process carbon tetrachloride metabolic process epoxygenase P450 pathway halogenated hydrocarbon metabolic process heterocycle metabolic process lipid hydroxylation long-chain fatty acid biosynthetic process long-chain fatty acid metabolic process monoterpenoid metabolic process response to bacterium steroid metabolic process xenobiotic metabolic process | cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bounded organelle; mitochondrial inner membrane | 4-nitrophenol 2-monooxygenase activity arachidonic acid epoxygenase activity aromatase activity enzyme binding heme binding Hsp70 protein binding Hsp90 protein binding iron ion binding long-chain fatty acid omega-1 hydroxylase activity monooxygenase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen oxygen binding | Homo sapiens | 3D-structure Direct protein sequencing Endoplasmic reticulum Fatty acid metabolism Heme Iron Lipid metabolism Membrane Metal-binding Microsome Mitochondrion Mitochondrion inner membrane Monooxygenase NADP Oxidoreductase Reference proteome | MSALGVTVAL | MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRLAQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGPTWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVIADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVAEVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRFITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGKFKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGCIPPRYKLCVIPRS | 4-nitrophenol metabolic process benzene metabolic process carbon tetrachloride metabolic process epoxygenase P450 pathway halogenated hydrocarbon metabolic process heterocycle metabolic process lipid hydroxylation long-chain fatty acid biosynthetic process long-chain fatty acid metabolic process monoterpenoid metabolic process response to bacterium steroid metabolic process xenobiotic metabolic process cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bounded organelle; mitochondrial inner membrane 4-nitrophenol 2-monooxygenase activity arachidonic acid epoxygenase activity aromatase activity enzyme binding heme binding Hsp70 protein binding Hsp90 protein binding iron ion binding long-chain fatty acid omega-1 hydroxylase activity monooxygenase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen oxygen binding Homo sapiens 3D-structure Direct protein sequencing Endoplasmic reticulum Fatty acid metabolism Heme Iron Lipid metabolism Membrane Metal-binding Microsome Mitochondrion Mitochondrion inner membrane Monooxygenase NADP Oxidoreductase Reference proteome MSALGVTVAL MSALGVTVALLVWAAFLLLVSMWRQVHSSWNLPPGPFPLPIIGNLFQLELKNIPKSFTRLAQRFGPVFTLYVGSQRMVVMHGYKAVKEALLDYKDEFSGRGDLPAFHAHRDRGIIFNNGPTWKDIRRFSLTTLRNYGMGKQGNESRIQREAHFLLEALRKTQGQPFDPTFLIGCAPCNVIADILFRKHFDYNDEKFLRLMYLFNENFHLLSTPWLQLYNNFPSFLHYLPGSHRKVIKNVAEVKEYVSERVKEHHQSLDPNCPRDLTDCLLVEMEKEKHSAERLYTMDGITVTVADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRIPAIKDRQEMPYMDAVVHEIQRFITLVPSNLPHEATRDTIFRGYLIPKGTVVVPTLDSVLYDNQEFPDPEKFKPEHFLNENGKFKYSDYFKPFSTGKRVCAGEGLARMELFLLLCAILQHFNLKPLVDPKDIDLSPIHIGFGCIPPRYKLCVIPRS |
4-nitrophenol metabolic process epoxygenase P450 pathway heterocycle metabolic process lipid hydroxylation long-chain fatty acid metabolic process monoterpenoid metabolic process response to 3-methylcholanthrene response to bacterium response to ethanol response to organonitrogen compound response to ozone response to xenobiotic stimulus steroid metabolic process triglyceride metabolic process xenobiotic metabolic process | cytoplasm; endoplasmic reticulum; endoplasmic reticulum membrane; Golgi membrane; intracellular membrane-bounded organelle; mitochondrial inner membrane | 4-nitrophenol 2-monooxygenase activity arachidonic acid epoxygenase activity aromatase activity enzyme binding heme binding Hsp70 protein binding Hsp90 protein binding iron ion binding long-chain fatty acid omega-1 hydroxylase activity monooxygenase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | Rattus norvegicus | Direct protein sequencing Endoplasmic reticulum Fatty acid metabolism Heme Iron Lipid metabolism Membrane Metal-binding Microsome Mitochondrion Mitochondrion inner membrane Monooxygenase NADP Oxidoreductase Reference proteome | MAVLGITIAL | MAVLGITIALLVWVATLLVISIWKQIYNSWNLPPGPFPLPILGNIFQLDLKDIPKSFTKLAKRFGPVFTLHLGSRRIVVLHGYKAVKEVLLNHKNEFSGRGDIPVFQEYKNKGIIFNNGPTWKDVRRFSLSILRDWGMGKQGNEARIQREAQFLVEELKKTKGQPFDPTFLIGCAPCNVIADILFNKRFDYNDKKCLRLMSLFNENFYLLSTPWIQLYNNFADYLRYLPGSHRKIMKNVSEIKQYTLEKAKEHLQSLDINCARDVTDCLLIEMEKEKHSQEPMYTMENVSVTLADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRVPAVRDRLDMPYMDAVVHEIQRFINLVPSNLPHEATRDTVFQGYVIPKGTVVIPTLDSLLYDSHEFPDPEKFKPEHFLNENGKFKYSDYFKAFSAGKRVCVGEGLARMELFLLLSAILQHFNLKSLVDPKDIDLSPVTVGFGSIPPQFKLCVIPRS | 4-nitrophenol metabolic process epoxygenase P450 pathway heterocycle metabolic process lipid hydroxylation long-chain fatty acid metabolic process monoterpenoid metabolic process response to 3-methylcholanthrene response to bacterium response to ethanol response to organonitrogen compound response to ozone response to xenobiotic stimulus steroid metabolic process triglyceride metabolic process xenobiotic metabolic process cytoplasm; endoplasmic reticulum; endoplasmic reticulum membrane; Golgi membrane; intracellular membrane-bounded organelle; mitochondrial inner membrane 4-nitrophenol 2-monooxygenase activity arachidonic acid epoxygenase activity aromatase activity enzyme binding heme binding Hsp70 protein binding Hsp90 protein binding iron ion binding long-chain fatty acid omega-1 hydroxylase activity monooxygenase activity oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Rattus norvegicus Direct protein sequencing Endoplasmic reticulum Fatty acid metabolism Heme Iron Lipid metabolism Membrane Metal-binding Microsome Mitochondrion Mitochondrion inner membrane Monooxygenase NADP Oxidoreductase Reference proteome MAVLGITIAL MAVLGITIALLVWVATLLVISIWKQIYNSWNLPPGPFPLPILGNIFQLDLKDIPKSFTKLAKRFGPVFTLHLGSRRIVVLHGYKAVKEVLLNHKNEFSGRGDIPVFQEYKNKGIIFNNGPTWKDVRRFSLSILRDWGMGKQGNEARIQREAQFLVEELKKTKGQPFDPTFLIGCAPCNVIADILFNKRFDYNDKKCLRLMSLFNENFYLLSTPWIQLYNNFADYLRYLPGSHRKIMKNVSEIKQYTLEKAKEHLQSLDINCARDVTDCLLIEMEKEKHSQEPMYTMENVSVTLADLFFAGTETTSTTLRYGLLILMKYPEIEEKLHEEIDRVIGPSRVPAVRDRLDMPYMDAVVHEIQRFINLVPSNLPHEATRDTVFQGYVIPKGTVVIPTLDSLLYDSHEFPDPEKFKPEHFLNENGKFKYSDYFKAFSAGKRVCVGEGLARMELFLLLSAILQHFNLKSLVDPKDIDLSPVTVGFGSIPPQFKLCVIPRS |
alkaloid catabolic process estrogen metabolic process heterocycle metabolic process lipid hydroxylation monoterpenoid metabolic process oxidative demethylation retinoic acid metabolic process retinol metabolic process steroid catabolic process steroid metabolic process vitamin D catabolic process xenobiotic catabolic process xenobiotic metabolic process | cytoplasm; endoplasmic reticulum membrane | 1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity aromatase activity caffeine oxidase activity demethylase activity enzyme binding estrogen 16-alpha-hydroxylase activity estrogen 2-hydroxylase activity heme binding iron ion binding monooxygenase activity oxidoreductase activity retinoic acid 4-hydroxylase activity steroid binding steroid hydroxylase activity testosterone 6-beta-hydroxylase activity vitamin D 24-hydroxylase activity vitamin D3 25-hydroxylase activity | Rattus norvegicus | Direct protein sequencing Endoplasmic reticulum Heme Iron Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome | MDLLSALTLE | MDLLSALTLETWVLLAVILVLLYRLGTHRHGIFKKQGIPGPKPLPFLGTVLNYYKGLGRFDMECYKKYGKIWGLFDGQTPVFAIMDTEMIKNVLVKECFSVFTNRRDFGPVGIMGKAVSVAKDEEWKRYRALLSPTFTSGRLKEMFPIIEQYGDILVKYLKQEAETGKPVTMKKVFGAYSMDVITSTSFGVNVDSLNNPKDPFVEKTKKLLRFDFFDPLFLSVVLFPFLTPIYEMLNICMFPKDSIAFFQKFVHRIKETRLDSKHKHRVDFLQLMLNAHNNSKDEVSHKALSDVEIIAQSVIFIFAGYETTSSTLSFVLYFLATHPDIQKKLQEEIDGALPSKAPPTYDIVMEMEYLDMVLNETLRLYPIGNRLERVCKKDIELDGLFIPKGSVVTIPTYALHHDPQHWPKPEEFHPERFSKENKGSIDPYVYLPFGNGPRNCIGMRFALMNMKLALTKVLQNFSFQPCKETQIPLKLSRQAILEPEKPIVLKVLPRDAVINGA | alkaloid catabolic process estrogen metabolic process heterocycle metabolic process lipid hydroxylation monoterpenoid metabolic process oxidative demethylation retinoic acid metabolic process retinol metabolic process steroid catabolic process steroid metabolic process vitamin D catabolic process xenobiotic catabolic process xenobiotic metabolic process cytoplasm; endoplasmic reticulum membrane 1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity aromatase activity caffeine oxidase activity demethylase activity enzyme binding estrogen 16-alpha-hydroxylase activity estrogen 2-hydroxylase activity heme binding iron ion binding monooxygenase activity oxidoreductase activity retinoic acid 4-hydroxylase activity steroid binding steroid hydroxylase activity testosterone 6-beta-hydroxylase activity vitamin D 24-hydroxylase activity vitamin D3 25-hydroxylase activity Rattus norvegicus Direct protein sequencing Endoplasmic reticulum Heme Iron Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome MDLLSALTLE MDLLSALTLETWVLLAVILVLLYRLGTHRHGIFKKQGIPGPKPLPFLGTVLNYYKGLGRFDMECYKKYGKIWGLFDGQTPVFAIMDTEMIKNVLVKECFSVFTNRRDFGPVGIMGKAVSVAKDEEWKRYRALLSPTFTSGRLKEMFPIIEQYGDILVKYLKQEAETGKPVTMKKVFGAYSMDVITSTSFGVNVDSLNNPKDPFVEKTKKLLRFDFFDPLFLSVVLFPFLTPIYEMLNICMFPKDSIAFFQKFVHRIKETRLDSKHKHRVDFLQLMLNAHNNSKDEVSHKALSDVEIIAQSVIFIFAGYETTSSTLSFVLYFLATHPDIQKKLQEEIDGALPSKAPPTYDIVMEMEYLDMVLNETLRLYPIGNRLERVCKKDIELDGLFIPKGSVVTIPTYALHHDPQHWPKPEEFHPERFSKENKGSIDPYVYLPFGNGPRNCIGMRFALMNMKLALTKVLQNFSFQPCKETQIPLKLSRQAILEPEKPIVLKVLPRDAVINGA |
glucocorticoid biosynthetic process hormone biosynthetic process progesterone metabolic process steroid metabolic process | endoplasmic reticulum membrane | 17-alpha-hydroxyprogesterone aldolase activity heme binding iron ion binding steroid 17-alpha-monooxygenase activity | Bos taurus | Endoplasmic reticulum Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome Steroidogenesis | MWLLLAVFLL | MWLLLAVFLLTLAYLFWPKTKHSGAKYPRSLPSLPLVGSLPFLPRRGQQHKNFFKLQEKYGPIYSFRLGSKTTVMIGHHQLAREVLLKKGKEFSGRPKVATLDILSDNQKGIAFADHGAHWQLHRKLALNAFALFKDGNLKLEKIINQEANVLCDFLATQHGEAIDLSEPLSLAVTNIISFICFNFSFKNEDPALKAIQNVNDGILEVLSKEVLLDIFPVLKIFPSKAMEKMKGCVQTRNELLNEILEKCQENFSSDSITNLLHILIQAKVNADNNNAGPDQDSKLLSNRHMLATIGDIFGAGVETTTSVIKWIVAYLLHHPSLKKRIQDDIDQIIGFNRTPTISDRNRLVLLEATIREVLRIRPVAPTLIPHKAVIDSSIGDLTIDKGTDVVVNLWALHHSEKEWQHPDLFMPERFLDPTGTQLISPSLSYLPFGAGPRSCVGEMLARQELFLFMSRLLQRFNLEIPDDGKLPSLEGHASLVLQIKPFKVKIEVRQAWKEAQAEGSTP | glucocorticoid biosynthetic process hormone biosynthetic process progesterone metabolic process steroid metabolic process endoplasmic reticulum membrane 17-alpha-hydroxyprogesterone aldolase activity heme binding iron ion binding steroid 17-alpha-monooxygenase activity Bos taurus Endoplasmic reticulum Heme Iron Lipid metabolism Lyase Membrane Metal-binding Microsome Monooxygenase Oxidoreductase Reference proteome Steroidogenesis MWLLLAVFLL MWLLLAVFLLTLAYLFWPKTKHSGAKYPRSLPSLPLVGSLPFLPRRGQQHKNFFKLQEKYGPIYSFRLGSKTTVMIGHHQLAREVLLKKGKEFSGRPKVATLDILSDNQKGIAFADHGAHWQLHRKLALNAFALFKDGNLKLEKIINQEANVLCDFLATQHGEAIDLSEPLSLAVTNIISFICFNFSFKNEDPALKAIQNVNDGILEVLSKEVLLDIFPVLKIFPSKAMEKMKGCVQTRNELLNEILEKCQENFSSDSITNLLHILIQAKVNADNNNAGPDQDSKLLSNRHMLATIGDIFGAGVETTTSVIKWIVAYLLHHPSLKKRIQDDIDQIIGFNRTPTISDRNRLVLLEATIREVLRIRPVAPTLIPHKAVIDSSIGDLTIDKGTDVVVNLWALHHSEKEWQHPDLFMPERFLDPTGTQLISPSLSYLPFGAGPRSCVGEMLARQELFLFMSRLLQRFNLEIPDDGKLPSLEGHASLVLQIKPFKVKIEVRQAWKEAQAEGSTP |
bone mineralization calcium ion homeostasis cellular homeostasis cellular response to organic cyclic compound cementum mineralization dephosphorylation developmental process involved in reproduction endochondral ossification futile creatine cycle inhibition of non-skeletal tissue mineralization osteoblast differentiation phosphate ion homeostasis positive regulation of cold-induced thermogenesis pyridoxal phosphate metabolic process response to antibiotic response to glucocorticoid response to insulin response to lipopolysaccharide response to macrophage colony-stimulating factor response to sodium phosphate response to vitamin B6 response to vitamin D skeletal system development | extracellular exosome; extracellular matrix; extracellular region; membrane; mitochondrial intermembrane space; mitochondrial membrane; plasma membrane; side of membrane | ADP phosphatase activity alkaline phosphatase activity ATP hydrolysis activity calcium ion binding inorganic diphosphate phosphatase activity phosphoamidase activity phosphoethanolamine phosphatase activity pyridoxal phosphatase activity pyrophosphatase activity | Homo sapiens | 3D-structure Alternative splicing Biomineralization Calcium Cell membrane Direct protein sequencing Disease variant Disulfide bond Glycoprotein GPI-anchor Hydrolase Lipoprotein Magnesium Membrane Metal-binding Mitochondrion Phosphoprotein Reference proteome Signal Zinc | MISPFLVLAI | MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF | bone mineralization calcium ion homeostasis cellular homeostasis cellular response to organic cyclic compound cementum mineralization dephosphorylation developmental process involved in reproduction endochondral ossification futile creatine cycle inhibition of non-skeletal tissue mineralization osteoblast differentiation phosphate ion homeostasis positive regulation of cold-induced thermogenesis pyridoxal phosphate metabolic process response to antibiotic response to glucocorticoid response to insulin response to lipopolysaccharide response to macrophage colony-stimulating factor response to sodium phosphate response to vitamin B6 response to vitamin D skeletal system development extracellular exosome; extracellular matrix; extracellular region; membrane; mitochondrial intermembrane space; mitochondrial membrane; plasma membrane; side of membrane ADP phosphatase activity alkaline phosphatase activity ATP hydrolysis activity calcium ion binding inorganic diphosphate phosphatase activity phosphoamidase activity phosphoethanolamine phosphatase activity pyridoxal phosphatase activity pyrophosphatase activity Homo sapiens 3D-structure Alternative splicing Biomineralization Calcium Cell membrane Direct protein sequencing Disease variant Disulfide bond Glycoprotein GPI-anchor Hydrolase Lipoprotein Magnesium Membrane Metal-binding Mitochondrion Phosphoprotein Reference proteome Signal Zinc MISPFLVLAI MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDEKARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELNRNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIGQAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPGYKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYVPHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF |
dephosphorylation | cell surface; plasma membrane; side of membrane | alkaline phosphatase activity magnesium ion binding zinc ion binding | Homo sapiens | 3D-structure Calcium Cell membrane Direct protein sequencing Disulfide bond Glycoprotein GPI-anchor Hydrolase Lipoprotein Magnesium Membrane Metal-binding Reference proteome Signal Transmembrane Transmembrane helix Zinc | MLGPCMLLLL | MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPPAGTTDAAHPGRSVVPALLPLLAGTLLLLETATAP | dephosphorylation cell surface; plasma membrane; side of membrane alkaline phosphatase activity magnesium ion binding zinc ion binding Homo sapiens 3D-structure Calcium Cell membrane Direct protein sequencing Disulfide bond Glycoprotein GPI-anchor Hydrolase Lipoprotein Magnesium Membrane Metal-binding Reference proteome Signal Transmembrane Transmembrane helix Zinc MLGPCMLLLL MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLIIFLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATAYLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGTYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYPDDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEIHRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFIAHVMAFAACLEPYTACDLAPPAGTTDAAHPGRSVVPALLPLLAGTLLLLETATAP |
penicillin biosynthetic process | cytosol | iron ion binding isopenicillin-N synthase activity | Hapsidospora chrysogena | Antibiotic biosynthesis Cytoplasm Direct protein sequencing Iron Metal-binding Oxidoreductase | MGSVPVPVAN | MGSVPVPVANVPRIDVSPLFGDDKEKKLEVARAIDAASRDTGFFYAVNHGVDLPWLSRETNKFHMSITDEEKWQLAIRAYNKEHESQIRAGYYLPIPGKKAVESFCYLNPSFSPDHPRIKEPTPMHEVNVWPDEAKHPGFRAFAEKYYWDVFGLSSAVLRGYALALGRDEDFFTRHSRRDTTLSSVVLIRYPYLDPYPEPAIKTADDGTKLSFEWHEDVSLITVLYQSDVQNLQVKTPQGWQDIQADDTGFLINCGSYMAHITDDYYPAPIHRVKWVNEERQSLPFFVNLGWEDTIQPWDPATAKDGAKDAAKDKPAISYGEYLQGGLRGLINKNGQT | penicillin biosynthetic process cytosol iron ion binding isopenicillin-N synthase activity Hapsidospora chrysogena Antibiotic biosynthesis Cytoplasm Direct protein sequencing Iron Metal-binding Oxidoreductase MGSVPVPVAN MGSVPVPVANVPRIDVSPLFGDDKEKKLEVARAIDAASRDTGFFYAVNHGVDLPWLSRETNKFHMSITDEEKWQLAIRAYNKEHESQIRAGYYLPIPGKKAVESFCYLNPSFSPDHPRIKEPTPMHEVNVWPDEAKHPGFRAFAEKYYWDVFGLSSAVLRGYALALGRDEDFFTRHSRRDTTLSSVVLIRYPYLDPYPEPAIKTADDGTKLSFEWHEDVSLITVLYQSDVQNLQVKTPQGWQDIQADDTGFLINCGSYMAHITDDYYPAPIHRVKWVNEERQSLPFFVNLGWEDTIQPWDPATAKDGAKDAAKDKPAISYGEYLQGGLRGLINKNGQT |
antibiotic catabolic process response to antibiotic | outer membrane-bounded periplasmic space | beta-lactamase activity | Citrobacter freundii | 3D-structure Antibiotic resistance Direct protein sequencing Hydrolase Periplasm Signal | MMKKSICCAL | MMKKSICCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAIIYEGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDRIARGEIKLSDPVTKYWPELTGKQWRGISLLHLATYTAGGLPLQIPGDVTDKAELLRFYQNWQPQWTPGAKRLYANSSIGLFGALAVKSSGMSYEEAMTRRVLQPLKLAHTWITVPQSEQKNYAWGYLEGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIELAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPARVEAAWRILEKLQ | antibiotic catabolic process response to antibiotic outer membrane-bounded periplasmic space beta-lactamase activity Citrobacter freundii3D-structure Antibiotic resistance Direct protein sequencing Hydrolase Periplasm Signal MMKKSICCAL MMKKSICCALLLTASFSTFAAAKTEQQIADIVNRTITPLMQEQAIPGMAVAIIYEGKPYYFTWGKADIANNHPVTQQTLFELGSVSKTFNGVLGGDRIARGEIKLSDPVTKYWPELTGKQWRGISLLHLATYTAGGLPLQIPGDVTDKAELLRFYQNWQPQWTPGAKRLYANSSIGLFGALAVKSSGMSYEEAMTRRVLQPLKLAHTWITVPQSEQKNYAWGYLEGKPVHVSPGQLDAEAYGVKSSVIDMARWVQANMDASHVQEKTLQQGIELAQSRYWRIGDMYQGLGWEMLNWPLKADSIINGSDSKVALAALPAVEVNPPAPAVKASWVHKTGSTGGFGSYVAFVPEKNLGIVMLANKSYPNPARVEAAWRILEKLQ |
3,4-dihydroxybenzoate biosynthetic process amino acid biosynthetic process aromatic amino acid family biosynthetic process chorismate biosynthetic process | cytosol | 3-dehydroquinate dehydratase activity protein homodimerization activity | Escherichia coli | Amino-acid biosynthesis Aromatic amino acid biosynthesis Direct protein sequencing Lyase Reference proteome Schiff base | MKTVTVKDLV | MKTVTVKDLVIGTGAPKIIVSLMAKDIASVKSEALAYREADFDILEWRVDHYADLSNVESVMAAAKILRETMPEKPLLFTFRSAKEGGEQAISTEAYIALNRAAIDSGLVDMIDLELFTGDDQVKETVAYAHAHDVKVVMSNHDFHKTPEAEEIIARLRKMQSFDADIPKIALMPQSTSDVLTLLAATLEMQEQYADRPIITMSMAKTGVISRLAGEVFGSAATFGAVKKASAPGQISVNDLRTVLTILHQA | 3,4-dihydroxybenzoate biosynthetic process amino acid biosynthetic process aromatic amino acid family biosynthetic process chorismate biosynthetic process cytosol 3-dehydroquinate dehydratase activity protein homodimerization activity Escherichia coli Amino-acid biosynthesis Aromatic amino acid biosynthesis Direct protein sequencing Lyase Reference proteome Schiff base MKTVTVKDLV MKTVTVKDLVIGTGAPKIIVSLMAKDIASVKSEALAYREADFDILEWRVDHYADLSNVESVMAAAKILRETMPEKPLLFTFRSAKEGGEQAISTEAYIALNRAAIDSGLVDMIDLELFTGDDQVKETVAYAHAHDVKVVMSNHDFHKTPEAEEIIARLRKMQSFDADIPKIALMPQSTSDVLTLLAATLEMQEQYADRPIITMSMAKTGVISRLAGEVFGSAATFGAVKKASAPGQISVNDLRTVLTILHQA |
cellular response to brain-derived neurotrophic factor stimulus glial cell proliferation hematopoietic progenitor cell differentiation positive regulation of cytoplasmic translation positive regulation of translation response to endoplasmic reticulum stress response to estradiol response to ethanol response to folic acid response to hydrogen peroxide response to ischemia response to xenobiotic stimulus skeletal muscle cell differentiation skeletal muscle contraction translation at postsynapse translational elongation | cytoplasm; cytosol; glutamatergic synapse; postsynapse; ribonucleoprotein complex; ribosome; synapse | 5S rRNA binding actin filament binding GTP binding GTPase activity p53 binding protein kinase binding ribosome binding RNA binding translation elongation factor activity | Rattus norvegicus | Acetylation Cytoplasm Direct protein sequencing Elongation factor GTP-binding Hydrolase Isopeptide bond Methylation Nucleotide-binding Nucleus Phosphoprotein Protein biosynthesis Reference proteome Ubl conjugation | MVNFTVDQIR | MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGAAERAKKVEDMMKKLWGDRYFDPANGKFSKSANSPDGKKLPRTFCQLILDPIFKVFDAIMNFRKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKARARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL | cellular response to brain-derived neurotrophic factor stimulus glial cell proliferation hematopoietic progenitor cell differentiation positive regulation of cytoplasmic translation positive regulation of translation response to endoplasmic reticulum stress response to estradiol response to ethanol response to folic acid response to hydrogen peroxide response to ischemia response to xenobiotic stimulus skeletal muscle cell differentiation skeletal muscle contraction translation at postsynapse translational elongation cytoplasm; cytosol; glutamatergic synapse; postsynapse; ribonucleoprotein complex; ribosome; synapse 5S rRNA binding actin filament binding GTP binding GTPase activity p53 binding protein kinase binding ribosome binding RNA binding translation elongation factor activity Rattus norvegicus Acetylation Cytoplasm Direct protein sequencing Elongation factor GTP-binding Hydrolase Isopeptide bond Methylation Nucleotide-binding Nucleus Phosphoprotein Protein biosynthesis Reference proteome Ubl conjugation MVNFTVDQIR MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGSGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGAAERAKKVEDMMKKLWGDRYFDPANGKFSKSANSPDGKKLPRTFCQLILDPIFKVFDAIMNFRKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGVVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKARARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL |
cellular response to amino acid starvation cellular response to heat cellular response to oxidative stress cellular response to UV negative regulation of translational initiation in response to stress PERK-mediated unfolded protein response positive regulation of type B pancreatic cell apoptotic process regulation of translation in response to endoplasmic reticulum stress regulation of translational initiation in response to stress response to endoplasmic reticulum stress response to kainic acid response to manganese-induced endoplasmic reticulum stress stress granule assembly translational initiation | cytoplasmic stress granule; cytosol; eukaryotic 48S preinitiation complex; eukaryotic translation initiation factor 2 complex; extracellular exosome; glial limiting end-foot; membrane; nucleus; polysome; synapse; translation initiation ternary complex | ribosome binding RNA binding translation initiation factor activity | Homo sapiens | 3D-structure Acetylation Cytoplasm Initiation factor Phosphoprotein Protein biosynthesis Reference proteome RNA-binding Translation regulation | MPGLSCRFYQ | MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTTTLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEVDGDDDAEEMEAKAED | cellular response to amino acid starvation cellular response to heat cellular response to oxidative stress cellular response to UV negative regulation of translational initiation in response to stress PERK-mediated unfolded protein response positive regulation of type B pancreatic cell apoptotic process regulation of translation in response to endoplasmic reticulum stress regulation of translational initiation in response to stress response to endoplasmic reticulum stress response to kainic acid response to manganese-induced endoplasmic reticulum stress stress granule assembly translational initiation cytoplasmic stress granule; cytosol; eukaryotic 48S preinitiation complex; eukaryotic translation initiation factor 2 complex; extracellular exosome; glial limiting end-foot; membrane; nucleus; polysome; synapse; translation initiation ternary complex ribosome binding RNA binding translation initiation factor activity Homo sapiens 3D-structure Acetylation Cytoplasm Initiation factor Phosphoprotein Protein biosynthesis Reference proteome RNA-binding Translation regulation MPGLSCRFYQ MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTTTLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEVDGDDDAEEMEAKAED |
memory modulation of chemical synaptic transmission negative regulation of neuron apoptotic process nerve development nerve growth factor signaling pathway neuron projection morphogenesis peripheral nervous system development positive regulation of collateral sprouting positive regulation of peptidyl-serine phosphorylation regulation of neuron differentiation transmembrane receptor protein tyrosine kinase signaling pathway | axon; dendrite; extracellular space; synaptic vesicle | growth factor activity nerve growth factor receptor binding | Gallus gallus | Cleavage on pair of basic residues Disulfide bond Growth factor Reference proteome Secreted Signal | MHSVMSMLYY | MHSVMSMLYYTLIIAFLIGTQAAPKSEDNGPLEYPAEHSLPSTQQSNGQHIAKAAPQTTHGRFAWMPDGTEDLNIAMDQNFFKKKRFRSSRVLFSTQPPPVSRKGQSTGFLSSAVSLNRTARTKRTAHPVLHRGEFSVCDSVSMWVGDKTTATDIKGKEVTVLGEVNINNNVFKQYFFETKCRDPRPVSSGCRGIDAKHWNSYCTTTHTFVKALTMEGKQAAWRFIRIDTACVCVLSRKSGRP | memory modulation of chemical synaptic transmission negative regulation of neuron apoptotic process nerve development nerve growth factor signaling pathway neuron projection morphogenesis peripheral nervous system development positive regulation of collateral sprouting positive regulation of peptidyl-serine phosphorylation regulation of neuron differentiation transmembrane receptor protein tyrosine kinase signaling pathway axon; dendrite; extracellular space; synaptic vesicle growth factor activity nerve growth factor receptor binding Gallus gallus Cleavage on pair of basic residues Disulfide bond Growth factor Reference proteome Secreted Signal MHSVMSMLYY MHSVMSMLYYTLIIAFLIGTQAAPKSEDNGPLEYPAEHSLPSTQQSNGQHIAKAAPQTTHGRFAWMPDGTEDLNIAMDQNFFKKKRFRSSRVLFSTQPPPVSRKGQSTGFLSSAVSLNRTARTKRTAHPVLHRGEFSVCDSVSMWVGDKTTATDIKGKEVTVLGEVNINNNVFKQYFFETKCRDPRPVSSGCRGIDAKHWNSYCTTTHTFVKALTMEGKQAAWRFIRIDTACVCVLSRKSGRP |
2-oxoglutarate metabolic process aspartate biosynthetic process aspartate catabolic process aspartate metabolic process cellular response to insulin stimulus cellular response to mechanical stimulus dicarboxylic acid metabolic process fatty acid homeostasis gluconeogenesis glutamate catabolic process to 2-oxoglutarate glutamate catabolic process to aspartate glutamate metabolic process glycerol biosynthetic process negative regulation of collagen biosynthetic process negative regulation of cytosolic calcium ion concentration negative regulation of mitochondrial depolarization Notch signaling pathway oxaloacetate metabolic process positive regulation of transforming growth factor beta receptor signaling pathway response to glucocorticoid response to transition metal nanoparticle transdifferentiation | axon terminus; cytoplasm; cytosol | carboxylic acid binding L-aspartate:2-oxoglutarate aminotransferase activity L-cysteine transaminase activity phosphatidylserine decarboxylase activity pyridoxal phosphate binding | Mus musculus | Amino-acid biosynthesis Aminotransferase Cytoplasm Direct protein sequencing Phosphoprotein Pyridoxal phosphate Reference proteome Transferase | MAPPSVFAQV | MAPPSVFAQVPQAPPVLVFKLTADFRDDPDPRKVNLGVGAYRTDESQPWVLPVVRKVEQKIANDNSLNHEYLPILGLAEFRSCASRLVLGDNSLAIRENRVGGVQSLGGTGALRIGADFLGRWYNGTDNKNTPIYVSSPTWENHNAVFSAAGFKDIRPYCYWDAEKRGLDLQGFLNDLENAPEFSIFVLHACAHNPTGTDPTPEQWKQIAAVMQRRFLFPFFDSAYQGFASGDLEKDAWAIRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVGKESDSVLRVLSQMEKIVRITWSNPPAQGARIVAATLSDPELFKEWKGNVKTMADRILTMRSELRARLEALKTPGTWSHITEQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINMCGLTTKNLDYVATSIHEAVTKIQ | 2-oxoglutarate metabolic process aspartate biosynthetic process aspartate catabolic process aspartate metabolic process cellular response to insulin stimulus cellular response to mechanical stimulus dicarboxylic acid metabolic process fatty acid homeostasis gluconeogenesis glutamate catabolic process to 2-oxoglutarate glutamate catabolic process to aspartate glutamate metabolic process glycerol biosynthetic process negative regulation of collagen biosynthetic process negative regulation of cytosolic calcium ion concentration negative regulation of mitochondrial depolarization Notch signaling pathway oxaloacetate metabolic process positive regulation of transforming growth factor beta receptor signaling pathway response to glucocorticoid response to transition metal nanoparticle transdifferentiation axon terminus; cytoplasm; cytosol carboxylic acid binding L-aspartate:2-oxoglutarate aminotransferase activity L-cysteine transaminase activity phosphatidylserine decarboxylase activity pyridoxal phosphate binding Mus musculus Amino-acid biosynthesis Aminotransferase Cytoplasm Direct protein sequencing Phosphoprotein Pyridoxal phosphate Reference proteome Transferase MAPPSVFAQV MAPPSVFAQVPQAPPVLVFKLTADFRDDPDPRKVNLGVGAYRTDESQPWVLPVVRKVEQKIANDNSLNHEYLPILGLAEFRSCASRLVLGDNSLAIRENRVGGVQSLGGTGALRIGADFLGRWYNGTDNKNTPIYVSSPTWENHNAVFSAAGFKDIRPYCYWDAEKRGLDLQGFLNDLENAPEFSIFVLHACAHNPTGTDPTPEQWKQIAAVMQRRFLFPFFDSAYQGFASGDLEKDAWAIRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVGKESDSVLRVLSQMEKIVRITWSNPPAQGARIVAATLSDPELFKEWKGNVKTMADRILTMRSELRARLEALKTPGTWSHITEQIGMFSFTGLNPKQVEYLVNEKHIYLLPSGRINMCGLTTKNLDYVATSIHEAVTKIQ |
2-oxoglutarate metabolic process amino acid metabolic process aspartate biosynthetic process aspartate catabolic process aspartate metabolic process dicarboxylic acid metabolic process fatty acid transport glutamate catabolic process to 2-oxoglutarate glutamate catabolic process to aspartate glutamate metabolic process oxaloacetate metabolic process response to ethanol | cell surface; mitochondrial inner membrane; mitochondrial matrix; mitochondrion; myelin sheath; perikaryon; plasma membrane; protein-containing complex; sarcolemma; T-tubule | amino acid binding carboxylic acid binding enzyme binding identical protein binding kynurenine-oxoglutarate transaminase activity L-aspartate:2-oxoglutarate aminotransferase activity phospholipid binding pyridoxal phosphate binding | Mus musculus | 3D-structure Acetylation Aminotransferase Cell membrane Direct protein sequencing Lipid transport Membrane Methylation Mitochondrion Nitration Phosphoprotein Pyridoxal phosphate Reference proteome Transferase Transit peptide Transport | MALLHSSRIL | MALLHSSRILSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK | 2-oxoglutarate metabolic process amino acid metabolic process aspartate biosynthetic process aspartate catabolic process aspartate metabolic process dicarboxylic acid metabolic process fatty acid transport glutamate catabolic process to 2-oxoglutarate glutamate catabolic process to aspartate glutamate metabolic process oxaloacetate metabolic process response to ethanol cell surface; mitochondrial inner membrane; mitochondrial matrix; mitochondrion; myelin sheath; perikaryon; plasma membrane; protein-containing complex; sarcolemma; T-tubule amino acid binding carboxylic acid binding enzyme binding identical protein binding kynurenine-oxoglutarate transaminase activity L-aspartate:2-oxoglutarate aminotransferase activity phospholipid binding pyridoxal phosphate binding Mus musculus 3D-structure Acetylation Aminotransferase Cell membrane Direct protein sequencing Lipid transport Membrane Methylation Mitochondrion Nitration Phosphoprotein Pyridoxal phosphate Reference proteome Transferase Transit peptide Transport MALLHSSRIL MALLHSSRILSGMAAAFHPGLAAAASARASSWWTHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLPSVRKAEAQIAAKNLDKEYLPIGGLAEFCKASAELALGENNEVLKSGRFVTVQTISGTGALRVGASFLQRFFKFSRDVFLPKPSWGNHTPIFRDAGMQLQGYRYYDPKTCGFDFSGALEDISKIPEQSVLLLHACAHNPTGVDPRPEQWKEIASVVKKKNLFAFFDMAYQGFASGDGDKDAWAVRHFIEQGINVCLCQSYAKNMGLYGERVGAFTVVCKDAEEAKRVESQLKILIRPLYSNPPLNGARIAATILTSPDLRKQWLQEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIGMFCFTGLKPEQVERLTKEFSVYMTKDGRISVAGVTSGNVGYLAHAIHQVTK |
antimicrobial humoral immune response mediated by antimicrobial peptide chromatin organization killing of cells of another organism | chromatin; cytoplasm; extracellular space; nucleus | chromatin binding nucleosomal DNA binding RNA binding | Homo sapiens | Acetylation ADP-ribosylation Cytoplasm Direct protein sequencing DNA-binding Isopeptide bond Nucleus Phosphoprotein Reference proteome Ubl conjugation | MPKRKAEGDA | MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK | antimicrobial humoral immune response mediated by antimicrobial peptide chromatin organization killing of cells of another organism chromatin; cytoplasm; extracellular space; nucleus chromatin binding nucleosomal DNA binding RNA binding Homo sapiens Acetylation ADP-ribosylation Cytoplasm Direct protein sequencing DNA-binding Isopeptide bond Nucleus Phosphoprotein Reference proteome Ubl conjugation MPKRKAEGDA MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK |
chromatin organization chromosome organization heterochromatin formation mitotic cell cycle negative regulation of DNA-templated transcription negative regulation of gene expression negative regulation of transcription by RNA polymerase II pericentric heterochromatin formation positive regulation of DNA methylation-dependent heterochromatin formation positive regulation of DNA-templated transcription positive regulation of FACT complex assembly positive regulation of transcription by RNA polymerase II protein localization to euchromatin regulation of DNA-templated transcription regulation of protein localization to chromatin telomere maintenance | chromocenter; chromosome; chromosome, centromeric region; chromosome, telomeric region; condensed chromosome; condensed chromosome, centromeric region; euchromatin; heterochromatin; nucleoplasm; nucleus; pericentric heterochromatin; polytene chromosome; polytene chromosome chromocenter; polytene chromosome puff | chromatin binding histone binding Hsp70 protein binding methylated histone binding mRNA binding protein-containing complex binding protein-macromolecule adaptor activity rDNA binding RNA binding RNA polymerase binding RNA polymerase II C-terminal domain binding satellite DNA binding | Drosophila melanogaster | 3D-structure Chromatin regulator Chromosome Nucleus Phosphoprotein Reference proteome Repeat Repressor Transcription Transcription regulation | MGKKIDNPES | MGKKIDNPESSAKVSDAEEEEEEYAVEKIIDRRVRKGKVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASRKDEEKSAASKKDRPSSSAKAKETQGRASSSTSTASKRKSEEPTAPSGNKSKRTTDAEQDTIPVSGSTGFDRGLEAEKILGASDNNGRLTFLIQFKGVDQAEMVPSSVANEKIPRMVIHFYEERLSWYSDNED | chromatin organization chromosome organization heterochromatin formation mitotic cell cycle negative regulation of DNA-templated transcription negative regulation of gene expression negative regulation of transcription by RNA polymerase II pericentric heterochromatin formation positive regulation of DNA methylation-dependent heterochromatin formation positive regulation of DNA-templated transcription positive regulation of FACT complex assembly positive regulation of transcription by RNA polymerase II protein localization to euchromatin regulation of DNA-templated transcription regulation of protein localization to chromatin telomere maintenance chromocenter; chromosome; chromosome, centromeric region; chromosome, telomeric region; condensed chromosome; condensed chromosome, centromeric region; euchromatin; heterochromatin; nucleoplasm; nucleus; pericentric heterochromatin; polytene chromosome; polytene chromosome chromocenter; polytene chromosome puff chromatin binding histone binding Hsp70 protein binding methylated histone binding mRNA binding protein-containing complex binding protein-macromolecule adaptor activity rDNA binding RNA binding RNA polymerase binding RNA polymerase II C-terminal domain binding satellite DNA binding Drosophila melanogaster 3D-structure Chromatin regulator Chromosome Nucleus Phosphoprotein Reference proteome Repeat Repressor Transcription Transcription regulation MGKKIDNPES MGKKIDNPESSAKVSDAEEEEEEYAVEKIIDRRVRKGKVEYYLKWKGYPETENTWEPENNLDCQDLIQQYEASRKDEEKSAASKKDRPSSSAKAKETQGRASSSTSTASKRKSEEPTAPSGNKSKRTTDAEQDTIPVSGSTGFDRGLEAEKILGASDNNGRLTFLIQFKGVDQAEMVPSSVANEKIPRMVIHFYEERLSWYSDNED |
negative regulation of cAMP-dependent protein kinase activity positive regulation of meiotic cell cycle process involved in oocyte maturation regulation of meiotic cell cycle process involved in oocyte maturation | cAMP-dependent protein kinase complex; cytoplasm; cytosol; germinal vesicle; plasma membrane | cAMP binding cAMP-dependent protein kinase inhibitor activity protein kinase A catalytic subunit binding | Sus scrofa | cAMP cAMP-binding Cell membrane Cytoplasm Direct protein sequencing Membrane Nucleotide-binding Phosphoprotein Reference proteome Repeat | SGSQDLEPSS | SGSQDLEPSSGLVTDAIADSESEDDEDLDVPIPSRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERTVKVDEHVIDQRDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMY | negative regulation of cAMP-dependent protein kinase activity positive regulation of meiotic cell cycle process involved in oocyte maturation regulation of meiotic cell cycle process involved in oocyte maturation cAMP-dependent protein kinase complex; cytoplasm; cytosol; germinal vesicle; plasma membrane cAMP binding cAMP-dependent protein kinase inhibitor activity protein kinase A catalytic subunit binding Sus scrofa cAMP cAMP-binding Cell membrane Cytoplasm Direct protein sequencing Membrane Nucleotide-binding Phosphoprotein Reference proteome Repeat SGSQDLEPSS SGSQDLEPSSGLVTDAIADSESEDDEDLDVPIPSRFDRRVSVCAETYNPDEEEEDTDPRVIHPKTDQQRCRLQEACKDILLFKNLDQEQLSQVLDAMFERTVKVDEHVIDQRDDGDNFYVIERGTYDILVTKDNQTRSVGQYDNHGSFGELALMY |
insulin catabolic process proteolysis regulation of insulin secretion regulation of platelet aggregation response to insulin | collagen-containing extracellular matrix; extracellular region; extracellular space; keratohyalin granule | endopeptidase activity serine hydrolase activity serine-type endopeptidase activity | Mus musculus | Disulfide bond Hydrolase Protease Reference proteome Secreted Serine protease Signal Zymogen | MIRTLLLSAL | MIRTLLLSALVAGALSCGYPTYEVEDDVSRVVGGQEATPNTWPWQVSLQVLSSGRWRHNCGGSLVANNWVLTAAHCLSNYQTYRVLLGAHSLSNPGAGSAAVQVSKLVVHQRWNSQNVGNGYDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQTNGNSPDTLRQGRLLVVDYATCSSASWWGSSVKSSMVCAGGDGVTSSCNGDSGGPLNCRASNGQWQVHGIVSFGSSLGCNYPRKPSVFTRVSNYIDWINSVMARN | insulin catabolic process proteolysis regulation of insulin secretion regulation of platelet aggregation response to insulin collagen-containing extracellular matrix; extracellular region; extracellular space; keratohyalin granule endopeptidase activity serine hydrolase activity serine-type endopeptidase activity Mus musculus Disulfide bond Hydrolase Protease Reference proteome Secreted Serine protease Signal Zymogen MIRTLLLSAL MIRTLLLSALVAGALSCGYPTYEVEDDVSRVVGGQEATPNTWPWQVSLQVLSSGRWRHNCGGSLVANNWVLTAAHCLSNYQTYRVLLGAHSLSNPGAGSAAVQVSKLVVHQRWNSQNVGNGYDIALIKLASPVTLSKNIQTACLPPAGTILPRNYVCYVTGWGLLQTNGNSPDTLRQGRLLVVDYATCSSASWWGSSVKSSMVCAGGDGVTSSCNGDSGGPLNCRASNGQWQVHGIVSFGSSLGCNYPRKPSVFTRVSNYIDWINSVMARN |
cellular response to interleukin-4 microtubule cytoskeleton organization mitotic cell cycle | cytoplasm; cytoplasmic microtubule; cytosol; membrane raft; microtubule; microtubule cytoskeleton; myelin sheath | double-stranded RNA binding GTP binding GTPase activity metal ion binding structural constituent of cytoskeleton ubiquitin protein ligase binding | Mus musculus | Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome Ubl conjugation | MRECISIHVG | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY | cellular response to interleukin-4 microtubule cytoskeleton organization mitotic cell cycle cytoplasm; cytoplasmic microtubule; cytosol; membrane raft; microtubule; microtubule cytoskeleton; myelin sheath double-stranded RNA binding GTP binding GTPase activity metal ion binding structural constituent of cytoskeleton ubiquitin protein ligase binding Mus musculus Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome Ubl conjugation MRECISIHVG MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY |
male germ-line stem cell population maintenance microtubule cytoskeleton organization mitotic cell cycle | ciliary basal body; cilium; cytoplasm; microtubule; microtubule cytoskeleton | GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton | Mus musculus | 3D-structure Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome | MRECISIHVG | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY | male germ-line stem cell population maintenance microtubule cytoskeleton organization mitotic cell cycle ciliary basal body; cilium; cytoplasm; microtubule; microtubule cytoskeleton GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton Mus musculus 3D-structure Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome MRECISIHVG MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY |
cytoplasmic microtubule organization intracellular distribution of mitochondria microtubule cytoskeleton organization mitotic cell cycle mitotic spindle elongation mitotic spindle pole body duplication nuclear migration by microtubule mediated pushing forces response to antibiotic | astral microtubule; cytoplasm; cytoplasmic microtubule; cytosol; microtubule; nucleus; spindle microtubule | GTP binding GTPase activity metal ion binding structural constituent of cytoskeleton | Schizosaccharomyces pombe | 3D-structure Antibiotic resistance Cytoplasm Cytoskeleton GTP-binding Magnesium Metal-binding Microtubule Nucleotide-binding Reference proteome | MREIVHIQAG | MREIVHIQAGQCGNQVGAAFWSTIADEHGLDSAGIYHGTSEAQHERLNVYFNEAAGGKYVPRAVLVDLEPGTMDAVKSGKFGNLFRPDNIIYGQSGAGNIWAKGHYTEGAELADAVLDVVRREAEACDALQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRMMATFSVAPAPKSSDTVVEPYNATLSMHQLVENSDETFCIDNEALSSIFANTLKIKSPSYDDLNHLVSAVMAGVTTSFRFPGELNSDLRKLAVNMVPFPRLHFFMVGFAPLAAIGSSSFQAVSVPELTQQMFDANNMMVAADPRHGRYLTVAALFRGKVSMKEVDEQIRSVQTKNSAYFVEWIPDNVLKAVCSVPPKDLKMSATFIGNSTSIQEIFRRLGDQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEAGIDEGDEDYEIEEEKEPLEY | cytoplasmic microtubule organization intracellular distribution of mitochondria microtubule cytoskeleton organization mitotic cell cycle mitotic spindle elongation mitotic spindle pole body duplication nuclear migration by microtubule mediated pushing forces response to antibiotic astral microtubule; cytoplasm; cytoplasmic microtubule; cytosol; microtubule; nucleus; spindle microtubule GTP binding GTPase activity metal ion binding structural constituent of cytoskeleton Schizosaccharomyces pombe 3D-structure Antibiotic resistance Cytoplasm Cytoskeleton GTP-binding Magnesium Metal-binding Microtubule Nucleotide-binding Reference proteome MREIVHIQAG MREIVHIQAGQCGNQVGAAFWSTIADEHGLDSAGIYHGTSEAQHERLNVYFNEAAGGKYVPRAVLVDLEPGTMDAVKSGKFGNLFRPDNIIYGQSGAGNIWAKGHYTEGAELADAVLDVVRREAEACDALQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRMMATFSVAPAPKSSDTVVEPYNATLSMHQLVENSDETFCIDNEALSSIFANTLKIKSPSYDDLNHLVSAVMAGVTTSFRFPGELNSDLRKLAVNMVPFPRLHFFMVGFAPLAAIGSSSFQAVSVPELTQQMFDANNMMVAADPRHGRYLTVAALFRGKVSMKEVDEQIRSVQTKNSAYFVEWIPDNVLKAVCSVPPKDLKMSATFIGNSTSIQEIFRRLGDQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEAGIDEGDEDYEIEEEKEPLEY |
sperm DNA decondensation | nucleoplasm | histone chaperone activity importin-alpha family protein binding nucleosome binding | Xenopus laevis | 3D-structure Acetylation Chaperone Chromatin regulator Developmental protein Fertilization Methylation Nucleus Phosphoprotein Reference proteome | MASTVSNTSK | MASTVSNTSKLEKPVSLIWGCELNEQDKTFEFKVEDDEEKCEHQLALRTVCLGDKAKDEFNIVEIVTQEEGAEKSVPIATLKPSILPMATMVGIELTPPVTFRLKAGSGPLYISGQHVAMEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK | sperm DNA decondensation nucleoplasm histone chaperone activity importin-alpha family protein binding nucleosome binding Xenopus laevis 3D-structure Acetylation Chaperone Chromatin regulator Developmental protein Fertilization Methylation Nucleus Phosphoprotein Reference proteome MASTVSNTSK MASTVSNTSKLEKPVSLIWGCELNEQDKTFEFKVEDDEEKCEHQLALRTVCLGDKAKDEFNIVEIVTQEEGAEKSVPIATLKPSILPMATMVGIELTPPVTFRLKAGSGPLYISGQHVAMEEDYSWAEEEDEGEAEGEEEEEEEEDQESPPKAVKRPAATKKAGQAKKKKLDKEDESSEEDSPTKKGKGAGRGRKPAAKK |
establishment of protein localization to organelle lysosomal lumen acidification | cytolytic granule membrane; endosome membrane; late endosome membrane; lysosomal membrane; membrane; plasma membrane | ion channel inhibitor activity | Gallus gallus | Cell membrane Disulfide bond Endosome Glycoprotein Lysosome Membrane Reference proteome Signal Transmembrane Transmembrane helix | MGGAARAVLL | MGGAARAVLLGFLQASSSFDVRDSTGKVCIIANLTVAFSVEYKSSGQKQFAHFFLPQNATSQSHSSCGEGNTSHPILALSFGAGHLISLNFSKTLDKYQVEELTFHYNLSDETLFPNATEGKVMVATQKSVIQARIGTEYRCINSKYVRMKHVNITFSNVTLEAYPTNDTFSANKTECREDMVSTTTVAPTTPKHATSQVPTTSPAPTAAPSSPAVGKYNVTGANGTCVLASMGLQLNITYVKKDEKMGLDLLNFIPHNTSASGMCESTSAFLNLAFEKTKITFHFVLNASSEKFFLQGVNVSTTLPSEAKAPTFEASNDSMSESRATVGNSYKCSAEENFQVTDKALVNVFNVQVQAFKVDGDKFGAMEECQLDENNMLIPIIVGAALAGLVLIVLIAYLIGRKRSHAGYQTI | establishment of protein localization to organelle lysosomal lumen acidification cytolytic granule membrane; endosome membrane; late endosome membrane; lysosomal membrane; membrane; plasma membrane ion channel inhibitor activity Gallus gallus Cell membrane Disulfide bond Endosome Glycoprotein Lysosome Membrane Reference proteome Signal Transmembrane Transmembrane helix MGGAARAVLL MGGAARAVLLGFLQASSSFDVRDSTGKVCIIANLTVAFSVEYKSSGQKQFAHFFLPQNATSQSHSSCGEGNTSHPILALSFGAGHLISLNFSKTLDKYQVEELTFHYNLSDETLFPNATEGKVMVATQKSVIQARIGTEYRCINSKYVRMKHVNITFSNVTLEAYPTNDTFSANKTECREDMVSTTTVAPTTPKHATSQVPTTSPAPTAAPSSPAVGKYNVTGANGTCVLASMGLQLNITYVKKDEKMGLDLLNFIPHNTSASGMCESTSAFLNLAFEKTKITFHFVLNASSEKFFLQGVNVSTTLPSEAKAPTFEASNDSMSESRATVGNSYKCSAEENFQVTDKALVNVFNVQVQAFKVDGDKFGAMEECQLDENNMLIPIIVGAALAGLVLIVLIAYLIGRKRSHAGYQTI |
peptidyl-proline hydroxylation to 4-hydroxy-L-proline protein folding response to endoplasmic reticulum stress | endoplasmic reticulum; endoplasmic reticulum lumen; external side of plasma membrane; melanosome | procollagen-proline 4-dioxygenase activity protein disulfide isomerase activity protein heterodimerization activity | Bos taurus | Acetylation Cell membrane Chaperone Direct protein sequencing Disulfide bond Endoplasmic reticulum Isomerase Membrane Phosphoprotein Redox-active center Reference proteome Repeat Signal | MLRRALLCLA | MLRRALLCLALTALFRAGAGAPDEEDHVLVLHKGNFDEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAASTLSDGAAAEALVESSEVAVIGFFKDMESDSAKQFFLAAEVIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYEGKLSNFKKAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITEFCHRFLEGKIKPHLMSQELPDDWDKQPVKVLVGKNFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDLEEDDDQKAVKDEL | peptidyl-proline hydroxylation to 4-hydroxy-L-proline protein folding response to endoplasmic reticulum stress endoplasmic reticulum; endoplasmic reticulum lumen; external side of plasma membrane; melanosome procollagen-proline 4-dioxygenase activity protein disulfide isomerase activity protein heterodimerization activity Bos taurus Acetylation Cell membrane Chaperone Direct protein sequencing Disulfide bond Endoplasmic reticulum Isomerase Membrane Phosphoprotein Redox-active center Reference proteome Repeat Signal MLRRALLCLA MLRRALLCLALTALFRAGAGAPDEEDHVLVLHKGNFDEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFKNGDTASPKEYTAGREADDIVNWLKKRTGPAASTLSDGAAAEALVESSEVAVIGFFKDMESDSAKQFFLAAEVIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKEKLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYEGKLSNFKKAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESDELTAEKITEFCHRFLEGKIKPHLMSQELPDDWDKQPVKVLVGKNFEEVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDLEEDDDQKAVKDEL |
cytoplasmic translation ribosomal large subunit assembly | 90S preribosome; cytoplasm; cytosolic large ribosomal subunit | large ribosomal subunit rRNA binding structural constituent of ribosome | Saccharomyces cerevisiae | 3D-structure Cytoplasm Isopeptide bond Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation | MGGIREKKAE | MGGIREKKAEYFAKLREYLEEYKSLFVVGVDNVSSQQMHEVRKELRGRAVVLMGKNTMVRRAIRGFLSDLPDFEKLLPFVKGNVGFVFTNEPLTEIKNVIVSNRVAAPARAGAVAPEDIWVRAVNTGMEPGKTSFFQALGVPTKIARGTIEIVSDVKVVDAGNKVGQSEASLLNLLNISPFTFGLTVVQVYDNGQVFPSSILDITDEELVSHFVSAVSTIASISLAIGYPTLPSVGHTLINNYKDLLAVAIAASYHYPEIEDLVDRIENPEKYAAAAPAATSAASGDAAPAEEAAAEEEEESDDDMGFGLFD | cytoplasmic translation ribosomal large subunit assembly 90S preribosome; cytoplasm; cytosolic large ribosomal subunit large ribosomal subunit rRNA binding structural constituent of ribosome Saccharomyces cerevisiae 3D-structure Cytoplasm Isopeptide bond Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation MGGIREKKAE MGGIREKKAEYFAKLREYLEEYKSLFVVGVDNVSSQQMHEVRKELRGRAVVLMGKNTMVRRAIRGFLSDLPDFEKLLPFVKGNVGFVFTNEPLTEIKNVIVSNRVAAPARAGAVAPEDIWVRAVNTGMEPGKTSFFQALGVPTKIARGTIEIVSDVKVVDAGNKVGQSEASLLNLLNISPFTFGLTVVQVYDNGQVFPSSILDITDEELVSHFVSAVSTIASISLAIGYPTLPSVGHTLINNYKDLLAVAIAASYHYPEIEDLVDRIENPEKYAAAAPAATSAASGDAAPAEEAAAEEEEESDDDMGFGLFD |
cytoplasmic translation translational elongation | cytosolic large ribosomal subunit | protein kinase activator activity ribonucleoprotein complex binding structural constituent of ribosome | Saccharomyces cerevisiae | 3D-structure Acetylation Cytoplasm Direct protein sequencing Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein | MSTESALSYA | MSTESALSYAALILADSEIEISSEKLLTLTNAANVPVENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD | cytoplasmic translation translational elongation cytosolic large ribosomal subunit protein kinase activator activity ribonucleoprotein complex binding structural constituent of ribosome Saccharomyces cerevisiae 3D-structure Acetylation Cytoplasm Direct protein sequencing Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein MSTESALSYA MSTESALSYAALILADSEIEISSEKLLTLTNAANVPVENIWADIFAKALDGQNLKDLLVNFSAGAAAPAGVAGGVAGGEAGEAEAEKEEEEAKEESDDDMGFGLFD |
cytoplasmic translation cytoplasmic translational elongation | cytosolic large ribosomal subunit | protein kinase activator activity structural constituent of ribosome | Saccharomyces cerevisiae | 3D-structure Cytoplasm Direct protein sequencing Isopeptide bond Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation | MKYLAAYLLL | MKYLAAYLLLNAAGNTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASAGGAAAASGDAAAEEEKEEEAAEESDDDMGFGLFD | cytoplasmic translation cytoplasmic translational elongation cytosolic large ribosomal subunit protein kinase activator activity structural constituent of ribosome Saccharomyces cerevisiae 3D-structure Cytoplasm Direct protein sequencing Isopeptide bond Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation MKYLAAYLLL MKYLAAYLLLNAAGNTPDATKIKAILESVGIEIEDEKVSSVLSALEGKSVDELITEGNEKLAAVPAAGPASAGGAAAASGDAAAEEEKEEEAAEESDDDMGFGLFD |
penicillin biosynthetic process | cytosol | iron ion binding isopenicillin-N synthase activity L-ascorbic acid binding | Emericella nidulans | 3D-structure Antibiotic biosynthesis Cytoplasm Iron Metal-binding Oxidoreductase Reference proteome Vitamin C | MGSVSKANVP | MGSVSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQRLSQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVESFCYLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGLSSALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKTAADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLINCGSYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREPNGKSDREPLSYGDYLQNGLVSLINKNGQT | penicillin biosynthetic process cytosol iron ion binding isopenicillin-N synthase activity L-ascorbic acid binding Emericella nidulans 3D-structure Antibiotic biosynthesis Cytoplasm Iron Metal-binding Oxidoreductase Reference proteome Vitamin C MGSVSKANVP MGSVSKANVPKIDVSPLFGDDQAAKMRVAQQIDAASRDTGFFYAVNHGINVQRLSQKTKEFHMSITPEEKWDLAIRAYNKEHQDQVRAGYYLSIPGKKAVESFCYLNPNFTPDHPRIQAKTPTHEVNVWPDETKHPGFQDFAEQYYWDVFGLSSALLKGYALALGKEENFFARHFKPDDTLASVVLIRYPYLDPYPEAAIKTAADGTKLSFEWHEDVSLITVLYQSNVQNLQVETAAGYQDIEADDTGYLINCGSYMAHLTNNYYKAPIHRVKWVNAERQSLPFFVNLGYDSVIDPFDPREPNGKSDREPLSYGDYLQNGLVSLINKNGQT |
adhesion of symbiont to host cell adhesion cell adhesion mediated by integrin cellular response to amyloid-beta cellular response to glucose stimulus cellular response to leukemia inhibitory factor establishment of endothelial barrier heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules leukocyte cell-cell adhesion leukocyte migration membrane to membrane docking negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors positive regulation of cellular extravasation positive regulation of ERK1 and ERK2 cascade receptor-mediated virion attachment to host cell regulation of leukocyte mediated cytotoxicity regulation of ruffle assembly T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell T cell antigen processing and presentation T cell extravasation | cell surface; collagen-containing extracellular matrix; external side of plasma membrane; extracellular exosome; extracellular space; focal adhesion; immunological synapse; membrane; membrane raft; plasma membrane | integrin binding signaling receptor activity transmembrane signaling receptor activity virus receptor activity | Homo sapiens | 3D-structure Cell adhesion Direct protein sequencing Disulfide bond Glycoprotein Host cell receptor for virus entry Host-virus interaction Immunoglobulin domain Membrane Phosphoprotein Receptor Reference proteome Repeat Signal Transmembrane Transmembrane helix Ubl conjugation | MAPSSPRPAL | MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP | adhesion of symbiont to host cell adhesion cell adhesion mediated by integrin cellular response to amyloid-beta cellular response to glucose stimulus cellular response to leukemia inhibitory factor establishment of endothelial barrier heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules leukocyte cell-cell adhesion leukocyte migration membrane to membrane docking negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors positive regulation of cellular extravasation positive regulation of ERK1 and ERK2 cascade receptor-mediated virion attachment to host cell regulation of leukocyte mediated cytotoxicity regulation of ruffle assembly T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell T cell antigen processing and presentation T cell extravasation cell surface; collagen-containing extracellular matrix; external side of plasma membrane; extracellular exosome; extracellular space; focal adhesion; immunological synapse; membrane; membrane raft; plasma membrane integrin binding signaling receptor activity transmembrane signaling receptor activity virus receptor activity Homo sapiens 3D-structure Cell adhesion Direct protein sequencing Disulfide bond Glycoprotein Host cell receptor for virus entry Host-virus interaction Immunoglobulin domain Membrane Phosphoprotein Receptor Reference proteome Repeat Signal Transmembrane Transmembrane helix Ubl conjugation MAPSSPRPAL MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEVTVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELRVLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYLCRARSTQGEVTRKVTVNVLSPRYEIVIITVVAAAVIMGTAGLSTYLYNRQRKIKKYRLQQAQKGTPMKPNTQATPP |
antibiotic catabolic process response to antibiotic | outer membrane-bounded periplasmic space | beta-lactamase activity | Enterobacter cloacae | 3D-structure Antibiotic resistance Hydrolase Periplasm Signal | MMRKSLCCAL | MMRKSLCCALLLGISCSALATPVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAANKPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQWQGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYANASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWGYRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQGIALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVAEVNPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPARVEAAYHILEALQ | antibiotic catabolic process response to antibiotic outer membrane-bounded periplasmic space beta-lactamase activity Enterobacter cloacae3D-structure Antibiotic resistance Hydrolase Periplasm Signal MMRKSLCCAL MMRKSLCCALLLGISCSALATPVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAANKPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQWQGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYANASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWGYRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQGIALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVAEVNPPAPPVKASWVHKTGSTGGFGSYVAFIPEKQIGIVMLANTSYPNPARVEAAYHILEALQ |
cellular response to fatty acid cholesterol biosynthetic process farnesyl diphosphate biosynthetic process geranyl diphosphate biosynthetic process male gonad development positive regulation of cell growth involved in cardiac muscle cell development positive regulation of cholesterol biosynthetic process response to cholesterol response to peptide hormone response to testosterone response to xenobiotic stimulus spermatogenesis | cytoplasm; mitochondrial matrix; peroxisome | dimethylallyltranstransferase activity geranyltranstransferase activity metal ion binding | Rattus norvegicus | Acetylation Cholesterol biosynthesis Cholesterol metabolism Cytoplasm Hydroxylation Isoprene biosynthesis Lipid biosynthesis Lipid metabolism Magnesium Metal-binding Reference proteome Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism Transferase | MNGDQKLDVH | MNGDQKLDVHNQEKQNFIQHFSQIVKVLTEDELGHPEKGDAITRIKEVLEYNTVGGKYNRGLTVVQTFQELVEPRKQDAESLQRALTVGWCVELLQAFFLVLDDIMDSSYTRRGQICWYQKPGIGLDAINDALLLEAAIYRLLKFYCREQPYYLNLLELFLQSSYQTEIGQTLDLITAPQGQVDLGRYTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANALKILLEMGEFFQIQDDYLDLFGDPSVTGKVGTDIQDNKCSWLVVQCLLRATPQQRQILEENYGQKDPEKVARVKALYEELDLRSVFFKYEEDSYNRLKSLIEQCSAPLPPSIFLELANKIYKRRK | cellular response to fatty acid cholesterol biosynthetic process farnesyl diphosphate biosynthetic process geranyl diphosphate biosynthetic process male gonad development positive regulation of cell growth involved in cardiac muscle cell development positive regulation of cholesterol biosynthetic process response to cholesterol response to peptide hormone response to testosterone response to xenobiotic stimulus spermatogenesis cytoplasm; mitochondrial matrix; peroxisome dimethylallyltranstransferase activity geranyltranstransferase activity metal ion binding Rattus norvegicus Acetylation Cholesterol biosynthesis Cholesterol metabolism Cytoplasm Hydroxylation Isoprene biosynthesis Lipid biosynthesis Lipid metabolism Magnesium Metal-binding Reference proteome Steroid biosynthesis Steroid metabolism Sterol biosynthesis Sterol metabolism Transferase MNGDQKLDVH MNGDQKLDVHNQEKQNFIQHFSQIVKVLTEDELGHPEKGDAITRIKEVLEYNTVGGKYNRGLTVVQTFQELVEPRKQDAESLQRALTVGWCVELLQAFFLVLDDIMDSSYTRRGQICWYQKPGIGLDAINDALLLEAAIYRLLKFYCREQPYYLNLLELFLQSSYQTEIGQTLDLITAPQGQVDLGRYTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANALKILLEMGEFFQIQDDYLDLFGDPSVTGKVGTDIQDNKCSWLVVQCLLRATPQQRQILEENYGQKDPEKVARVKALYEELDLRSVFFKYEEDSYNRLKSLIEQCSAPLPPSIFLELANKIYKRRK |
heme biosynthetic process protoporphyrinogen IX biosynthetic process | cytoplasm; cytosol; nucleus | porphobilinogen synthase activity zinc ion binding | Saccharomyces cerevisiae | 3D-structure Heme biosynthesis Lyase Metal-binding Phosphoprotein Porphyrin biosynthesis Reference proteome Zinc | MHTAEFLETE | MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDNPDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDPVGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDGTINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAHKTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALERDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAAEKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDEEN | heme biosynthetic process protoporphyrinogen IX biosynthetic process cytoplasm; cytosol; nucleus porphobilinogen synthase activity zinc ion binding Saccharomyces cerevisiae 3D-structure Heme biosynthesis Lyase Metal-binding Phosphoprotein Porphyrin biosynthesis Reference proteome Zinc MHTAEFLETE MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDNPDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDPVGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDGTINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAHKTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALERDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAAEKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDEEN |
methylation phosphatidylcholine biosynthetic process | cell periphery; endoplasmic reticulum; endoplasmic reticulum membrane | phosphatidylethanolamine N-methyltransferase activity | Saccharomyces cerevisiae | Acetylation Endoplasmic reticulum Lipid biosynthesis Lipid metabolism Membrane Methyltransferase Phospholipid biosynthesis Phospholipid metabolism Reference proteome S-adenosyl-L-methionine Transferase Transmembrane Transmembrane helix | MSSCKTTLSE | MSSCKTTLSEMVGSVTKDRGTINVEARTRSSNVTFKPPVTHDMVRSLFDPTLKKSLLEKCIALAIISNFFICYWVFQRFGLQFTKYFFLVQYLFWRIAYNLGIGLVLHYQSHYETLTNCAKTHAIFSKIPQNKDANSNFSTNSNSFSEKFWNFIRKFCQYEIRSKMPKEYDLFAYPEEINVWLIFRQFVDLILMQDFVTYIIYVYLSIPYSWVQIFNWRSLLGVILILFNIWVKLDAHRVVKDYAWYWGDFFFLEESELIFDGVFNISPHPMYSIGYLGYYGLSLICNDYKVLLVSVFGHYSQFLFLKYVENPHIERTYGDGTDSDSQMNSRIDDLISKENYDYSRPLINMGLSFNNFNKLRFTDYFTIGTVAALMLGTIMNARFINLNYLFITVFVTKLVSWLFISTILYKQSQSKWFTRLFLENGYTQVYSYEQWQFIYNYYLVLTYTLMIIHTGLQIWSNFSNINNSQLIFGLILVALQTWCDKETRLAISDFGWFYGDFFLSNYISTRKLTSQGIYRYLNHPEAVLGVVGVWGTVLMTNFAVTNIILAVLWTLTNFILVKFIETPHVNKIYGKTKRVSGVGKTLLGLKPLRQVSDIVNRIENIIIKSLVDESKNSNGGAELLPKNYQDNKEWNILIQEAMDSVATRLSPYCELKIENEQVETNFVLPTPVTLNWKMPIELYNGDDWIGLYKVIDTRADREKTRVGSGGHWSATSKDSYMNHGLRHKESVTEIKATEKYVQGKVTFDTSLLYFENGIYEFRYHSGNSHKVLLISTPFEISLPVLNTTTPELFEKDLTEFLTKVNVLKDGKFRPLGNKFFGMDSLKQLIKNSIGVELSSEYMRRVNGDAHVISHRAWDIKQTLDSLA | methylation phosphatidylcholine biosynthetic process cell periphery; endoplasmic reticulum; endoplasmic reticulum membrane phosphatidylethanolamine N-methyltransferase activity Saccharomyces cerevisiae Acetylation Endoplasmic reticulum Lipid biosynthesis Lipid metabolism Membrane Methyltransferase Phospholipid biosynthesis Phospholipid metabolism Reference proteome S-adenosyl-L-methionine Transferase Transmembrane Transmembrane helix MSSCKTTLSE MSSCKTTLSEMVGSVTKDRGTINVEARTRSSNVTFKPPVTHDMVRSLFDPTLKKSLLEKCIALAIISNFFICYWVFQRFGLQFTKYFFLVQYLFWRIAYNLGIGLVLHYQSHYETLTNCAKTHAIFSKIPQNKDANSNFSTNSNSFSEKFWNFIRKFCQYEIRSKMPKEYDLFAYPEEINVWLIFRQFVDLILMQDFVTYIIYVYLSIPYSWVQIFNWRSLLGVILILFNIWVKLDAHRVVKDYAWYWGDFFFLEESELIFDGVFNISPHPMYSIGYLGYYGLSLICNDYKVLLVSVFGHYSQFLFLKYVENPHIERTYGDGTDSDSQMNSRIDDLISKENYDYSRPLINMGLSFNNFNKLRFTDYFTIGTVAALMLGTIMNARFINLNYLFITVFVTKLVSWLFISTILYKQSQSKWFTRLFLENGYTQVYSYEQWQFIYNYYLVLTYTLMIIHTGLQIWSNFSNINNSQLIFGLILVALQTWCDKETRLAISDFGWFYGDFFLSNYISTRKLTSQGIYRYLNHPEAVLGVVGVWGTVLMTNFAVTNIILAVLWTLTNFILVKFIETPHVNKIYGKTKRVSGVGKTLLGLKPLRQVSDIVNRIENIIIKSLVDESKNSNGGAELLPKNYQDNKEWNILIQEAMDSVATRLSPYCELKIENEQVETNFVLPTPVTLNWKMPIELYNGDDWIGLYKVIDTRADREKTRVGSGGHWSATSKDSYMNHGLRHKESVTEIKATEKYVQGKVTFDTSLLYFENGIYEFRYHSGNSHKVLLISTPFEISLPVLNTTTPELFEKDLTEFLTKVNVLKDGKFRPLGNKFFGMDSLKQLIKNSIGVELSSEYMRRVNGDAHVISHRAWDIKQTLDSLA |
methylation phosphatidylcholine biosynthetic process | cell periphery; endoplasmic reticulum; endoplasmic reticulum membrane; mitochondrial membrane; mitochondrion | phosphatidyl-N-dimethylethanolamine N-methyltransferase activity phosphatidyl-N-methylethanolamine N-methyltransferase activity phosphatidylethanolamine N-methyltransferase activity | Saccharomyces cerevisiae | Endoplasmic reticulum Lipid biosynthesis Lipid metabolism Membrane Methyltransferase Mitochondrion Phospholipid biosynthesis Phospholipid metabolism Reference proteome S-adenosyl-L-methionine Transferase Transmembrane Transmembrane helix | MKESVQEIIQ | MKESVQEIIQQLIHSVDLQSSKFQLAIVCTMFNPIFWNIVARMEYHKHSLTKMCGGARKGCYMLAATIFSLGIVRDMVYESALREQPTCSLITGENWTKLGVALFGLGQVLVLSSMYKLGITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYFMYKIALRWEEPFTAMIYANRDKAKKNM | methylation phosphatidylcholine biosynthetic process cell periphery; endoplasmic reticulum; endoplasmic reticulum membrane; mitochondrial membrane; mitochondrion phosphatidyl-N-dimethylethanolamine N-methyltransferase activity phosphatidyl-N-methylethanolamine N-methyltransferase activity phosphatidylethanolamine N-methyltransferase activity Saccharomyces cerevisiae Endoplasmic reticulum Lipid biosynthesis Lipid metabolism Membrane Methyltransferase Mitochondrion Phospholipid biosynthesis Phospholipid metabolism Reference proteome S-adenosyl-L-methionine Transferase Transmembrane Transmembrane helix MKESVQEIIQ MKESVQEIIQQLIHSVDLQSSKFQLAIVCTMFNPIFWNIVARMEYHKHSLTKMCGGARKGCYMLAATIFSLGIVRDMVYESALREQPTCSLITGENWTKLGVALFGLGQVLVLSSMYKLGITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYFMYKIALRWEEPFTAMIYANRDKAKKNM |
negative regulation of TORC1 signaling protein kinase A signaling protein phosphorylation | cAMP-dependent protein kinase complex; cytosol; nucleus; plasma membrane | AMP-activated protein kinase activity ATP binding cAMP-dependent protein kinase activity magnesium ion binding protein serine kinase activity | Sus scrofa | ATP-binding cAMP Cell membrane Cytoplasm Direct protein sequencing Kinase Lipoprotein Membrane Myristate Nucleotide-binding Nucleus Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase | MGNAATAKKG | MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPAPNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCGKEFCEF | negative regulation of TORC1 signaling protein kinase A signaling protein phosphorylation cAMP-dependent protein kinase complex; cytosol; nucleus; plasma membrane AMP-activated protein kinase activity ATP binding cAMP-dependent protein kinase activity magnesium ion binding protein serine kinase activity Sus scrofa ATP-binding cAMP Cell membrane Cytoplasm Direct protein sequencing Kinase Lipoprotein Membrane Myristate Nucleotide-binding Nucleus Phosphoprotein Reference proteome Serine/threonine-protein kinase Transferase MGNAATAKKG MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPAPNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEDIRVSITEKCGKEFCEF |
cytoplasmic translation translation translational elongation | cytoplasm; cytosol; cytosolic large ribosomal subunit; cytosolic ribosome; focal adhesion | protein kinase activator activity ribonucleoprotein complex binding structural constituent of ribosome | Homo sapiens | 3D-structure Acetylation Alternative splicing Isopeptide bond Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation | MASVSELACI | MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD | cytoplasmic translation translation translational elongation cytoplasm; cytosol; cytosolic large ribosomal subunit; cytosolic ribosome; focal adhesion protein kinase activator activity ribonucleoprotein complex binding structural constituent of ribosome Homo sapiens 3D-structure Acetylation Alternative splicing Isopeptide bond Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation MASVSELACI MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD |
cytoplasmic translation cytoplasmic translational elongation translation | cytoplasm; cytosol; cytosolic large ribosomal subunit; extracellular exosome; focal adhesion; membrane | structural constituent of ribosome | Homo sapiens | 3D-structure Acetylation Direct protein sequencing Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein | MRYVASYLLA | MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD | cytoplasmic translation cytoplasmic translational elongation translation cytoplasm; cytosol; cytosolic large ribosomal subunit; extracellular exosome; focal adhesion; membrane structural constituent of ribosome Homo sapiens 3D-structure Acetylation Direct protein sequencing Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein MRYVASYLLA MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD |
cytoplasmic translation ribosome biogenesis translation | cytoplasm; cytoplasmic ribonucleoprotein granule; cytosol; cytosolic large ribosomal subunit; cytosolic ribosome; endoplasmic reticulum; extracellular exosome; focal adhesion; membrane; nucleus; postsynapse; postsynaptic density; ribonucleoprotein complex | large ribosomal subunit rRNA binding RNA binding structural constituent of ribosome | Homo sapiens | 3D-structure Alternative splicing Cytoplasm Direct protein sequencing Isopeptide bond Nucleus Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation | MPREDRATWK | MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADPSAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD | cytoplasmic translation ribosome biogenesis translation cytoplasm; cytoplasmic ribonucleoprotein granule; cytosol; cytosolic large ribosomal subunit; cytosolic ribosome; endoplasmic reticulum; extracellular exosome; focal adhesion; membrane; nucleus; postsynapse; postsynaptic density; ribonucleoprotein complex large ribosomal subunit rRNA binding RNA binding structural constituent of ribosome Homo sapiens 3D-structure Alternative splicing Cytoplasm Direct protein sequencing Isopeptide bond Nucleus Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein Ubl conjugation MPREDRATWK MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADPSAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD |
intracellular protein transport neuropeptide signaling pathway peptide hormone processing regulation of hormone secretion | extracellular region; nucleus; secretory granule | enzyme inhibitor activity enzyme regulator activity GTP binding unfolded protein binding | Homo sapiens | Alternative splicing Chaperone Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Neuropeptide Phosphoprotein Reference proteome Secreted Signal Sulfation Transport | MVSRMVSTML | MVSRMVSTMLSGLLFWLASGWTPAFAYSPRTPDRVSEADIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPVGKTADDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGERRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE | intracellular protein transport neuropeptide signaling pathway peptide hormone processing regulation of hormone secretion extracellular region; nucleus; secretory granule enzyme inhibitor activity enzyme regulator activity GTP binding unfolded protein binding Homo sapiens Alternative splicing Chaperone Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Neuropeptide Phosphoprotein Reference proteome Secreted Signal Sulfation Transport MVSRMVSTML MVSRMVSTMLSGLLFWLASGWTPAFAYSPRTPDRVSEADIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPVGKTADDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGERRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE |
cellular response to cadmium ion cellular response to reactive oxygen species integrated stress response signaling negative regulation by host of viral transcription negative regulation of DNA binding negative regulation of DNA-templated transcription negative regulation of transcription by RNA polymerase II positive regulation by host of viral transcription positive regulation of apoptotic process positive regulation of DNA-templated transcription positive regulation of DNA-templated transcription initiation positive regulation of miRNA transcription positive regulation of transcription by RNA polymerase II positive regulation of vascular associated smooth muscle cell proliferation regulation of cell cycle regulation of cell population proliferation regulation of transcription by RNA polymerase II release from viral latency response to endoplasmic reticulum stress SMAD protein signal transduction transforming growth factor beta receptor signaling pathway | chromatin; euchromatin; nuclear chromosome; nucleoplasm; nucleus; RNA polymerase II transcription regulator complex; transcription factor AP-1 complex; transcription regulator complex | cAMP response element binding DNA binding DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific DNA-binding transcription repressor activity, RNA polymerase II-specific enzyme binding general transcription initiation factor binding GTPase activator activity identical protein binding R-SMAD binding RNA binding RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II-specific DNA-binding transcription factor binding sequence-specific double-stranded DNA binding transcription cis-regulatory region binding ubiquitin protein ligase binding ubiquitin-like protein ligase binding | Homo sapiens | 3D-structure Acetylation Activator Direct protein sequencing DNA-binding Isopeptide bond Nucleus Phosphoprotein Proto-oncogene Reference proteome Transcription Transcription regulation Ubl conjugation | MTAKMETTFY | MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF | cellular response to cadmium ion cellular response to reactive oxygen species integrated stress response signaling negative regulation by host of viral transcription negative regulation of DNA binding negative regulation of DNA-templated transcription negative regulation of transcription by RNA polymerase II positive regulation by host of viral transcription positive regulation of apoptotic process positive regulation of DNA-templated transcription positive regulation of DNA-templated transcription initiation positive regulation of miRNA transcription positive regulation of transcription by RNA polymerase II positive regulation of vascular associated smooth muscle cell proliferation regulation of cell cycle regulation of cell population proliferation regulation of transcription by RNA polymerase II release from viral latency response to endoplasmic reticulum stress SMAD protein signal transduction transforming growth factor beta receptor signaling pathway chromatin; euchromatin; nuclear chromosome; nucleoplasm; nucleus; RNA polymerase II transcription regulator complex; transcription factor AP-1 complex; transcription regulator complex cAMP response element binding DNA binding DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific DNA-binding transcription repressor activity, RNA polymerase II-specific enzyme binding general transcription initiation factor binding GTPase activator activity identical protein binding R-SMAD binding RNA binding RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II-specific DNA-binding transcription factor binding sequence-specific double-stranded DNA binding transcription cis-regulatory region binding ubiquitin protein ligase binding ubiquitin-like protein ligase binding Homo sapiens 3D-structure Acetylation Activator Direct protein sequencing DNA-binding Isopeptide bond Nucleus Phosphoprotein Proto-oncogene Reference proteome Transcription Transcription regulation Ubl conjugation MTAKMETTFY MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF |
brown fat cell differentiation cholesterol homeostasis intracellular lipid transport long-chain fatty acid transport negative regulation of cell population proliferation phospholipid homeostasis positive regulation of long-chain fatty acid import into cell positive regulation of phospholipid biosynthetic process regulation of fatty acid oxidation regulation of phosphatidylcholine biosynthetic process | cytosol; extracellular exosome; extracellular space; nucleus | cytoskeletal protein binding long-chain fatty acid binding oleic acid binding | Homo sapiens | 3D-structure Acetylation Cytoplasm Direct protein sequencing Lipid-binding Phosphoprotein Reference proteome Transport | MVDAFLGTWK | MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA | brown fat cell differentiation cholesterol homeostasis intracellular lipid transport long-chain fatty acid transport negative regulation of cell population proliferation phospholipid homeostasis positive regulation of long-chain fatty acid import into cell positive regulation of phospholipid biosynthetic process regulation of fatty acid oxidation regulation of phosphatidylcholine biosynthetic process cytosol; extracellular exosome; extracellular space; nucleus cytoskeletal protein binding long-chain fatty acid binding oleic acid binding Homo sapiens 3D-structure Acetylation Cytoplasm Direct protein sequencing Lipid-binding Phosphoprotein Reference proteome Transport MVDAFLGTWK MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA |
oxidative photosynthetic carbon pathway response to other organism | peroxisome | (S)-2-hydroxy-acid oxidase activity FMN binding | Spinacia oleracea | 3D-structure Acetylation Direct protein sequencing Flavoprotein FMN Glycolate pathway Oxidoreductase Peroxisome Photorespiration Reference proteome | MEITNVNEYE | MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKMDKANDSGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAADWDGPSSRAVARL | oxidative photosynthetic carbon pathway response to other organism peroxisome (S)-2-hydroxy-acid oxidase activity FMN binding Spinacia oleracea 3D-structure Acetylation Direct protein sequencing Flavoprotein FMN Glycolate pathway Oxidoreductase Peroxisome Photorespiration Reference proteome MEITNVNEYE MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKMDKANDSGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGEAGVKKVLQMMRDEFELTMALSGCRSLKEISRSHIAADWDGPSSRAVARL |
defense response to virus innate immune response positive regulation of innate immune response positive regulation of interferon-beta production tRNA transcription by RNA polymerase III | cytosol; nucleoplasm; RNA polymerase III complex | chromatin binding DNA binding | Homo sapiens | 3D-structure Acetylation Antiviral defense DNA-directed RNA polymerase Immunity Innate immunity Isopeptide bond Methylation Nucleus Phosphoprotein Reference proteome Transcription Ubl conjugation | MSEGNAAGEP | MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTPNIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKKGNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQLPLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAARKTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVLIKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQELVSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR | defense response to virus innate immune response positive regulation of innate immune response positive regulation of interferon-beta production tRNA transcription by RNA polymerase III cytosol; nucleoplasm; RNA polymerase III complex chromatin binding DNA binding Homo sapiens 3D-structure Acetylation Antiviral defense DNA-directed RNA polymerase Immunity Innate immunity Isopeptide bond Methylation Nucleus Phosphoprotein Reference proteome Transcription Ubl conjugation MSEGNAAGEP MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTPNIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKKGNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQLPLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAARKTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVLIKQEKDREAKLAENACTLADLTEGQVGKLLIRKSGRVQLLLGKVTLDVTMGTACSFLQELVSVGLGDSRTGEMTVLGHVKHKLVCSPDFESLLDHKHR |
liver regeneration maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) ribosomal large subunit biogenesis rRNA processing | A band; cytoplasm; cytosolic large ribosomal subunit; cytosolic ribosome; postsynaptic density; ribonucleoprotein complex; ribosome; synapse | 5S rRNA binding DNA binding identical protein binding mRNA binding RNA binding structural constituent of ribosome | Rattus norvegicus | 3D-structure Acetylation Cytoplasm Direct protein sequencing Phosphoprotein Reference proteome Repeat Ribonucleoprotein Ribosomal protein RNA-binding | MEAVPEKKKK | MEAVPEKKKKVAAALGTLKKKKVPAVPETLKKKRRNFAELKVKRLRKKFALKTLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASVNMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNSLVARSLGKFGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN | liver regeneration maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) ribosomal large subunit biogenesis rRNA processing A band; cytoplasm; cytosolic large ribosomal subunit; cytosolic ribosome; postsynaptic density; ribonucleoprotein complex; ribosome; synapse 5S rRNA binding DNA binding identical protein binding mRNA binding RNA binding structural constituent of ribosome Rattus norvegicus 3D-structure Acetylation Cytoplasm Direct protein sequencing Phosphoprotein Reference proteome Repeat Ribonucleoprotein Ribosomal protein RNA-binding MEAVPEKKKK MEAVPEKKKKVAAALGTLKKKKVPAVPETLKKKRRNFAELKVKRLRKKFALKTLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASVNMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNSLVARSLGKFGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN |
antimicrobial humoral immune response mediated by antimicrobial peptide disruption of cell wall in another organism positive regulation of cell population proliferation response to peptide hormone | extracellular exosome; extracellular space | growth factor activity molecular function inhibitor activity oligosaccharide binding peptidoglycan binding signaling receptor activity | Homo sapiens | 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Lectin Pyrrolidone carboxylic acid Reference proteome Secreted Signal | MAQTSSYFML | MAQTSSYFMLISCLMFLSQSQGQEAQTELPQARISCPEGTNAYRSYCYYFNEDRETWVDADLYCQNMNSGNLVSVLTQAEGAFVASLIKESGTDDFNVWIGLHDPKKNRRWHWSSGSLVSYKSWGIGAPSSVNPGYCVSLTSSTGFQKWKDVPCEDKFSFVCKFKN | antimicrobial humoral immune response mediated by antimicrobial peptide disruption of cell wall in another organism positive regulation of cell population proliferation response to peptide hormone extracellular exosome; extracellular space growth factor activity molecular function inhibitor activity oligosaccharide binding peptidoglycan binding signaling receptor activity Homo sapiens 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Lectin Pyrrolidone carboxylic acid Reference proteome Secreted Signal MAQTSSYFML MAQTSSYFMLISCLMFLSQSQGQEAQTELPQARISCPEGTNAYRSYCYYFNEDRETWVDADLYCQNMNSGNLVSVLTQAEGAFVASLIKESGTDDFNVWIGLHDPKKNRRWHWSSGSLVSYKSWGIGAPSSVNPGYCVSLTSSTGFQKWKDVPCEDKFSFVCKFKN |
bone mineralization cellular response to organic substance cellular response to transforming growth factor beta stimulus ossification positive regulation of plasminogen activation | collagen-containing extracellular matrix; cytoplasm; extracellular exosome; extracellular region; extracellular space; granular component; platelet dense granule lumen | calcium ion binding carbohydrate binding heparin binding kringle domain binding | Homo sapiens | 3D-structure Direct protein sequencing Disease variant Disulfide bond Glycoprotein Lectin Reference proteome Secreted Signal | MELWGAYLLL | MELWGAYLLLCLFSLLTQVTTEPPTQKPKKIVNAKKDVVNTKMFEELKSRLDTLAQEVALLKEQQALQTVCLKGTKVHMKCFLAFTQTKTFHEASEDCISRGGTLGTPQTGSENDALYEYLRQSVGNEAEIWLGLNDMAAEGTWVDMTGARIAYKNWETEITAQPDGGKTENCAVLSGAANGKWFDKRCRDQLPYICQFGIV | bone mineralization cellular response to organic substance cellular response to transforming growth factor beta stimulus ossification positive regulation of plasminogen activation collagen-containing extracellular matrix; cytoplasm; extracellular exosome; extracellular region; extracellular space; granular component; platelet dense granule lumen calcium ion binding carbohydrate binding heparin binding kringle domain binding Homo sapiens 3D-structure Direct protein sequencing Disease variant Disulfide bond Glycoprotein Lectin Reference proteome Secreted Signal MELWGAYLLL MELWGAYLLLCLFSLLTQVTTEPPTQKPKKIVNAKKDVVNTKMFEELKSRLDTLAQEVALLKEQQALQTVCLKGTKVHMKCFLAFTQTKTFHEASEDCISRGGTLGTPQTGSENDALYEYLRQSVGNEAEIWLGLNDMAAEGTWVDMTGARIAYKNWETEITAQPDGGKTENCAVLSGAANGKWFDKRCRDQLPYICQFGIV |
nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay translation translational termination | cytoplasm; cytoplasmic stress granule; cytosol; translation release factor complex | GTP binding GTPase activity identical protein binding mRNA binding translation release factor activity | Saccharomyces cerevisiae | 3D-structure Acetylation Amyloid Cytoplasm GTP-binding Hydrolase Nucleotide-binding Phosphoprotein Prion Protein biosynthesis Reference proteome Repeat | MSDSNQGNNQ | MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYDQCVSNVSNFLRAIGYNIKTDVVFMPVSGYSGANLKDHVDPKECPWYTGPTLLEYLDTMNHVDRHINAPFMLPIAAKMKDLGTIVEGKIESGHIKKGQSTLLMPNKTAVEIQNIYNETENEVDMAMCGEQVKLRIKGVEEEDISPGFVLTSPKNPIKSVTKFVAQIAIVELKSIIAAGFSCVMHVHTAIEEVHIVKLLHKLEKGTNRKSKKPPAFAKKGMKVIAVLETEAPVCVETYQDYPQLGRFTLRDQGTTIAIGKIVKIAE | nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay translation translational termination cytoplasm; cytoplasmic stress granule; cytosol; translation release factor complex GTP binding GTPase activity identical protein binding mRNA binding translation release factor activity Saccharomyces cerevisiae 3D-structure Acetylation Amyloid Cytoplasm GTP-binding Hydrolase Nucleotide-binding Phosphoprotein Prion Protein biosynthesis Reference proteome Repeat MSDSNQGNNQ MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETEKRRYTILDAPGHKMYVSEMIGGASQADVGVLVISARKGEYETGFERGGQTREHALLAKTQGVNKMVVVVNKMDDPTVNWSKERYDQCVSNVSNFLRAIGYNIKTDVVFMPVSGYSGANLKDHVDPKECPWYTGPTLLEYLDTMNHVDRHINAPFMLPIAAKMKDLGTIVEGKIESGHIKKGQSTLLMPNKTAVEIQNIYNETENEVDMAMCGEQVKLRIKGVEEEDISPGFVLTSPKNPIKSVTKFVAQIAIVELKSIIAAGFSCVMHVHTAIEEVHIVKLLHKLEKGTNRKSKKPPAFAKKGMKVIAVLETEAPVCVETYQDYPQLGRFTLRDQGTTIAIGKIVKIAE |
histone mRNA metabolic process IRES-dependent viral translational initiation nuclear histone mRNA catabolic process positive regulation of translation protein localization to cytoplasmic stress granule tRNA 3'-end processing tRNA 5'-leader removal tRNA export from nucleus tRNA modification tRNA processing | chromosome, telomeric region; cytoplasm; cytoplasmic stress granule; cytosol; nucleus; ribonucleoprotein complex | mRNA binding poly(U) RNA binding RNA binding sequence-specific mRNA binding tRNA binding | Homo sapiens | 3D-structure Acetylation Nucleus Phosphoprotein Reference proteome RNA-binding Systemic lupus erythematosus | MAENGDNEKM | MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ | histone mRNA metabolic process IRES-dependent viral translational initiation nuclear histone mRNA catabolic process positive regulation of translation protein localization to cytoplasmic stress granule tRNA 3'-end processing tRNA 5'-leader removal tRNA export from nucleus tRNA modification tRNA processing chromosome, telomeric region; cytoplasm; cytoplasmic stress granule; cytosol; nucleus; ribonucleoprotein complex mRNA binding poly(U) RNA binding RNA binding sequence-specific mRNA binding tRNA binding Homo sapiens 3D-structure Acetylation Nucleus Phosphoprotein Reference proteome RNA-binding Systemic lupus erythematosus MAENGDNEKM MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIEDQQESLNKWKSKGRRFKGKGKGNKAAQPGSGKGKVQFQGKKTKFASDDEHDEHDENGATGPVKRAREETDKEEPASKQQKTENGAGDQ |
proteolysis | cytoplasm; outer membrane-bounded periplasmic space | metalloendopeptidase activity zinc ion binding | Escherichia coli | 3D-structure Hydrolase Magnesium Metal-binding Metalloprotease Periplasm Protease Reference proteome Signal Zinc | MPRSTWFKAL | MPRSTWFKALLLLVALWAPLSQAETGWQPIQETIRKSDKDNRQYQAIRLDNGMVVLLVSDPQAVKSLSALVVPVGSLEDPEAYQGLAHYLEHMSLMGSKKYPQADSLAEYLKMHGGSHNASTAPYRTAFYLEVENDALPGAVDRLADAIAEPLLDKKYAERERNAVNAELTMARTRDGMRMAQVSAETINPAHPGSKFSGGNLETLSDKPGNPVQQALKDFHEKYYSANLMKAVIYSNKPLPELAKMAADTFGRVPNKESKKPEITVPVVTDAQKGIIIHYVPALPRKVLRVEFRIDNNSAKFRSKTDELITYLIGNRSPGTLSDWLQKQGLVEGISANSDPIVNGNSGVLAISASLTDKGLANRDQVVAAIFSYLNLLREKGIDKQYFDELANVLDIDFRYPSITRDMDYVEWLADTMIRVPVEHTLDAVNIADRYDAKAVKERLAMMTPQNARIWYISPKEPHNKTAYFVDAPYQVDKISAQTFADWQKKAADIALSLPELNPYIPDDFSLIKSEKKYDHPELIVDESNLRVVYAPSRYFASEPKADVSLILRNPKAMDSARNQVMFALNDYLAGLALDQLSNQASVGGISFSTNANNGLMVNANGYTQRLPQLFQALLEGYFSYTATEDQLEQAKSWYNQMMDSAEKGKAFEQAIMPAQMLSQVPYFSRDERRKILPSITLKEVLAYRDALKSGARPEFMVIGNMTEAQATTLARDVQKQLGADGSEWCRNKDVVVDKKQSVIFEKAGNSTDSALAAVFVPTGYDEYTSSAYSSLLGQIVQPWFYNQLRTEEQLGYAVFAFPMSVGRQWGMGFLLQSNDKQPSFLWERYKAFFPTAEAKLRAMKPDEFAQIQQAVITQMLQAPQTLGEEASKLSKDFDRGNMRFDSRDKIVAQIKLLTPQKLADFFHQAVVEPQGMAILSQISGSQNGKAEYVHPEGWKVWENVSALQQTMPLMSEKNE | proteolysis cytoplasm; outer membrane-bounded periplasmic space metalloendopeptidase activity zinc ion binding Escherichia coli 3D-structure Hydrolase Magnesium Metal-binding Metalloprotease Periplasm Protease Reference proteome Signal Zinc MPRSTWFKAL MPRSTWFKALLLLVALWAPLSQAETGWQPIQETIRKSDKDNRQYQAIRLDNGMVVLLVSDPQAVKSLSALVVPVGSLEDPEAYQGLAHYLEHMSLMGSKKYPQADSLAEYLKMHGGSHNASTAPYRTAFYLEVENDALPGAVDRLADAIAEPLLDKKYAERERNAVNAELTMARTRDGMRMAQVSAETINPAHPGSKFSGGNLETLSDKPGNPVQQALKDFHEKYYSANLMKAVIYSNKPLPELAKMAADTFGRVPNKESKKPEITVPVVTDAQKGIIIHYVPALPRKVLRVEFRIDNNSAKFRSKTDELITYLIGNRSPGTLSDWLQKQGLVEGISANSDPIVNGNSGVLAISASLTDKGLANRDQVVAAIFSYLNLLREKGIDKQYFDELANVLDIDFRYPSITRDMDYVEWLADTMIRVPVEHTLDAVNIADRYDAKAVKERLAMMTPQNARIWYISPKEPHNKTAYFVDAPYQVDKISAQTFADWQKKAADIALSLPELNPYIPDDFSLIKSEKKYDHPELIVDESNLRVVYAPSRYFASEPKADVSLILRNPKAMDSARNQVMFALNDYLAGLALDQLSNQASVGGISFSTNANNGLMVNANGYTQRLPQLFQALLEGYFSYTATEDQLEQAKSWYNQMMDSAEKGKAFEQAIMPAQMLSQVPYFSRDERRKILPSITLKEVLAYRDALKSGARPEFMVIGNMTEAQATTLARDVQKQLGADGSEWCRNKDVVVDKKQSVIFEKAGNSTDSALAAVFVPTGYDEYTSSAYSSLLGQIVQPWFYNQLRTEEQLGYAVFAFPMSVGRQWGMGFLLQSNDKQPSFLWERYKAFFPTAEAKLRAMKPDEFAQIQQAVITQMLQAPQTLGEEASKLSKDFDRGNMRFDSRDKIVAQIKLLTPQKLADFFHQAVVEPQGMAILSQISGSQNGKAEYVHPEGWKVWENVSALQQTMPLMSEKNE |
proton motive force-driven ATP synthesis | mitochondrial inner membrane; mitochondrial proton-transporting ATP synthase complex; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); mitochondrion | lipid binding proton transmembrane transporter activity | Homo sapiens | 3D-structure CF(0) Hydrogen ion transport Ion transport Lipid-binding Membrane Methylation Mitochondrion Reference proteome Transit peptide Transmembrane Transmembrane helix Transport | MQTAGALFIS | MQTAGALFISPALIRCCTRGLIRPVSASFLNSPVNSSKQPSYSNFPLQVARREFQTSVVSRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM | proton motive force-driven ATP synthesis mitochondrial inner membrane; mitochondrial proton-transporting ATP synthase complex; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); mitochondrion lipid binding proton transmembrane transporter activity Homo sapiens 3D-structure CF(0) Hydrogen ion transport Ion transport Lipid-binding Membrane Methylation Mitochondrion Reference proteome Transit peptide Transmembrane Transmembrane helix Transport MQTAGALFIS MQTAGALFISPALIRCCTRGLIRPVSASFLNSPVNSSKQPSYSNFPLQVARREFQTSVVSRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM |
cerebellum development electron transport coupled proton transport mitochondrial electron transport, cytochrome c to oxygen response to copper ion response to electrical stimulus response to hypoxia response to oxidative stress | mitochondrial inner membrane; mitochondrial membrane; mitochondrial respiratory chain complex III; mitochondrial respiratory chain complex IV; mitochondrion; respiratory chain complex IV | cytochrome-c oxidase activity heme binding metal ion binding | Rattus norvegicus | Calcium Copper Electron transport Heme Iron Magnesium Membrane Metal-binding Mitochondrion Mitochondrion inner membrane Reference proteome Respiratory chain Sodium Translocase Transmembrane Transmembrane helix Transport | MLVNRWLFST | MLVNRWLFSTNHKDIGTLYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFSGYTLNDTWAKAHFAIMFVGVNMTFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVLVMIFMIWEAFASKREVLSISYSSTNLEWLHGCPPPYHTFEEPSYVKVK | cerebellum development electron transport coupled proton transport mitochondrial electron transport, cytochrome c to oxygen response to copper ion response to electrical stimulus response to hypoxia response to oxidative stress mitochondrial inner membrane; mitochondrial membrane; mitochondrial respiratory chain complex III; mitochondrial respiratory chain complex IV; mitochondrion; respiratory chain complex IV cytochrome-c oxidase activity heme binding metal ion binding Rattus norvegicus Calcium Copper Electron transport Heme Iron Magnesium Membrane Metal-binding Mitochondrion Mitochondrion inner membrane Reference proteome Respiratory chain Sodium Translocase Transmembrane Transmembrane helix Transport MLVNRWLFST MLVNRWLFSTNHKDIGTLYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLSNSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFSGYTLNDTWAKAHFAIMFVGVNMTFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVLVMIFMIWEAFASKREVLSISYSSTNLEWLHGCPPPYHTFEEPSYVKVK |
base-excision repair DNA damage response | cytoplasm | 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity class I DNA-(apurinic or apyrimidinic site) endonuclease activity damaged DNA binding DNA N-glycosylase activity DNA-(apurinic or apyrimidinic site) endonuclease activity endonuclease activity metal ion binding oxidized purine nucleobase lesion DNA N-glycosylase activity oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity zinc ion binding | Escherichia coli | 3D-structure Direct protein sequencing DNA damage DNA repair DNA-binding Glycosidase Hydrolase Lyase Metal-binding Multifunctional enzyme Reference proteome Zinc Zinc-finger | MPELPEVETS | MPELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLSVQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGKVLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKKTAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARVIKAVLLRSIEQGGTTLKDFLQSDGKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQRATFYCRQCQK | base-excision repair DNA damage response cytoplasm 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity class I DNA-(apurinic or apyrimidinic site) endonuclease activity damaged DNA binding DNA N-glycosylase activity DNA-(apurinic or apyrimidinic site) endonuclease activity endonuclease activity metal ion binding oxidized purine nucleobase lesion DNA N-glycosylase activity oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity zinc ion binding Escherichia coli 3D-structure Direct protein sequencing DNA damage DNA repair DNA-binding Glycosidase Hydrolase Lyase Metal-binding Multifunctional enzyme Reference proteome Zinc Zinc-finger MPELPEVETS MPELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLSVQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGKVLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKKTAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARVIKAVLLRSIEQGGTTLKDFLQSDGKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQRATFYCRQCQK |
animal organ morphogenesis cell differentiation fibroblast growth factor receptor signaling pathway negative regulation of cardiac muscle tissue development organ induction otic vesicle formation positive regulation of cell division positive regulation of cell population proliferation positive regulation of gene expression positive regulation of protein phosphorylation post-anal tail morphogenesis regulation of cell migration semicircular canal morphogenesis thymus development | cytoplasm; endoplasmic reticulum; extracellular space; Golgi apparatus; nucleus | fibroblast growth factor receptor binding growth factor activity | Mus musculus | Alternative initiation Developmental protein Differentiation Endoplasmic reticulum Glycoprotein Golgi apparatus Growth factor Mitogen Nucleus Proto-oncogene Reference proteome Signal | MGLIWLLLLS | MGLIWLLLLSLLEPSWPTTGPGTRLRRDAGGRGGVYEHLGGAPRRRKLYCATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELGYNTYASRLYRTGSSGPGAQRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVLGHKDHEMVRLLQSSQPRAPGEGSQPRQRRQKKQSPGDHGKMETLSTRATPSTQLHTGGLAVA | animal organ morphogenesis cell differentiation fibroblast growth factor receptor signaling pathway negative regulation of cardiac muscle tissue development organ induction otic vesicle formation positive regulation of cell division positive regulation of cell population proliferation positive regulation of gene expression positive regulation of protein phosphorylation post-anal tail morphogenesis regulation of cell migration semicircular canal morphogenesis thymus development cytoplasm; endoplasmic reticulum; extracellular space; Golgi apparatus; nucleus fibroblast growth factor receptor binding growth factor activity Mus musculus Alternative initiation Developmental protein Differentiation Endoplasmic reticulum Glycoprotein Golgi apparatus Growth factor Mitogen Nucleus Proto-oncogene Reference proteome Signal MGLIWLLLLS MGLIWLLLLSLLEPSWPTTGPGTRLRRDAGGRGGVYEHLGGAPRRRKLYCATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELGYNTYASRLYRTGSSGPGAQRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVLGHKDHEMVRLLQSSQPRAPGEGSQPRQRRQKKQSPGDHGKMETLSTRATPSTQLHTGGLAVA |
acetylcholine receptor signaling pathway response to bacterium | external side of plasma membrane; plasma membrane; synapse | acetylcholine receptor binding acetylcholine receptor inhibitor activity | Mus musculus | Cell membrane Direct protein sequencing Disulfide bond Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Signal | MDTSHTTKSC | MDTSHTTKSCLLILLVALLCAERAQGLECYQCYGVPFETSCPSITCPYPDGVCVTQEAAVIVDSQTRKVKNNLCLPICPPNIESMEILGTKVNVKTSCCQEDLCNVAVPNGGSTWTMAGVLLFSLSSVLLQTLL | acetylcholine receptor signaling pathway response to bacterium external side of plasma membrane; plasma membrane; synapse acetylcholine receptor binding acetylcholine receptor inhibitor activity Mus musculus Cell membrane Direct protein sequencing Disulfide bond Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Signal MDTSHTTKSC MDTSHTTKSCLLILLVALLCAERAQGLECYQCYGVPFETSCPSITCPYPDGVCVTQEAAVIVDSQTRKVKNNLCLPICPPNIESMEILGTKVNVKTSCCQEDLCNVAVPNGGSTWTMAGVLLFSLSSVLLQTLL |
adaptive immune response antigen processing and presentation of exogenous peptide antigen via MHC class II immune response peptide antigen assembly with MHC class II protein complex positive regulation of immune response positive regulation of T cell activation | clathrin-coated endocytic vesicle membrane; endocytic vesicle membrane; ER to Golgi transport vesicle membrane; Golgi membrane; late endosome membrane; lumenal side of endoplasmic reticulum membrane; lysosomal membrane; MHC class II protein complex; plasma membrane; trans-Golgi network membrane; transport vesicle membrane | MHC class II protein complex binding MHC class II receptor activity peptide antigen binding | Homo sapiens | Adaptive immunity Alternative splicing Cell membrane Disulfide bond Endoplasmic reticulum Endosome Glycoprotein Golgi apparatus Immunity Lysosome Membrane MHC II Reference proteome Signal Transmembrane Transmembrane helix | MSWKMALQIP | MSWKMALQIPGGFWAAAVTVMLVMLSTPVAEARDFPKDFLVQFKGMCYFTNGTERVRGVARYIYNREEYGRFDSDVGEFQAVTELGRSIEDWNNYKDFLEQERAAVDKVCRHNYEAELRTTLQRQVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTSLIRNGDWTFQILVMLEITPQRGDIYTCQVEHPSLQSPITVEWRAQSESAQSKMLSGIGGFVLGLIFLGLGLIIRHRGQKGPRGPPPAGLLH | adaptive immune response antigen processing and presentation of exogenous peptide antigen via MHC class II immune response peptide antigen assembly with MHC class II protein complex positive regulation of immune response positive regulation of T cell activation clathrin-coated endocytic vesicle membrane; endocytic vesicle membrane; ER to Golgi transport vesicle membrane; Golgi membrane; late endosome membrane; lumenal side of endoplasmic reticulum membrane; lysosomal membrane; MHC class II protein complex; plasma membrane; trans-Golgi network membrane; transport vesicle membrane MHC class II protein complex binding MHC class II receptor activity peptide antigen binding Homo sapiens Adaptive immunity Alternative splicing Cell membrane Disulfide bond Endoplasmic reticulum Endosome Glycoprotein Golgi apparatus Immunity Lysosome Membrane MHC II Reference proteome Signal Transmembrane Transmembrane helix MSWKMALQIP MSWKMALQIPGGFWAAAVTVMLVMLSTPVAEARDFPKDFLVQFKGMCYFTNGTERVRGVARYIYNREEYGRFDSDVGEFQAVTELGRSIEDWNNYKDFLEQERAAVDKVCRHNYEAELRTTLQRQVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTSLIRNGDWTFQILVMLEITPQRGDIYTCQVEHPSLQSPITVEWRAQSESAQSKMLSGIGGFVLGLIFLGLGLIIRHRGQKGPRGPPPAGLLH |
thyroid hormone transport | extracellular exosome; extracellular region; extracellular space | serine-type endopeptidase inhibitor activity | Homo sapiens | 3D-structure Direct protein sequencing Glycoprotein Reference proteome Secreted Signal | MSPFLYLVLL | MSPFLYLVLLVLGLHATIHCASPEGKVTACHSSQPNATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA | thyroid hormone transport extracellular exosome; extracellular region; extracellular space serine-type endopeptidase inhibitor activity Homo sapiens 3D-structure Direct protein sequencing Glycoprotein Reference proteome Secreted Signal MSPFLYLVLL MSPFLYLVLLVLGLHATIHCASPEGKVTACHSSQPNATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATLLKMGIQHAYSENADFSGLTEDNGLKLSNAAHKAVLHIGEKGTEAAAVPEVELSDQPENTFLHPIIQIDRSFMLLILERSTRSILFLGKVVNPTEA |
blood coagulation chemotaxis | endoplasmic reticulum lumen; extracellular exosome; extracellular region; extracellular space | endopeptidase inhibitor activity heparin binding serine-type endopeptidase inhibitor activity | Homo sapiens | 3D-structure Blood coagulation Chemotaxis Direct protein sequencing Disease variant Glycoprotein Hemostasis Heparin-binding Phosphoprotein Protease inhibitor Reference proteome Repeat Serine protease inhibitor Signal Sulfation Thrombophilia | MKHSLNALLI | MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTLEAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPSRS | blood coagulation chemotaxis endoplasmic reticulum lumen; extracellular exosome; extracellular region; extracellular space endopeptidase inhibitor activity heparin binding serine-type endopeptidase inhibitor activity Homo sapiens 3D-structure Blood coagulation Chemotaxis Direct protein sequencing Disease variant Glycoprotein Hemostasis Heparin-binding Phosphoprotein Protease inhibitor Reference proteome Repeat Serine protease inhibitor Signal Sulfation Thrombophilia MKHSLNALLI MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREVVKVSMMQTKGNFLAANDQELDCDILQLEYVGGISMLIVVPHKMSGMKTLEAQLTPRVVERWQKSMTNRTREVLLPKFKLEKNYNLVESLKLMGIRMLFDKNGNMAGISDQRIAIDLFKHQGTITVNEEGTQATTVTTVGFMPLSTQVRFTVDRPFLFLIYEHRTSCLLFMGRVANPSRS |
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