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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negative regulation of apoptotic process negative regulation of DNA-templated transcription negative regulation of intracellular transport protein refolding response to heat | cytoplasm; extracellular region; lysosome; nucleus; protein-containing complex | metal ion binding protein homodimerization activity structural constituent of eye lens unfolded protein binding | Bos taurus | Acetylation Chaperone Cytoplasm Direct protein sequencing Eye lens protein Glycation Glycoprotein Lysosome Metal-binding Methylation Nucleus Phosphoprotein Reference proteome Secreted Zinc | MDIAIHHPWI | MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPASTSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLAITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK | negative regulation of apoptotic process negative regulation of DNA-templated transcription negative regulation of intracellular transport protein refolding response to heat cytoplasm; extracellular region; lysosome; nucleus; protein-containing complex metal ion binding protein homodimerization activity structural constituent of eye lens unfolded protein binding Bos taurus Acetylation Chaperone Cytoplasm Direct protein sequencing Eye lens protein Glycation Glycoprotein Lysosome Metal-binding Methylation Nucleus Phosphoprotein Reference proteome Secreted Zinc MDIAIHHPWI MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPASTSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLAITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK |
apoptotic process involved in morphogenesis cellular response to gamma radiation lens development in camera-type eye microtubule polymerization or depolymerization muscle contraction muscle organ development negative regulation of amyloid fibril formation negative regulation of apoptotic process negative regulation of cell growth negative regulation of DNA-templated transcription negative regulation of gene expression negative regulation of intracellular transport negative regulation of protein-containing complex assembly negative regulation of reactive oxygen species metabolic process protein folding protein refolding protein stabilization regulation of programmed cell death response to estradiol response to heat response to hydrogen peroxide response to hypoxia stress-activated MAPK cascade tubulin complex assembly | actin filament bundle; axon; cardiac myofibril; cell surface; cytoplasm; cytosol; dendritic spine; extracellular exosome; lysosome; M band; mitochondrion; nucleoplasm; nucleus; perikaryon; protein-containing complex; synaptic membrane; Z disc | amyloid-beta binding identical protein binding metal ion binding microtubule binding protein homodimerization activity protein-containing complex binding structural constituent of eye lens structural molecule activity unfolded protein binding | Homo sapiens | 3D-structure Acetylation Cardiomyopathy Cataract Chaperone Cytoplasm Direct protein sequencing Disease variant Eye lens protein Glycoprotein Lysosome Metal-binding Myofibrillar myopathy Nucleus Oxidation Phosphoprotein Reference proteome Secreted Zinc | MDIAIHHPWI | MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK | apoptotic process involved in morphogenesis cellular response to gamma radiation lens development in camera-type eye microtubule polymerization or depolymerization muscle contraction muscle organ development negative regulation of amyloid fibril formation negative regulation of apoptotic process negative regulation of cell growth negative regulation of DNA-templated transcription negative regulation of gene expression negative regulation of intracellular transport negative regulation of protein-containing complex assembly negative regulation of reactive oxygen species metabolic process protein folding protein refolding protein stabilization regulation of programmed cell death response to estradiol response to heat response to hydrogen peroxide response to hypoxia stress-activated MAPK cascade tubulin complex assembly actin filament bundle; axon; cardiac myofibril; cell surface; cytoplasm; cytosol; dendritic spine; extracellular exosome; lysosome; M band; mitochondrion; nucleoplasm; nucleus; perikaryon; protein-containing complex; synaptic membrane; Z disc amyloid-beta binding identical protein binding metal ion binding microtubule binding protein homodimerization activity protein-containing complex binding structural constituent of eye lens structural molecule activity unfolded protein binding Homo sapiens 3D-structure Acetylation Cardiomyopathy Cataract Chaperone Cytoplasm Direct protein sequencing Disease variant Eye lens protein Glycoprotein Lysosome Metal-binding Myofibrillar myopathy Nucleus Oxidation Phosphoprotein Reference proteome Secreted Zinc MDIAIHHPWI MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK |
behavioral response to starvation chaperone-mediated protein folding defense response to bacterium defense response to fungus determination of adult lifespan protein refolding response to heat | cytoplasm; endoplasmic reticulum chaperone complex; nucleus | unfolded protein binding | Drosophila melanogaster | Phosphoprotein Reference proteome Stress response | MSIIPLLHLA | MSIIPLLHLARELDHDYRTDWGHLLEDDFGFGVHAHDLFHPRRLLLPNTLGLGRRRYSPYERSHGHHNQMSRRASGGPNALLPAVGKDGFQVCMDVSQFKPNELTVKVVDNTVVVEGKHEEREDGHGMIQRHFVRKYTLPKGFDPNEVVSTVSSDGVLTLKAPPPPSKEQAKSERIVQIQQTGPAHLSVKAPAPEAGDGKAENGSGEKMETSK | behavioral response to starvation chaperone-mediated protein folding defense response to bacterium defense response to fungus determination of adult lifespan protein refolding response to heat cytoplasm; endoplasmic reticulum chaperone complex; nucleus unfolded protein binding Drosophila melanogaster Phosphoprotein Reference proteome Stress response MSIIPLLHLA MSIIPLLHLARELDHDYRTDWGHLLEDDFGFGVHAHDLFHPRRLLLPNTLGLGRRRYSPYERSHGHHNQMSRRASGGPNALLPAVGKDGFQVCMDVSQFKPNELTVKVVDNTVVVEGKHEEREDGHGMIQRHFVRKYTLPKGFDPNEVVSTVSSDGVLTLKAPPPPSKEQAKSERIVQIQQTGPAHLSVKAPAPEAGDGKAENGSGEKMETSK |
epidermis development epithelial cell differentiation hair cycle intermediate filament bundle assembly intermediate filament organization keratinocyte differentiation stem cell differentiation | basal part of cell; cornified envelope; cytoplasm; cytoskeleton; cytosol; extracellular exosome; intermediate filament; keratin filament; nucleus | keratin filament binding structural constituent of cytoskeleton | Homo sapiens | 3D-structure Coiled coil Cytoplasm Disease variant Disulfide bond Ectodermal dysplasia Epidermolysis bullosa Intermediate filament Keratin Nucleus Palmoplantar keratoderma Phosphoprotein Reference proteome Ubl conjugation | MTTCSRQFTS | MTTCSRQFTSSSSMKGSCGIGGGIGGGSSRISSVLAGGSCRAPSTYGGGLSVSSSRFSSGGACGLGGGYGGGFSSSSSSFGSGFGGGYGGGLGAGLGGGFGGGFAGGDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLSSSQFSSGSQSSRDVTSSSRQIRTKVMDVHDGKVVSTHEQVLRTKN | epidermis development epithelial cell differentiation hair cycle intermediate filament bundle assembly intermediate filament organization keratinocyte differentiation stem cell differentiation basal part of cell; cornified envelope; cytoplasm; cytoskeleton; cytosol; extracellular exosome; intermediate filament; keratin filament; nucleus keratin filament binding structural constituent of cytoskeleton Homo sapiens 3D-structure Coiled coil Cytoplasm Disease variant Disulfide bond Ectodermal dysplasia Epidermolysis bullosa Intermediate filament Keratin Nucleus Palmoplantar keratoderma Phosphoprotein Reference proteome Ubl conjugation MTTCSRQFTS MTTCSRQFTSSSSMKGSCGIGGGIGGGSSRISSVLAGGSCRAPSTYGGGLSVSSSRFSSGGACGLGGGYGGGFSSSSSSFGSGFGGGYGGGLGAGLGGGFGGGFAGGDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLSSSQFSSGSQSSRDVTSSSRQIRTKVMDVHDGKVVSTHEQVLRTKN |
cellular response to calcium ion epidermis development epithelial cell differentiation intermediate filament organization keratinocyte development keratinocyte differentiation positive regulation of epidermis development protein heterotetramerization stem cell differentiation | cell surface; cornified envelope; cytoplasm; cytoskeleton; extracellular region; keratin filament | cytoskeletal protein binding protein heterodimerization activity structural constituent of skin epidermis | Mus musculus | Alternative splicing Coiled coil Cytoplasm Direct protein sequencing Disulfide bond Intermediate filament Keratin Methylation Phosphoprotein Reference proteome Secreted | MSVLYSSSSK | MSVLYSSSSKQFSSSRSGGGGGGGSVRVSSTRGSLGGGYSSGGFSGGSFSRGSSGGGCFGGSSGGYGGFGGGGSFGGGYGGSSFGGGYGGSSFGGGYGGSSFGGAGFGGGGSFGGGSFGGGSYGGGFGGGGFGGDGGSLLSGNGRVTMQNLNDRLASYMDKVRALEESNYELEGKIKEWYEKHGNSSQREPRDYSKYYKTIEDLKGQILTLTTDNANVLLQIDNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVSTGDVNVEMNAAPGVDLTQLLNNMRNQYEQLAEKNRKDAEEWFNQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGRYCVQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLEGEGSSSGGGGGRRGGSGGGSYGGSSGGGSYGGSSGGGGSYGGSSGGGGSYGGGSSGGGSHGGSSGGGYGGGSSSGGAGGHGGSSGGGYGGGSSSGGQGGSGGFKSSGGGDQSSKGPRY | cellular response to calcium ion epidermis development epithelial cell differentiation intermediate filament organization keratinocyte development keratinocyte differentiation positive regulation of epidermis development protein heterotetramerization stem cell differentiation cell surface; cornified envelope; cytoplasm; cytoskeleton; extracellular region; keratin filament cytoskeletal protein binding protein heterodimerization activity structural constituent of skin epidermis Mus musculus Alternative splicing Coiled coil Cytoplasm Direct protein sequencing Disulfide bond Intermediate filament Keratin Methylation Phosphoprotein Reference proteome Secreted MSVLYSSSSK MSVLYSSSSKQFSSSRSGGGGGGGSVRVSSTRGSLGGGYSSGGFSGGSFSRGSSGGGCFGGSSGGYGGFGGGGSFGGGYGGSSFGGGYGGSSFGGGYGGSSFGGAGFGGGGSFGGGSFGGGSYGGGFGGGGFGGDGGSLLSGNGRVTMQNLNDRLASYMDKVRALEESNYELEGKIKEWYEKHGNSSQREPRDYSKYYKTIEDLKGQILTLTTDNANVLLQIDNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVSTGDVNVEMNAAPGVDLTQLLNNMRNQYEQLAEKNRKDAEEWFNQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGRYCVQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLEGEGSSSGGGGGRRGGSGGGSYGGSSGGGSYGGSSGGGGSYGGSSGGGGSYGGGSSGGGSHGGSSGGGYGGGSSSGGAGGHGGSSGGGYGGGSSSGGQGGSGGFKSSGGGDQSSKGPRY |
antimicrobial humoral immune response mediated by antimicrobial peptide cell differentiation defense response to Gram-positive bacterium intermediate filament organization keratinization killing of cells of another organism morphogenesis of an epithelium negative regulation of entry of bacterium into host cell positive regulation of cell population proliferation wound healing | cytosol; extracellular exosome; keratin filament; membrane; nucleus | structural constituent of cytoskeleton structural constituent of skin epidermis | Homo sapiens | 3D-structure Acetylation Allergen Coiled coil Direct protein sequencing Disease variant Ectodermal dysplasia Intermediate filament Keratin Palmoplantar keratoderma Reference proteome | MASTSTTIRS | MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSVSVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNISVVQSTVSSGYGGASGVGSGLGLGGGSSYSYGSGLGVGGGFSSSSGRAIGGGLSSVGGGSSTIKYTTTSSSSRKSYKH | antimicrobial humoral immune response mediated by antimicrobial peptide cell differentiation defense response to Gram-positive bacterium intermediate filament organization keratinization killing of cells of another organism morphogenesis of an epithelium negative regulation of entry of bacterium into host cell positive regulation of cell population proliferation wound healing cytosol; extracellular exosome; keratin filament; membrane; nucleus structural constituent of cytoskeleton structural constituent of skin epidermis Homo sapiens 3D-structure Acetylation Allergen Coiled coil Direct protein sequencing Disease variant Ectodermal dysplasia Intermediate filament Keratin Palmoplantar keratoderma Reference proteome MASTSTTIRS MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSVSVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNISVVQSTVSSGYGGASGVGSGLGLGGGSSYSYGSGLGVGGGFSSSSGRAIGGGLSSVGGGSSTIKYTTTSSSSRKSYKH |
intermediate filament organization skeletal muscle organ development | cardiac myofibril; cell-cell junction; cytoplasm; fascia adherens; intercalated disc; intermediate filament; neuromuscular junction; nucleus; sarcolemma; Z disc | cytoskeletal protein binding identical protein binding | Sus scrofa | ADP-ribosylation Cell membrane Coiled coil Cytoplasm Direct protein sequencing Intermediate filament Membrane Methylation Muscle protein Nucleus Phosphoprotein Reference proteome Ubl conjugation | MSQAYSSSQR | MSQAYSSSQRVSSYRRTFGGAPSFPLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGPLRASRLGATRVPSSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL | intermediate filament organization skeletal muscle organ development cardiac myofibril; cell-cell junction; cytoplasm; fascia adherens; intercalated disc; intermediate filament; neuromuscular junction; nucleus; sarcolemma; Z disc cytoskeletal protein binding identical protein binding Sus scrofa ADP-ribosylation Cell membrane Coiled coil Cytoplasm Direct protein sequencing Intermediate filament Membrane Methylation Muscle protein Nucleus Phosphoprotein Reference proteome Ubl conjugation MSQAYSSSQR MSQAYSSSQRVSSYRRTFGGAPSFPLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGPLRASRLGATRVPSSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL |
intermediate filament organization | cardiac myofibril; cytoplasm; fascia adherens; intercalated disc; intermediate filament; neuromuscular junction; nucleus; sarcolemma; Z disc | cytoskeletal protein binding identical protein binding | Mesocricetus auratus | ADP-ribosylation Cell membrane Coiled coil Cytoplasm Intermediate filament Membrane Methylation Muscle protein Nucleus Phosphoprotein Reference proteome Ubl conjugation | MSQAYSSSQR | MSQAYSSSQRVSSYRRTFGGAPSFSLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGSTRAPSYGAGELLDFSLADAVNQEFLATRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL | intermediate filament organization cardiac myofibril; cytoplasm; fascia adherens; intercalated disc; intermediate filament; neuromuscular junction; nucleus; sarcolemma; Z disc cytoskeletal protein binding identical protein binding Mesocricetus auratus ADP-ribosylation Cell membrane Coiled coil Cytoplasm Intermediate filament Membrane Methylation Muscle protein Nucleus Phosphoprotein Reference proteome Ubl conjugation MSQAYSSSQR MSQAYSSSQRVSSYRRTFGGAPSFSLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGSTRAPSYGAGELLDFSLADAVNQEFLATRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL |
cellular response to lipopolysaccharide cellular response to muramyl dipeptide intermediate filament organization | axon; cytoplasm; intermediate filament; nuclear matrix; plasma membrane | structural constituent of cytoskeleton | Sus scrofa | Acetylation Cell membrane Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Glycoprotein Intermediate filament Isopeptide bond Membrane Nucleus Phosphoprotein Reference proteome S-nitrosylation Ubl conjugation | MSTRTVSSSS | MSTRTVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYTSSPGGVYATRSSAVRLRSSVPGVRLLQDAVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEETLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDMDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE | cellular response to lipopolysaccharide cellular response to muramyl dipeptide intermediate filament organization axon; cytoplasm; intermediate filament; nuclear matrix; plasma membrane structural constituent of cytoskeleton Sus scrofa Acetylation Cell membrane Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Glycoprotein Intermediate filament Isopeptide bond Membrane Nucleus Phosphoprotein Reference proteome S-nitrosylation Ubl conjugation MSTRTVSSSS MSTRTVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYTSSPGGVYATRSSAVRLRSSVPGVRLLQDAVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEETLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDMDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE |
cellular response to lipopolysaccharide cellular response to muramyl dipeptide intermediate filament organization intermediate filament polymerization | cytoplasm; intermediate filament; nuclear matrix; plasma membrane | structural constituent of cytoskeleton | Mesocricetus auratus | Acetylation Cell membrane Coiled coil Cytoplasm Cytoskeleton Glycoprotein Intermediate filament Isopeptide bond Membrane Nucleus Phosphoprotein Reference proteome S-nitrosylation Ubl conjugation | MSTRSVSSSS | MSTRSVSSSSYRRMFGGPGTSNRQSSNRSYVTTSTRTYSLGSLRPSTSRSLYSSSPGGAYVTRSSAVRLRSSMPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE | cellular response to lipopolysaccharide cellular response to muramyl dipeptide intermediate filament organization intermediate filament polymerization cytoplasm; intermediate filament; nuclear matrix; plasma membrane structural constituent of cytoskeleton Mesocricetus auratus Acetylation Cell membrane Coiled coil Cytoplasm Cytoskeleton Glycoprotein Intermediate filament Isopeptide bond Membrane Nucleus Phosphoprotein Reference proteome S-nitrosylation Ubl conjugation MSTRSVSSSS MSTRSVSSSSYRRMFGGPGTSNRQSSNRSYVTTSTRTYSLGSLRPSTSRSLYSSSPGGAYVTRSSAVRLRSSMPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE |
cellular response to hypoxia cellular senescence DNA double-strand break attachment to nuclear envelope establishment or maintenance of microtubule cytoskeleton polarity heterochromatin formation muscle organ development negative regulation of cardiac muscle hypertrophy in response to stress negative regulation of cell population proliferation negative regulation of extrinsic apoptotic signaling pathway negative regulation of mesenchymal cell proliferation negative regulation of release of cytochrome c from mitochondria nuclear envelope organization nuclear migration nuclear pore localization positive regulation of gene expression protein import into nucleus protein localization protein localization to nuclear envelope protein localization to nucleus regulation of cell migration regulation of protein localization to nucleus regulation of protein stability regulation of telomere maintenance ventricular cardiac muscle cell development | cytosol; intermediate filament; lamin filament; nuclear envelope; nuclear lamina; nuclear matrix; nuclear membrane; nuclear speck; nucleoplasm; nucleus; perinuclear region of cytoplasm; site of double-strand break | identical protein binding structural constituent of cytoskeleton structural molecule activity | Homo sapiens | 3D-structure Acetylation Alternative splicing Cardiomyopathy Charcot-Marie-Tooth disease Coiled coil Congenital muscular dystrophy Direct protein sequencing Disease variant Emery-Dreifuss muscular dystrophy Intermediate filament Isopeptide bond Limb-girdle muscular dystrophy Lipoprotein Methylation Neurodegeneration Neuropathy Nucleus Phosphoprotein Prenylation Reference proteome Ubl conjugation | METPSQRRAT | METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM | cellular response to hypoxia cellular senescence DNA double-strand break attachment to nuclear envelope establishment or maintenance of microtubule cytoskeleton polarity heterochromatin formation muscle organ development negative regulation of cardiac muscle hypertrophy in response to stress negative regulation of cell population proliferation negative regulation of extrinsic apoptotic signaling pathway negative regulation of mesenchymal cell proliferation negative regulation of release of cytochrome c from mitochondria nuclear envelope organization nuclear migration nuclear pore localization positive regulation of gene expression protein import into nucleus protein localization protein localization to nuclear envelope protein localization to nucleus regulation of cell migration regulation of protein localization to nucleus regulation of protein stability regulation of telomere maintenance ventricular cardiac muscle cell development cytosol; intermediate filament; lamin filament; nuclear envelope; nuclear lamina; nuclear matrix; nuclear membrane; nuclear speck; nucleoplasm; nucleus; perinuclear region of cytoplasm; site of double-strand break identical protein binding structural constituent of cytoskeleton structural molecule activity Homo sapiens 3D-structure Acetylation Alternative splicing Cardiomyopathy Charcot-Marie-Tooth disease Coiled coil Congenital muscular dystrophy Direct protein sequencing Disease variant Emery-Dreifuss muscular dystrophy Intermediate filament Isopeptide bond Limb-girdle muscular dystrophy Lipoprotein Methylation Neurodegeneration Neuropathy Nucleus Phosphoprotein Prenylation Reference proteome Ubl conjugation METPSQRRAT METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM |
anterograde axonal transport axonal transport of mitochondrion intermediate filament organization neurofilament bundle assembly retrograde axonal transport | axon; axon cytoplasm; cytoplasm; intermediate filament; neurofilament; postsynaptic intermediate filament cytoskeleton | identical protein binding structural constituent of cytoskeleton structural constituent of postsynaptic intermediate filament cytoskeleton | Sus scrofa | Acetylation Cell projection Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Glycoprotein Intermediate filament Methylation Phosphoprotein Reference proteome Ubl conjugation | MSSFYSEPYY | MSSFYSEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAQLLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEGKEKEEAEAEAEAEEEGAQEEEEAAEKEESEEAKEEEGGEGEQGEETKEAEEEEKKDEGAGEEQATKKKD | anterograde axonal transport axonal transport of mitochondrion intermediate filament organization neurofilament bundle assembly retrograde axonal transport axon; axon cytoplasm; cytoplasm; intermediate filament; neurofilament; postsynaptic intermediate filament cytoskeleton identical protein binding structural constituent of cytoskeleton structural constituent of postsynaptic intermediate filament cytoskeleton Sus scrofa Acetylation Cell projection Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Glycoprotein Intermediate filament Methylation Phosphoprotein Reference proteome Ubl conjugation MSSFYSEPYY MSSFYSEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAQLLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEGKEKEEAEAEAEAEEEGAQEEEEAAEKEESEEAKEEEGGEGEQGEETKEAEEEEKKDEGAGEEQATKKKD |
anterograde axonal transport axonal transport of mitochondrion axonogenesis intermediate filament bundle assembly intermediate filament organization locomotion microtubule cytoskeleton organization motor neuron apoptotic process negative regulation of motor neuron apoptotic process negative regulation of neuron apoptotic process neurofilament bundle assembly neurofilament cytoskeleton organization neuromuscular process controlling balance neuron projection morphogenesis peripheral nervous system axon regeneration positive regulation of axonogenesis postsynaptic modulation of chemical synaptic transmission regulation of axon diameter regulation of synapse maturation retrograde axonal transport | axon; axon cytoplasm; cholinergic synapse; cytoplasm; intermediate filament; neurofilament; neuromuscular junction; postsynaptic intermediate filament cytoskeleton; presynaptic intermediate filament cytoskeleton; Schaffer collateral - CA1 synapse | identical protein binding protein-macromolecule adaptor activity structural constituent of cytoskeleton structural constituent of postsynaptic intermediate filament cytoskeleton | Bos taurus | Acetylation Cell projection Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Glycoprotein Intermediate filament Methylation Phosphoprotein Reference proteome Ubl conjugation | MSSFSYEPYY | MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLESLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYTQSSQVFGRSAYGGLQTSSYLMSARSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEEKEKEEAEAEAEAEAEAEAEEEEGAQEEEAAKEDAEEAKEEEGGEGEEAEETKEAEEEEKKDEGAGEEQATKKKD | anterograde axonal transport axonal transport of mitochondrion axonogenesis intermediate filament bundle assembly intermediate filament organization locomotion microtubule cytoskeleton organization motor neuron apoptotic process negative regulation of motor neuron apoptotic process negative regulation of neuron apoptotic process neurofilament bundle assembly neurofilament cytoskeleton organization neuromuscular process controlling balance neuron projection morphogenesis peripheral nervous system axon regeneration positive regulation of axonogenesis postsynaptic modulation of chemical synaptic transmission regulation of axon diameter regulation of synapse maturation retrograde axonal transport axon; axon cytoplasm; cholinergic synapse; cytoplasm; intermediate filament; neurofilament; neuromuscular junction; postsynaptic intermediate filament cytoskeleton; presynaptic intermediate filament cytoskeleton; Schaffer collateral - CA1 synapse identical protein binding protein-macromolecule adaptor activity structural constituent of cytoskeleton structural constituent of postsynaptic intermediate filament cytoskeleton Bos taurus Acetylation Cell projection Coiled coil Cytoplasm Cytoskeleton Direct protein sequencing Glycoprotein Intermediate filament Methylation Phosphoprotein Reference proteome Ubl conjugation MSSFSYEPYY MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLESLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYTQSSQVFGRSAYGGLQTSSYLMSARSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEEKEKEEAEAEAEAEAEAEAEEEEGAQEEEAAKEDAEEAKEEEGGEGEEAEETKEAEEEEKKDEGAGEEQATKKKD |
microtubule cytoskeleton organization mitotic cell cycle | cytoplasm; microtubule | GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton | Sus scrofa | 3D-structure Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome | MRECISIHVG | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRAHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY | microtubule cytoskeleton organization mitotic cell cycle cytoplasm; microtubule GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton Sus scrofa 3D-structure Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome MRECISIHVG MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRAHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY |
microtubule cytoskeleton organization mitotic cell cycle | cytoplasm; microtubule | GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton | Gallus gallus | Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Microtubule Nucleotide-binding Reference proteome | ETIGGGDDSF | ETIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPARQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY | microtubule cytoskeleton organization mitotic cell cycle cytoplasm; microtubule GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton Gallus gallus Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Microtubule Nucleotide-binding Reference proteome ETIGGGDDSF ETIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPARQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY |
microtubule cytoskeleton organization mitotic cell cycle | cytoplasm; microtubule | GTP binding GTPase activity metal ion binding structural constituent of cytoskeleton | Sus scrofa | 3D-structure Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nucleotide-binding Phosphoprotein Reference proteome Ubl conjugation | MREIVHIQAG | MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA | microtubule cytoskeleton organization mitotic cell cycle cytoplasm; microtubule GTP binding GTPase activity metal ion binding structural constituent of cytoskeleton Sus scrofa 3D-structure Acetylation Cytoplasm Cytoskeleton Direct protein sequencing GTP-binding Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nucleotide-binding Phosphoprotein Reference proteome Ubl conjugation MREIVHIQAG MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA |
cytoplasmic microtubule organization cytoskeleton organization microtubule cytoskeleton organization microtubule-based process mitotic cell cycle mitotic spindle assembly mitotic spindle elongation positive regulation of intracellular protein transport response to antibiotic | cytoplasm; microtubule; tubulin complex | GTP binding GTPase activity metal ion binding structural constituent of cytoskeleton | Saccharomyces cerevisiae | 3D-structure Antibiotic resistance Cytoplasm Cytoskeleton GTP-binding Magnesium Metal-binding Microtubule Nucleotide-binding Phosphoprotein Reference proteome | MREIIHISTG | MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVIRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMMAAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQGLDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVSEYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFE | cytoplasmic microtubule organization cytoskeleton organization microtubule cytoskeleton organization microtubule-based process mitotic cell cycle mitotic spindle assembly mitotic spindle elongation positive regulation of intracellular protein transport response to antibiotic cytoplasm; microtubule; tubulin complex GTP binding GTPase activity metal ion binding structural constituent of cytoskeleton Saccharomyces cerevisiae 3D-structure Antibiotic resistance Cytoplasm Cytoskeleton GTP-binding Magnesium Metal-binding Microtubule Nucleotide-binding Phosphoprotein Reference proteome MREIIHISTG MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVIRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMMAAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQGLDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVSEYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFE |
mitotic cytokinesis | brahma complex; cytoplasm; cytoskeleton | ATP binding hydrolase activity | Drosophila melanogaster | Acetylation ATP-binding Cytoplasm Cytoskeleton Hydrolase Methylation Nucleotide-binding Oxidation Reference proteome | MCDEEVAALV | MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | mitotic cytokinesis brahma complex; cytoplasm; cytoskeleton ATP binding hydrolase activity Drosophila melanogaster Acetylation ATP-binding Cytoplasm Cytoskeleton Hydrolase Methylation Nucleotide-binding Oxidation Reference proteome MCDEEVAALV MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF |
mitotic cytokinesis | cytoplasm; cytoskeleton | ATP binding hydrolase activity | Drosophila melanogaster | Acetylation ATP-binding Cytoplasm Cytoskeleton Hydrolase Methylation Muscle protein Nucleotide-binding Oxidation Reference proteome | MCDEEASALV | MCDEEASALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDCYVGDEAQSKRGILSLKYPIEHGIITNWDDMEKVWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRTPEALFQPSFLGMESCGIHETVYQSIMKCDVDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTIKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVHRKCF | mitotic cytokinesis cytoplasm; cytoskeleton ATP binding hydrolase activity Drosophila melanogaster Acetylation ATP-binding Cytoplasm Cytoskeleton Hydrolase Methylation Muscle protein Nucleotide-binding Oxidation Reference proteome MCDEEASALV MCDEEASALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDCYVGDEAQSKRGILSLKYPIEHGIITNWDDMEKVWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRTPEALFQPSFLGMESCGIHETVYQSIMKCDVDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTIKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVHRKCF |
phagocytosis response to chemical | actin cytoskeleton; cytoplasm | ATP binding hydrolase activity | Physarum polycephalum | ATP-binding Cytoplasm Cytoskeleton Direct protein sequencing Hydrolase Methylation Nucleotide-binding Phosphoprotein | MEGEDVQALV | MEGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEQEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMQKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF | phagocytosis response to chemical actin cytoskeleton; cytoplasm ATP binding hydrolase activity Physarum polycephalum ATP-binding Cytoplasm Cytoskeleton Direct protein sequencing Hydrolase Methylation Nucleotide-binding Phosphoprotein MEGEDVQALV MEGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEQEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMQKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF |
regulation of muscle contraction skeletal muscle contraction | cytosol; troponin complex | calcium ion binding | Homo sapiens | 3D-structure Acetylation Calcium Direct protein sequencing Disease variant Metal-binding Muscle protein Reference proteome Repeat | MTDQQAEARS | MTDQQAEARSYLSEEMIAEFKAAFDMFDADGGGDISVKELGTVMRMLGQTPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELAECFRIFDRNADGYIDPEELAEIFRASGEHVTDEEIESLMKDGDKNNDGRIDFDEFLKMMEGVQ | regulation of muscle contraction skeletal muscle contraction cytosol; troponin complex calcium ion binding Homo sapiens 3D-structure Acetylation Calcium Direct protein sequencing Disease variant Metal-binding Muscle protein Reference proteome Repeat MTDQQAEARS MTDQQAEARSYLSEEMIAEFKAAFDMFDADGGGDISVKELGTVMRMLGQTPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELAECFRIFDRNADGYIDPEELAEIFRASGEHVTDEEIESLMKDGDKNNDGRIDFDEFLKMMEGVQ |
establishment of protein localization to vacuole mitotic cytokinesis negative regulation of asexual reproduction negative regulation of proteolysis plasma membrane repair positive regulation of positive chemotaxis to cAMP positive regulation of sequestering of calcium ion protein export from nucleus regulation of sorocarp stalk cell differentiation | contractile vacuole; cytoplasm; extracellular matrix; extracellular space; nucleus | calcium ion binding calcium-dependent protein binding cell adhesion molecule binding cyclic nucleotide phosphodiesterase activator activity cyclic-nucleotide phosphodiesterase activity enzyme regulator activity kinase binding myosin I binding protein kinase binding protein kinase regulator activity troponin I binding | Dictyostelium discoideum | Acetylation Calcium Cell cycle Cell division Direct protein sequencing Metal-binding Reference proteome Repeat Vacuole | MASQESLTEE | MASQESLTEEQIAEFKEAFSLFDKDGDGSITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGNIDFPEFLTMMARKMQDTDTEEEIREAFKVFDKDGNGYISAAELRHVMTSLGEKLTNEEVDEMIREADLDGDGQVNYDEFVKMMIVRN | establishment of protein localization to vacuole mitotic cytokinesis negative regulation of asexual reproduction negative regulation of proteolysis plasma membrane repair positive regulation of positive chemotaxis to cAMP positive regulation of sequestering of calcium ion protein export from nucleus regulation of sorocarp stalk cell differentiation contractile vacuole; cytoplasm; extracellular matrix; extracellular space; nucleus calcium ion binding calcium-dependent protein binding cell adhesion molecule binding cyclic nucleotide phosphodiesterase activator activity cyclic-nucleotide phosphodiesterase activity enzyme regulator activity kinase binding myosin I binding protein kinase binding protein kinase regulator activity troponin I binding Dictyostelium discoideum Acetylation Calcium Cell cycle Cell division Direct protein sequencing Metal-binding Reference proteome Repeat Vacuole MASQESLTEE MASQESLTEEQIAEFKEAFSLFDKDGDGSITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGNIDFPEFLTMMARKMQDTDTEEEIREAFKVFDKDGNGYISAAELRHVMTSLGEKLTNEEVDEMIREADLDGDGQVNYDEFVKMMIVRN |
actomyosin structure organization myofibril assembly | actomyosin; cytosol; muscle myosin complex; myosin II complex; myosin II filament | ADP binding calcium ion binding magnesium ion binding microfilament motor activity myosin heavy chain binding myosin II binding structural constituent of muscle | Gallus gallus | 3D-structure Acetylation Alternative splicing Direct protein sequencing Motor protein Muscle protein Myosin Reference proteome Repeat | MCDFSEEQTA | MCDFSEEQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVMKVLGNPKSDEMNLKTLKFEQFLPMMQTIAKNKDQGCFEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEVEQLVAGHEDSNGCINYEELVRMVLSG | actomyosin structure organization myofibril assembly actomyosin; cytosol; muscle myosin complex; myosin II complex; myosin II filament ADP binding calcium ion binding magnesium ion binding microfilament motor activity myosin heavy chain binding myosin II binding structural constituent of muscle Gallus gallus 3D-structure Acetylation Alternative splicing Direct protein sequencing Motor protein Muscle protein Myosin Reference proteome Repeat MCDFSEEQTA MCDFSEEQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVMKVLGNPKSDEMNLKTLKFEQFLPMMQTIAKNKDQGCFEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEVEQLVAGHEDSNGCINYEELVRMVLSG |
muscle contraction skeletal muscle tissue development | cytoplasm; myosin complex | calcium ion binding | Gallus gallus | 3D-structure Calcium Direct protein sequencing Metal-binding Methylation Motor protein Muscle protein Myosin Phosphoprotein Reference proteome Repeat | MAPKKAKRRA | MAPKKAKRRAAEGSSNVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKDDLRETFAAMGRLNVKNEELDAMIKEASGPINFTVFLTMFGEKLKGADPEDVIMGAFKVLDPDGKGSIKKSFLEELLTTQCDRFTPEEIKNMWAAFPPDVAGNVDYKNICYVITHGEDKEGE | muscle contraction skeletal muscle tissue development cytoplasm; myosin complex calcium ion binding Gallus gallus 3D-structure Calcium Direct protein sequencing Metal-binding Methylation Motor protein Muscle protein Myosin Phosphoprotein Reference proteome Repeat MAPKKAKRRA MAPKKAKRRAAEGSSNVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKDDLRETFAAMGRLNVKNEELDAMIKEASGPINFTVFLTMFGEKLKGADPEDVIMGAFKVLDPDGKGSIKKSFLEELLTTQCDRFTPEEIKNMWAAFPPDVAGNVDYKNICYVITHGEDKEGE |
myofibril assembly | cytoplasm; muscle myosin complex; myofibril; stress fiber | calcium ion binding myosin II binding structural constituent of muscle | Gallus gallus | 3D-structure Acetylation Calcium Direct protein sequencing Metal-binding Motor protein Muscle protein Myosin Reference proteome Repeat | MSSKRAKAKT | MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASMGKNPTDEYLEGMMSEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD | myofibril assembly cytoplasm; muscle myosin complex; myofibril; stress fiber calcium ion binding myosin II binding structural constituent of muscle Gallus gallus 3D-structure Acetylation Calcium Direct protein sequencing Metal-binding Motor protein Muscle protein Myosin Reference proteome Repeat MSSKRAKAKT MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASMGKNPTDEYLEGMMSEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD |
cochlea development excitatory chemical synaptic transmission gene expression inhibitory chemical synaptic transmission | axon; cuticular plate; cytoplasm; neuronal cell body; protein-containing complex; stereocilium; terminal bouton | calcium ion binding identical protein binding protein-containing complex binding | Rattus norvegicus | 3D-structure Acetylation Calcium Direct protein sequencing Metal-binding Muscle protein Phosphoprotein Reference proteome Repeat | MSMTDLLSAE | MSMTDLLSAEDIKKAIGAFTAADSFDHKKFFQMVGLKKKSADDVKKVFHILDKDKSGFIEEDELGSILKGFSSDARDLSAKETKTLMAAGDKDGDGKIGVEEFSTLVAES | cochlea development excitatory chemical synaptic transmission gene expression inhibitory chemical synaptic transmission axon; cuticular plate; cytoplasm; neuronal cell body; protein-containing complex; stereocilium; terminal bouton calcium ion binding identical protein binding protein-containing complex binding Rattus norvegicus 3D-structure Acetylation Calcium Direct protein sequencing Metal-binding Muscle protein Phosphoprotein Reference proteome Repeat MSMTDLLSAE MSMTDLLSAEDIKKAIGAFTAADSFDHKKFFQMVGLKKKSADDVKKVFHILDKDKSGFIEEDELGSILKGFSSDARDLSAKETKTLMAAGDKDGDGKIGVEEFSTLVAES |
cochlea development response to wounding | cuticular plate; cytoplasm; extracellular space; protein-containing complex; stereocilium; supramolecular fiber; vesicle | calcium ion binding identical protein binding ion binding protein homodimerization activity protein-containing complex binding | Rattus norvegicus | 3D-structure Acetylation Calcium Direct protein sequencing Metal-binding Reference proteome Repeat | MSITDILSAE | MSITDILSAEDIAAALQECQDPDTFEPQKFFQTSGLSKMSASQVKDIFRFIDNDQSGYLDGDELKYFLQKFQSDARELTESETKSLMDAADNDGDGKIGADEFQEMVHS | cochlea development response to wounding cuticular plate; cytoplasm; extracellular space; protein-containing complex; stereocilium; supramolecular fiber; vesicle calcium ion binding identical protein binding ion binding protein homodimerization activity protein-containing complex binding Rattus norvegicus 3D-structure Acetylation Calcium Direct protein sequencing Metal-binding Reference proteome Repeat MSITDILSAE MSITDILSAEDIAAALQECQDPDTFEPQKFFQTSGLSKMSASQVKDIFRFIDNDQSGYLDGDELKYFLQKFQSDARELTESETKSLMDAADNDGDGKIGADEFQEMVHS |
adaptive thermogenesis astrocyte activation axonogenesis cell adhesion learning or memory negative regulation of monocyte chemotactic protein-1 production phosphorylation positive regulation of canonical NF-kappaB signal transduction positive regulation of cell population proliferation positive regulation of complement activation regulation of translation sympathetic neuron projection extension | cytoplasm; extracellular region; extracellular space; nucleus | calcium ion binding calcium-dependent protein binding kinase inhibitor activity protein homodimerization activity RAGE receptor binding S100 protein binding tau protein binding zinc ion binding | Bos taurus | 3D-structure Acetylation Calcium Cell adhesion Cytoplasm Direct protein sequencing Metal-binding Nucleus Reference proteome Repeat Secreted Zinc | MSELEKAVVA | MSELEKAVVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDSDGDGECDFQEFMAFVAMITTACHEFFEHE | adaptive thermogenesis astrocyte activation axonogenesis cell adhesion learning or memory negative regulation of monocyte chemotactic protein-1 production phosphorylation positive regulation of canonical NF-kappaB signal transduction positive regulation of cell population proliferation positive regulation of complement activation regulation of translation sympathetic neuron projection extension cytoplasm; extracellular region; extracellular space; nucleus calcium ion binding calcium-dependent protein binding kinase inhibitor activity protein homodimerization activity RAGE receptor binding S100 protein binding tau protein binding zinc ion binding Bos taurus 3D-structure Acetylation Calcium Cell adhesion Cytoplasm Direct protein sequencing Metal-binding Nucleus Reference proteome Repeat Secreted Zinc MSELEKAVVA MSELEKAVVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDSDGDGECDFQEFMAFVAMITTACHEFFEHE |
regulation of heart contraction | cytoplasm; mitochondrion; sarcoplasmic reticulum | calcium ion binding calcium-dependent protein binding S100 protein binding | Bos taurus | 3D-structure Calcium Cytoplasm Direct protein sequencing Metal-binding Mitochondrion Reference proteome Repeat S-nitrosylation Sarcoplasmic reticulum | MGSELETAME | MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDADAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS | regulation of heart contraction cytoplasm; mitochondrion; sarcoplasmic reticulum calcium ion binding calcium-dependent protein binding S100 protein binding Bos taurus 3D-structure Calcium Cytoplasm Direct protein sequencing Metal-binding Mitochondrion Reference proteome Repeat S-nitrosylation Sarcoplasmic reticulum MGSELETAME MGSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDADAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS |
actin filament capping actin filament depolymerization actin filament polymerization actin filament severing actin polymerization or depolymerization barbed-end actin filament capping cellular response to epidermal growth factor stimulus cellular response to hepatocyte growth factor stimulus cytoplasmic actin-based contraction involved in cell motility epidermal growth factor receptor signaling pathway positive regulation of actin filament bundle assembly positive regulation of cell migration positive regulation of epithelial cell migration regulation of actin nucleation regulation of cell shape regulation of lamellipodium morphogenesis regulation of wound healing response to bacterium | actin cytoskeleton; actin filament bundle; cytoplasm; filopodium; filopodium tip; lamellipodium; microvillus; ruffle | actin filament binding calcium ion binding cysteine-type endopeptidase inhibitor activity involved in apoptotic process lysophosphatidic acid binding phosphatidylinositol-4,5-bisphosphate binding protein homodimerization activity | Gallus gallus | 3D-structure Actin capping Actin-binding Calcium Cell projection Cytoplasm Cytoskeleton Direct protein sequencing Reference proteome Repeat | MVELSKKVTG | MVELSKKVTGKLDKTTPGIQIWRIENMEMVPVPTKSYGNFYEGDCYVLLSTRKTGSGFSYNIHYWLGKNSSQDEQGAAAIYTTQMDEYLGSVAVQHREVQGHESETFRAYFKQGLIYKQGGVASGMKHVETNTYNVQRLLHVKGKKNVVAAEVEMSWKSFNLGDVFLLDLGQLIIQWNGPESNRAERLRAMTLAKDIRDRERAGRAKVGVVEGENEAASPELMQALTHVLGEKKNIKAATPDEQVHQALNSALKLYHVSDASGNLVIQEVAIRPLTQDMLQHEDCYILDQAGLKIFVWKGKNANKEEKQQAMSRALGFIKAKNYLASTSVETENDGSESAVFRQLFQKWTVPNQTSGLGKTHTVGKVAKVEQVKFDATTMHVKPEVAAQQKMVDDGSGEAEVWRVENQELVPVEKRWLGHFYGGDCYLVLYTYYVGPKVNRIIYIWQGRHASTDELAASAYQAVFLDQKYNNEPVQVRVTMGKEPAHLMAIFKGKMVVYENGSSRAGGTEPASSTRLFHVHGTNEYNTKAFEVPVRAASLNSNDVFVLKTPSSCYLWYGKGCSGDEREMGKMVADIISKTEKPVVAEGQEPPEFWVALGGKTSYANSKRLQEENPSVPPRLFECSNKTGRFLATEIVDFTQDDLDENDVYLLDTWDQIFFWIGKGANESEKEAAAETAQEYLRSHPGSRDLDTPIIVVKQGFEPPTFTGWFMAWDPLCWSDRKSYDELKAELGDNASIGQLVSGLTSKNEVFTATTTLVPTKLETFPLDVLVNTAAEDLPRGVDPSRKENHLSDEDFKAVFGMTRSAFANLPLWKQQNLKKEKGLF | actin filament capping actin filament depolymerization actin filament polymerization actin filament severing actin polymerization or depolymerization barbed-end actin filament capping cellular response to epidermal growth factor stimulus cellular response to hepatocyte growth factor stimulus cytoplasmic actin-based contraction involved in cell motility epidermal growth factor receptor signaling pathway positive regulation of actin filament bundle assembly positive regulation of cell migration positive regulation of epithelial cell migration regulation of actin nucleation regulation of cell shape regulation of lamellipodium morphogenesis regulation of wound healing response to bacterium actin cytoskeleton; actin filament bundle; cytoplasm; filopodium; filopodium tip; lamellipodium; microvillus; ruffle actin filament binding calcium ion binding cysteine-type endopeptidase inhibitor activity involved in apoptotic process lysophosphatidic acid binding phosphatidylinositol-4,5-bisphosphate binding protein homodimerization activity Gallus gallus 3D-structure Actin capping Actin-binding Calcium Cell projection Cytoplasm Cytoskeleton Direct protein sequencing Reference proteome Repeat MVELSKKVTG MVELSKKVTGKLDKTTPGIQIWRIENMEMVPVPTKSYGNFYEGDCYVLLSTRKTGSGFSYNIHYWLGKNSSQDEQGAAAIYTTQMDEYLGSVAVQHREVQGHESETFRAYFKQGLIYKQGGVASGMKHVETNTYNVQRLLHVKGKKNVVAAEVEMSWKSFNLGDVFLLDLGQLIIQWNGPESNRAERLRAMTLAKDIRDRERAGRAKVGVVEGENEAASPELMQALTHVLGEKKNIKAATPDEQVHQALNSALKLYHVSDASGNLVIQEVAIRPLTQDMLQHEDCYILDQAGLKIFVWKGKNANKEEKQQAMSRALGFIKAKNYLASTSVETENDGSESAVFRQLFQKWTVPNQTSGLGKTHTVGKVAKVEQVKFDATTMHVKPEVAAQQKMVDDGSGEAEVWRVENQELVPVEKRWLGHFYGGDCYLVLYTYYVGPKVNRIIYIWQGRHASTDELAASAYQAVFLDQKYNNEPVQVRVTMGKEPAHLMAIFKGKMVVYENGSSRAGGTEPASSTRLFHVHGTNEYNTKAFEVPVRAASLNSNDVFVLKTPSSCYLWYGKGCSGDEREMGKMVADIISKTEKPVVAEGQEPPEFWVALGGKTSYANSKRLQEENPSVPPRLFECSNKTGRFLATEIVDFTQDDLDENDVYLLDTWDQIFFWIGKGANESEKEAAAETAQEYLRSHPGSRDLDTPIIVVKQGFEPPTFTGWFMAWDPLCWSDRKSYDELKAELGDNASIGQLVSGLTSKNEVFTATTTLVPTKLETFPLDVLVNTAAEDLPRGVDPSRKENHLSDEDFKAVFGMTRSAFANLPLWKQQNLKKEKGLF |
cholesterol metabolic process lipid transport lipoprotein metabolic process peptidyl-methionine modification phosphatidylcholine metabolic process positive regulation of cholesterol efflux positive regulation of phagocytosis positive regulation of phospholipid efflux protein oxidation protein stabilization regulation of intestinal cholesterol absorption | high-density lipoprotein particle | high-density lipoprotein particle receptor binding lipid binding protein homodimerization activity | Canis lupus familiaris | Cholesterol metabolism Direct protein sequencing Glycoprotein HDL Lipid metabolism Lipid transport Lipoprotein Oxidation Palmitate Phosphoprotein Reference proteome Repeat Secreted Signal Steroid metabolism Sterol metabolism Transport | MKAALLTLAV | MKAALLTLAVLFLTGSQARHFWQQDEPQSPWDRVKDLATVYVDAVKDSGRDYVAQFEASALGKQLNLKLLDNWDSLSSTVTKLREQIGPVTQEFWDNLEKETEVLRQEMSKDLEEVKQKVQPYLDDFQKKWQEEVELYRQKVAPLGSELREGARQKLQELQEKLSPLAEELRDRARTHVDALRAQLAPYSDDLRERLAARLEALKEGGGASLAEYHARASEQLSALGEKARPALEDLRQGLLPVLESFKVSLLAAIDEATKKLNAQ | cholesterol metabolic process lipid transport lipoprotein metabolic process peptidyl-methionine modification phosphatidylcholine metabolic process positive regulation of cholesterol efflux positive regulation of phagocytosis positive regulation of phospholipid efflux protein oxidation protein stabilization regulation of intestinal cholesterol absorption high-density lipoprotein particle high-density lipoprotein particle receptor binding lipid binding protein homodimerization activity Canis lupus familiaris Cholesterol metabolism Direct protein sequencing Glycoprotein HDL Lipid metabolism Lipid transport Lipoprotein Oxidation Palmitate Phosphoprotein Reference proteome Repeat Secreted Signal Steroid metabolism Sterol metabolism Transport MKAALLTLAV MKAALLTLAVLFLTGSQARHFWQQDEPQSPWDRVKDLATVYVDAVKDSGRDYVAQFEASALGKQLNLKLLDNWDSLSSTVTKLREQIGPVTQEFWDNLEKETEVLRQEMSKDLEEVKQKVQPYLDDFQKKWQEEVELYRQKVAPLGSELREGARQKLQELQEKLSPLAEELRDRARTHVDALRAQLAPYSDDLRERLAARLEALKEGGGASLAEYHARASEQLSALGEKARPALEDLRQGLLPVLESFKVSLLAAIDEATKKLNAQ |
cholesterol efflux cholesterol homeostasis cholesterol metabolic process high-density lipoprotein particle remodeling hydrogen peroxide catabolic process innate immune response in mucosa leukocyte cell-cell adhesion lipid catabolic process lipid homeostasis lipid transport lipoprotein metabolic process negative regulation of plasma lipoprotein oxidation peripheral nervous system axon regeneration phosphatidylcholine metabolic process phospholipid efflux positive regulation of fatty acid biosynthetic process positive regulation of triglyceride catabolic process protein-lipid complex assembly regulation of cholesterol transport regulation of intestinal cholesterol absorption removal of superoxide radicals response to food response to lipid hydroperoxide response to stilbenoid response to triglyceride reverse cholesterol transport triglyceride homeostasis very-low-density lipoprotein particle remodeling | cell surface; chylomicron; extracellular space; high-density lipoprotein particle; synapse; very-low-density lipoprotein particle | antioxidant activity cholesterol transfer activity copper ion binding identical protein binding lipid binding phosphatidylcholine binding phosphatidylcholine-sterol O-acyltransferase activator activity protein homodimerization activity | Rattus norvegicus | Chylomicron HDL Lipid transport Phosphoprotein Reference proteome Repeat Secreted Signal Transport | MFLKAVVLTV | MFLKAVVLTVALVAITGTQAEVTSDQVANVMWDYFTQLSNNAKEAVEQLQKTDVTQQLNTLFQDKLGNINTYADDLQNKLVPFAVQLSGHLTKETERVREEIQKELEDLRANMMPHANKVSQMFGDNVQKLQEHLRPYATDLQAQINAQTQDMKRQLTPYIQRMQTTIQDNVENLQSSMVPFANELKEKFNQNMEGLKGQLTPRANELKATIDQNLEDLRSRLAPLAEGVQEKLNHQMEGLAFQMKKNAEELQTKVSTNIDQLQKNLAPLVEDVQSKLKGNTEGLQKSLEDLNKQLDQQVEVFRRAVEPLGDKFNMALVQQMEKFRQQLGSDSGDVESHLSFLEKNLREKVSSFMSTLQKKGSPDQPLALPLPEQVQEQVQEQVQPKPLES | cholesterol efflux cholesterol homeostasis cholesterol metabolic process high-density lipoprotein particle remodeling hydrogen peroxide catabolic process innate immune response in mucosa leukocyte cell-cell adhesion lipid catabolic process lipid homeostasis lipid transport lipoprotein metabolic process negative regulation of plasma lipoprotein oxidation peripheral nervous system axon regeneration phosphatidylcholine metabolic process phospholipid efflux positive regulation of fatty acid biosynthetic process positive regulation of triglyceride catabolic process protein-lipid complex assembly regulation of cholesterol transport regulation of intestinal cholesterol absorption removal of superoxide radicals response to food response to lipid hydroperoxide response to stilbenoid response to triglyceride reverse cholesterol transport triglyceride homeostasis very-low-density lipoprotein particle remodeling cell surface; chylomicron; extracellular space; high-density lipoprotein particle; synapse; very-low-density lipoprotein particle antioxidant activity cholesterol transfer activity copper ion binding identical protein binding lipid binding phosphatidylcholine binding phosphatidylcholine-sterol O-acyltransferase activator activity protein homodimerization activity Rattus norvegicus Chylomicron HDL Lipid transport Phosphoprotein Reference proteome Repeat Secreted Signal Transport MFLKAVVLTV MFLKAVVLTVALVAITGTQAEVTSDQVANVMWDYFTQLSNNAKEAVEQLQKTDVTQQLNTLFQDKLGNINTYADDLQNKLVPFAVQLSGHLTKETERVREEIQKELEDLRANMMPHANKVSQMFGDNVQKLQEHLRPYATDLQAQINAQTQDMKRQLTPYIQRMQTTIQDNVENLQSSMVPFANELKEKFNQNMEGLKGQLTPRANELKATIDQNLEDLRSRLAPLAEGVQEKLNHQMEGLAFQMKKNAEELQTKVSTNIDQLQKNLAPLVEDVQSKLKGNTEGLQKSLEDLNKQLDQQVEVFRRAVEPLGDKFNMALVQQMEKFRQQLGSDSGDVESHLSFLEKNLREKVSSFMSTLQKKGSPDQPLALPLPEQVQEQVQEQVQPKPLES |
cholesterol homeostasis cholesterol metabolic process cholesterol transport high-density lipoprotein particle assembly high-density lipoprotein particle remodeling lipoprotein metabolic process low-density lipoprotein particle remodeling peptidyl-methionine modification positive regulation of interleukin-8 production positive regulation of phagocytosis protein oxidation protein stabilization triglyceride-rich lipoprotein particle remodeling | chylomicron; spherical high-density lipoprotein particle; very-low-density lipoprotein particle | apolipoprotein receptor binding cholesterol binding high-density lipoprotein particle binding high-density lipoprotein particle receptor binding lipase inhibitor activity phosphatidylcholine binding protein heterodimerization activity | Macaca mulatta | Direct protein sequencing HDL Lipid transport Oxidation Phosphoprotein Pyrrolidone carboxylic acid Reference proteome Secreted Transport | QAEEPSVESL | QAEEPSVESLVSQYFQTVTDYGKDLMEKVKSPELQAQAKAYFEKSKEQLTPLVKKAGTDLVNFLSYFVELRTQPATQ | cholesterol homeostasis cholesterol metabolic process cholesterol transport high-density lipoprotein particle assembly high-density lipoprotein particle remodeling lipoprotein metabolic process low-density lipoprotein particle remodeling peptidyl-methionine modification positive regulation of interleukin-8 production positive regulation of phagocytosis protein oxidation protein stabilization triglyceride-rich lipoprotein particle remodeling chylomicron; spherical high-density lipoprotein particle; very-low-density lipoprotein particle apolipoprotein receptor binding cholesterol binding high-density lipoprotein particle binding high-density lipoprotein particle receptor binding lipase inhibitor activity phosphatidylcholine binding protein heterodimerization activity Macaca mulatta Direct protein sequencing HDL Lipid transport Oxidation Phosphoprotein Pyrrolidone carboxylic acid Reference proteome Secreted Transport QAEEPSVESL QAEEPSVESLVSQYFQTVTDYGKDLMEKVKSPELQAQAKAYFEKSKEQLTPLVKKAGTDLVNFLSYFVELRTQPATQ |
cholesterol efflux cholesterol metabolic process chylomicron remnant clearance high-density lipoprotein particle remodeling lipid metabolic process lipoprotein metabolic process negative regulation of cholesterol transport negative regulation of fatty acid biosynthetic process negative regulation of lipid catabolic process negative regulation of lipid metabolic process negative regulation of lipoprotein lipase activity negative regulation of phosphatidylcholine catabolic process negative regulation of receptor-mediated endocytosis negative regulation of very-low-density lipoprotein particle clearance phospholipid efflux plasma lipoprotein particle remodeling regulation of cholesterol transport triglyceride metabolic process very-low-density lipoprotein particle assembly very-low-density lipoprotein particle clearance | chylomicron; endoplasmic reticulum; extracellular region; high-density lipoprotein particle; very-low-density lipoprotein particle | fatty acid binding lipase inhibitor activity phosphatidylcholine binding phosphatidylcholine-sterol O-acyltransferase activator activity phospholipase inhibitor activity | Homo sapiens | 3D-structure Direct protein sequencing Lipid transport Reference proteome Secreted Signal Transport VLDL | MRLFLSLPVL | MRLFLSLPVLVVVLSIVLEGPAPAQGTPDVSSALDKLKEFGNTLEDKARELISRIKQSELSAKMREWFSETFQKVKEKLKIDS | cholesterol efflux cholesterol metabolic process chylomicron remnant clearance high-density lipoprotein particle remodeling lipid metabolic process lipoprotein metabolic process negative regulation of cholesterol transport negative regulation of fatty acid biosynthetic process negative regulation of lipid catabolic process negative regulation of lipid metabolic process negative regulation of lipoprotein lipase activity negative regulation of phosphatidylcholine catabolic process negative regulation of receptor-mediated endocytosis negative regulation of very-low-density lipoprotein particle clearance phospholipid efflux plasma lipoprotein particle remodeling regulation of cholesterol transport triglyceride metabolic process very-low-density lipoprotein particle assembly very-low-density lipoprotein particle clearance chylomicron; endoplasmic reticulum; extracellular region; high-density lipoprotein particle; very-low-density lipoprotein particle fatty acid binding lipase inhibitor activity phosphatidylcholine binding phosphatidylcholine-sterol O-acyltransferase activator activity phospholipase inhibitor activity Homo sapiens 3D-structure Direct protein sequencing Lipid transport Reference proteome Secreted Signal Transport VLDL MRLFLSLPVL MRLFLSLPVLVVVLSIVLEGPAPAQGTPDVSSALDKLKEFGNTLEDKARELISRIKQSELSAKMREWFSETFQKVKEKLKIDS |
cholesterol efflux cholesterol homeostasis chylomicron remnant clearance chylomicron remodeling high-density lipoprotein particle clearance lipid catabolic process negative regulation of cholesterol transport negative regulation of lipid metabolic process negative regulation of receptor-mediated endocytosis negative regulation of very-low-density lipoprotein particle clearance phospholipid efflux positive regulation of fatty acid biosynthetic process positive regulation of lipoprotein lipase activity positive regulation of phospholipase activity positive regulation of phospholipid catabolic process positive regulation of triglyceride catabolic process positive regulation of very-low-density lipoprotein particle remodeling reverse cholesterol transport triglyceride homeostasis triglyceride-rich lipoprotein particle remodeling very-low-density lipoprotein particle remodeling | chylomicron; early endosome; extracellular region; extracellular space; intermediate-density lipoprotein particle; low-density lipoprotein particle; spherical high-density lipoprotein particle; very-low-density lipoprotein particle | lipase inhibitor activity lipid binding lipoprotein lipase activator activity molecular function activator activity phospholipase activator activity phospholipase binding | Homo sapiens | 3D-structure Chylomicron Direct protein sequencing Disease variant Glycoprotein HDL Hyperlipidemia LDL Lipid degradation Lipid metabolism Lipid transport Reference proteome Secreted Sialic acid Signal Transport VLDL | MGTRLLPALF | MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE | cholesterol efflux cholesterol homeostasis chylomicron remnant clearance chylomicron remodeling high-density lipoprotein particle clearance lipid catabolic process negative regulation of cholesterol transport negative regulation of lipid metabolic process negative regulation of receptor-mediated endocytosis negative regulation of very-low-density lipoprotein particle clearance phospholipid efflux positive regulation of fatty acid biosynthetic process positive regulation of lipoprotein lipase activity positive regulation of phospholipase activity positive regulation of phospholipid catabolic process positive regulation of triglyceride catabolic process positive regulation of very-low-density lipoprotein particle remodeling reverse cholesterol transport triglyceride homeostasis triglyceride-rich lipoprotein particle remodeling very-low-density lipoprotein particle remodeling chylomicron; early endosome; extracellular region; extracellular space; intermediate-density lipoprotein particle; low-density lipoprotein particle; spherical high-density lipoprotein particle; very-low-density lipoprotein particle lipase inhibitor activity lipid binding lipoprotein lipase activator activity molecular function activator activity phospholipase activator activity phospholipase binding Homo sapiens 3D-structure Chylomicron Direct protein sequencing Disease variant Glycoprotein HDL Hyperlipidemia LDL Lipid degradation Lipid metabolism Lipid transport Reference proteome Secreted Sialic acid Signal Transport VLDL MGTRLLPALF MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYEKTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE |
negative regulation of supramolecular fiber organization protein stabilization response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to growth hormone response to progesterone | extracellular space; Golgi apparatus; Golgi lumen | amyloid-beta binding antioxidant activity | Bos taurus | Allergen Antioxidant Direct protein sequencing Milk protein Phosphoprotein Reference proteome Repeat Secreted Signal | MKLLILTCLV | MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW | negative regulation of supramolecular fiber organization protein stabilization response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to growth hormone response to progesterone extracellular space; Golgi apparatus; Golgi lumen amyloid-beta binding antioxidant activity Bos taurus Allergen Antioxidant Direct protein sequencing Milk protein Phosphoprotein Reference proteome Repeat Secreted Signal MKLLILTCLV MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW |
defense response to bacterium response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to growth hormone response to progesterone | extracellular space; Golgi apparatus; Golgi lumen | protein homodimerization activity zymogen binding | Bos taurus | 3D-structure Antibiotic Antimicrobial Direct protein sequencing Milk protein Phosphoprotein Reference proteome Repeat Secreted Signal | MKFFIFTCLL | MKFFIFTCLLAVALAKNTMEHVSSSEESIISQETYKQEKNMAINPSKENLCSTFCKEVVRNANEEEYSIGSSSEESAEVATEEVKITVDDKHYQKALNEINQFYQKFPQYLQYLYQGPIVLNPWDQVKRNAVPITPTLNREQLSTSEENSKKTVDMESTEVFTKKTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQKAMKPWIQPKTKVIPYVRYL | defense response to bacterium response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to growth hormone response to progesterone extracellular space; Golgi apparatus; Golgi lumen protein homodimerization activity zymogen binding Bos taurus 3D-structure Antibiotic Antimicrobial Direct protein sequencing Milk protein Phosphoprotein Reference proteome Repeat Secreted Signal MKFFIFTCLL MKFFIFTCLLAVALAKNTMEHVSSSEESIISQETYKQEKNMAINPSKENLCSTFCKEVVRNANEEEYSIGSSSEESAEVATEEVKITVDDKHYQKALNEINQFYQKFPQYLQYLYQGPIVLNPWDQVKRNAVPITPTLNREQLSTSEENSKKTVDMESTEVFTKKTKLTEEEKNRLNFLKKISQRYQKFALPQYLKTVYQHQKAMKPWIQPKTKVIPYVRYL |
negative regulation of canonical NF-kappaB signal transduction negative regulation of cysteine-type endopeptidase activity negative regulation of inflammatory response negative regulation of lactation negative regulation of tumor necrosis factor-mediated signaling pathway regulation of blood pressure response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to heat response to progesterone | extracellular space; Golgi apparatus; Golgi lumen | antioxidant activity cysteine-type endopeptidase inhibitor activity ion binding metal ion binding metalloendopeptidase inhibitor activity potassium channel inhibitor activity protein homodimerization activity | Bos taurus | 3D-structure Antioxidant Direct protein sequencing Hypotensive agent Metalloenzyme inhibitor Metalloprotease inhibitor Milk protein Phosphoprotein Protease inhibitor Reference proteome Secreted Signal | MKVLILACLV | MKVLILACLVALALARELEELNVPGEIVESLSSSEESITRINKKIEKFQSEEQQQTEDELQDKIHPFAQTQSLVYPFPGPIPNSLPQNIPPLTQTPVVVPPFLQPEVMGVSKVKEAMAPKHKEMPFPKYPVEPFTESQSLTLTDVENLHLPLPLLQSWMHQPHQPLPPTVMFPPQSVLSLSQSKVLPVPQKAVPYPQRDMPIQAFLLYQEPVLGPVRGPFPIIV | negative regulation of canonical NF-kappaB signal transduction negative regulation of cysteine-type endopeptidase activity negative regulation of inflammatory response negative regulation of lactation negative regulation of tumor necrosis factor-mediated signaling pathway regulation of blood pressure response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to heat response to progesterone extracellular space; Golgi apparatus; Golgi lumen antioxidant activity cysteine-type endopeptidase inhibitor activity ion binding metal ion binding metalloendopeptidase inhibitor activity potassium channel inhibitor activity protein homodimerization activity Bos taurus 3D-structure Antioxidant Direct protein sequencing Hypotensive agent Metalloenzyme inhibitor Metalloprotease inhibitor Milk protein Phosphoprotein Protease inhibitor Reference proteome Secreted Signal MKVLILACLV MKVLILACLVALALARELEELNVPGEIVESLSSSEESITRINKKIEKFQSEEQQQTEDELQDKIHPFAQTQSLVYPFPGPIPNSLPQNIPPLTQTPVVVPPFLQPEVMGVSKVKEAMAPKHKEMPFPKYPVEPFTESQSLTLTDVENLHLPLPLLQSWMHQPHQPLPPTVMFPPQSVLSLSQSKVLPVPQKAVPYPQRDMPIQAFLLYQEPVLGPVRGPFPIIV |
lactation protein stabilization response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to progesterone | extracellular space; Golgi apparatus; Golgi lumen | identical protein binding zymogen binding | Bos taurus | Direct protein sequencing Disulfide bond Glycoprotein Milk protein Phosphoprotein Pyrrolidone carboxylic acid Reference proteome Secreted Signal | MMKSFFLVVT | MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTAV | lactation protein stabilization response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to progesterone extracellular space; Golgi apparatus; Golgi lumen identical protein binding zymogen binding Bos taurus Direct protein sequencing Disulfide bond Glycoprotein Milk protein Phosphoprotein Pyrrolidone carboxylic acid Reference proteome Secreted Signal MMKSFFLVVT MMKSFFLVVTILALTLPFLGAQEQNQEQPIRCEKDERFFSDKIAKYIPIQYVLSRYPSYGLNYYQQKPVALINNQFLPYPYYAKPAAVRSPAQILQWQVLSNTVPAKSCQAQPTTMARHPHPHLSFMAIPPKKNQDKTEIPTINTIASGEPTSTPTTEAVESTVATLEDSPEVIESPPEINTVQVTSTAV |
adaptive immune response blood coagulation, common pathway blood coagulation, fibrin clot formation cell-matrix adhesion fibrinolysis induction of bacterial agglutination innate immune response negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors plasminogen activation platelet aggregation positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion positive regulation of protein secretion positive regulation of substrate adhesion-dependent cell spreading positive regulation of vasoconstriction protein polymerization protein-containing complex assembly response to calcium ion | blood microparticle; cell surface; collagen-containing extracellular matrix; endoplasmic reticulum; endoplasmic reticulum lumen; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; extracellular vesicle; fibrinogen complex; plasma membrane; platelet alpha granule; platelet alpha granule lumen | extracellular matrix structural constituent metal ion binding signaling receptor binding structural molecule activity | Homo sapiens | 3D-structure Adaptive immunity Alternative splicing Amyloid Amyloidosis Blood coagulation Calcium Coiled coil Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemostasis Hydroxylation Immunity Innate immunity Isopeptide bond Metal-binding Phosphoprotein Reference proteome Secreted Signal | MFSMRIVCLV | MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ | adaptive immune response blood coagulation, common pathway blood coagulation, fibrin clot formation cell-matrix adhesion fibrinolysis induction of bacterial agglutination innate immune response negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors plasminogen activation platelet aggregation positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion positive regulation of protein secretion positive regulation of substrate adhesion-dependent cell spreading positive regulation of vasoconstriction protein polymerization protein-containing complex assembly response to calcium ion blood microparticle; cell surface; collagen-containing extracellular matrix; endoplasmic reticulum; endoplasmic reticulum lumen; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; extracellular vesicle; fibrinogen complex; plasma membrane; platelet alpha granule; platelet alpha granule lumen extracellular matrix structural constituent metal ion binding signaling receptor binding structural molecule activity Homo sapiens 3D-structure Adaptive immunity Alternative splicing Amyloid Amyloidosis Blood coagulation Calcium Coiled coil Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemostasis Hydroxylation Immunity Innate immunity Isopeptide bond Metal-binding Phosphoprotein Reference proteome Secreted Signal MFSMRIVCLV MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTATWKPGSSGPGSTGSWNSGSSGTGSTGNQNPGSPRPGSTGTWNPGSSERGSAGHWTSESSVSGSTGQWHSESGSFRPDSPGSGNARPNNPDWGTFEEVSGNVSPGTRREYHTEKLVTSKGDKELRTGKEKVTSGSTTTTRRSCSKTVTKTVIGPDGHKEVTKEVVTSEDGSDCPEAMDLGTLSGIGTLDGFRHRHPDEAAFFDTASTGKTFPGFFSPMLGEFVSETESRGSESGIFTNTKESSSHHPGIAEFPSRGKSSSYSKQFTSSTSYNRGDSTFESKSYKMADEAGSEADHEGTHSTKRGHAKSRPVRDCDDVLQTHPSGTQSGIFNIKLPGSSKIFSVYCDQETSLGGWLLIQQRMDGSLNFNRTWQDYKRGFGSLNDEGEGEFWLGNDYLHLLTQRGSVLRVELEDWAGNEAYAEYHFRVGSEAEGYALQVSSYEGTAGDALIEGSVEEGAEYTSHNNMQFSTFDRDADQWEENCAEVYGGGWWYNNCQAANLNGIYYPGGSYDPRNNSPYEIENGVVWVSFRGADYSLRAVRMKIRPLVTQ |
adaptive immune response blood coagulation, common pathway fibrinolysis innate immune response negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors platelet aggregation positive regulation of ERK1 and ERK2 cascade positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion protein polymerization | fibrinogen complex | signaling receptor binding | Bos taurus | 3D-structure Adaptive immunity Blood coagulation Coiled coil Direct protein sequencing Disulfide bond Glycoprotein Hemostasis Immunity Innate immunity Reference proteome Secreted Signal | MFSVRDLCLV | MFSVRDLCLVLSLVGAIKTEDGSDPPSGDFLTEGGGVRGPRLVERQQSACKETGWPFCSDEDWNTKCPSGCRMKGLIDEVDQDFTSRINKLRDSLFNYQKNSKDSNTLTKNIVELMRGDFAKANNNDNTFKQISEDLRSRIEILRRKVIEQVQRIKVLQKNVRDQLVDMKRLEVDIDIKIRSCKGSCSRALEHKVDLEDYKNQQKQLEQVIAINLLPSRDIQYLPLIKMSTITGPVPREFKSQLQEAPLEWKALLEMQQTKMVLETFGGDGHARGDSVSQGTGLAPGSPRKPGTSSIGNVNPGSYGPGSSGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNTGSSGSSSFRPDSSGHGNIRPSSPDWGTFREEGSVSSGTKQEFHTGKLVTTKGDKELLIDNEKVTSGHTTTTRRSCSKVITKTVTNADGRTETTKEVVKSEDGSDCGDADFDWHHTFPSRGNLDDFFHRDKDDFFTRSSHEFDGRTGLAPEFAALGESGSSSSKTSTHSKQFVSSSTTVNRGGSAIESKHFKMEDEAESLEDLGFKGAHGTQKGHTKARPARGIHTSPLGEPSLTP | adaptive immune response blood coagulation, common pathway fibrinolysis innate immune response negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors platelet aggregation positive regulation of ERK1 and ERK2 cascade positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion protein polymerization fibrinogen complex signaling receptor binding Bos taurus 3D-structure Adaptive immunity Blood coagulation Coiled coil Direct protein sequencing Disulfide bond Glycoprotein Hemostasis Immunity Innate immunity Reference proteome Secreted Signal MFSVRDLCLV MFSVRDLCLVLSLVGAIKTEDGSDPPSGDFLTEGGGVRGPRLVERQQSACKETGWPFCSDEDWNTKCPSGCRMKGLIDEVDQDFTSRINKLRDSLFNYQKNSKDSNTLTKNIVELMRGDFAKANNNDNTFKQISEDLRSRIEILRRKVIEQVQRIKVLQKNVRDQLVDMKRLEVDIDIKIRSCKGSCSRALEHKVDLEDYKNQQKQLEQVIAINLLPSRDIQYLPLIKMSTITGPVPREFKSQLQEAPLEWKALLEMQQTKMVLETFGGDGHARGDSVSQGTGLAPGSPRKPGTSSIGNVNPGSYGPGSSGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNPGRPEPGSAGTWNTGSSGSSSFRPDSSGHGNIRPSSPDWGTFREEGSVSSGTKQEFHTGKLVTTKGDKELLIDNEKVTSGHTTTTRRSCSKVITKTVTNADGRTETTKEVVKSEDGSDCGDADFDWHHTFPSRGNLDDFFHRDKDDFFTRSSHEFDGRTGLAPEFAALGESGSSSSKTSTHSKQFVSSSTTVNRGGSAIESKHFKMEDEAESLEDLGFKGAHGTQKGHTKARPARGIHTSPLGEPSLTP |
platelet activation protein polymerization | fibrinogen complex | signaling receptor binding | Petromyzon marinus | 3D-structure Blood coagulation Coiled coil Direct protein sequencing Disulfide bond Hemostasis Repeat Secreted Signal | QVCIADDISL | QVCIADDISLRGPRLTEQRSAGQGSCASATADLCVHGDWGRKCPNGCRMQGLMSHAEKDIGKRIGDLTERLARLGRLYTQVHTDFRAVSDTSGQTLNEHNELEVRYSEVLRELERRIIHLQRRINMQLQQLTLLQHNIKTQVSQILRVEVDIDVALRTCKGSCARYLEYRLDKEKNLQLEKAASYIANLKFERFEEVVVEETLNRRVETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVPHRQPTYVDHGRLSNPNEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFHDESTPGNGPRDEAAASSSAHSPSTASHDTATSTTSFSSGTSGKDVAPLGTGVTHDGGVRTSGSLMDGGSSDTGTGGVSKTTTFTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQGGGGYAAGGTGAQTGSGSTSTHSAHSASGGMSSLDMLPALPDFGTWDMPDHSDIFSRRRVSTSSTTSSSSGGGHAGAAAGGGGDGASRFGSLFTTDFGPEFHEEFRSMLPGASRLSSSSSSSTRSTSSTSGGKVVTESVVTKVLSNGTTITHHTKHVSTSDGTGAASDGVSPLLTGRKTKAARSRRAKATRP | platelet activation protein polymerization fibrinogen complex signaling receptor binding Petromyzon marinus 3D-structure Blood coagulation Coiled coil Direct protein sequencing Disulfide bond Hemostasis Repeat Secreted Signal QVCIADDISL QVCIADDISLRGPRLTEQRSAGQGSCASATADLCVHGDWGRKCPNGCRMQGLMSHAEKDIGKRIGDLTERLARLGRLYTQVHTDFRAVSDTSGQTLNEHNELEVRYSEVLRELERRIIHLQRRINMQLQQLTLLQHNIKTQVSQILRVEVDIDVALRTCKGSCARYLEYRLDKEKNLQLEKAASYIANLKFERFEEVVVEETLNRRVETSSHAFQPTHGQGTPQPGHGTHSLSATSSITSAPNFVPHRQPTYVDHGRLSNPNEVAHSASSSSTHTSSSSSPSQPVSRDSAFPLPGSNTGTSEWDFNFHDESTPGNGPRDEAAASSSAHSPSTASHDTATSTTSFSSGTSGKDVAPLGTGVTHDGGVRTSGSLMDGGSSDTGTGGVSKTTTFTGSAQGGSWSTGGSTATNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAKGGSWSTGGRTEPNTGSAKGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSGQGGSWSTGGRTEPNTGSGQGGSWGTGGRTEPNTGSAQGGSWGTGGRTEPNTGSAQGGSWGTGGSTATNTGSAQGGGGYAAGGTGAQTGSGSTSTHSAHSASGGMSSLDMLPALPDFGTWDMPDHSDIFSRRRVSTSSTTSSSSGGGHAGAAAGGGGDGASRFGSLFTTDFGPEFHEEFRSMLPGASRLSSSSSSSTRSTSSTSGGKVVTESVVTKVLSNGTTITHHTKHVSTSDGTGAASDGVSPLLTGRKTKAARSRRAKATRP |
adaptive immune response blood coagulation, fibrin clot formation cell-matrix adhesion cellular response to interleukin-1 cellular response to leptin stimulus fibrinolysis induction of bacterial agglutination innate immune response negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors plasminogen activation platelet aggregation positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion positive regulation of protein secretion positive regulation of substrate adhesion-dependent cell spreading positive regulation of vasoconstriction protein polymerization protein-containing complex assembly response to calcium ion | blood microparticle; cell cortex; cell surface; collagen-containing extracellular matrix; endoplasmic reticulum; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; extracellular vesicle; fibrinogen complex; plasma membrane; platelet alpha granule; platelet alpha granule lumen; synapse | extracellular matrix structural constituent protein-folding chaperone binding signaling receptor binding structural molecule activity | Homo sapiens | 3D-structure Adaptive immunity Blood coagulation Coiled coil Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemostasis Immunity Innate immunity Pyrrolidone carboxylic acid Reference proteome Secreted Signal | MKRMVSWSFH | MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ | adaptive immune response blood coagulation, fibrin clot formation cell-matrix adhesion cellular response to interleukin-1 cellular response to leptin stimulus fibrinolysis induction of bacterial agglutination innate immune response negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors plasminogen activation platelet aggregation positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion positive regulation of protein secretion positive regulation of substrate adhesion-dependent cell spreading positive regulation of vasoconstriction protein polymerization protein-containing complex assembly response to calcium ion blood microparticle; cell cortex; cell surface; collagen-containing extracellular matrix; endoplasmic reticulum; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; extracellular vesicle; fibrinogen complex; plasma membrane; platelet alpha granule; platelet alpha granule lumen; synapse extracellular matrix structural constituent protein-folding chaperone binding signaling receptor binding structural molecule activity Homo sapiens 3D-structure Adaptive immunity Blood coagulation Coiled coil Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemostasis Immunity Innate immunity Pyrrolidone carboxylic acid Reference proteome Secreted Signal MKRMVSWSFH MKRMVSWSFHKLKTMKHLLLLLLCVFLVKSQGVNDNEEGFFSARGHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ |
adaptive immune response blood coagulation, fibrin clot formation cell-matrix adhesion innate immune response platelet aggregation protein polymerization | collagen-containing extracellular matrix; extracellular space; fibrinogen complex | signaling receptor binding | Bos taurus | 3D-structure Adaptive immunity Blood coagulation Coiled coil Direct protein sequencing Disulfide bond Glycoprotein Hemostasis Immunity Innate immunity Pyrrolidone carboxylic acid Reference proteome Secreted Sulfation | QFPTDYDEGQ | QFPTDYDEGQDDRPKVGLGARGHRPYDKKKEEAPSLRPVPPPISGGGYRARPATATVGQKKVERKPPDADGCLHADPDLGVLCPTGCKLQDTLVRQERPIRKSIEDLRNTVDSVSRTSSSTFQYITLLKNMWKGRQNQVQDNENVVNEYSSHLEKHQLYIDETVKNNIPTKLRVLRSILENLRSKIQKLESDVSTQMEYCRTPCTVTCNIPVVSGKECEKIIRNEGETSEMYLIQPEDSSKPYRVYCDMKTEKGGWTVIQNRQDGSVDFGRKWDPYKQGFGNIATNAEGKKYCGVPGEYWLGNDRISQLTNMGPTKLLIEMEDWKGDKVTALYEGFTVQNEANKYQLSVSKYKGTAGNALIEGASQLVGENRTMTIHNSMFFSTYDRDNDGWKTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGAYTWDMAKHGTDDGVVWMNWQGSWYSMKKMSMKIRPYFPEQ | adaptive immune response blood coagulation, fibrin clot formation cell-matrix adhesion innate immune response platelet aggregation protein polymerization collagen-containing extracellular matrix; extracellular space; fibrinogen complex signaling receptor binding Bos taurus 3D-structure Adaptive immunity Blood coagulation Coiled coil Direct protein sequencing Disulfide bond Glycoprotein Hemostasis Immunity Innate immunity Pyrrolidone carboxylic acid Reference proteome Secreted Sulfation QFPTDYDEGQ QFPTDYDEGQDDRPKVGLGARGHRPYDKKKEEAPSLRPVPPPISGGGYRARPATATVGQKKVERKPPDADGCLHADPDLGVLCPTGCKLQDTLVRQERPIRKSIEDLRNTVDSVSRTSSSTFQYITLLKNMWKGRQNQVQDNENVVNEYSSHLEKHQLYIDETVKNNIPTKLRVLRSILENLRSKIQKLESDVSTQMEYCRTPCTVTCNIPVVSGKECEKIIRNEGETSEMYLIQPEDSSKPYRVYCDMKTEKGGWTVIQNRQDGSVDFGRKWDPYKQGFGNIATNAEGKKYCGVPGEYWLGNDRISQLTNMGPTKLLIEMEDWKGDKVTALYEGFTVQNEANKYQLSVSKYKGTAGNALIEGASQLVGENRTMTIHNSMFFSTYDRDNDGWKTTDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGAYTWDMAKHGTDDGVVWMNWQGSWYSMKKMSMKIRPYFPEQ |
blood coagulation, fibrin clot formation cell-matrix adhesion cellular response to interleukin-1 cellular response to interleukin-6 fibrinolysis negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors plasminogen activation platelet aggregation platelet maturation positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion positive regulation of protein secretion positive regulation of substrate adhesion-dependent cell spreading positive regulation of vasoconstriction protein polymerization protein secretion protein-containing complex assembly response to calcium ion | blood microparticle; cell surface; collagen-containing extracellular matrix; endoplasmic reticulum lumen; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; fibrinogen complex; plasma membrane; platelet alpha granule; platelet alpha granule lumen | cell adhesion molecule binding extracellular matrix structural constituent identical protein binding metal ion binding signaling receptor binding structural molecule activity | Homo sapiens | 3D-structure Alternative splicing Blood coagulation Calcium Coiled coil Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemostasis Isopeptide bond Metal-binding Phosphoprotein Reference proteome Secreted Signal Sulfation | MSWSLHPRNL | MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL | blood coagulation, fibrin clot formation cell-matrix adhesion cellular response to interleukin-1 cellular response to interleukin-6 fibrinolysis negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors plasminogen activation platelet aggregation platelet maturation positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion positive regulation of protein secretion positive regulation of substrate adhesion-dependent cell spreading positive regulation of vasoconstriction protein polymerization protein secretion protein-containing complex assembly response to calcium ion blood microparticle; cell surface; collagen-containing extracellular matrix; endoplasmic reticulum lumen; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; fibrinogen complex; plasma membrane; platelet alpha granule; platelet alpha granule lumen cell adhesion molecule binding extracellular matrix structural constituent identical protein binding metal ion binding signaling receptor binding structural molecule activity Homo sapiens 3D-structure Alternative splicing Blood coagulation Calcium Coiled coil Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemostasis Isopeptide bond Metal-binding Phosphoprotein Reference proteome Secreted Signal Sulfation MSWSLHPRNL MSWSLHPRNLILYFYALLFLSSTCVAYVATRDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKTSEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHDSSIRYLQEIYNSNNQKIVNLKEKVAQLEAQCQEPCKDTVQIHDITGKDCQDIANKGAKQSGLYFIKPLKANQQFLVYCEIDGSGNGWTVFQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISTQSAIPYALRVELEDWNGRTSTADYAMFKVGPEADKYRLTYAYFAGGDAGDAFDGFDFGDDPSDKFFTSHNGMQFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKASTPNGYDNGIIWATWKTRWYSMKKTTMKIIPFNRLTIGEGQQHHLGGAKQVRPEHPAETEYDSLYPEDDL |
blood coagulation, fibrin clot formation cell-matrix adhesion cellular response to interleukin-1 cellular response to interleukin-6 fibrinolysis negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors plasminogen activation platelet aggregation platelet maturation positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion positive regulation of protein secretion positive regulation of vasoconstriction protein polymerization protein secretion protein-containing complex assembly response to calcium ion | blood microparticle; cell cortex; cell surface; collagen-containing extracellular matrix; external side of plasma membrane; extracellular space; fibrinogen complex; platelet alpha granule; synapse | cell adhesion molecule binding identical protein binding metal ion binding signaling receptor binding structural molecule activity | Rattus norvegicus | Alternative splicing Blood coagulation Calcium Coiled coil Direct protein sequencing Disulfide bond Glycoprotein Hemostasis Isopeptide bond Metal-binding Phosphoprotein Reference proteome Secreted Signal | MNWSLQLRSF | MNWSLQLRSFILCWALLLLSPTGLAQYTATRDNCCILDERFGSYCPTTCGISDFLNSYQTDVDTDLQTLENILQRAENRTTEAKELIKAIQVYYNPDQPPKPGMIEGATQKSKKMVEEILKYEALLLTHESSIRYLQDIYTSNKQKITNLKQKVAQLEAQCQEPCKDSVRIHDTTGKDCQDIANKGAKESGLYFIRPLKATQQFLVYCEIDGSGNGWTVLQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWSGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMHFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKSSTPNGYDNGIIWATWKTRWYSMKETTMKIIPFNRLSIGDGQQHHMGGSKQVSVEHEVDVEYP | blood coagulation, fibrin clot formation cell-matrix adhesion cellular response to interleukin-1 cellular response to interleukin-6 fibrinolysis negative regulation of endothelial cell apoptotic process negative regulation of extrinsic apoptotic signaling pathway via death domain receptors plasminogen activation platelet aggregation platelet maturation positive regulation of ERK1 and ERK2 cascade positive regulation of exocytosis positive regulation of heterotypic cell-cell adhesion positive regulation of peptide hormone secretion positive regulation of protein secretion positive regulation of vasoconstriction protein polymerization protein secretion protein-containing complex assembly response to calcium ion blood microparticle; cell cortex; cell surface; collagen-containing extracellular matrix; external side of plasma membrane; extracellular space; fibrinogen complex; platelet alpha granule; synapse cell adhesion molecule binding identical protein binding metal ion binding signaling receptor binding structural molecule activity Rattus norvegicus Alternative splicing Blood coagulation Calcium Coiled coil Direct protein sequencing Disulfide bond Glycoprotein Hemostasis Isopeptide bond Metal-binding Phosphoprotein Reference proteome Secreted Signal MNWSLQLRSF MNWSLQLRSFILCWALLLLSPTGLAQYTATRDNCCILDERFGSYCPTTCGISDFLNSYQTDVDTDLQTLENILQRAENRTTEAKELIKAIQVYYNPDQPPKPGMIEGATQKSKKMVEEILKYEALLLTHESSIRYLQDIYTSNKQKITNLKQKVAQLEAQCQEPCKDSVRIHDTTGKDCQDIANKGAKESGLYFIRPLKATQQFLVYCEIDGSGNGWTVLQKRLDGSVDFKKNWIQYKEGFGHLSPTGTTEFWLGNEKIHLISMQSTIPYALRIQLKDWSGRTSTADYAMFRVGPESDKYRLTYAYFIGGDAGDAFDGYDFGDDPSDKFFTSHNGMHFSTWDNDNDKFEGNCAEQDGSGWWMNKCHAGHLNGVYYQGGTYSKSSTPNGYDNGIIWATWKTRWYSMKETTMKIIPFNRLSIGDGQQHHMGGSKQVSVEHEVDVEYP |
amyloid precursor protein metabolic process apoptotic process clathrin coat assembly dopamine receptor signaling pathway endosomal transport neurotransmitter receptor cycle neurotransmitter receptor transport, endosome to postsynaptic membrane positive regulation of receptor recycling postsynaptic neurotransmitter receptor cycle receptor recycling regulation of long-term synaptic potentiation spontaneous synaptic transmission vesicle-mediated transport in synapse | dendrite; early endosome; early endosome membrane; endoplasmic reticulum; endoplasmic reticulum membrane; endosome; glutamatergic synapse; Golgi cisterna membrane; late endosome; lateral plasma membrane; lysosomal lumen; multivesicular body membrane; postsynaptic endosome; postsynaptic membrane; recycling endosome membrane; somatodendritic compartment; synapse; trans-Golgi network membrane | clathrin light chain binding ionotropic glutamate receptor binding signaling receptor binding | Rattus norvegicus | Cell projection Cytoplasmic vesicle Endoplasmic reticulum Endosome Golgi apparatus Lysosome Membrane Reference proteome Signal-anchor Transmembrane Transmembrane helix | MVKLGNNFAE | MVKLGNNFAEKGTKQPLLEDGFDTIPLMTPLDVNQLQFPPPDKVVVKTKTEYEPDRKKGKARPPKIAEFTVSITEGVTERFKVSVLVLFALAFLTCVVFLVVYKVYKYDRACPDGFVLKNTQCIPEGLESYYTEQDSSAREKFYTVINHYNLAKQSITRSVSPWMSVLSEEKLSEQETEAAEKSA | amyloid precursor protein metabolic process apoptotic process clathrin coat assembly dopamine receptor signaling pathway endosomal transport neurotransmitter receptor cycle neurotransmitter receptor transport, endosome to postsynaptic membrane positive regulation of receptor recycling postsynaptic neurotransmitter receptor cycle receptor recycling regulation of long-term synaptic potentiation spontaneous synaptic transmission vesicle-mediated transport in synapse dendrite; early endosome; early endosome membrane; endoplasmic reticulum; endoplasmic reticulum membrane; endosome; glutamatergic synapse; Golgi cisterna membrane; late endosome; lateral plasma membrane; lysosomal lumen; multivesicular body membrane; postsynaptic endosome; postsynaptic membrane; recycling endosome membrane; somatodendritic compartment; synapse; trans-Golgi network membrane clathrin light chain binding ionotropic glutamate receptor binding signaling receptor binding Rattus norvegicus Cell projection Cytoplasmic vesicle Endoplasmic reticulum Endosome Golgi apparatus Lysosome Membrane Reference proteome Signal-anchor Transmembrane Transmembrane helix MVKLGNNFAE MVKLGNNFAEKGTKQPLLEDGFDTIPLMTPLDVNQLQFPPPDKVVVKTKTEYEPDRKKGKARPPKIAEFTVSITEGVTERFKVSVLVLFALAFLTCVVFLVVYKVYKYDRACPDGFVLKNTQCIPEGLESYYTEQDSSAREKFYTVINHYNLAKQSITRSVSPWMSVLSEEKLSEQETEAAEKSA |
axon ensheathment central nervous system development chemical synaptic transmission immune response maintenance of blood-brain barrier MAPK cascade membrane organization myelination negative regulation of heterotypic cell-cell adhesion positive regulation of chemokine (C-X-C motif) ligand 2 production positive regulation of interleukin-6 production positive regulation of metalloendopeptidase activity response to toxic substance sensory perception of sound substantia nigra development | cell periphery; cell surface; compact myelin; cytosol; internode region of axon; myelin sheath; neuronal cell body; nucleus; plasma membrane; protein-containing complex; synapse | calmodulin binding lipid binding protease binding structural constituent of myelin sheath | Homo sapiens | 3D-structure Acetylation Alternative splicing Autoimmune encephalomyelitis Cell membrane Citrullination Direct protein sequencing Membrane Methylation Nucleus Phosphoprotein Reference proteome | MGNHAGKREL | MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR | axon ensheathment central nervous system development chemical synaptic transmission immune response maintenance of blood-brain barrier MAPK cascade membrane organization myelination negative regulation of heterotypic cell-cell adhesion positive regulation of chemokine (C-X-C motif) ligand 2 production positive regulation of interleukin-6 production positive regulation of metalloendopeptidase activity response to toxic substance sensory perception of sound substantia nigra development cell periphery; cell surface; compact myelin; cytosol; internode region of axon; myelin sheath; neuronal cell body; nucleus; plasma membrane; protein-containing complex; synapse calmodulin binding lipid binding protease binding structural constituent of myelin sheath Homo sapiens 3D-structure Acetylation Alternative splicing Autoimmune encephalomyelitis Cell membrane Citrullination Direct protein sequencing Membrane Methylation Nucleus Phosphoprotein Reference proteome MGNHAGKREL MGNHAGKRELNAEKASTNSETNRGESEKKRNLGELSRTTSEDNEVFGEADANQNNGTSSQDTAVTDSKRTADPKNAWQDAHPADPGSRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDSAATSESLDVMASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFGGDRGAPKRGSGKDSHHPARTAHYGSLPQKSHGRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQRPGFGYGGRASDYKSAHKGFKGVDAQGTLSKIFKLGGRDSRSGSPMARR |
myelination | cell periphery; compact myelin; internode region of axon; myelin sheath; neuronal cell body; plasma membrane; protein-containing complex | calmodulin binding lipid binding phospholipid binding structural constituent of myelin sheath | Bos taurus | Acetylation Autoimmune encephalomyelitis Cell membrane Citrullination Direct protein sequencing Membrane Methylation Phosphoprotein Reference proteome | AAQKRPSQRS | AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR | myelination cell periphery; compact myelin; internode region of axon; myelin sheath; neuronal cell body; plasma membrane; protein-containing complex calmodulin binding lipid binding phospholipid binding structural constituent of myelin sheath Bos taurus Acetylation Autoimmune encephalomyelitis Cell membrane Citrullination Direct protein sequencing Membrane Methylation Phosphoprotein Reference proteome AAQKRPSQRS AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR |
maintenance of blood-brain barrier MAPK cascade membrane organization myelination negative regulation of axonogenesis negative regulation of heterotypic cell-cell adhesion positive regulation of chemokine (C-X-C motif) ligand 2 production positive regulation of interleukin-6 production response to fatty acid response to mercury ion response to progesterone response to toxic substance response to tumor necrosis factor sensory perception of sound | cell periphery; cell projection; cell surface; compact myelin; internode region of axon; myelin sheath; neuronal cell body; plasma membrane; protein-containing complex | calmodulin binding protease binding structural constituent of myelin sheath | Rattus norvegicus | Acetylation Alternative splicing Autoimmune encephalomyelitis Cell membrane Citrullination Direct protein sequencing Membrane Methylation Phosphoprotein Reference proteome | MASQKRPSQR | MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKVPWLKQSRSPLPSHARSRPGLCHMYKDSHTRTTHYGSLPQKSQRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR | maintenance of blood-brain barrier MAPK cascade membrane organization myelination negative regulation of axonogenesis negative regulation of heterotypic cell-cell adhesion positive regulation of chemokine (C-X-C motif) ligand 2 production positive regulation of interleukin-6 production response to fatty acid response to mercury ion response to progesterone response to toxic substance response to tumor necrosis factor sensory perception of sound cell periphery; cell projection; cell surface; compact myelin; internode region of axon; myelin sheath; neuronal cell body; plasma membrane; protein-containing complex calmodulin binding protease binding structural constituent of myelin sheath Rattus norvegicus Acetylation Alternative splicing Autoimmune encephalomyelitis Cell membrane Citrullination Direct protein sequencing Membrane Methylation Phosphoprotein Reference proteome MASQKRPSQR MASQKRPSQRHGSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKVPWLKQSRSPLPSHARSRPGLCHMYKDSHTRTTHYGSLPQKSQRTQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKLGGRDSRSGSPMARR |
fatty acid transport membrane organization | cytosol; extracellular exosome; myelin sheath; nucleus | cholesterol binding fatty acid binding | Homo sapiens | 3D-structure Acetylation Charcot-Marie-Tooth disease Cytoplasm Direct protein sequencing Disease variant Disulfide bond Lipid-binding Neurodegeneration Neuropathy Reference proteome Transport | MSNKFLGTWK | MSNKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKSIVTLQRGSLNQVQRWDGKETTIKRKLVNGKMVAECKMKGVVCTRIYEKV | fatty acid transport membrane organization cytosol; extracellular exosome; myelin sheath; nucleus cholesterol binding fatty acid binding Homo sapiens 3D-structure Acetylation Charcot-Marie-Tooth disease Cytoplasm Direct protein sequencing Disease variant Disulfide bond Lipid-binding Neurodegeneration Neuropathy Reference proteome Transport MSNKFLGTWK MSNKFLGTWKLVSSENFDDYMKALGVGLATRKLGNLAKPTVIISKKGDIITIRTESTFKNTEISFKLGQEFEETTADNRKTKSIVTLQRGSLNQVQRWDGKETTIKRKLVNGKMVAECKMKGVVCTRIYEKV |
fatty acid transport membrane organization | cytosol; myelin sheath; nucleus | cholesterol binding fatty acid binding | Bos taurus | 3D-structure Acetylation Cytoplasm Direct protein sequencing Disulfide bond Lipid-binding Reference proteome Transport | MSNKFLGTWK | MSNKFLGTWKLVSSENFDEYMKALGVGLATRKLGNLAKPRVIISKKGDIITIRTESPFKNTEISFKLGQEFEETTADNRKTKSTVTLARGSLNQVQKWDGNETTIKRKLVDGKMVVECKMKDVVCTRIYEKV | fatty acid transport membrane organization cytosol; myelin sheath; nucleus cholesterol binding fatty acid binding Bos taurus 3D-structure Acetylation Cytoplasm Direct protein sequencing Disulfide bond Lipid-binding Reference proteome Transport MSNKFLGTWK MSNKFLGTWKLVSSENFDEYMKALGVGLATRKLGNLAKPRVIISKKGDIITIRTESPFKNTEISFKLGQEFEETTADNRKTKSTVTLARGSLNQVQKWDGNETTIKRKLVDGKMVVECKMKDVVCTRIYEKV |
cellular response to hydrogen peroxide cellular response to hypoxia fatty acid transport intestinal absorption long-chain fatty acid transport negative regulation of apoptotic process positive regulation of fatty acid beta-oxidation response to vitamin B3 | apical cortex; cytoplasm; cytosol; nucleoplasm; nucleus; peroxisomal matrix; protein-containing complex | antioxidant activity bile acid binding chromatin binding fatty acid binding heterocyclic compound binding long-chain fatty acid transporter activity lysophospholipid:sodium symporter activity oleic acid binding phospholipid binding | Rattus norvegicus | 3D-structure Acetylation Cytoplasm Direct protein sequencing Isopeptide bond Lipid-binding Phosphoprotein Reference proteome Transport | MNFSGKYQVQ | MNFSGKYQVQSQENFEPFMKAMGLPEDLIQKGKDIKGVSEIVHEGKKVKLTITYGSKVIHNEFTLGEECELETMTGEKVKAVVKMEGDNKMVTTFKGIKSVTEFNGDTITNTMTLGDIVYKRVSKRI | cellular response to hydrogen peroxide cellular response to hypoxia fatty acid transport intestinal absorption long-chain fatty acid transport negative regulation of apoptotic process positive regulation of fatty acid beta-oxidation response to vitamin B3 apical cortex; cytoplasm; cytosol; nucleoplasm; nucleus; peroxisomal matrix; protein-containing complex antioxidant activity bile acid binding chromatin binding fatty acid binding heterocyclic compound binding long-chain fatty acid transporter activity lysophospholipid:sodium symporter activity oleic acid binding phospholipid binding Rattus norvegicus 3D-structure Acetylation Cytoplasm Direct protein sequencing Isopeptide bond Lipid-binding Phosphoprotein Reference proteome Transport MNFSGKYQVQ MNFSGKYQVQSQENFEPFMKAMGLPEDLIQKGKDIKGVSEIVHEGKKVKLTITYGSKVIHNEFTLGEECELETMTGEKVKAVVKMEGDNKMVTTFKGIKSVTEFNGDTITNTMTLGDIVYKRVSKRI |
fatty acid metabolic process fatty acid transport intestinal absorption intestinal lipid absorption long-chain fatty acid transport | apical cortex; cytosol; microvillus; nucleus | fatty acid binding long-chain fatty acid binding long-chain fatty acid transporter activity | Rattus norvegicus | 3D-structure Acetylation Cytoplasm Direct protein sequencing Lipid-binding Reference proteome Transport | MAFDGTWKVD | MAFDGTWKVDRNENYEKFMEKMGINVVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIDVVFELGVDFAYSLADGTELTGTWTMEGNKLVGKFKRVDNGKELIAVREISGNELIQTYTYEGVEAKRIFKKE | fatty acid metabolic process fatty acid transport intestinal absorption intestinal lipid absorption long-chain fatty acid transport apical cortex; cytosol; microvillus; nucleus fatty acid binding long-chain fatty acid binding long-chain fatty acid transporter activity Rattus norvegicus 3D-structure Acetylation Cytoplasm Direct protein sequencing Lipid-binding Reference proteome Transport MAFDGTWKVD MAFDGTWKVDRNENYEKFMEKMGINVVKRKLGAHDNLKLTITQEGNKFTVKESSNFRNIDVVFELGVDFAYSLADGTELTGTWTMEGNKLVGKFKRVDNGKELIAVREISGNELIQTYTYEGVEAKRIFKKE |
fatty acid transport lipid homeostasis regulation of granulocyte differentiation response to benzoic acid response to retinoic acid response to vitamin A retinoic acid biosynthetic process retinoic acid metabolic process retinol metabolic process vitamin A metabolic process | cell body; cytosol; lipid droplet; nucleoplasm; nucleus | all-trans-retinol binding fatty acid binding retinal binding retinol binding | Rattus norvegicus | 3D-structure Cytoplasm Direct protein sequencing Lipid droplet Reference proteome Retinol-binding Transport Vitamin A | MPVDFNGYWK | MPVDFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRAEGVTCKQVFKKVH | fatty acid transport lipid homeostasis regulation of granulocyte differentiation response to benzoic acid response to retinoic acid response to vitamin A retinoic acid biosynthetic process retinoic acid metabolic process retinol metabolic process vitamin A metabolic process cell body; cytosol; lipid droplet; nucleoplasm; nucleus all-trans-retinol binding fatty acid binding retinal binding retinol binding Rattus norvegicus 3D-structure Cytoplasm Direct protein sequencing Lipid droplet Reference proteome Retinol-binding Transport Vitamin A MPVDFNGYWK MPVDFNGYWKMLSNENFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDFQVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRAEGVTCKQVFKKVH |
eye photoreceptor cell development G protein-coupled receptor signaling pathway phototransduction protein localization | heterotrimeric G-protein complex; photoreceptor disc membrane | G-protein beta-subunit binding | Bos taurus | 3D-structure Cell membrane Direct protein sequencing Lipoprotein Membrane Methylation Prenylation Reference proteome Transducer | MPVINIEDLT | MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEFRDYVEERSGEDPLVKGIPEDKNPFKELKGGCVIS | eye photoreceptor cell development G protein-coupled receptor signaling pathway phototransduction protein localization heterotrimeric G-protein complex; photoreceptor disc membrane G-protein beta-subunit binding Bos taurus 3D-structure Cell membrane Direct protein sequencing Lipoprotein Membrane Methylation Prenylation Reference proteome Transducer MPVINIEDLT MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEFRDYVEERSGEDPLVKGIPEDKNPFKELKGGCVIS |
absorption of visible light adaptation of rhodopsin mediated signaling cellular response to light stimulus detection of temperature stimulus involved in thermoception G protein-coupled receptor signaling pathway gene expression microtubule cytoskeleton organization photoreceptor cell maintenance phototransduction phototransduction, visible light podosome assembly response to light stimulus rhodopsin mediated signaling pathway rod bipolar cell differentiation thermotaxis visual perception | cell-cell junction; G protein-coupled receptor complex; Golgi membrane; membrane; outer membrane; photoreceptor disc membrane; photoreceptor inner segment membrane; photoreceptor outer segment; photoreceptor outer segment membrane; plasma membrane; rod photoreceptor outer segment; sperm head plasma membrane; sperm midpiece | 11-cis retinal binding arrestin family protein binding G protein-coupled photoreceptor activity G-protein alpha-subunit binding guanyl-nucleotide exchange factor activity identical protein binding opsin binding zinc ion binding | Bos taurus | 3D-structure Acetylation Cell projection Chromophore Direct protein sequencing Disulfide bond G-protein coupled receptor Glycoprotein Lipoprotein Membrane Metal-binding Palmitate Phosphoprotein Photoreceptor protein Receptor Reference proteome Retinal protein Sensory transduction Transducer Transmembrane Transmembrane helix Vision Zinc | MNGTEGPNFY | MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA | absorption of visible light adaptation of rhodopsin mediated signaling cellular response to light stimulus detection of temperature stimulus involved in thermoception G protein-coupled receptor signaling pathway gene expression microtubule cytoskeleton organization photoreceptor cell maintenance phototransduction phototransduction, visible light podosome assembly response to light stimulus rhodopsin mediated signaling pathway rod bipolar cell differentiation thermotaxis visual perception cell-cell junction; G protein-coupled receptor complex; Golgi membrane; membrane; outer membrane; photoreceptor disc membrane; photoreceptor inner segment membrane; photoreceptor outer segment; photoreceptor outer segment membrane; plasma membrane; rod photoreceptor outer segment; sperm head plasma membrane; sperm midpiece 11-cis retinal binding arrestin family protein binding G protein-coupled photoreceptor activity G-protein alpha-subunit binding guanyl-nucleotide exchange factor activity identical protein binding opsin binding zinc ion binding Bos taurus 3D-structure Acetylation Cell projection Chromophore Direct protein sequencing Disulfide bond G-protein coupled receptor Glycoprotein Lipoprotein Membrane Metal-binding Palmitate Phosphoprotein Photoreceptor protein Receptor Reference proteome Retinal protein Sensory transduction Transducer Transmembrane Transmembrane helix Vision Zinc MNGTEGPNFY MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPEGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAVYNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA |
absorption of visible light rhodopsin mediated signaling pathway visual perception | membrane; photoreceptor disc membrane; photoreceptor inner segment membrane; photoreceptor outer segment membrane; plasma membrane | 11-cis retinal binding G protein-coupled photoreceptor activity metal ion binding | Ovis aries | Acetylation Cell projection Chromophore Direct protein sequencing Disulfide bond G-protein coupled receptor Glycoprotein Lipoprotein Membrane Metal-binding Palmitate Phosphoprotein Photoreceptor protein Receptor Reference proteome Retinal protein Sensory transduction Transducer Transmembrane Transmembrane helix Vision Zinc | MNGTEGPNFY | MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPQGMQCSCGALYFTLKPEINNESFVIYMFVVHFSIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKSSSVYNPVIYIMMNKQFRNCMLTTLCCGKNPLGDDEASTTVSKTETSQVAPA | absorption of visible light rhodopsin mediated signaling pathway visual perception membrane; photoreceptor disc membrane; photoreceptor inner segment membrane; photoreceptor outer segment membrane; plasma membrane 11-cis retinal binding G protein-coupled photoreceptor activity metal ion binding Ovis aries Acetylation Cell projection Chromophore Direct protein sequencing Disulfide bond G-protein coupled receptor Glycoprotein Lipoprotein Membrane Metal-binding Palmitate Phosphoprotein Photoreceptor protein Receptor Reference proteome Retinal protein Sensory transduction Transducer Transmembrane Transmembrane helix Vision Zinc MNGTEGPNFY MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIPQGMQCSCGALYFTLKPEINNESFVIYMFVVHFSIPLIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKSSSVYNPVIYIMMNKQFRNCMLTTLCCGKNPLGDDEASTTVSKTETSQVAPA |
antibacterial humoral response | extracellular region | biotin binding | Gallus gallus | 3D-structure Biotin Direct protein sequencing Disulfide bond Glycoprotein Reference proteome Secreted Signal | MVHATSPLLL | MVHATSPLLLLLLLSLALVAPGLSARKCSLTGKWTNDLGSNMTIGAVNSRGEFTGTYITAVTATSNEIKESPLHGTQNTINKRTQPTFGFTVNWKFSESTTVFTGQCFIDRNGKEVLKTMWLLRSSVNDIGDDWKATRVGINIFTRLRTQKE | antibacterial humoral response extracellular region biotin binding Gallus gallus 3D-structure Biotin Direct protein sequencing Disulfide bond Glycoprotein Reference proteome Secreted Signal MVHATSPLLL MVHATSPLLLLLLLSLALVAPGLSARKCSLTGKWTNDLGSNMTIGAVNSRGEFTGTYITAVTATSNEIKESPLHGTQNTINKRTQPTFGFTVNWKFSESTTVFTGQCFIDRNGKEVLKTMWLLRSSVNDIGDDWKATRVGINIFTRLRTQKE |
cell adhesion folic acid transport fusion of sperm to egg plasma membrane involved in single fertilization sperm-egg recognition | apical plasma membrane; basolateral plasma membrane; clathrin-coated vesicle; endosome; external side of plasma membrane; extracellular region | folic acid binding folic acid receptor activity signaling receptor activity | Bos taurus | Cell membrane Cytoplasmic vesicle Direct protein sequencing Disulfide bond Endosome Folate-binding Glycoprotein GPI-anchor Lipoprotein Membrane Milk protein Receptor Reference proteome Secreted Signal Transport | MAWQMTQLLL | MAWQMTQLLLLALVAAAWGAQAPRTPRARTDLLNVCMDAKHHKAEPGPEDSLHEQCSPWRKNACCSVNTSIEAHKDISYLYRFNWDHCGKMEPACKRHFIQDTCLYECSPNLGPWIREVNQRWRKERVLGVPLCKEDCQSWWEDCRTSYTCKSNWHKGWNWTSGYNQCPVKAACHRFDFYFPTPAALCNEIWSHSYKVSNYSRGSGRCIQMWFDPFQGNPNEEVARFYAENPTSGSTPQGI | cell adhesion folic acid transport fusion of sperm to egg plasma membrane involved in single fertilization sperm-egg recognition apical plasma membrane; basolateral plasma membrane; clathrin-coated vesicle; endosome; external side of plasma membrane; extracellular region folic acid binding folic acid receptor activity signaling receptor activity Bos taurus Cell membrane Cytoplasmic vesicle Direct protein sequencing Disulfide bond Endosome Folate-binding Glycoprotein GPI-anchor Lipoprotein Membrane Milk protein Receptor Reference proteome Secreted Signal Transport MAWQMTQLLL MAWQMTQLLLLALVAAAWGAQAPRTPRARTDLLNVCMDAKHHKAEPGPEDSLHEQCSPWRKNACCSVNTSIEAHKDISYLYRFNWDHCGKMEPACKRHFIQDTCLYECSPNLGPWIREVNQRWRKERVLGVPLCKEDCQSWWEDCRTSYTCKSNWHKGWNWTSGYNQCPVKAACHRFDFYFPTPAALCNEIWSHSYKVSNYSRGSGRCIQMWFDPFQGNPNEEVARFYAENPTSGSTPQGI |
cellular response to extracellular stimulus | external side of plasma membrane | asialoglycoprotein receptor activity fucose binding identical protein binding mannose binding metal ion binding | Rattus norvegicus | Calcium Coiled coil Disulfide bond Endocytosis Glycoprotein Lectin Lipoprotein Membrane Metal-binding Palmitate Phosphoprotein Receptor Reference proteome Signal-anchor Transmembrane Transmembrane helix | MTKDYQDFQH | MTKDYQDFQHLDNENDHHQLQRGPPPAPRLLQRLCSGFRLFLLSLGLSILLLVVVCVITSQNSQLREDLRVLRQNFSNFTVSTEDQVKALTTQGERVGRKMKLVESQLEKHQEDLREDHSRLLLHVKQLVSDVRSLSCQMAALRGNGSERICCPINWVEYEGSCYWFSSSVKPWTEADKYCQLENAHLVVVTSWEEQRFVQQHMGPLNTWIGLTDQNGPWKWVDGTDYETGFKNWRPGQPDDWYGHGLGGGEDCAHFTTDGHWNDDVCRRPYRWVCETELGKAN | cellular response to extracellular stimulus external side of plasma membrane asialoglycoprotein receptor activity fucose binding identical protein binding mannose binding metal ion binding Rattus norvegicus Calcium Coiled coil Disulfide bond Endocytosis Glycoprotein Lectin Lipoprotein Membrane Metal-binding Palmitate Phosphoprotein Receptor Reference proteome Signal-anchor Transmembrane Transmembrane helix MTKDYQDFQH MTKDYQDFQHLDNENDHHQLQRGPPPAPRLLQRLCSGFRLFLLSLGLSILLLVVVCVITSQNSQLREDLRVLRQNFSNFTVSTEDQVKALTTQGERVGRKMKLVESQLEKHQEDLREDHSRLLLHVKQLVSDVRSLSCQMAALRGNGSERICCPINWVEYEGSCYWFSSSVKPWTEADKYCQLENAHLVVVTSWEEQRFVQQHMGPLNTWIGLTDQNGPWKWVDGTDYETGFKNWRPGQPDDWYGHGLGGGEDCAHFTTDGHWNDDVCRRPYRWVCETELGKAN |
muscle cell cellular homeostasis musculoskeletal movement neuromuscular junction development neuromuscular process neuromuscular synaptic transmission neuron cellular homeostasis neuronal action potential regulation of membrane potential response to nicotine signal transduction skeletal muscle contraction skeletal muscle tissue growth synaptic transmission, cholinergic | acetylcholine-gated channel complex; cell surface; neuromuscular junction; neuron projection; plasma membrane; postsynaptic membrane; postsynaptic specialization membrane; synapse | acetylcholine binding acetylcholine receptor activity acetylcholine-gated monoatomic cation-selective channel activity monoatomic ion channel activity transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | Homo sapiens | 3D-structure Alternative splicing Cell membrane Congenital myasthenic syndrome Direct protein sequencing Disease variant Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport | MEPWPLLLLF | MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG | muscle cell cellular homeostasis musculoskeletal movement neuromuscular junction development neuromuscular process neuromuscular synaptic transmission neuron cellular homeostasis neuronal action potential regulation of membrane potential response to nicotine signal transduction skeletal muscle contraction skeletal muscle tissue growth synaptic transmission, cholinergic acetylcholine-gated channel complex; cell surface; neuromuscular junction; neuron projection; plasma membrane; postsynaptic membrane; postsynaptic specialization membrane; synapse acetylcholine binding acetylcholine receptor activity acetylcholine-gated monoatomic cation-selective channel activity monoatomic ion channel activity transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential Homo sapiens 3D-structure Alternative splicing Cell membrane Congenital myasthenic syndrome Direct protein sequencing Disease variant Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport MEPWPLLLLF MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG |
muscle cell cellular homeostasis neuromuscular junction development neuromuscular synaptic transmission neuron cellular homeostasis neuronal action potential response to nicotine skeletal muscle contraction skeletal muscle tissue growth synaptic transmission, cholinergic | acetylcholine-gated channel complex; cell surface; neuromuscular junction; neuron projection; postsynaptic specialization membrane; synapse | acetylcholine binding acetylcholine receptor activity acetylcholine-gated monoatomic cation-selective channel activity | Bos taurus | Cell membrane Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport | MEPRPLLLLL | MEPRPLLLLLGLCSAGLVLGSEHETRLVAKLFEDYNSVVRPVEDHRQAVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVVINPESDQPDLSNFMESGEWVIKESRGWKHWVFYACCPSTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPEWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAEEWKYVAMVMDHILLAVFMLVCIIGTLAVFAGRLIELNQQG | muscle cell cellular homeostasis neuromuscular junction development neuromuscular synaptic transmission neuron cellular homeostasis neuronal action potential response to nicotine skeletal muscle contraction skeletal muscle tissue growth synaptic transmission, cholinergic acetylcholine-gated channel complex; cell surface; neuromuscular junction; neuron projection; postsynaptic specialization membrane; synapse acetylcholine binding acetylcholine receptor activity acetylcholine-gated monoatomic cation-selective channel activity Bos taurus Cell membrane Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport MEPRPLLLLL MEPRPLLLLLGLCSAGLVLGSEHETRLVAKLFEDYNSVVRPVEDHRQAVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVVINPESDQPDLSNFMESGEWVIKESRGWKHWVFYACCPSTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPEWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAEEWKYVAMVMDHILLAVFMLVCIIGTLAVFAGRLIELNQQG |
monoatomic cation transport musculoskeletal movement regulation of membrane potential skeletal muscle contraction skeletal muscle tissue growth | acetylcholine-gated channel complex; neuromuscular junction; neuron projection; plasma membrane; postsynaptic specialization membrane; synapse | acetylcholine-gated monoatomic cation-selective channel activity ligand-gated monoatomic ion channel activity transmembrane signaling receptor activity transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential | Mus musculus | Cell membrane Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Phosphoprotein Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport | MAGPVLTLGL | MAGPVLTLGLLAALVVCALPGSWGLNEEQRLIQHLFNEKGYDKDLRPVARKEDKVDVALSLTLSNLISLKEVEETLTTNVWIDHAWVDSRLQWDANDFGNITVLRLPPDMVWLPEIVLENNNDGSFQISYACNVLVYDSGYVTWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEITLSLKQEEENNRSYPIEWIIIDPEGFTENGEWEIVHRAAKLNVDPSVPMDSTNHQDVTFYLIIRRKPLFYIINILVPCVLISFMINLVFYLPGDCGEKTSVAISVLLAQSVFLLLISKRLPATSMAIPLVGKFLLFGMVLVTMVVVICVIVLNIHFRTPSTHVLSEGVKKFFLETLPKLLHMSRPAEEDPGPRALIRRSSSLGYICKAEEYFSLKSRSDLMFEKQSERHGLARRLTTARRPPASSEQVQQELFNEMKPAVDGANFIVNHMRDQNSYNEEKDNWNQVARTVDRLCLFVVTPVMVVGTAWIFLQGVYNQPPLQPFPGDPFSYSEQDKRFI | monoatomic cation transport musculoskeletal movement regulation of membrane potential skeletal muscle contraction skeletal muscle tissue growth acetylcholine-gated channel complex; neuromuscular junction; neuron projection; plasma membrane; postsynaptic specialization membrane; synapse acetylcholine-gated monoatomic cation-selective channel activity ligand-gated monoatomic ion channel activity transmembrane signaling receptor activity transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential Mus musculus Cell membrane Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Phosphoprotein Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport MAGPVLTLGL MAGPVLTLGLLAALVVCALPGSWGLNEEQRLIQHLFNEKGYDKDLRPVARKEDKVDVALSLTLSNLISLKEVEETLTTNVWIDHAWVDSRLQWDANDFGNITVLRLPPDMVWLPEIVLENNNDGSFQISYACNVLVYDSGYVTWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEITLSLKQEEENNRSYPIEWIIIDPEGFTENGEWEIVHRAAKLNVDPSVPMDSTNHQDVTFYLIIRRKPLFYIINILVPCVLISFMINLVFYLPGDCGEKTSVAISVLLAQSVFLLLISKRLPATSMAIPLVGKFLLFGMVLVTMVVVICVIVLNIHFRTPSTHVLSEGVKKFFLETLPKLLHMSRPAEEDPGPRALIRRSSSLGYICKAEEYFSLKSRSDLMFEKQSERHGLARRLTTARRPPASSEQVQQELFNEMKPAVDGANFIVNHMRDQNSYNEEKDNWNQVARTVDRLCLFVVTPVMVVGTAWIFLQGVYNQPPLQPFPGDPFSYSEQDKRFI |
adaptive thermogenesis ADP transport mitochondrial ADP transmembrane transport mitochondrial ATP transmembrane transport negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway positive regulation of mitophagy regulation of mitochondrial membrane permeability | mitochondrial inner membrane; mitochondrial membrane; mitochondrial permeability transition pore complex | ATP:ADP antiporter activity oxidative phosphorylation uncoupler activity | Bos taurus | 3D-structure Acetylation Antiport Direct protein sequencing Membrane Methylation Mitochondrion Mitochondrion inner membrane Phosphoprotein Reference proteome Repeat S-nitrosylation Transmembrane Transmembrane helix Transport | MSDQALSFLK | MSDQALSFLKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFTGLGNCITKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQTVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGPKAFFKGAWSNVLRGMGGAFVLVLYDEIKKFV | adaptive thermogenesis ADP transport mitochondrial ADP transmembrane transport mitochondrial ATP transmembrane transport negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway positive regulation of mitophagy regulation of mitochondrial membrane permeability mitochondrial inner membrane; mitochondrial membrane; mitochondrial permeability transition pore complex ATP:ADP antiporter activity oxidative phosphorylation uncoupler activity Bos taurus 3D-structure Acetylation Antiport Direct protein sequencing Membrane Methylation Mitochondrion Mitochondrion inner membrane Phosphoprotein Reference proteome Repeat S-nitrosylation Transmembrane Transmembrane helix Transport MSDQALSFLK MSDQALSFLKDFLAGGVAAAISKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQIFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFTGLGNCITKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIIVSWMIAQTVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGPKAFFKGAWSNVLRGMGGAFVLVLYDEIKKFV |
bicarbonate transport blood coagulation chloride transmembrane transport chloride transport erythrocyte development intracellular monoatomic ion homeostasis monoatomic anion transport negative regulation of glycolytic process through fructose-6-phosphate negative regulation of urine volume pH elevation plasma membrane phospholipid scrambling protein localization to plasma membrane regulation of intracellular pH transmembrane transport | ankyrin-1 complex; basolateral plasma membrane; blood microparticle; cortical cytoskeleton; cytoplasmic side of plasma membrane; extracellular exosome; membrane; plasma membrane; Z disc | ankyrin binding bicarbonate transmembrane transporter activity chloride transmembrane transporter activity chloride:bicarbonate antiporter activity hemoglobin binding monoatomic anion transmembrane transporter activity protein homodimerization activity protein-membrane adaptor activity solute:inorganic anion antiporter activity | Homo sapiens | 3D-structure Acetylation Alternative splicing Anion exchange Blood group antigen Cell membrane Direct protein sequencing Disease variant Elliptocytosis Glycoprotein Hereditary hemolytic anemia Ion transport Lipoprotein Membrane Palmitate Phosphoprotein Reference proteome Transmembrane Transmembrane helix Transport | MEELQDDYED | MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV | bicarbonate transport blood coagulation chloride transmembrane transport chloride transport erythrocyte development intracellular monoatomic ion homeostasis monoatomic anion transport negative regulation of glycolytic process through fructose-6-phosphate negative regulation of urine volume pH elevation plasma membrane phospholipid scrambling protein localization to plasma membrane regulation of intracellular pH transmembrane transport ankyrin-1 complex; basolateral plasma membrane; blood microparticle; cortical cytoskeleton; cytoplasmic side of plasma membrane; extracellular exosome; membrane; plasma membrane; Z disc ankyrin binding bicarbonate transmembrane transporter activity chloride transmembrane transporter activity chloride:bicarbonate antiporter activity hemoglobin binding monoatomic anion transmembrane transporter activity protein homodimerization activity protein-membrane adaptor activity solute:inorganic anion antiporter activity Homo sapiens 3D-structure Acetylation Alternative splicing Anion exchange Blood group antigen Cell membrane Direct protein sequencing Disease variant Elliptocytosis Glycoprotein Hereditary hemolytic anemia Ion transport Lipoprotein Membrane Palmitate Phosphoprotein Reference proteome Transmembrane Transmembrane helix Transport MEELQDDYED MEELQDDYEDMMEENLEQEEYEDPDIPESQMEEPAAHDTEATATDYHTTSHPGTHKVYVELQELVMDEKNQELRWMEAARWVQLEENLGENGAWGRPHLSHLTFWSLLELRRVFTKGTVLLDLQETSLAGVANQLLDRFIFEDQIRPQDREELLRALLLKHSHAGELEALGGVKPAVLTRSGDPSQPLLPQHSSLETQLFCEQGDGGTEGHSPSGILEKIPPDSEATLVLVGRADFLEQPVLGFVRLQEAAELEAVELPVPIRFLFVLLGPEAPHIDYTQLGRAAATLMSERVFRIDAYMAQSRGELLHSLEGFLDCSLVLPPTDAPSEQALLSLVPVQRELLRRRYQSSPAKPDSSFYKGLDLNGGPDDPLQQTGQLFGGLVRDIRRRYPYYLSDITDAFSPQVLAAVIFIYFAALSPAITFGGLLGEKTRNQMGVSELLISTAVQGILFALLGAQPLLVVGFSGPLLVFEEAFFSFCETNGLEYIVGRVWIGFWLILLVVLVVAFEGSFLVRFISRYTQEIFSFLISLIFIYETFSKLIKIFQDHPLQKTYNYNVLMVPKPQGPLPNTALLSLVLMAGTFFFAMMLRKFKNSSYFPGKLRRVIGDFGVPISILIMVLVDFFIQDTYTQKLSVPDGFKVSNSSARGWVIHPLGLRSEFPIWMMFASALPALLVFILIFLESQITTLIVSKPERKMVKGSGFHLDLLLVVGMGGVAALFGMPWLSATTVRSVTHANALTVMGKASTPGAAAQIQEVKEQRISGLLVAVLVGLSILMEPILSRIPLAVLFGIFLYMGVTSLSGIQLFDRILLLFKPPKYHPDVPYVKRVKTWRMHLFTGIQIICLAVLWVVKSTPASLALPFVLILTVPLRRVLLPLIFRNVELQCLDADDAKATFDEEEGRDEYDEVAMPV |
acute-phase response defense response to Gram-positive bacterium inflammatory response innate immune response negative regulation of lipid storage negative regulation of macrophage derived foam cell differentiation negative regulation of mononuclear cell proliferation opsonization positive regulation of gene expression positive regulation of superoxide anion generation regulation of interleukin-8 production vasoconstriction | extracellular region; extracellular space | calcium ion binding choline binding complement component C1q complex binding identical protein binding low-density lipoprotein particle binding low-density lipoprotein particle receptor binding | Homo sapiens | 3D-structure Acute phase Alternative splicing Calcium Direct protein sequencing Disulfide bond Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal | MEKLLCFLVL | MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP | acute-phase response defense response to Gram-positive bacterium inflammatory response innate immune response negative regulation of lipid storage negative regulation of macrophage derived foam cell differentiation negative regulation of mononuclear cell proliferation opsonization positive regulation of gene expression positive regulation of superoxide anion generation regulation of interleukin-8 production vasoconstriction extracellular region; extracellular space calcium ion binding choline binding complement component C1q complex binding identical protein binding low-density lipoprotein particle binding low-density lipoprotein particle receptor binding Homo sapiens 3D-structure Acute phase Alternative splicing Calcium Direct protein sequencing Disulfide bond Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal MEKLLCFLVL MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP |
acute-phase response chaperone-mediated protein complex assembly innate immune response negative regulation by host of viral exo-alpha-sialidase activity negative regulation by host of viral glycoprotein metabolic process negative regulation of acute inflammatory response negative regulation of exo-alpha-sialidase activity negative regulation of glycoprotein metabolic process negative regulation of monocyte differentiation negative regulation of viral entry into host cell negative regulation of viral process negative regulation of wound healing protein folding | blood microparticle; collagen-containing extracellular matrix; extracellular exosome; extracellular region; extracellular space; nucleus | calcium ion binding carbohydrate binding complement component C1q complex binding identical protein binding unfolded protein binding virion binding | Homo sapiens | 3D-structure Amyloid Calcium Direct protein sequencing Disulfide bond Glycoprotein Lectin Metal-binding Reference proteome Secreted Signal | MNKPLLWISV | MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV | acute-phase response chaperone-mediated protein complex assembly innate immune response negative regulation by host of viral exo-alpha-sialidase activity negative regulation by host of viral glycoprotein metabolic process negative regulation of acute inflammatory response negative regulation of exo-alpha-sialidase activity negative regulation of glycoprotein metabolic process negative regulation of monocyte differentiation negative regulation of viral entry into host cell negative regulation of viral process negative regulation of wound healing protein folding blood microparticle; collagen-containing extracellular matrix; extracellular exosome; extracellular region; extracellular space; nucleus calcium ion binding carbohydrate binding complement component C1q complex binding identical protein binding unfolded protein binding virion binding Homo sapiens 3D-structure Amyloid Calcium Direct protein sequencing Disulfide bond Glycoprotein Lectin Metal-binding Reference proteome Secreted Signal MNKPLLWISV MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV |
astrocyte activation cell-cell signaling complement activation complement activation, classical pathway complement-mediated synapse pruning innate immune response microglial cell activation neuron remodeling synapse organization synapse pruning vertebrate eye-specific patterning | collagen trimer; collagen-containing extracellular matrix; complement component C1 complex; complement component C1q complex; extracellular region; postsynapse; synapse | amyloid-beta binding | Homo sapiens | 3D-structure Collagen Complement pathway Direct protein sequencing Disulfide bond Glycoprotein Host-virus interaction Hydroxylation Immunity Innate immunity Reference proteome Repeat Secreted Signal | MEGPRGWLVL | MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFLIFPSA | astrocyte activation cell-cell signaling complement activation complement activation, classical pathway complement-mediated synapse pruning innate immune response microglial cell activation neuron remodeling synapse organization synapse pruning vertebrate eye-specific patterning collagen trimer; collagen-containing extracellular matrix; complement component C1 complex; complement component C1q complex; extracellular region; postsynapse; synapse amyloid-beta binding Homo sapiens 3D-structure Collagen Complement pathway Direct protein sequencing Disulfide bond Glycoprotein Host-virus interaction Hydroxylation Immunity Innate immunity Reference proteome Repeat Secreted Signal MEGPRGWLVL MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFLIFPSA |
blood coagulation, intrinsic pathway negative regulation of angiogenesis negative regulation of blood coagulation negative regulation of endothelial cell migration negative regulation of endothelial cell proliferation negative regulation of fibrinolysis negative regulation of myeloid cell apoptotic process negative regulation of smooth muscle cell apoptotic process plasminogen activation positive regulation of blood coagulation positive regulation of lipoprotein lipase activity regulation of fibrinolysis triglyceride metabolic process triglyceride transport | cell surface; chylomicron; collagen-containing extracellular matrix; extracellular exosome; extracellular region; extracellular space; high-density lipoprotein particle; platelet dense granule lumen; very-low-density lipoprotein particle | heparin binding identical protein binding lipid binding lipoprotein lipase activator activity phospholipid binding | Homo sapiens | 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Heparin-binding Reference proteome Repeat Secreted Signal Sushi | MISPVLILFS | MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTIEVPKCFKEHSSLAFWKTDASDVKPC | blood coagulation, intrinsic pathway negative regulation of angiogenesis negative regulation of blood coagulation negative regulation of endothelial cell migration negative regulation of endothelial cell proliferation negative regulation of fibrinolysis negative regulation of myeloid cell apoptotic process negative regulation of smooth muscle cell apoptotic process plasminogen activation positive regulation of blood coagulation positive regulation of lipoprotein lipase activity regulation of fibrinolysis triglyceride metabolic process triglyceride transport cell surface; chylomicron; collagen-containing extracellular matrix; extracellular exosome; extracellular region; extracellular space; high-density lipoprotein particle; platelet dense granule lumen; very-low-density lipoprotein particle heparin binding identical protein binding lipid binding lipoprotein lipase activator activity phospholipid binding Homo sapiens 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Heparin-binding Reference proteome Repeat Secreted Signal Sushi MISPVLILFS MISPVLILFSSFLCHVAIAGRTCPKPDDLPFSTVVPLKTFYEPGEEITYSCKPGYVSRGGMRKFICPLTGLWPINTLKCTPRVCPFAGILENGAVRYTTFEYPNTISFSCNTGFYLNGADSAKCTEEGKWSPELPVCAPIICPPPSIPTFATLRVYKPSAGNNSLYRDTAVFECLPQHAMFGNDTITCTTHGNWTKLPECREVKCPFPSRPDNGFVNYPAKPTLYYKDKATFGCHDGYSLDGPEEIECTKLGNWSAMPSCKASCKVPVKKATVVYQGERVKIQEKFKNGMLHGDKVSFFCKNKEKKCSYTEDAQCIDGTIEVPKCFKEHSSLAFWKTDASDVKPC |
brown fat cell differentiation keratinocyte migration leukocyte adhesion to vascular endothelial cell positive regulation of angiogenesis positive regulation of endothelial cell proliferation positive regulation of epithelial cell proliferation involved in wound healing positive regulation of epithelial to mesenchymal transition positive regulation of keratinocyte proliferation positive regulation of transforming growth factor beta receptor signaling pathway response to bacterium wound healing, spreading of epidermal cells | extracellular exosome; extracellular region; extracellular space; ficolin-1-rich granule lumen; intracellular membrane-bounded organelle; membrane; specific granule lumen; tertiary granule lumen | type I transforming growth factor beta receptor binding type II transforming growth factor beta receptor binding | Homo sapiens | 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Leucine-rich repeat Reference proteome Repeat Secreted Signal | MSSWSRQRPK | MSSWSRQRPKSPGGIQPHVSRTLFLLLLLAASAWGVTLSPKDCQVFRSDHGSSISCQPPAEIPGYLPADTVHLAVEFFNLTHLPANLLQGASKLQELHLSSNGLESLSPEFLRPVPQLRVLDLTRNALTGLPPGLFQASATLDTLVLKENQLEVLEVSWLHGLKALGHLDLSGNRLRKLPPGLLANFTLLRTLDLGENQLETLPPDLLRGPLQLERLHLEGNKLQVLGKDLLLPQPDLRYLFLNGNKLARVAAGAFQGLRQLDMLDLSNNSLASVPEGLWASLGQPNWDMRDGFDISGNPWICDQNLSDLYRWLQAQKDKMFSQNDTRCAGPEAVKGQTLLAVAKSQ | brown fat cell differentiation keratinocyte migration leukocyte adhesion to vascular endothelial cell positive regulation of angiogenesis positive regulation of endothelial cell proliferation positive regulation of epithelial cell proliferation involved in wound healing positive regulation of epithelial to mesenchymal transition positive regulation of keratinocyte proliferation positive regulation of transforming growth factor beta receptor signaling pathway response to bacterium wound healing, spreading of epidermal cells extracellular exosome; extracellular region; extracellular space; ficolin-1-rich granule lumen; intracellular membrane-bounded organelle; membrane; specific granule lumen; tertiary granule lumen type I transforming growth factor beta receptor binding type II transforming growth factor beta receptor binding Homo sapiens 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Leucine-rich repeat Reference proteome Repeat Secreted Signal MSSWSRQRPK MSSWSRQRPKSPGGIQPHVSRTLFLLLLLAASAWGVTLSPKDCQVFRSDHGSSISCQPPAEIPGYLPADTVHLAVEFFNLTHLPANLLQGASKLQELHLSSNGLESLSPEFLRPVPQLRVLDLTRNALTGLPPGLFQASATLDTLVLKENQLEVLEVSWLHGLKALGHLDLSGNRLRKLPPGLLANFTLLRTLDLGENQLETLPPDLLRGPLQLERLHLEGNKLQVLGKDLLLPQPDLRYLFLNGNKLARVAAGAFQGLRQLDMLDLSNNSLASVPEGLWASLGQPNWDMRDGFDISGNPWICDQNLSDLYRWLQAQKDKMFSQNDTRCAGPEAVKGQTLLAVAKSQ |
negative regulation of sensory perception of bitter taste negative regulation of sensory perception of sweet taste riboflavin transport | external side of plasma membrane | riboflavin binding riboflavin transmembrane transporter activity signaling receptor activity | Gallus gallus | 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Phosphoprotein Pyrrolidone carboxylic acid Reference proteome Signal Transport | MLRFAITLFA | MLRFAITLFAVITSSTCQQYGCLEGDTHKANPSPEPNMHECTLYSESSCCYANFTEQLAHSPIIKVSNSYWNRCGQLSKSCEDFTKKIECFYRCSPHAARWIDPRYTAAIQSVPLCQSFCDDWYEACKDDSICAHNWLTDWERDESGENHCKSKCVPYSEMYANGTDMCQSMWGESFKVSESSCLCLQMNKKDMVAIKHLLSESSEESSSMSSSEEHACQKKLLKFEALQQEEGEERR | negative regulation of sensory perception of bitter taste negative regulation of sensory perception of sweet taste riboflavin transport external side of plasma membrane riboflavin binding riboflavin transmembrane transporter activity signaling receptor activity Gallus gallus 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Phosphoprotein Pyrrolidone carboxylic acid Reference proteome Signal Transport MLRFAITLFA MLRFAITLFAVITSSTCQQYGCLEGDTHKANPSPEPNMHECTLYSESSCCYANFTEQLAHSPIIKVSNSYWNRCGQLSKSCEDFTKKIECFYRCSPHAARWIDPRYTAAIQSVPLCQSFCDDWYEACKDDSICAHNWLTDWERDESGENHCKSKCVPYSEMYANGTDMCQSMWGESFKVSESSCLCLQMNKKDMVAIKHLLSESSEESSSMSSSEEHACQKKLLKFEALQQEEGEERR |
cardiac muscle tissue development embryonic organ morphogenesis embryonic retina morphogenesis in camera-type eye embryonic skeletal system development eye development female genitalia morphogenesis gluconeogenesis glucose homeostasis heart development heart trabecula formation lung development maintenance of gastrointestinal epithelium negative regulation of cardiac muscle cell proliferation positive regulation of immunoglobulin production positive regulation of insulin secretion response to retinoic acid retinol metabolic process retinol transport urinary bladder development uterus development vagina development visual perception | extracellular exosome; extracellular region; extracellular space | retinal binding retinol binding retinol transmembrane transporter activity | Homo sapiens | 3D-structure Direct protein sequencing Disease variant Disulfide bond Methylation Microphthalmia Reference proteome Retinol-binding Secreted Sensory transduction Signal Transport Vision Vitamin A | MKWVWALLLL | MKWVWALLLLAALGSGRAERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSCRLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDGRSERNLL | cardiac muscle tissue development embryonic organ morphogenesis embryonic retina morphogenesis in camera-type eye embryonic skeletal system development eye development female genitalia morphogenesis gluconeogenesis glucose homeostasis heart development heart trabecula formation lung development maintenance of gastrointestinal epithelium negative regulation of cardiac muscle cell proliferation positive regulation of immunoglobulin production positive regulation of insulin secretion response to retinoic acid retinol metabolic process retinol transport urinary bladder development uterus development vagina development visual perception extracellular exosome; extracellular region; extracellular space retinal binding retinol binding retinol transmembrane transporter activity Homo sapiens 3D-structure Direct protein sequencing Disease variant Disulfide bond Methylation Microphthalmia Reference proteome Retinol-binding Secreted Sensory transduction Signal Transport Vision Vitamin A MKWVWALLLL MKWVWALLLLAALGSGRAERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGRVRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSCRLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDGRSERNLL |
cell adhesion female pregnancy heme catabolic process negative regulation of immune response negative regulation of JNK cascade | blood microparticle; cell surface; collagen-containing extracellular matrix; cytosol; endoplasmic reticulum; extracellular exosome; extracellular region; extracellular space; mitochondrial inner membrane; nuclear membrane; plasma membrane | calcium channel inhibitor activity calcium oxalate binding carbohydrate binding heme binding IgA binding oxidoreductase activity protein homodimerization activity serine-type endopeptidase inhibitor activity | Homo sapiens | 3D-structure Cell membrane Chromophore Cleavage on pair of basic residues Cytoplasm Direct protein sequencing Disulfide bond Endoplasmic reticulum Extracellular matrix Glycoprotein Host-virus interaction Membrane Mitochondrion Mitochondrion inner membrane Nucleus Oxidoreductase Protease inhibitor Proteoglycan Reference proteome Repeat Secreted Serine protease inhibitor Signal | MRSLGALLLL | MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN | cell adhesion female pregnancy heme catabolic process negative regulation of immune response negative regulation of JNK cascade blood microparticle; cell surface; collagen-containing extracellular matrix; cytosol; endoplasmic reticulum; extracellular exosome; extracellular region; extracellular space; mitochondrial inner membrane; nuclear membrane; plasma membrane calcium channel inhibitor activity calcium oxalate binding carbohydrate binding heme binding IgA binding oxidoreductase activity protein homodimerization activity serine-type endopeptidase inhibitor activity Homo sapiens 3D-structure Cell membrane Chromophore Cleavage on pair of basic residues Cytoplasm Direct protein sequencing Disulfide bond Endoplasmic reticulum Extracellular matrix Glycoprotein Host-virus interaction Membrane Mitochondrion Mitochondrion inner membrane Nucleus Oxidoreductase Protease inhibitor Proteoglycan Reference proteome Repeat Secreted Serine protease inhibitor Signal MRSLGALLLL MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN |
aerobic respiration cellular response to lipid energy reserve metabolic process glucose homeostasis heat generation locomotor rhythm mitochondrion organization negative regulation of DNA-templated transcription negative regulation of gluconeogenesis negative regulation of insulin secretion involved in cellular response to glucose stimulus negative regulation of lipid biosynthetic process negative regulation of lipid storage positive regulation of gene expression positive regulation of glucose metabolic process positive regulation of lipid metabolic process positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | cytosol; extracellular space; nucleus | insulin receptor activity odorant binding pheromone binding small molecule binding | Rattus norvegicus | 3D-structure Allergen Behavior Cytoplasm Direct protein sequencing Disulfide bond Glycoprotein Pheromone-binding Reference proteome Secreted Signal Transport | MKLLLLLLCL | MKLLLLLLCLGLTLVCGHAEEASSTRGNLDVAKLNGDWFSIVVASNKREKIEENGSMRVFMQHIDVLENSLGFKFRIKENGECRELYLVAYKTPEDGEYFVEYDGGNTFTILKTDYDRYVMFHLINFKNGETFQLMVLYGRTKDLSSDIKEKFAKLCEAHGITRDNIIDLTKTDRCLQARG | aerobic respiration cellular response to lipid energy reserve metabolic process glucose homeostasis heat generation locomotor rhythm mitochondrion organization negative regulation of DNA-templated transcription negative regulation of gluconeogenesis negative regulation of insulin secretion involved in cellular response to glucose stimulus negative regulation of lipid biosynthetic process negative regulation of lipid storage positive regulation of gene expression positive regulation of glucose metabolic process positive regulation of lipid metabolic process positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction cytosol; extracellular space; nucleus insulin receptor activity odorant binding pheromone binding small molecule binding Rattus norvegicus 3D-structure Allergen Behavior Cytoplasm Direct protein sequencing Disulfide bond Glycoprotein Pheromone-binding Reference proteome Secreted Signal Transport MKLLLLLLCL MKLLLLLLCLGLTLVCGHAEEASSTRGNLDVAKLNGDWFSIVVASNKREKIEENGSMRVFMQHIDVLENSLGFKFRIKENGECRELYLVAYKTPEDGEYFVEYDGGNTFTILKTDYDRYVMFHLINFKNGETFQLMVLYGRTKDLSSDIKEKFAKLCEAHGITRDNIIDLTKTDRCLQARG |
aerobic respiration cellular response to lipid energy reserve metabolic process glucose homeostasis heat generation locomotor rhythm mitochondrion organization negative regulation of DNA-templated transcription negative regulation of gluconeogenesis negative regulation of insulin secretion involved in cellular response to glucose stimulus negative regulation of lipid biosynthetic process negative regulation of lipid storage positive regulation of gene expression positive regulation of glucose metabolic process positive regulation of lipid metabolic process positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | cytosol; extracellular space; nucleus | insulin receptor activity odorant binding pheromone binding small molecule binding | Mus musculus | 3D-structure Allergen Disulfide bond Pheromone-binding Reference proteome Secreted Signal Transport | MKMLLLLCLG | MKMLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE | aerobic respiration cellular response to lipid energy reserve metabolic process glucose homeostasis heat generation locomotor rhythm mitochondrion organization negative regulation of DNA-templated transcription negative regulation of gluconeogenesis negative regulation of insulin secretion involved in cellular response to glucose stimulus negative regulation of lipid biosynthetic process negative regulation of lipid storage positive regulation of gene expression positive regulation of glucose metabolic process positive regulation of lipid metabolic process positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction cytosol; extracellular space; nucleus insulin receptor activity odorant binding pheromone binding small molecule binding Mus musculus 3D-structure Allergen Disulfide bond Pheromone-binding Reference proteome Secreted Signal Transport MKMLLLLCLG MKMLLLLCLGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE |
acute inflammatory response to antigenic stimulus acute-phase response animal organ regeneration cellular response to glucocorticoid stimulus cellular response to growth hormone stimulus cellular response to retinoic acid chronic inflammatory response to antigenic stimulus negative regulation of interleukin-6 production negative regulation of tumor necrosis factor production positive regulation of interleukin-1 beta production positive regulation of interleukin-1 production positive regulation of tumor necrosis factor production regulation of immune system process response to lipopolysaccharide response to organic cyclic compound response to vitamin E response to xenobiotic stimulus | extracellular space | small molecule binding | Rattus norvegicus | Acute phase Disulfide bond Glycoprotein Reference proteome Secreted Signal Transport | MALHMVLVVL | MALHMVLVVLSLLPLLEAQNPEPANITLGIPITNETLKWLSDKWFYMGAAFRDPVFKQAVQTIQTEYFYLTPNLINDTIELREFQTTDDQCVYNFTHLGVQRENGTLSKCAGAVKIFAHLIVLKKHGTFMLAFNLTDENRGLSFYAKKPDLSPELRKIFQQAVKDVGMDESEIVFVDWTKDKCSEQQKQQLELEKETKKETKKDP | acute inflammatory response to antigenic stimulus acute-phase response animal organ regeneration cellular response to glucocorticoid stimulus cellular response to growth hormone stimulus cellular response to retinoic acid chronic inflammatory response to antigenic stimulus negative regulation of interleukin-6 production negative regulation of tumor necrosis factor production positive regulation of interleukin-1 beta production positive regulation of interleukin-1 production positive regulation of tumor necrosis factor production regulation of immune system process response to lipopolysaccharide response to organic cyclic compound response to vitamin E response to xenobiotic stimulus extracellular space small molecule binding Rattus norvegicus Acute phase Disulfide bond Glycoprotein Reference proteome Secreted Signal Transport MALHMVLVVL MALHMVLVVLSLLPLLEAQNPEPANITLGIPITNETLKWLSDKWFYMGAAFRDPVFKQAVQTIQTEYFYLTPNLINDTIELREFQTTDDQCVYNFTHLGVQRENGTLSKCAGAVKIFAHLIVLKKHGTFMLAFNLTDENRGLSFYAKKPDLSPELRKIFQQAVKDVGMDESEIVFVDWTKDKCSEQQKQQLELEKETKKETKKDP |
acute-phase response negative regulation of bone mineralization negative regulation of insulin receptor signaling pathway ossification pinocytosis positive regulation of phagocytosis regulation of bone mineralization regulation of inflammatory response skeletal system development | blood microparticle; collagen-containing extracellular matrix; endoplasmic reticulum lumen; extracellular exosome; extracellular matrix; extracellular region; extracellular space; Golgi apparatus; platelet alpha granule lumen; secretory granule lumen | cysteine-type endopeptidase inhibitor activity endopeptidase inhibitor activity kinase inhibitor activity | Homo sapiens | Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hypotrichosis Intellectual disability Mineral balance Phosphoprotein Reference proteome Repeat Secreted Signal | MKSLVLLLCL | MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCMVFQTQPVSSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKV | acute-phase response negative regulation of bone mineralization negative regulation of insulin receptor signaling pathway ossification pinocytosis positive regulation of phagocytosis regulation of bone mineralization regulation of inflammatory response skeletal system development blood microparticle; collagen-containing extracellular matrix; endoplasmic reticulum lumen; extracellular exosome; extracellular matrix; extracellular region; extracellular space; Golgi apparatus; platelet alpha granule lumen; secretory granule lumen cysteine-type endopeptidase inhibitor activity endopeptidase inhibitor activity kinase inhibitor activity Homo sapiens Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hypotrichosis Intellectual disability Mineral balance Phosphoprotein Reference proteome Repeat Secreted Signal MKSLVLLLCL MKSLVLLLCLAQLWGCHSAPHGPGLIYRQPNCDDPETEEAALVAIDYINQNLPWGYKHTLNQIDEVKVWPQQPSGELFEIEIDTLETTCHVLDPTPVARCSVRQLKEHAVEGDCDFQLLKLDGKFSVVYAKCDSSPDSAEDVRKVCQDCPLLAPLNDTRVVHAAKAALAAFNAQNNGSNFQLEEISRAQLVPLPPSTYVEFTVSGTDCVAKEATEAAKCNLLAEKQYGFCKATLSEKLGGAEVAVTCMVFQTQPVSSQPQPEGANEAVPTPVVDPDAPPSPPLGAPGLPPAGSPPDSHVLLAAPPGHQLHRAHYDLRHTFMGVVSLGSPSGEVSHPRKTRTVVQPSVGAAAGPVVPPCPGRIRHFKV |
purine nucleobase metabolic process | azurophil granule lumen; extracellular exosome; extracellular region; extracellular space | hormone activity identical protein binding thyroid hormone binding | Homo sapiens | 3D-structure Amyloid Amyloidosis Cytoplasm Direct protein sequencing Disease variant Gamma-carboxyglutamic acid Glycoprotein Hormone Neuropathy Phosphoprotein Reference proteome Secreted Signal Sulfation Thyroid hormone Transport | MASHRLLLLC | MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE | purine nucleobase metabolic process azurophil granule lumen; extracellular exosome; extracellular region; extracellular space hormone activity identical protein binding thyroid hormone binding Homo sapiens 3D-structure Amyloid Amyloidosis Cytoplasm Direct protein sequencing Disease variant Gamma-carboxyglutamic acid Glycoprotein Hormone Neuropathy Phosphoprotein Reference proteome Secreted Signal Sulfation Thyroid hormone Transport MASHRLLLLC MASHRLLLLCLAGLVFVSEAGPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE |
purine nucleobase metabolic process thyroid hormone metabolic process | extracellular space; protein-containing complex | hormone activity hormone binding identical protein binding protein-containing complex binding thyroid hormone binding | Rattus norvegicus | 3D-structure Direct protein sequencing Gamma-carboxyglutamic acid Glycoprotein Hormone Phosphoprotein Reference proteome Secreted Signal Sulfation Thyroid hormone Transport | MASLRLFLLC | MASLRLFLLCLAGLIFASEAGPGGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDTKSYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN | purine nucleobase metabolic process thyroid hormone metabolic process extracellular space; protein-containing complex hormone activity hormone binding identical protein binding protein-containing complex binding thyroid hormone binding Rattus norvegicus 3D-structure Direct protein sequencing Gamma-carboxyglutamic acid Glycoprotein Hormone Phosphoprotein Reference proteome Secreted Signal Sulfation Thyroid hormone Transport MASLRLFLLC MASLRLFLLCLAGLIFASEAGPGGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDTKSYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN |
cellular response to calcium ion starvation cellular response to starvation negative regulation of mitochondrial depolarization | blood microparticle; cytoplasm; endoplasmic reticulum; endoplasmic reticulum lumen; extracellular exosome; extracellular region; extracellular space; Golgi apparatus; nucleus; platelet alpha granule lumen; protein-containing complex | antioxidant activity copper ion binding DNA binding enterobactin binding exogenous protein binding fatty acid binding identical protein binding protein-folding chaperone binding pyridoxal phosphate binding toxic substance binding | Homo sapiens | 3D-structure Alternative splicing Calcium Cleavage on pair of basic residues Copper Direct protein sequencing Disease variant Disulfide bond Glycation Glycoprotein Lipid-binding Metal-binding Methylation Phosphoprotein Reference proteome Repeat Secreted Signal Zinc | MKWVTFISLL | MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL | cellular response to calcium ion starvation cellular response to starvation negative regulation of mitochondrial depolarization blood microparticle; cytoplasm; endoplasmic reticulum; endoplasmic reticulum lumen; extracellular exosome; extracellular region; extracellular space; Golgi apparatus; nucleus; platelet alpha granule lumen; protein-containing complex antioxidant activity copper ion binding DNA binding enterobactin binding exogenous protein binding fatty acid binding identical protein binding protein-folding chaperone binding pyridoxal phosphate binding toxic substance binding Homo sapiens 3D-structure Alternative splicing Calcium Cleavage on pair of basic residues Copper Direct protein sequencing Disease variant Disulfide bond Glycation Glycoprotein Lipid-binding Metal-binding Methylation Phosphoprotein Reference proteome Repeat Secreted Signal Zinc MKWVTFISLL MKWVTFISLLFLFSSAYSRGVFRRDAHKSEVAHRFKDLGEENFKALVLIAFAQYLQQCPFEDHVKLVNEVTEFAKTCVADESAENCDKSLHTLFGDKLCTVATLRETYGEMADCCAKQEPERNECFLQHKDDNPNLPRLVRPEVDVMCTAFHDNEETFLKKYLYEIARRHPYFYAPELLFFAKRYKAAFTECCQAADKAACLLPKLDELRDEGKASSAKQRLKCASLQKFGERAFKAWAVARLSQRFPKAEFAEVSKLVTDLTKVHTECCHGDLLECADDRADLAKYICENQDSISSKLKECCEKPLLEKSHCIAEVENDEMPADLPSLAADFVESKDVCKNYAEAKDVFLGMFLYEYARRHPDYSVVLLLRLAKTYETTLEKCCAAADPHECYAKVFDEFKPLVEEPQNLIKQNCELFEQLGEYKFQNALLVRYTKKVPQVSTPTLVEVSRNLGKVGSKCCKHPEAKRMPCAEDYLSVVLNQLCVLHEKTPVSDRVTKCCTESLVNRRPCFSALEVDETYVPKEFNAETFTFHADICTLSEKERQIKKQTALVELVKHKPKATKEQLKAVMDDFAAFVEKCCKADDKETCFAEEGKKLVAASQAALGL |
cellular response to calcium ion starvation cellular response to starvation negative regulation of mitochondrial depolarization | cytoplasm; extracellular region; extracellular space; protein-containing complex | DNA binding enterobactin binding fatty acid binding metal ion binding pyridoxal phosphate binding toxic substance binding | Bos taurus | 3D-structure Allergen Calcium Cleavage on pair of basic residues Copper Direct protein sequencing Disulfide bond Glycation Glycoprotein Lipid-binding Metal-binding Methylation Phosphoprotein Reference proteome Repeat Secreted Signal Zinc | MKWVTFISLL | MKWVTFISLLLLFSSAYSRGVFRRDTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA | cellular response to calcium ion starvation cellular response to starvation negative regulation of mitochondrial depolarization cytoplasm; extracellular region; extracellular space; protein-containing complex DNA binding enterobactin binding fatty acid binding metal ion binding pyridoxal phosphate binding toxic substance binding Bos taurus 3D-structure Allergen Calcium Cleavage on pair of basic residues Copper Direct protein sequencing Disulfide bond Glycation Glycoprotein Lipid-binding Metal-binding Methylation Phosphoprotein Reference proteome Repeat Secreted Signal Zinc MKWVTFISLL MKWVTFISLLLLFSSAYSRGVFRRDTHKSEIAHRFKDLGEEHFKGLVLIAFSQYLQQCPFDEHVKLVNELTEFAKTCVADESHAGCEKSLHTLFGDELCKVASLRETYGDMADCCEKQEPERNECFLSHKDDSPDLPKLKPDPNTLCDEFKADEKKFWGKYLYEIARRHPYFYAPELLYYANKYNGVFQECCQAEDKGACLLPKIETMREKVLASSARQRLRCASIQKFGERALKAWSVARLSQKFPKAEFVEVTKLVTDLTKVHKECCHGDLLECADDRADLAKYICDNQDTISSKLKECCDKPLLEKSHCIAEVEKDAIPENLPPLTADFAEDKDVCKNYQEAKDAFLGSFLYEYSRRHPEYAVSVLLRLAKEYEATLEECCAKDDPHACYSTVFDKLKHLVDEPQNLIKQNCDQFEKLGEYGFQNALIVRYTRKVPQVSTPTLVEVSRSLGKVGTRCCTKPESERMPCTEDYLSLILNRLCVLHEKTPVSEKVTKCCTESLVNRRPCFSALTPDETYVPKAFDEKLFTFHADICTLPDTEKQIKKQTALVELLKHKPKATEEQLKTVMENFVAFVDKCCAADDKEACFAVEGPKLVVSTQTALA |
cellular response to calcium ion starvation cellular response to starvation negative regulation of mitochondrial depolarization positive regulation of circadian sleep/wake cycle, non-REM sleep response to mercury ion response to nutrient response to organic substance response to platinum ion vasodilation | basement membrane; cytoplasm; extracellular exosome; extracellular region; extracellular space; protein-containing complex | DNA binding enterobactin binding enzyme binding exogenous protein binding fatty acid binding identical protein binding modified amino acid binding protein-folding chaperone binding pyridoxal phosphate binding toxic substance binding zinc ion binding | Rattus norvegicus | Calcium Cleavage on pair of basic residues Copper Direct protein sequencing Disulfide bond Lipid-binding Metal-binding Methylation Phosphoprotein Reference proteome Repeat Secreted Signal Zinc | MKWVTFLLLL | MKWVTFLLLLFISGSAFSRGVFRREAHKSEIAHRFKDLGEQHFKGLVLIAFSQYLQKCPYEEHIKLVQEVTDFAKTCVADENAENCDKSIHTLFGDKLCAIPKLRDNYGELADCCAKQEPERNECFLQHKDDNPNLPPFQRPEAEAMCTSFQENPTSFLGHYLHEVARRHPYFYAPELLYYAEKYNEVLTQCCTESDKAACLTPKLDAVKEKALVAAVRQRMKCSSMQRFGERAFKAWAVARMSQRFPNAEFAEITKLATDVTKINKECCHGDLLECADDRAELAKYMCENQATISSKLQACCDKPVLQKSQCLAEIEHDNIPADLPSIAADFVEDKEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEGDPPACYGTVLAEFQPLVEEPKNLVKTNCELYEKLGEYGFQNAVLVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEAQRLPCVEDYLSAILNRLCVLHEKTPVSEKVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPDKEKQIKKQTALAELVKHKPKATEDQLKTVMGDFAQFVDKCCKAADKDNCFATEGPNLVARSKEALA | cellular response to calcium ion starvation cellular response to starvation negative regulation of mitochondrial depolarization positive regulation of circadian sleep/wake cycle, non-REM sleep response to mercury ion response to nutrient response to organic substance response to platinum ion vasodilation basement membrane; cytoplasm; extracellular exosome; extracellular region; extracellular space; protein-containing complex DNA binding enterobactin binding enzyme binding exogenous protein binding fatty acid binding identical protein binding modified amino acid binding protein-folding chaperone binding pyridoxal phosphate binding toxic substance binding zinc ion binding Rattus norvegicus Calcium Cleavage on pair of basic residues Copper Direct protein sequencing Disulfide bond Lipid-binding Metal-binding Methylation Phosphoprotein Reference proteome Repeat Secreted Signal Zinc MKWVTFLLLL MKWVTFLLLLFISGSAFSRGVFRREAHKSEIAHRFKDLGEQHFKGLVLIAFSQYLQKCPYEEHIKLVQEVTDFAKTCVADENAENCDKSIHTLFGDKLCAIPKLRDNYGELADCCAKQEPERNECFLQHKDDNPNLPPFQRPEAEAMCTSFQENPTSFLGHYLHEVARRHPYFYAPELLYYAEKYNEVLTQCCTESDKAACLTPKLDAVKEKALVAAVRQRMKCSSMQRFGERAFKAWAVARMSQRFPNAEFAEITKLATDVTKINKECCHGDLLECADDRAELAKYMCENQATISSKLQACCDKPVLQKSQCLAEIEHDNIPADLPSIAADFVEDKEVCKNYAEAKDVFLGTFLYEYSRRHPDYSVSLLLRLAKKYEATLEKCCAEGDPPACYGTVLAEFQPLVEEPKNLVKTNCELYEKLGEYGFQNAVLVRYTQKAPQVSTPTLVEAARNLGRVGTKCCTLPEAQRLPCVEDYLSAILNRLCVLHEKTPVSEKVTKCCSGSLVERRPCFSALTVDETYVPKEFKAETFTFHSDICTLPDKEKQIKKQTALAELVKHKPKATEDQLKTVMGDFAQFVDKCCKAADKDNCFATEGPNLVARSKEALA |
ovulation from ovarian follicle progesterone metabolic process | cytoplasm; endoplasmic reticulum lumen; extracellular space | metal ion binding | Homo sapiens | 3D-structure Copper Direct protein sequencing Disulfide bond Glycoprotein Metal-binding Nickel Phosphoprotein Reference proteome Repeat Secreted Signal Sulfation | MKWVESIFLI | MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVKDALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSEEGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAENDEKPEGLSPNLNRFLGDRDFNQFSSGEKNIFLASFVHEYSRRHPQLAVSVILRVAKGYQELLEKCFQTENPLECQDKGEEELQKYIQESQALAKRSCGLFQKLGEYYLQNAFLVAYTKKAPQLTSSELMAITRKMAATAATCCQLSEDKLLACGEGAADIIIGHLCIRHEMTPVNPGVGQCCTSSYANRRPCFSSLVVDETYVPPAFSDDKFIFHKDLCQAQGVALQTMKQEFLINLVKQKPQITEEQLEAVIADFSGLLEKCCQGQEQEVCFAEEGQKLISKTRAALGV | ovulation from ovarian follicle progesterone metabolic process cytoplasm; endoplasmic reticulum lumen; extracellular space metal ion binding Homo sapiens 3D-structure Copper Direct protein sequencing Disulfide bond Glycoprotein Metal-binding Nickel Phosphoprotein Reference proteome Repeat Secreted Signal Sulfation MKWVESIFLI MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVKDALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSEEGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAENDEKPEGLSPNLNRFLGDRDFNQFSSGEKNIFLASFVHEYSRRHPQLAVSVILRVAKGYQELLEKCFQTENPLECQDKGEEELQKYIQESQALAKRSCGLFQKLGEYYLQNAFLVAYTKKAPQLTSSELMAITRKMAATAATCCQLSEDKLLACGEGAADIIIGHLCIRHEMTPVNPGVGQCCTSSYANRRPCFSSLVVDETYVPPAFSDDKFIFHKDLCQAQGVALQTMKQEFLINLVKQKPQITEEQLEAVIADFSGLLEKCCQGQEQEVCFAEEGQKLISKTRAALGV |
ovulation from ovarian follicle progesterone metabolic process sexual reproduction | cytoplasm; extracellular space | metal ion binding | Mus musculus | Copper Disulfide bond Glycoprotein Metal-binding Nickel Phosphoprotein Reference proteome Repeat Secreted Signal Sulfation | MKWITPASLI | MKWITPASLILLLHFAASKALHENEFGIASTLDSSQCVTEKNVLSIATITFTQFVPEATEEEVNKMTSDVLAAMKKNSGDGCLESQLSVFLDEICHETELSNKYGLSGCCSQSGVERHQCLLARKKTAPASVPPFQFPEPAESCKAHEENRAVFMNRFIYEVSRRNPFMYAPAILSLAAQYDKVVLACCKADNKEECFQTKRASIAKELREGSMLNEHVCSVIRKFGSRNLQATTIIKLSQKLTEANFTEIQKLALDVAHIHEECCQGNSLECLQDGEKVMTYICSQQNILSSKIAECCKLPMIQLGFCIIHAENGVKPEGLSLNPSQFLGDRNFAQFSSEEKIMFMASFLHEYSRTHPNLPVSVILRIAKTYQEILEKCSQSGNLPGCQDNLEEELQKHIEESQALSKQSCALYQTLGDYKLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKWSGCGEGMADIFIGHLCIRNEASPVNSGISHCCNSSYSNRRLCITSFLRDETYAPPPFSEDKFIFHKDLCQAQGKALQTMKQELLINLVKQKPELTEEQLAAVTADFSGLLEKCCKAQDQEVCFTEEGPKLISKTRDALGV | ovulation from ovarian follicle progesterone metabolic process sexual reproduction cytoplasm; extracellular space metal ion binding Mus musculus Copper Disulfide bond Glycoprotein Metal-binding Nickel Phosphoprotein Reference proteome Repeat Secreted Signal Sulfation MKWITPASLI MKWITPASLILLLHFAASKALHENEFGIASTLDSSQCVTEKNVLSIATITFTQFVPEATEEEVNKMTSDVLAAMKKNSGDGCLESQLSVFLDEICHETELSNKYGLSGCCSQSGVERHQCLLARKKTAPASVPPFQFPEPAESCKAHEENRAVFMNRFIYEVSRRNPFMYAPAILSLAAQYDKVVLACCKADNKEECFQTKRASIAKELREGSMLNEHVCSVIRKFGSRNLQATTIIKLSQKLTEANFTEIQKLALDVAHIHEECCQGNSLECLQDGEKVMTYICSQQNILSSKIAECCKLPMIQLGFCIIHAENGVKPEGLSLNPSQFLGDRNFAQFSSEEKIMFMASFLHEYSRTHPNLPVSVILRIAKTYQEILEKCSQSGNLPGCQDNLEEELQKHIEESQALSKQSCALYQTLGDYKLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKWSGCGEGMADIFIGHLCIRNEASPVNSGISHCCNSSYSNRRLCITSFLRDETYAPPPFSEDKFIFHKDLCQAQGKALQTMKQELLINLVKQKPELTEEQLAAVTADFSGLLEKCCKAQDQEVCFTEEGPKLISKTRDALGV |
animal organ regeneration cellular response to retinoic acid liver development liver regeneration ovulation from ovarian follicle pancreas development progesterone metabolic process response to dexamethasone response to organic substance sexual reproduction | cytoplasm; extracellular space | metal ion binding | Rattus norvegicus | Alternative splicing Copper Cytoplasm Disulfide bond Glycoprotein Metal-binding Phosphoprotein Reference proteome Repeat Secreted Signal Sulfation | MKQPATMKWS | MKQPATMKWSASISFLLLLNFAEPRVLHTNEFGIESTLDSSQCPTEKNMFNVATIVVAQFVQDATKAEVNKMSSDALAAMKENTGDGCLENQLSVFLDEICHETELSNKYGFSGCCNQSGVERHQCLLARKKTAPDSVPPFHFPETAESCPAYEENRAMSINTFIYDVSKRNPFLYAPTILYLAAQYDKAVPACCKADNMEECFQTKRASMAKELREGSMLNEHVCAVIRKFGSRNLQAVLIIKLSQKFPKANITEIRKLALDVAHIHEQCCHGNAMECLQDGESVMTHMCSQQEILSSKTAECCKLPTIELGYCIIHAENGDKPEGLTLNPSEFLGDRNFAQFSSEEKLLFMASFLHEYSRNHPNLPVSVILKTAKSYQEILEKCSQSETPSKCQDNMEEELQKHIQESQALAKQSCNLYQKLGPYYLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKRSACGEGLADIYIGHLCLRHEANPVNSGINHCCSSSYSNRRLCITSFLRDETYVPPPFSEDKFIFHKDLCQAQGRALQTMKQELLINLVKQKPEMTEEQHAAVTADFSGLLEKCCKDQDQEACFAKEGPKLISKTREALGV | animal organ regeneration cellular response to retinoic acid liver development liver regeneration ovulation from ovarian follicle pancreas development progesterone metabolic process response to dexamethasone response to organic substance sexual reproduction cytoplasm; extracellular space metal ion binding Rattus norvegicus Alternative splicing Copper Cytoplasm Disulfide bond Glycoprotein Metal-binding Phosphoprotein Reference proteome Repeat Secreted Signal Sulfation MKQPATMKWS MKQPATMKWSASISFLLLLNFAEPRVLHTNEFGIESTLDSSQCPTEKNMFNVATIVVAQFVQDATKAEVNKMSSDALAAMKENTGDGCLENQLSVFLDEICHETELSNKYGFSGCCNQSGVERHQCLLARKKTAPDSVPPFHFPETAESCPAYEENRAMSINTFIYDVSKRNPFLYAPTILYLAAQYDKAVPACCKADNMEECFQTKRASMAKELREGSMLNEHVCAVIRKFGSRNLQAVLIIKLSQKFPKANITEIRKLALDVAHIHEQCCHGNAMECLQDGESVMTHMCSQQEILSSKTAECCKLPTIELGYCIIHAENGDKPEGLTLNPSEFLGDRNFAQFSSEEKLLFMASFLHEYSRNHPNLPVSVILKTAKSYQEILEKCSQSETPSKCQDNMEEELQKHIQESQALAKQSCNLYQKLGPYYLQNLFLIGYTRKAPQLTSAELIDLTGKMVSIASTCCQLSEEKRSACGEGLADIYIGHLCLRHEANPVNSGINHCCSSSYSNRRLCITSFLRDETYVPPPFSEDKFIFHKDLCQAQGRALQTMKQELLINLVKQKPEMTEEQHAAVTADFSGLLEKCCKDQDQEACFAKEGPKLISKTREALGV |
vitamin D metabolic process vitamin transport | blood microparticle; cytoplasm; cytosol; extracellular exosome; extracellular region; extracellular space; lysosomal lumen | actin binding calcidiol binding vitamin D binding vitamin transmembrane transporter activity | Homo sapiens | 3D-structure Actin-binding Alternative splicing Direct protein sequencing Disulfide bond Glycoprotein Reference proteome Repeat Secreted Signal Transport Vitamin D | MKRVLVLLLA | MKRVLVLLLAVAFGHALERGRDYEKNKVCKEFSHLGKEDFTSLSLVLYSRKFPSGTFEQVSQLVKEVVSLTEACCAEGADPDCYDTRTSALSAKSCESNSPFPVHPGTAECCTKEGLERKLCMAALKHQPQEFPTYVEPTNDEICEAFRKDPKEYANQFMWEYSTNYGQAPLSLLVSYTKSYLSMVGSCCTSASPTVCFLKERLQLKHLSLLTTLSNRVCSQYAAYGEKKSRLSNLIKLAQKVPTADLEDVLPLAEDITNILSKCCESASEDCMAKELPEHTVKLCDNLSTKNSKFEDCCQEKTAMDVFVCTYFMPAAQLPELPDVELPTNKDVCDPGNTKVMDKYTFELSRRTHLPEVFLSKVLEPTLKSLGECCDVEDSTTCFNAKGPLLKKELSSFIDKGQELCADYSENTFTEYKKKLAERLKAKLPDATPTELAKLVNKHSDFASNCCSINSPPLYCDSEIDAELKNIL | vitamin D metabolic process vitamin transport blood microparticle; cytoplasm; cytosol; extracellular exosome; extracellular region; extracellular space; lysosomal lumen actin binding calcidiol binding vitamin D binding vitamin transmembrane transporter activity Homo sapiens 3D-structure Actin-binding Alternative splicing Direct protein sequencing Disulfide bond Glycoprotein Reference proteome Repeat Secreted Signal Transport Vitamin D MKRVLVLLLA MKRVLVLLLAVAFGHALERGRDYEKNKVCKEFSHLGKEDFTSLSLVLYSRKFPSGTFEQVSQLVKEVVSLTEACCAEGADPDCYDTRTSALSAKSCESNSPFPVHPGTAECCTKEGLERKLCMAALKHQPQEFPTYVEPTNDEICEAFRKDPKEYANQFMWEYSTNYGQAPLSLLVSYTKSYLSMVGSCCTSASPTVCFLKERLQLKHLSLLTTLSNRVCSQYAAYGEKKSRLSNLIKLAQKVPTADLEDVLPLAEDITNILSKCCESASEDCMAKELPEHTVKLCDNLSTKNSKFEDCCQEKTAMDVFVCTYFMPAAQLPELPDVELPTNKDVCDPGNTKVMDKYTFELSRRTHLPEVFLSKVLEPTLKSLGECCDVEDSTTCFNAKGPLLKKELSSFIDKGQELCADYSENTFTEYKKKLAERLKAKLPDATPTELAKLVNKHSDFASNCCSINSPPLYCDSEIDAELKNIL |
antimicrobial humoral immune response mediated by antimicrobial peptide cellular response to lipopolysaccharide chemokine-mediated signaling pathway defense response to bacterium glucose transmembrane transport inflammatory response neutrophil chemotaxis positive regulation of cell division | extracellular region; extracellular space; platelet alpha granule lumen; tertiary granule lumen | chemokine activity CXCR chemokine receptor binding glucose transmembrane transporter activity growth factor activity | Homo sapiens | 3D-structure Antibiotic Antimicrobial Chemotaxis Cleavage on pair of basic residues Cytokine Direct protein sequencing Disulfide bond Growth factor Mitogen Reference proteome Secreted Signal | MSLRLDTTPS | MSLRLDTTPSCNSARPLHALQVLLLLSLLLTALASSTKGQTKRNLAKGKEESLDSDLYAELRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKKLAGDESAD | antimicrobial humoral immune response mediated by antimicrobial peptide cellular response to lipopolysaccharide chemokine-mediated signaling pathway defense response to bacterium glucose transmembrane transport inflammatory response neutrophil chemotaxis positive regulation of cell division extracellular region; extracellular space; platelet alpha granule lumen; tertiary granule lumen chemokine activity CXCR chemokine receptor binding glucose transmembrane transporter activity growth factor activity Homo sapiens 3D-structure Antibiotic Antimicrobial Chemotaxis Cleavage on pair of basic residues Cytokine Direct protein sequencing Disulfide bond Growth factor Mitogen Reference proteome Secreted Signal MSLRLDTTPS MSLRLDTTPSCNSARPLHALQVLLLLSLLLTALASSTKGQTKRNLAKGKEESLDSDLYAELRCMCIKTTSGIHPKNIQSLEVIGKGTHCNQVEVIATLKDGRKICLDPDAPRIKKIVQKKLAGDESAD |
adenylate cyclase-activating G protein-coupled receptor signaling pathway antimicrobial humoral immune response mediated by antimicrobial peptide cellular response to lipopolysaccharide chemokine-mediated signaling pathway cytokine-mediated signaling pathway defense response to protozoan inflammatory response killing by host of symbiont cells leukocyte chemotaxis negative regulation of angiogenesis negative regulation of extrinsic apoptotic signaling pathway in absence of ligand negative regulation of megakaryocyte differentiation negative regulation of MHC class II biosynthetic process neutrophil chemotaxis platelet activation positive regulation of gene expression positive regulation of macrophage derived foam cell differentiation positive regulation of macrophage differentiation positive regulation of transcription by RNA polymerase II positive regulation of tumor necrosis factor production regulation of cell population proliferation | collagen-containing extracellular matrix; cytoplasm; extracellular region; extracellular space; platelet alpha granule lumen | chemokine activity CXCR chemokine receptor binding CXCR3 chemokine receptor binding heparin binding | Homo sapiens | 3D-structure Chemotaxis Cytokine Direct protein sequencing Disulfide bond Heparin-binding Phosphoprotein Reference proteome Secreted Signal | MSSAAGFCAS | MSSAAGFCASRPGLLFLGLLLLPLVVAFASAEAEEDGDLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQAPLYKKIIKKLLES | adenylate cyclase-activating G protein-coupled receptor signaling pathway antimicrobial humoral immune response mediated by antimicrobial peptide cellular response to lipopolysaccharide chemokine-mediated signaling pathway cytokine-mediated signaling pathway defense response to protozoan inflammatory response killing by host of symbiont cells leukocyte chemotaxis negative regulation of angiogenesis negative regulation of extrinsic apoptotic signaling pathway in absence of ligand negative regulation of megakaryocyte differentiation negative regulation of MHC class II biosynthetic process neutrophil chemotaxis platelet activation positive regulation of gene expression positive regulation of macrophage derived foam cell differentiation positive regulation of macrophage differentiation positive regulation of transcription by RNA polymerase II positive regulation of tumor necrosis factor production regulation of cell population proliferation collagen-containing extracellular matrix; cytoplasm; extracellular region; extracellular space; platelet alpha granule lumen chemokine activity CXCR chemokine receptor binding CXCR3 chemokine receptor binding heparin binding Homo sapiens 3D-structure Chemotaxis Cytokine Direct protein sequencing Disulfide bond Heparin-binding Phosphoprotein Reference proteome Secreted Signal MSSAAGFCAS MSSAAGFCASRPGLLFLGLLLLPLVVAFASAEAEEDGDLQCLCVKTTSQVRPRHITSLEVIKAGPHCPTAQLIATLKNGRKICLDLQAPLYKKIIKKLLES |
adenylate cyclase-activating G protein-coupled receptor signaling pathway antimicrobial humoral immune response mediated by antimicrobial peptide cellular response to lipopolysaccharide chemokine-mediated signaling pathway cytokine-mediated signaling pathway inflammatory response leukocyte chemotaxis negative regulation of angiogenesis negative regulation of megakaryocyte differentiation neutrophil chemotaxis platelet activation positive regulation of transcription by RNA polymerase II regulation of cell population proliferation | extracellular space | chemokine activity CXCR chemokine receptor binding CXCR3 chemokine receptor binding heparin binding | Bos taurus | 3D-structure Chemotaxis Cytokine Direct protein sequencing Disulfide bond Glycoprotein Heparin-binding Phosphoprotein Proteoglycan Reference proteome Secreted | ESSFPATFVP | ESSFPATFVPLPADSEGGEDEDLQCVCLKTTSGINPRHISSLEVIGAGTHCPSPQLLATKKTGRKICLDQQRPLYKKILKKLLDGDES | adenylate cyclase-activating G protein-coupled receptor signaling pathway antimicrobial humoral immune response mediated by antimicrobial peptide cellular response to lipopolysaccharide chemokine-mediated signaling pathway cytokine-mediated signaling pathway inflammatory response leukocyte chemotaxis negative regulation of angiogenesis negative regulation of megakaryocyte differentiation neutrophil chemotaxis platelet activation positive regulation of transcription by RNA polymerase II regulation of cell population proliferation extracellular space chemokine activity CXCR chemokine receptor binding CXCR3 chemokine receptor binding heparin binding Bos taurus 3D-structure Chemotaxis Cytokine Direct protein sequencing Disulfide bond Glycoprotein Heparin-binding Phosphoprotein Proteoglycan Reference proteome Secreted ESSFPATFVP ESSFPATFVPLPADSEGGEDEDLQCVCLKTTSGINPRHISSLEVIGAGTHCPSPQLLATKKTGRKICLDQQRPLYKKILKKLLDGDES |
phospholipid efflux positive regulation of sperm capacitation single fertilization sperm capacitation | cell surface; extracellular space | heparin binding | Bos taurus | 3D-structure Direct protein sequencing Disulfide bond Fertilization Glycoprotein Reference proteome Repeat Secreted Signal | MALQLGLFLI | MALQLGLFLIWAGVSVFLQLDPVNGDQDEGVSTEPTQDGPAELPEDEECVFPFVYRNRKHFDCTVHGSLFPWCSLDADYVGRWKYCAQRDYAKCVFPFIYGGKKYETCTKIGSMWMSWCSLSPNYDKDRAWKYC | phospholipid efflux positive regulation of sperm capacitation single fertilization sperm capacitation cell surface; extracellular space heparin binding Bos taurus 3D-structure Direct protein sequencing Disulfide bond Fertilization Glycoprotein Reference proteome Repeat Secreted Signal MALQLGLFLI MALQLGLFLIWAGVSVFLQLDPVNGDQDEGVSTEPTQDGPAELPEDEECVFPFVYRNRKHFDCTVHGSLFPWCSLDADYVGRWKYCAQRDYAKCVFPFIYGGKKYETCTKIGSMWMSWCSLSPNYDKDRAWKYC |
actin filament organization antibacterial humoral response cellular response to iron ion ERK1 and ERK2 cascade intracellular iron ion homeostasis iron ion transport osteoclast differentiation positive regulation of bone resorption positive regulation of cell motility positive regulation of DNA-templated transcription positive regulation of phosphorylation positive regulation of receptor-mediated endocytosis regulation of iron ion transport regulation of protein stability | apical plasma membrane; basal part of cell; basal plasma membrane; blood microparticle; cell surface; clathrin-coated endocytic vesicle membrane; clathrin-coated pit; cytoplasmic vesicle; early endosome; endocytic vesicle; endoplasmic reticulum lumen; endosome membrane; extracellular exosome; extracellular region; extracellular space; HFE-transferrin receptor complex; late endosome; perinuclear region of cytoplasm; plasma membrane; recycling endosome; secretory granule lumen; vesicle | ferric iron binding ferrous iron binding iron chaperone activity transferrin receptor binding | Homo sapiens | 3D-structure Direct protein sequencing Disease variant Disulfide bond Glycoprotein Ion transport Iron Iron transport Metal-binding Methylation Phosphoprotein Reference proteome Repeat Secreted Signal Transport | MRLAVGALLV | MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP | actin filament organization antibacterial humoral response cellular response to iron ion ERK1 and ERK2 cascade intracellular iron ion homeostasis iron ion transport osteoclast differentiation positive regulation of bone resorption positive regulation of cell motility positive regulation of DNA-templated transcription positive regulation of phosphorylation positive regulation of receptor-mediated endocytosis regulation of iron ion transport regulation of protein stability apical plasma membrane; basal part of cell; basal plasma membrane; blood microparticle; cell surface; clathrin-coated endocytic vesicle membrane; clathrin-coated pit; cytoplasmic vesicle; early endosome; endocytic vesicle; endoplasmic reticulum lumen; endosome membrane; extracellular exosome; extracellular region; extracellular space; HFE-transferrin receptor complex; late endosome; perinuclear region of cytoplasm; plasma membrane; recycling endosome; secretory granule lumen; vesicle ferric iron binding ferrous iron binding iron chaperone activity transferrin receptor binding Homo sapiens 3D-structure Direct protein sequencing Disease variant Disulfide bond Glycoprotein Ion transport Iron Iron transport Metal-binding Methylation Phosphoprotein Reference proteome Repeat Secreted Signal Transport MRLAVGALLV MRLAVGALLVCAVLGLCLAVPDKTVRWCAVSEHEATKCQSFRDHMKSVIPSDGPSVACVKKASYLDCIRAIAANEADAVTLDAGLVYDAYLAPNNLKPVVAEFYGSKEDPQTFYYAVAVVKKDSGFQMNQLRGKKSCHTGLGRSAGWNIPIGLLYCDLPEPRKPLEKAVANFFSGSCAPCADGTDFPQLCQLCPGCGCSTLNQYFGYSGAFKCLKDGAGDVAFVKHSTIFENLANKADRDQYELLCLDNTRKPVDEYKDCHLAQVPSHTVVARSMGGKEDLIWELLNQAQEHFGKDKSKEFQLFSSPHGKDLLFKDSAHGFLKVPPRMDAKMYLGYEYVTAIRNLREGTCPEAPTDECKPVKWCALSHHERLKCDEWSVNSVGKIECVSAETTEDCIAKIMNGEADAMSLDGGFVYIAGKCGLVPVLAENYNKSDNCEDTPEAGYFAVAVVKKSASDLTWDNLKGKKSCHTAVGRTAGWNIPMGLLYNKINHCRFDEFFSEGCAPGSKKDSSLCKLCMGSGLNLCEPNNKEGYYGYTGAFRCLVEKGDVAFVKHQTVPQNTGGKNPDPWAKNLNEKDYELLCLDGTRKPVEEYANCHLARAPNHAVVTRKDKEACVHKILRQQQHLFGSNVTDCSGNFCLFRSETKDLLFRDDTVCLAKLHDRNTYEKYLGEEYVKAVGNLRKCSTSSLLEACTFRRP |
acute-phase response antibacterial humoral response antimicrobial humoral response extracellular sequestering of iron ion intracellular sequestering of iron ion iron ion transport response to lipopolysaccharide response to xenobiotic stimulus | early endosome; extracellular space; organomineral extracellular matrix; plasma membrane; recycling endosome | ferric iron binding iron ion binding | Gallus gallus | 3D-structure Allergen Direct protein sequencing Disulfide bond Glycoprotein Ion transport Iron Iron transport Metal-binding Reference proteome Repeat Secreted Signal Transport | MKLILCTVLS | MKLILCTVLSLGIAAVCFAAPPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQAFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYKTCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPSLMDSQLYLGFEYYSAIQSMRKDQLTPSPRENRIQWCAVGKDEKSKCDRWSVVSNGDVECTVVDETKDCIIKIMKGEADAVALDGGLVYTAGVCGLVPVMAERYDDESQCSKTDERPASYFAVAVARKDSNVNWNNLKGKKSCHTAVGRTAGWVIPMGLIHNRTGTCNFDEYFSEGCAPGSPPNSRLCQLCQGSGGIPPEKCVASSHEKYFGYTGALRCLVEKGDVAFIQHSTVEENTGGKNKADWAKNLQMDDFELLCTDGRRANVMDYRECNLAEVPTHAVVVRPEKANKIRDLLERQEKRFGVNGSEKSKFMMFESQNKDLLFKDLTKCLFKVREGTTYKEFLGDKFYTVISSLKTCNPSDILQMCSFLEGK | acute-phase response antibacterial humoral response antimicrobial humoral response extracellular sequestering of iron ion intracellular sequestering of iron ion iron ion transport response to lipopolysaccharide response to xenobiotic stimulus early endosome; extracellular space; organomineral extracellular matrix; plasma membrane; recycling endosome ferric iron binding iron ion binding Gallus gallus 3D-structure Allergen Direct protein sequencing Disulfide bond Glycoprotein Ion transport Iron Iron transport Metal-binding Reference proteome Repeat Secreted Signal Transport MKLILCTVLS MKLILCTVLSLGIAAVCFAAPPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQAFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYKTCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPSLMDSQLYLGFEYYSAIQSMRKDQLTPSPRENRIQWCAVGKDEKSKCDRWSVVSNGDVECTVVDETKDCIIKIMKGEADAVALDGGLVYTAGVCGLVPVMAERYDDESQCSKTDERPASYFAVAVARKDSNVNWNNLKGKKSCHTAVGRTAGWVIPMGLIHNRTGTCNFDEYFSEGCAPGSPPNSRLCQLCQGSGGIPPEKCVASSHEKYFGYTGALRCLVEKGDVAFIQHSTVEENTGGKNKADWAKNLQMDDFELLCTDGRRANVMDYRECNLAEVPTHAVVVRPEKANKIRDLLERQEKRFGVNGSEKSKFMMFESQNKDLLFKDLTKCLFKVREGTTYKEFLGDKFYTVISSLKTCNPSDILQMCSFLEGK |
heme metabolic process heme transport hemoglobin metabolic process intracellular iron ion homeostasis positive regulation of humoral immune response mediated by circulating immunoglobulin positive regulation of immunoglobulin production positive regulation of type II interferon-mediated signaling pathway positive regulation of tyrosine phosphorylation of STAT protein type II interferon-mediated signaling pathway | blood microparticle; collagen-containing extracellular matrix; endocytic vesicle lumen; extracellular exosome; extracellular region; extracellular space | heme transmembrane transporter activity metal ion binding | Homo sapiens | Direct protein sequencing Disulfide bond Glycoprotein Heme Host-virus interaction Iron Metal-binding Reference proteome Repeat Secreted Signal Transport | MARVLGAPVA | MARVLGAPVALGLWSLCWSLAIATPLPPTSAHGNVAEGETKPDPDVTERCSDGWSFDATTLDDNGTMLFFKGEFVWKSHKWDRELISERWKNFPSPVDAAFRQGHNSVFLIKGDKVWVYPPEKKEKGYPKLLQDEFPGIPSPLDAAVECHRGECQAEGVLFFQGDREWFWDLATGTMKERSWPAVGNCSSALRWLGRYYCFQGNQFLRFDPVRGEVPPRYPRDVRDYFMPCPGRGHGHRNGTGHGNSTHHGPEYMRCSPHLVLSALTSDNHGATYAFSGTHYWRLDTSRDGWHSWPIAHQWPQGPSAVDAAFSWEEKLYLVQGTQVYVFLTKGGYTLVSGYPKRLEKEVGTPHGIILDSVDAAFICPGSSRLHIMAGRRLWWLDLKSGAQATWTELPWPHEKVDGALCMEKSLGPNSCSANGPGLYLIHGPNLYCYSDVEKLNAAKALPQPQNVTSLLGCTH | heme metabolic process heme transport hemoglobin metabolic process intracellular iron ion homeostasis positive regulation of humoral immune response mediated by circulating immunoglobulin positive regulation of immunoglobulin production positive regulation of type II interferon-mediated signaling pathway positive regulation of tyrosine phosphorylation of STAT protein type II interferon-mediated signaling pathway blood microparticle; collagen-containing extracellular matrix; endocytic vesicle lumen; extracellular exosome; extracellular region; extracellular space heme transmembrane transporter activity metal ion binding Homo sapiens Direct protein sequencing Disulfide bond Glycoprotein Heme Host-virus interaction Iron Metal-binding Reference proteome Repeat Secreted Signal Transport MARVLGAPVA MARVLGAPVALGLWSLCWSLAIATPLPPTSAHGNVAEGETKPDPDVTERCSDGWSFDATTLDDNGTMLFFKGEFVWKSHKWDRELISERWKNFPSPVDAAFRQGHNSVFLIKGDKVWVYPPEKKEKGYPKLLQDEFPGIPSPLDAAVECHRGECQAEGVLFFQGDREWFWDLATGTMKERSWPAVGNCSSALRWLGRYYCFQGNQFLRFDPVRGEVPPRYPRDVRDYFMPCPGRGHGHRNGTGHGNSTHHGPEYMRCSPHLVLSALTSDNHGATYAFSGTHYWRLDTSRDGWHSWPIAHQWPQGPSAVDAAFSWEEKLYLVQGTQVYVFLTKGGYTLVSGYPKRLEKEVGTPHGIILDSVDAAFICPGSSRLHIMAGRRLWWLDLKSGAQATWTELPWPHEKVDGALCMEKSLGPNSCSANGPGLYLIHGPNLYCYSDVEKLNAAKALPQPQNVTSLLGCTH |
intracellular iron ion homeostasis intracellular sequestering of iron ion iron ion transport | autolysosome; azurophil granule lumen; cytoplasm; cytosol; extracellular exosome; extracellular region; intracellular ferritin complex; membrane | ferric iron binding ferrous iron binding identical protein binding iron ion binding | Homo sapiens | 3D-structure Acetylation Cataract Direct protein sequencing Disease variant Iron Iron storage Metal-binding Neurodegeneration Reference proteome | MSSQIRQNYS | MSSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD | intracellular iron ion homeostasis intracellular sequestering of iron ion iron ion transport autolysosome; azurophil granule lumen; cytoplasm; cytosol; extracellular exosome; extracellular region; intracellular ferritin complex; membrane ferric iron binding ferrous iron binding identical protein binding iron ion binding Homo sapiens 3D-structure Acetylation Cataract Direct protein sequencing Disease variant Iron Iron storage Metal-binding Neurodegeneration Reference proteome MSSQIRQNYS MSSQIRQNYSTDVEAAVNSLVNLYLQASYTYLSLGFYFDRDDVALEGVSHFFRELAEEKREGYERLLKMQNQRGGRALFQDIKKPAEDEWGKTPDAMKAAMALEKKLNQALLDLHALGSARTDPHLCDFLETHFLDEEVKLIKKMGDHLTNLHRLGGPEAGLGEYLFERLTLKHD |
immune response intracellular iron ion homeostasis intracellular sequestering of iron ion iron ion transport negative regulation of cell population proliferation negative regulation of fibroblast proliferation | autolysosome; cytoplasm; cytosol; extracellular exosome; extracellular region; ficolin-1-rich granule lumen; intracellular ferritin complex; nucleus; tertiary granule lumen | ferric iron binding ferrous iron binding ferroxidase activity identical protein binding iron ion binding iron ion sequestering activity | Homo sapiens | 3D-structure Acetylation Cytoplasm Iron Iron storage Metal-binding Oxidoreductase Phosphoprotein Reference proteome | MTTASTSQVR | MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES | immune response intracellular iron ion homeostasis intracellular sequestering of iron ion iron ion transport negative regulation of cell population proliferation negative regulation of fibroblast proliferation autolysosome; cytoplasm; cytosol; extracellular exosome; extracellular region; ficolin-1-rich granule lumen; intracellular ferritin complex; nucleus; tertiary granule lumen ferric iron binding ferrous iron binding ferroxidase activity identical protein binding iron ion binding iron ion sequestering activity Homo sapiens 3D-structure Acetylation Cytoplasm Iron Iron storage Metal-binding Oxidoreductase Phosphoprotein Reference proteome MTTASTSQVR MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKKPDCDDWESGLNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES |
cellular response to cadmium ion cellular response to copper ion cellular response to erythropoietin cellular response to interleukin-3 cellular response to zinc ion detoxification of copper ion intracellular copper ion homeostasis intracellular zinc ion homeostasis negative regulation of growth | cytoplasm; cytosol; nucleus | metal ion binding zinc ion binding | Homo sapiens | 3D-structure Acetylation Cadmium Direct protein sequencing Metal-binding Metal-thiolate cluster Phosphoprotein Reference proteome Zinc | MDPNCSCAAG | MDPNCSCAAGDSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA | cellular response to cadmium ion cellular response to copper ion cellular response to erythropoietin cellular response to interleukin-3 cellular response to zinc ion detoxification of copper ion intracellular copper ion homeostasis intracellular zinc ion homeostasis negative regulation of growth cytoplasm; cytosol; nucleus metal ion binding zinc ion binding Homo sapiens 3D-structure Acetylation Cadmium Direct protein sequencing Metal-binding Metal-thiolate cluster Phosphoprotein Reference proteome Zinc MDPNCSCAAG MDPNCSCAAGDSCTCAGSCKCKECKCTSCKKSCCSCCPVGCAKCAQGCICKGASDKCSCCA |
cellular response to cadmium ion cellular response to copper ion cellular response to zinc ion detoxification of copper ion intracellular zinc ion homeostasis negative regulation of growth nitric oxide mediated signal transduction response to bacterium | cytoplasm; cytosol; nucleus | cadmium ion binding metal ion binding zinc ion binding | Mus musculus | Acetylation Direct protein sequencing Metal-binding Metal-thiolate cluster Phosphoprotein Reference proteome | MDPNCSCASD | MDPNCSCASDGSCSCAGACKCKQCKCTSCKKSCCSCCPVGCAKCSQGCICKEASDKCSCCA | cellular response to cadmium ion cellular response to copper ion cellular response to zinc ion detoxification of copper ion intracellular zinc ion homeostasis negative regulation of growth nitric oxide mediated signal transduction response to bacterium cytoplasm; cytosol; nucleus cadmium ion binding metal ion binding zinc ion binding Mus musculus Acetylation Direct protein sequencing Metal-binding Metal-thiolate cluster Phosphoprotein Reference proteome MDPNCSCASD MDPNCSCASDGSCSCAGACKCKQCKCTSCKKSCCSCCPVGCAKCSQGCICKEASDKCSCCA |
cellular response to cadmium ion cellular response to chromate cellular response to copper ion cellular response to zinc ion detoxification of copper ion intracellular monoatomic cation homeostasis intracellular zinc ion homeostasis negative regulation of growth negative regulation of neuron apoptotic process nitric oxide mediated signal transduction | cytoplasm; cytosol; lysosome; nucleus | copper ion binding metal ion binding zinc ion binding | Mus musculus | 3D-structure Acetylation Direct protein sequencing Metal-binding Metal-thiolate cluster Reference proteome | MDPNCSCSTG | MDPNCSCSTGGSCTCTSSCACKNCKCTSCKKSCCSCCPVGCSKCAQGCVCKGAADKCTCCA | cellular response to cadmium ion cellular response to chromate cellular response to copper ion cellular response to zinc ion detoxification of copper ion intracellular monoatomic cation homeostasis intracellular zinc ion homeostasis negative regulation of growth negative regulation of neuron apoptotic process nitric oxide mediated signal transduction cytoplasm; cytosol; lysosome; nucleus copper ion binding metal ion binding zinc ion binding Mus musculus 3D-structure Acetylation Direct protein sequencing Metal-binding Metal-thiolate cluster Reference proteome MDPNCSCSTG MDPNCSCSTGGSCTCTSSCACKNCKCTSCKKSCCSCCPVGCSKCAQGCVCKGAADKCTCCA |
biomineral tissue development defense response to bacterium negative regulation of bone mineralization ossification saliva secretion | extracellular region | extracellular matrix constituent, lubricant activity hydroxyapatite binding structural constituent of tooth enamel | Homo sapiens | Alternative splicing Biomineralization Direct protein sequencing Isopeptide bond Phosphoprotein Reference proteome Secreted Signal Sulfation | MKFLVFAFIL | MKFLVFAFILALMVSMIGADSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF | biomineral tissue development defense response to bacterium negative regulation of bone mineralization ossification saliva secretion extracellular region extracellular matrix constituent, lubricant activity hydroxyapatite binding structural constituent of tooth enamel Homo sapiens Alternative splicing Biomineralization Direct protein sequencing Isopeptide bond Phosphoprotein Reference proteome Secreted Signal Sulfation MKFLVFAFIL MKFLVFAFILALMVSMIGADSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF |
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