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 |
|---|---|---|---|---|---|---|---|
response to jasmonic acid response to salicylic acid response to UV-C terpenoid biosynthetic process | membrane | heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Thymus vulgaris | Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix | MDISISWVVI | MDISISWVVIIVFVLSYLILMDKWRASKLPGNLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVHSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNDDMIFSRYNDHWRQIRKICVSELLSPRNVRSFGFIRQDEMARLIRVFESSEGAAINASEEISKMSCAIVCRAAFGSVLKDQGKLADLVKEALSMASGFELADLYPSSWLLNLLCFNKYRLQRMRGRLDNILDGFLEEHKVKKSGEFGGEDIIDVLYRMQKDTEMKAPITNNGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKMVKAQAEVREKLKGKTNPDVADVQELKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRILVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRVCPGLHFGLANVEVPLAQLLYHFDYKLPSAMTAADMDMSETPGLSGPRKNPLIMIPTIHNPTS | response to jasmonic acid response to salicylic acid response to UV-C terpenoid biosynthetic process membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Thymus vulgaris Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix MDISISWVVI MDISISWVVIIVFVLSYLILMDKWRASKLPGNLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVHSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNDDMIFSRYNDHWRQIRKICVSELLSPRNVRSFGFIRQDEMARLIRVFESSEGAAINASEEISKMSCAIVCRAAFGSVLKDQGKLADLVKEALSMASGFELADLYPSSWLLNLLCFNKYRLQRMRGRLDNILDGFLEEHKVKKSGEFGGEDIIDVLYRMQKDTEMKAPITNNGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKMVKAQAEVREKLKGKTNPDVADVQELKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRILVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRVCPGLHFGLANVEVPLAQLLYHFDYKLPSAMTAADMDMSETPGLSGPRKNPLIMIPTIHNPTS |
defense response to insect response to insect response to water deprivation terpenoid biosynthetic process | membrane | heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Origanum vulgare | Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix | MDISISWVVI | MDISISWVVIIVFVLSYLILMDKWRASKLPGNLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVHSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNDDMIFSRYNDHWRQIRKICVSELLSPRNVRSFGFIRQDEMARLIRVFESSEGAAINASEEISKMSCAIVCRAAFGSVLKDQGKLADLVKEALSMASGFELADLYPSSWLLNLLCVNKYRLQRMRGRLDNILDGFLEEHKVKKSGEFGGEDIVDVLYRMQKDTEMKAPITNNGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKMVKAQAEVREKLKGKTNPDVADVQELKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRTLVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRVCPGLHFGLANVEVPLAQLLYHFDYKLPSAMTAADMDMSETPGLSGPRKNPLIMIPTIHNPTS | defense response to insect response to insect response to water deprivation terpenoid biosynthetic process membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Origanum vulgare Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix MDISISWVVI MDISISWVVIIVFVLSYLILMDKWRASKLPGNLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVHSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNDDMIFSRYNDHWRQIRKICVSELLSPRNVRSFGFIRQDEMARLIRVFESSEGAAINASEEISKMSCAIVCRAAFGSVLKDQGKLADLVKEALSMASGFELADLYPSSWLLNLLCVNKYRLQRMRGRLDNILDGFLEEHKVKKSGEFGGEDIVDVLYRMQKDTEMKAPITNNGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKMVKAQAEVREKLKGKTNPDVADVQELKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRTLVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRVCPGLHFGLANVEVPLAQLLYHFDYKLPSAMTAADMDMSETPGLSGPRKNPLIMIPTIHNPTS |
response to insect terpenoid biosynthetic process | membrane | heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Origanum vulgare | Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix | MDISISWVAI | MDISISWVAIILVISSYFIFMNKWRAAKLPENLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVYSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNNDMIFSRYNDHWRQIRKICVSELLSPKNVRSFGFIRQDEMARLIRVFESSVGVPINASEEISKMSCAIVCRAAFGSVLKDQGLLADLVKEALGMASGFELADLYPSSWLLNLLCFNKYRLRRMRQRLDDILDGFLEEHRVKKSGEFGGEDIIDVLYRMQKDSENKVPITNSGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKLAKAQAEVREKLKGKTNPDVAEVQEIKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRILVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRICPGLHFGLANVEVPLAQLLYHFEWKLPQGMTPADMDMSETPGLSGPRKNPLIMVPTIHNPTS | response to insect terpenoid biosynthetic process membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Origanum vulgare Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix MDISISWVAI MDISISWVAIILVISSYFIFMNKWRAAKLPENLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVYSVVLSSAESTKQAMKVLDPTFADRFDSIGSQIMWYNNNDMIFSRYNDHWRQIRKICVSELLSPKNVRSFGFIRQDEMARLIRVFESSVGVPINASEEISKMSCAIVCRAAFGSVLKDQGLLADLVKEALGMASGFELADLYPSSWLLNLLCFNKYRLRRMRQRLDDILDGFLEEHRVKKSGEFGGEDIIDVLYRMQKDSENKVPITNSGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKLAKAQAEVREKLKGKTNPDVAEVQEIKYLHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRILVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRICPGLHFGLANVEVPLAQLLYHFEWKLPQGMTPADMDMSETPGLSGPRKNPLIMVPTIHNPTS |
terpenoid biosynthetic process | membrane | heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Thymus vulgaris | Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix | MDISILWVAI | MDISILWVAIILVISSYFIFMNKWRAAKLPENLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVYSVVLSSAESTKQAMKVLDPTFADRFDSFGSQIMWYNNNDMIFSRYNDHWRQIRKICVSELLSPKNVRSFGFIRQDEMARLIRVFESSVGVPINASEEISKMSCAIVCRAAFGSVLKDQGLLADLVKEALGMASGFELADLYPSSWLLNLLCFNKYRLRRMRQRLDDILDGFLEEHRVKKSGEFGGEDIIDVLYRMQKDSENKVPITNSGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKLAKAQAEVREKLKGKTNPDVAEVQEIKYPHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRILVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRICPGLHFGLANVEVPLAQLLYHFEWKLPQGMTPADMDMSETPGLSGPRKNPLIMVPTIHNPTS | terpenoid biosynthetic process membrane heme binding iron ion binding monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen Thymus vulgaris Heme Iron Membrane Metal-binding Monooxygenase Oxidoreductase Signal-anchor Transmembrane Transmembrane helix MDISILWVAI MDISILWVAIILVISSYFIFMNKWRAAKLPENLPPSPPKLPVIGHLHLLRGGLPQHVLRGITQKYGAVAHLQLGEVYSVVLSSAESTKQAMKVLDPTFADRFDSFGSQIMWYNNNDMIFSRYNDHWRQIRKICVSELLSPKNVRSFGFIRQDEMARLIRVFESSVGVPINASEEISKMSCAIVCRAAFGSVLKDQGLLADLVKEALGMASGFELADLYPSSWLLNLLCFNKYRLRRMRQRLDDILDGFLEEHRVKKSGEFGGEDIIDVLYRMQKDSENKVPITNSGIKGFIFDVFSAGTETSATTIQWALSELMKNPEKLAKAQAEVREKLKGKTNPDVAEVQEIKYPHSVVKETLRLHPPFPLIPRLCKEECEVTGYTIPAKTRILVNVWSIGRDPAYWKDPDTFNPDRFDEVSRDVIGNDFELIPFGAGRRICPGLHFGLANVEVPLAQLLYHFEWKLPQGMTPADMDMSETPGLSGPRKNPLIMVPTIHNPTS |
cinnamic acid biosynthetic process L-phenylalanine catabolic process lignin biosynthetic process protein homotetramerization response to water deprivation salicylic acid biosynthetic process | cytoplasm | phenylalanine ammonia-lyase activity protein self-association tyrosine ammonia-lyase activity | Fritillaria unibracteata | Cytoplasm Lyase Phenylalanine catabolism Phenylpropanoid metabolism | MAHIGNGNGN | MAHIGNGNGNGNGFANGNGNGNGAAGLCLHPDPLNWRAAADALTGSHLDEVRRMAAEFRKPVVRLEGASLSISQVAAVAAGREVKVELSEEARGRVKASSDWVMDSMGKGTDSYGVTTGFGATSHRRTKEGGALQKELIRFLNAGIFGAGPEDGQTLPPTTTRAAMLVRVNTLLQGYSGIRFEILEAISSLLNHNVTPILPLRGTISSSGDLVPLSYIAGVLIGRPNSKSIGPDGTYVDATEAFRLAGISGGFFELQPKEGLAMVNGTAVGSGLASMVLFEANIIAVLAEVISAIFCEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILAGSSYMKMAAKIHEQDPLQKPKQDRYALRTSPQWLGPLIEVIRTSTKSIEREINSVNDNPLIDVSRNKAIHGGNFQGTPIGVSMDNTRLVLAAIGKLMFAQISELVNDFYNNGLPSNLSGGRNPSLDYGFKGAEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISARKTAEAVEILKLMSSTFLVALCQAVDLRHLEENLKAAVKNTVSQVAKRVLTMGVNGELHPSRFCEKDLIKVIDREYVFAYADDPCSATYPLMQKLRGVLVEHALVNGDKEKEMGTSIFQKITAFEEELKATLPKEVEGVRVAFDNGTNVIPNRISECRSYPLYKFVREELGAGYLTGEKVVSPGEEFNKVFVAMNQWKLIDPLLECLSDWNGAPLPIC | cinnamic acid biosynthetic process L-phenylalanine catabolic process lignin biosynthetic process protein homotetramerization response to water deprivation salicylic acid biosynthetic process cytoplasm phenylalanine ammonia-lyase activity protein self-association tyrosine ammonia-lyase activity Fritillaria unibracteata Cytoplasm Lyase Phenylalanine catabolism Phenylpropanoid metabolism MAHIGNGNGN MAHIGNGNGNGNGFANGNGNGNGAAGLCLHPDPLNWRAAADALTGSHLDEVRRMAAEFRKPVVRLEGASLSISQVAAVAAGREVKVELSEEARGRVKASSDWVMDSMGKGTDSYGVTTGFGATSHRRTKEGGALQKELIRFLNAGIFGAGPEDGQTLPPTTTRAAMLVRVNTLLQGYSGIRFEILEAISSLLNHNVTPILPLRGTISSSGDLVPLSYIAGVLIGRPNSKSIGPDGTYVDATEAFRLAGISGGFFELQPKEGLAMVNGTAVGSGLASMVLFEANIIAVLAEVISAIFCEVMQGKPEFTDHLTHKLKHHPGQIEAAAIMEHILAGSSYMKMAAKIHEQDPLQKPKQDRYALRTSPQWLGPLIEVIRTSTKSIEREINSVNDNPLIDVSRNKAIHGGNFQGTPIGVSMDNTRLVLAAIGKLMFAQISELVNDFYNNGLPSNLSGGRNPSLDYGFKGAEIAMASYCSELQFLANPVTNHVQSAEQHNQDVNSLGLISARKTAEAVEILKLMSSTFLVALCQAVDLRHLEENLKAAVKNTVSQVAKRVLTMGVNGELHPSRFCEKDLIKVIDREYVFAYADDPCSATYPLMQKLRGVLVEHALVNGDKEKEMGTSIFQKITAFEEELKATLPKEVEGVRVAFDNGTNVIPNRISECRSYPLYKFVREELGAGYLTGEKVVSPGEEFNKVFVAMNQWKLIDPLLECLSDWNGAPLPIC |
aromatic compound biosynthetic process | cytoplasm | acyltransferase activity transferase activity | Piper nigrum | Acyltransferase Cytoplasm Transferase | MAPSSQLEFN | MAPSSQLEFNVVRKQPELLPPAEPTPFEWKELSDIDDQDGLRLHISGFFIYPPSTMSNVGRDNVARDIRLGLSKAMVFYYPLAGRIREGPNRKLSVECTGEGIMYCEADADVRLEQFGDIGALSMPFPFMDKVMFETVDDGILGTPLMYFQSTRFICGGIVIAGCYNHAIADGLGFYMFMAAAAQLARGAASPTPLPVWQRERLLSRVPPRVTFIHHEYIHDTPKTETANPLDNEPWPLHSIFFTRVDVAALRAQLPGHLRKSATSFEIISACLWRCRTAALRFAPDELSRLIIAVNARTKFGPPLPQGYYGNSIMLPMVVSEAGKLVLSGLGYAVELVIEAKGKVTEEYVKSVADYLVLNGRPHYVVTNTYLVSDLRQLVEMSKFDWGWGKPAYVGPADVGENAISFLATLKNGEEEGVVVPIRLPESAVGRFKSEVSKMVSFGCLEDVKPNRDGYLSRM | aromatic compound biosynthetic process cytoplasm acyltransferase activity transferase activity Piper nigrum Acyltransferase Cytoplasm Transferase MAPSSQLEFN MAPSSQLEFNVVRKQPELLPPAEPTPFEWKELSDIDDQDGLRLHISGFFIYPPSTMSNVGRDNVARDIRLGLSKAMVFYYPLAGRIREGPNRKLSVECTGEGIMYCEADADVRLEQFGDIGALSMPFPFMDKVMFETVDDGILGTPLMYFQSTRFICGGIVIAGCYNHAIADGLGFYMFMAAAAQLARGAASPTPLPVWQRERLLSRVPPRVTFIHHEYIHDTPKTETANPLDNEPWPLHSIFFTRVDVAALRAQLPGHLRKSATSFEIISACLWRCRTAALRFAPDELSRLIIAVNARTKFGPPLPQGYYGNSIMLPMVVSEAGKLVLSGLGYAVELVIEAKGKVTEEYVKSVADYLVLNGRPHYVVTNTYLVSDLRQLVEMSKFDWGWGKPAYVGPADVGENAISFLATLKNGEEEGVVVPIRLPESAVGRFKSEVSKMVSFGCLEDVKPNRDGYLSRM |
aromatic compound biosynthetic process | cytoplasm | acyltransferase activity transferase activity | Piper nigrum | Acyltransferase Cytoplasm Transferase | MASSQLEFNV | MASSQLEFNVERKQPELLGPAEPTPYELKELSDIDDQDGVRLFLTAIFIYPPPTKTSMPTRKTDPASDIRRGLSKAMVYYYPFAGRIREGPNRKLSVDCTGEGIVFCEADADIRLDGLGDVEVLRPPYPFIDKMTLGEGSAILGAPLVYVQVTRFACGGFIITGRFNHVMADAPGFTMFMKAAADLARGATVPMPLPVWERERYRSRVPPRVTFAHHEYMHVDDPPPRPTSEPWSLHSAFFTKADVATLRAQLPADLRKAATSFDIITACMWRCRVSALQYGPDEVVRLIVAVNSRTKFDPPLTGYYGNGLMLPAAVTEAGKLVGSDLGYAVELVREAKGKVTEEYVRSAADFLVLNGRVHFVVSNTFLVSDLRRLIDLANMDWGWGKAVSGGPVDVGENVISFLATSKNSAGEEGAVVPFCLPDSALGRFTSEVKKLVCFRPLENAAASNPDHGYMSRM | aromatic compound biosynthetic process cytoplasm acyltransferase activity transferase activity Piper nigrum Acyltransferase Cytoplasm Transferase MASSQLEFNV MASSQLEFNVERKQPELLGPAEPTPYELKELSDIDDQDGVRLFLTAIFIYPPPTKTSMPTRKTDPASDIRRGLSKAMVYYYPFAGRIREGPNRKLSVDCTGEGIVFCEADADIRLDGLGDVEVLRPPYPFIDKMTLGEGSAILGAPLVYVQVTRFACGGFIITGRFNHVMADAPGFTMFMKAAADLARGATVPMPLPVWERERYRSRVPPRVTFAHHEYMHVDDPPPRPTSEPWSLHSAFFTKADVATLRAQLPADLRKAATSFDIITACMWRCRVSALQYGPDEVVRLIVAVNSRTKFDPPLTGYYGNGLMLPAAVTEAGKLVGSDLGYAVELVREAKGKVTEEYVRSAADFLVLNGRVHFVVSNTFLVSDLRRLIDLANMDWGWGKAVSGGPVDVGENVISFLATSKNSAGEEGAVVPFCLPDSALGRFTSEVKKLVCFRPLENAAASNPDHGYMSRM |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Cebus capucinus | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKVLWAALLV | MKVLWAALLVAFLAGCQGKVEQVVEPELEPELEPHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMEETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGTLVEQGRARAATVGSSLASQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTTPVPSDNH | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation neuron projection development positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Cebus capucinus Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKVLWAALLV MKVLWAALLVAFLAGCQGKVEQVVEPELEPELEPHQQADWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSSQVTQELTALMEETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLAQYRSEVQAMLGQSTDELRARLASHLRKLRKRLLRDVDDLQKRLAVYQAGAREGAERGVSAIRERLGTLVEQGRARAATVGSSLASQPLQERAQAWGERLRARMEEVGSRTRDRLDEVKEQVEEVRAKLEEQAQQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTTPVPSDNH |
fructose 6-phosphate metabolic process | cell surface; cytoplasm | 6-phosphofructokinase activity ATP binding mannan binding metal ion binding | Lactococcus lactis subsp. lactis | Allosteric enzyme ATP-binding Cytoplasm Direct protein sequencing Glycolysis Kinase Magnesium Metal-binding Nucleotide-binding Transferase | MKRIAVLTSG | MKRIAVLTSGGDAPGMNAAIRAVVRKAISEGIEVYGINHGYAGMVAGDIFPLTSASVGDKIGRGGTFLYSARYPEFAQVEGQLAGIEQLKKFGIEGVVVIGGDGSYHGAMRLTEHGFPAVGLPGTIDNDIVGTDFTIGFDTAVSTVVDALDKIRDTSSSHNRTFVVEVMGRNAGDIALNAGIAAGADDISIPELEFKFENVVNNINKGYEKGKNHHIIIVAEGVMTGEEFATKLKEAGYKGDLRVSVLGHIQRGGSPTARDRVLASRMGARAVELLRDGIGGVAVGIRNEELVESPILGTAEEGALFSLTTEGGIKVNNPHKAGLELYRLNSALNNLNLN | fructose 6-phosphate metabolic process cell surface; cytoplasm 6-phosphofructokinase activity ATP binding mannan binding metal ion binding Lactococcus lactis subsp. lactis Allosteric enzyme ATP-binding Cytoplasm Direct protein sequencing Glycolysis Kinase Magnesium Metal-binding Nucleotide-binding Transferase MKRIAVLTSG MKRIAVLTSGGDAPGMNAAIRAVVRKAISEGIEVYGINHGYAGMVAGDIFPLTSASVGDKIGRGGTFLYSARYPEFAQVEGQLAGIEQLKKFGIEGVVVIGGDGSYHGAMRLTEHGFPAVGLPGTIDNDIVGTDFTIGFDTAVSTVVDALDKIRDTSSSHNRTFVVEVMGRNAGDIALNAGIAAGADDISIPELEFKFENVVNNINKGYEKGKNHHIIIVAEGVMTGEEFATKLKEAGYKGDLRVSVLGHIQRGGSPTARDRVLASRMGARAVELLRDGIGGVAVGIRNEELVESPILGTAEEGALFSLTTEGGIKVNNPHKAGLELYRLNSALNNLNLN |
cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance | chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle | heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding | Camelus dromedarius | Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL | MKALWVALVV | MKALWVALVVTLLAGCRAEVEPEPEPEVQLGQEQPEWQGSQPWELALGRLWDYLRWVQTLSDQVQEELLSTQVTQELTALMEETMKEVKAYKAELEEQLSPVAQETRARLSKELQAAQARLGTDMEDLRSRLAHYRNEVQAMLGQTTDELRNRLASHLRKLRKRLLRDAEDLQKRLAVYRAGAVEGAERSVSALRERLGPLVEQGRLGTATTSTLGSQPLRERAEAWGQKLRGRLEAVGARAQDRLDKMREQLEEVRAKVEEQASQMRLQAETFQARLKGWFQPLVEDLQRQWAGLVEKVQQLAVGTTPTPAASKNQ | cholesterol efflux chylomicron remnant clearance high-density lipoprotein particle assembly intermediate-density lipoprotein particle clearance lipoprotein biosynthetic process melanosome organization negative regulation of amyloid fibril formation positive regulation of amyloid-beta clearance triglyceride-rich lipoprotein particle clearance very-low-density lipoprotein particle clearance chylomicron; extracellular exosome; extracellular matrix; extracellular space; high-density lipoprotein particle; intermediate-density lipoprotein particle; low-density lipoprotein particle; multivesicular body, internal vesicle; very-low-density lipoprotein particle heparan sulfate proteoglycan binding heparin binding identical protein binding lipid binding low-density lipoprotein particle receptor binding Camelus dromedarius Chylomicron Endosome Extracellular matrix Glycoprotein HDL Heparin-binding Lipid transport Lipid-binding Oxidation Phosphoprotein Repeat Secreted Signal Transport VLDL MKALWVALVV MKALWVALVVTLLAGCRAEVEPEPEPEVQLGQEQPEWQGSQPWELALGRLWDYLRWVQTLSDQVQEELLSTQVTQELTALMEETMKEVKAYKAELEEQLSPVAQETRARLSKELQAAQARLGTDMEDLRSRLAHYRNEVQAMLGQTTDELRNRLASHLRKLRKRLLRDAEDLQKRLAVYRAGAVEGAERSVSALRERLGPLVEQGRLGTATTSTLGSQPLRERAEAWGQKLRGRLEAVGARAQDRLDKMREQLEEVRAKVEEQASQMRLQAETFQARLKGWFQPLVEDLQRQWAGLVEKVQQLAVGTTPTPAASKNQ |
modulation of voltage-gated sodium channel activity in another organism | extracellular region | ion channel inhibitor activity sodium channel regulator activity toxin activity | Heteroscodra maculata | 3D-structure Amidation Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Pharmaceutical Secreted Toxin Voltage-gated sodium channel impairing toxin | ECRYLFGGCK | ECRYLFGGCKTTADCCKHLGCRTDLYYCAWDGTF | modulation of voltage-gated sodium channel activity in another organism extracellular region ion channel inhibitor activity sodium channel regulator activity toxin activity Heteroscodra maculata 3D-structure Amidation Direct protein sequencing Disulfide bond Ion channel impairing toxin Knottin Neurotoxin Pharmaceutical Secreted Toxin Voltage-gated sodium channel impairing toxin ECRYLFGGCK ECRYLFGGCKTTADCCKHLGCRTDLYYCAWDGTF |
blood vessel development definitive hemopoiesis endocardium development endothelial cell development endothelial cell differentiation heart development hematopoietic progenitor cell differentiation hematopoietic stem cell differentiation myeloid cell differentiation negative regulation of cardioblast differentiation positive regulation of hematopoietic stem cell differentiation positive regulation of hematopoietic stem cell migration primitive hemopoiesis regulation of DNA-templated transcription regulation of endothelial cell differentiation regulation of transcription by RNA polymerase II vasculogenesis | nucleus | DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific protein dimerization activity RNA polymerase II transcription regulatory region sequence-specific DNA binding | Danio rerio | Activator Differentiation DNA-binding Nucleus Reference proteome Repeat Transcription Transcription regulation | MSCGDSGIRR | MSCGDSGIRRILRASKRFRSTKGASKARRDQMNSEIRNLRALLPISPEHRLSYLHSMSITCTYIRKSVELRGVCEESTVFSAVNGCVPQDCALQDCALQECVLQECVLQECVLQECVLQALPGFIVAFTTDGKLLYVSENVHEYLGLSMVDVLQSDSFFDMLDRSDVEAVRSVLADASPSGERWVVCRMLVSKAMRLRSSCCPLLVRIRLRDGVCVSLCRPTADRLPARNADFHTHHSADMRLASASSSVLFHLGFSADELIGRSWYELLHPDDLRHAADRHAAILAAATADAEMLIRVQCKDLSWVWMYTHASATAERDAISCSNYMISEAEAVYLQQRLSSSSSSSSSSSSSSASPQCSSVSDSSDAHSAHTLFCTPPYSPTSSQCSDFLSEGYGSLEALVDSAFCSPPYPPLFPNPCCTPTVCPPDTALDPARLCPPDSALVPAALCPPDAALDPTQLCPPGAALDPTLLCPPGAALDPTQLCLPDGALVPAVFCPPNGALVPARLCPSDAALVPAALGRPDAALVPVCRPLQVCECPLDGAVPLEDLSMFPLPQGGGSRLMPPEASPTTHTHFSYDAAQQAGIGTLAMQIHTLICSFDAYSAARHTHSHHTSCWAPEPLLDEGIIDSILRELDSTHTDAHTLI | blood vessel development definitive hemopoiesis endocardium development endothelial cell development endothelial cell differentiation heart development hematopoietic progenitor cell differentiation hematopoietic stem cell differentiation myeloid cell differentiation negative regulation of cardioblast differentiation positive regulation of hematopoietic stem cell differentiation positive regulation of hematopoietic stem cell migration primitive hemopoiesis regulation of DNA-templated transcription regulation of endothelial cell differentiation regulation of transcription by RNA polymerase II vasculogenesis nucleus DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific protein dimerization activity RNA polymerase II transcription regulatory region sequence-specific DNA binding Danio rerio Activator Differentiation DNA-binding Nucleus Reference proteome Repeat Transcription Transcription regulation MSCGDSGIRR MSCGDSGIRRILRASKRFRSTKGASKARRDQMNSEIRNLRALLPISPEHRLSYLHSMSITCTYIRKSVELRGVCEESTVFSAVNGCVPQDCALQDCALQECVLQECVLQECVLQECVLQALPGFIVAFTTDGKLLYVSENVHEYLGLSMVDVLQSDSFFDMLDRSDVEAVRSVLADASPSGERWVVCRMLVSKAMRLRSSCCPLLVRIRLRDGVCVSLCRPTADRLPARNADFHTHHSADMRLASASSSVLFHLGFSADELIGRSWYELLHPDDLRHAADRHAAILAAATADAEMLIRVQCKDLSWVWMYTHASATAERDAISCSNYMISEAEAVYLQQRLSSSSSSSSSSSSSSASPQCSSVSDSSDAHSAHTLFCTPPYSPTSSQCSDFLSEGYGSLEALVDSAFCSPPYPPLFPNPCCTPTVCPPDTALDPARLCPPDSALVPAALCPPDAALDPTQLCPPGAALDPTLLCPPGAALDPTQLCLPDGALVPAVFCPPNGALVPARLCPSDAALVPAALGRPDAALVPVCRPLQVCECPLDGAVPLEDLSMFPLPQGGGSRLMPPEASPTTHTHFSYDAAQQAGIGTLAMQIHTLICSFDAYSAARHTHSHHTSCWAPEPLLDEGIIDSILRELDSTHTDAHTLI |
induction by virus of host apoptotic process perturbation by virus of host apoptosis protein complex oligomerization virus-mediated pore formation in host cell membrane | host cell endoplasmic reticulum membrane; host cell Golgi membrane; host cell plasma membrane; membrane; virion membrane | chloride channel activity outward rectifier potassium channel activity potassium channel activity sodium channel activity | Human respiratory syncytial virus A | Activation of host caspases by virus Alternative initiation Glycoprotein Host cell membrane Host endoplasmic reticulum Host Golgi apparatus Host membrane Host-virus interaction Ion channel Ion transport Membrane Modulation of host cell apoptosis by virus Phosphoprotein Signal-anchor Transmembrane Transmembrane helix Transport Viral ion channel Virion | MENTSITIEF | MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT | induction by virus of host apoptotic process perturbation by virus of host apoptosis protein complex oligomerization virus-mediated pore formation in host cell membrane host cell endoplasmic reticulum membrane; host cell Golgi membrane; host cell plasma membrane; membrane; virion membrane chloride channel activity outward rectifier potassium channel activity potassium channel activity sodium channel activity Human respiratory syncytial virus A Activation of host caspases by virus Alternative initiation Glycoprotein Host cell membrane Host endoplasmic reticulum Host Golgi apparatus Host membrane Host-virus interaction Ion channel Ion transport Membrane Modulation of host cell apoptosis by virus Phosphoprotein Signal-anchor Transmembrane Transmembrane helix Transport Viral ion channel Virion MENTSITIEF MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT |
induction by virus of host apoptotic process perturbation by virus of host apoptosis protein complex oligomerization suppression by virus of host apoptotic process virus-mediated pore formation in host cell membrane | host cell endoplasmic reticulum membrane; host cell Golgi membrane; host cell plasma membrane; membrane; virion membrane | identical protein binding monoatomic cation channel activity | Human respiratory syncytial virus A | 3D-structure Activation of host caspases by virus Alternative initiation Glycoprotein Host cell membrane Host endoplasmic reticulum Host Golgi apparatus Host membrane Host-virus interaction Ion channel Ion transport Membrane Modulation of host cell apoptosis by virus Phosphoprotein Signal-anchor Transmembrane Transmembrane helix Transport Viral ion channel Virion | MENTSITIEF | MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT | induction by virus of host apoptotic process perturbation by virus of host apoptosis protein complex oligomerization suppression by virus of host apoptotic process virus-mediated pore formation in host cell membrane host cell endoplasmic reticulum membrane; host cell Golgi membrane; host cell plasma membrane; membrane; virion membrane identical protein binding monoatomic cation channel activity Human respiratory syncytial virus A 3D-structure Activation of host caspases by virus Alternative initiation Glycoprotein Host cell membrane Host endoplasmic reticulum Host Golgi apparatus Host membrane Host-virus interaction Ion channel Ion transport Membrane Modulation of host cell apoptosis by virus Phosphoprotein Signal-anchor Transmembrane Transmembrane helix Transport Viral ion channel Virion MENTSITIEF MENTSITIEFSSKFWPYFTLIHMITTIISLLIIISIMIAILNKLCEYNVFHNKTFELPRARVNT |
virion assembly | host cell cytoplasm; host cell nucleus; host cell plasma membrane; membrane; viral envelope | structural constituent of virion | Human respiratory syncytial virus A | 3D-structure Host cell membrane Host cytoplasm Host membrane Host nucleus Host-virus interaction Membrane Phosphoprotein Viral matrix protein Virion | METYVNKLHE | METYVNKLHEGSTYTAAVQYNVLEKDDDPASLTIWVPMFQSSMPADLLIKELANVNILVKQISTPKGPSLRVMINSRSAVLAQMPSKFTICANVSLDERSKLAYDVTTPCEIKACSLTCLKSKNMLTTVKDLTMKTLNPTHDIIALCEFENIVTSKKVIIPTYLRSISVRNKDLNTLENITTTEFKNAITNAKIIPYSGLLLVITVTDNKGAFKYIKPQSQFIVDLGAYLEKESIYYVTTNWKHTATRFAIKPMED | virion assembly host cell cytoplasm; host cell nucleus; host cell plasma membrane; membrane; viral envelope structural constituent of virion Human respiratory syncytial virus A 3D-structure Host cell membrane Host cytoplasm Host membrane Host nucleus Host-virus interaction Membrane Phosphoprotein Viral matrix protein Virion METYVNKLHE METYVNKLHEGSTYTAAVQYNVLEKDDDPASLTIWVPMFQSSMPADLLIKELANVNILVKQISTPKGPSLRVMINSRSAVLAQMPSKFTICANVSLDERSKLAYDVTTPCEIKACSLTCLKSKNMLTTVKDLTMKTLNPTHDIIALCEFENIVTSKKVIIPTYLRSISVRNKDLNTLENITTTEFKNAITNAKIIPYSGLLLVITVTDNKGAFKYIKPQSQFIVDLGAYLEKESIYYVTTNWKHTATRFAIKPMED |
protein complex oligomerization suppression by virus of host autophagy virus-mediated pore formation in host cell membrane | host cell plasma membrane; membrane; virion membrane | identical protein binding monoatomic ion channel activity proton transmembrane transporter activity | Influenza A virus | 3D-structure Alternative splicing Disulfide bond Glycoprotein Host cell membrane Host membrane Host-virus interaction Hydrogen ion transport Inhibition of host autophagy by virus Ion channel Ion transport Lipoprotein Membrane Palmitate Phosphoprotein Signal-anchor Transmembrane Transmembrane helix Transport Viral ion channel Virion | MSLLTEVETP | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE | protein complex oligomerization suppression by virus of host autophagy virus-mediated pore formation in host cell membrane host cell plasma membrane; membrane; virion membrane identical protein binding monoatomic ion channel activity proton transmembrane transporter activity Influenza A virus 3D-structure Alternative splicing Disulfide bond Glycoprotein Host cell membrane Host membrane Host-virus interaction Hydrogen ion transport Inhibition of host autophagy by virus Ion channel Ion transport Lipoprotein Membrane Palmitate Phosphoprotein Signal-anchor Transmembrane Transmembrane helix Transport Viral ion channel Virion MSLLTEVETP MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE |
protein complex oligomerization suppression by virus of host autophagy virus-mediated pore formation in host cell membrane | host cell plasma membrane; membrane; virion membrane | monoatomic ion channel activity proton transmembrane transporter activity | Influenza A virus | Alternative splicing Disulfide bond Glycoprotein Host cell membrane Host membrane Host-virus interaction Hydrogen ion transport Inhibition of host autophagy by virus Ion channel Ion transport Lipoprotein Membrane Palmitate Phosphoprotein Reference proteome Signal-anchor Transmembrane Transmembrane helix Transport Viral ion channel Virion | MSLLTEVETP | MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE | protein complex oligomerization suppression by virus of host autophagy virus-mediated pore formation in host cell membrane host cell plasma membrane; membrane; virion membrane monoatomic ion channel activity proton transmembrane transporter activity Influenza A virus Alternative splicing Disulfide bond Glycoprotein Host cell membrane Host membrane Host-virus interaction Hydrogen ion transport Inhibition of host autophagy by virus Ion channel Ion transport Lipoprotein Membrane Palmitate Phosphoprotein Reference proteome Signal-anchor Transmembrane Transmembrane helix Transport Viral ion channel Virion MSLLTEVETP MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRFFEHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVSIELE |
proteolysis viral budding via host ESCRT complex | viral nucleocapsid | aspartic-type endopeptidase activity nucleic acid binding structural constituent of virion zinc ion binding | Bovine leukemia virus | Aspartyl protease Capsid protein Host-virus interaction Hydrolase Lipoprotein Metal-binding Myristate Phosphoprotein Protease Repeat Ribosomal frameshifting Viral budding Viral budding via the host ESCRT complexes Viral matrix protein Viral nucleoprotein Viral release from host cell Virion Zinc Zinc-finger | MGNSPSYNPP | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPTSCPPGRFGRVPLVLATLNEVLSNEGGAPGASAPEEQPPPYDPPAILPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAAEAANTLQGFNPKTGTLTQQSAQPNAGDLRSQYQNLWLQAGKNLPTRPSAPWSTIVQGPAESSVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANRECQQILQGRGPVAAVGQKLQACAQWAPKNKQPALLVHTPGPKMPGPRQPAPKRPPPGPCYRCLKEGHWARDCPTKATGPPPGPCPICKDPSHWKRDCPTLKSKNKLIEGGLSAPQTITPITDSLSEAELECLLSIPLARSRPSVAVYLSGPWLQPSQNQALMLVDTGAENTVLPQNWLVRDYPRIPAAVLGAGGVSRNRYNWLQGPLTLALKPEGPFITIPKILVDTSDKWQILGRDVPSRLQASISIPEEVRPPVVGVLDTPPSHIGLEHLPPPPEVPQFPLN | proteolysis viral budding via host ESCRT complex viral nucleocapsid aspartic-type endopeptidase activity nucleic acid binding structural constituent of virion zinc ion binding Bovine leukemia virus Aspartyl protease Capsid protein Host-virus interaction Hydrolase Lipoprotein Metal-binding Myristate Phosphoprotein Protease Repeat Ribosomal frameshifting Viral budding Viral budding via the host ESCRT complexes Viral matrix protein Viral nucleoprotein Viral release from host cell Virion Zinc Zinc-finger MGNSPSYNPP MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPTSCPPGRFGRVPLVLATLNEVLSNEGGAPGASAPEEQPPPYDPPAILPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAAEAANTLQGFNPKTGTLTQQSAQPNAGDLRSQYQNLWLQAGKNLPTRPSAPWSTIVQGPAESSVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANRECQQILQGRGPVAAVGQKLQACAQWAPKNKQPALLVHTPGPKMPGPRQPAPKRPPPGPCYRCLKEGHWARDCPTKATGPPPGPCPICKDPSHWKRDCPTLKSKNKLIEGGLSAPQTITPITDSLSEAELECLLSIPLARSRPSVAVYLSGPWLQPSQNQALMLVDTGAENTVLPQNWLVRDYPRIPAAVLGAGGVSRNRYNWLQGPLTLALKPEGPFITIPKILVDTSDKWQILGRDVPSRLQASISIPEEVRPPVVGVLDTPPSHIGLEHLPPPPEVPQFPLN |
proteolysis viral budding via host ESCRT complex | viral nucleocapsid | aspartic-type endopeptidase activity nucleic acid binding structural constituent of virion zinc ion binding | Bovine leukemia virus | Aspartyl protease Capsid protein Host-virus interaction Hydrolase Lipoprotein Metal-binding Myristate Phosphoprotein Protease Repeat Ribosomal frameshifting Viral budding Viral budding via the host ESCRT complexes Viral matrix protein Viral nucleoprotein Viral release from host cell Virion Zinc Zinc-finger | MGNSPSYNPP | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPASCPPGKFGRVPLVLATLNEVLSNDEGAPGASAPEEQPPPYDPPAVLPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAEAANTLQGFNPKMGTLTQQSAQPNAGDLRSQYQNLWLQAWKNLPTRPSVQPWSTIVQGPAESYVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANKECQQILQGRGLVAAPVGQKLQACAHWAPKTKQPAILVHTPGPKMPGPRQPAPKRPPPGPCYRCLKEGHWARDCPTKTTGPPPGPCPICKDPSHWKRDCPTLKSKKLIEGGPSAPQIITPITDSLSEAELECLLSIPLARSRPSVAVYLSGPWLQPSQNQALMLVDTGAENTVLPQNWLVRDYPRTPAAVLGAGGISRNRYNWLQGPLTLALKPEGPFITIPKILVDTFDKWQILGRDVLSRLQASISIPEEVHPPVVGVLDAPPSHIGLEHLPPPPEVPQFPLN | proteolysis viral budding via host ESCRT complex viral nucleocapsid aspartic-type endopeptidase activity nucleic acid binding structural constituent of virion zinc ion binding Bovine leukemia virus Aspartyl protease Capsid protein Host-virus interaction Hydrolase Lipoprotein Metal-binding Myristate Phosphoprotein Protease Repeat Ribosomal frameshifting Viral budding Viral budding via the host ESCRT complexes Viral matrix protein Viral nucleoprotein Viral release from host cell Virion Zinc Zinc-finger MGNSPSYNPP MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPASCPPGKFGRVPLVLATLNEVLSNDEGAPGASAPEEQPPPYDPPAVLPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAEAANTLQGFNPKMGTLTQQSAQPNAGDLRSQYQNLWLQAWKNLPTRPSVQPWSTIVQGPAESYVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANKECQQILQGRGLVAAPVGQKLQACAHWAPKTKQPAILVHTPGPKMPGPRQPAPKRPPPGPCYRCLKEGHWARDCPTKTTGPPPGPCPICKDPSHWKRDCPTLKSKKLIEGGPSAPQIITPITDSLSEAELECLLSIPLARSRPSVAVYLSGPWLQPSQNQALMLVDTGAENTVLPQNWLVRDYPRTPAAVLGAGGISRNRYNWLQGPLTLALKPEGPFITIPKILVDTFDKWQILGRDVLSRLQASISIPEEVHPPVVGVLDAPPSHIGLEHLPPPPEVPQFPLN |
clathrin-dependent endocytosis of virus by host cell fusion of virus membrane with host endosome membrane proteolysis suppression by virus of host toll-like receptor signaling pathway virion attachment to host cell | host cell cytoplasm; host cell nucleus; host cell plasma membrane; membrane; T=4 icosahedral viral capsid; viral envelope; virion membrane | serine-type endopeptidase activity structural molecule activity | Sindbis virus | Capsid protein Clathrin-mediated endocytosis of virus by host Cleavage on pair of basic residues Disulfide bond Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Glycoprotein Host cell membrane Host cytoplasm Host membrane Host nucleus Host-virus interaction Hydrolase Lipoprotein Membrane Palmitate Protease Reference proteome Ribosomal frameshifting Serine protease T=4 icosahedral capsid protein Transmembrane Transmembrane helix Viral attachment to host cell Viral envelope protein Viral penetration into host cytoplasm Virion Virus endocytosis by host Virus entry into host cell | MNRGFFNMLG | MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQPPRPRPPPRQKKQAPKQPPKPKKPKTQEKKKKQPAKPKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEWSAAPLVTAMCLLGNVSFPCDRPPTCYTREPSRALDILEENVNHEAYDTLLNAILRCGSSGRSKRSVIDDFTLTSPYLGTCSYCHHTVPCFSPVKIEQVWDEADDNTIRIQTSAQFGYDQSGAASANKYRYMSLKQDHTVKEGTMDDIKISTSGPCRRLSYKGYFLLAKCPPGDSVTVSIVSSNSATSCTLARKIKPKFVGREKYDLPPVHGKKIPCTVYDRLKETTAGYITMHRPRPHAYTSYLEESSGKVYAKPPSGKNITYECKCGDYKTGTVSTRTEITGCTAIKQCVAYKSDQTKWVFNSPDLIRHDDHTAQGKLHLPFKLIPSTCMVPVAHAPNVIHGFKHISLQLDTDHLTLLTTRRLGANPEPTTEWIVGKTVRNFTVDRDGLEYIWGNHEPVRVYAQESAPGDPHGWPHEIVQHYYHRHPVYTILAVASATVAMMIGVTVAVLCACKARRECLTPYALAPNAVIPTSLALLCCVRSANAETFTETMSYLWSNSQPFFWVQLCIPLAAFIVLMRCCSCCLPFLSGCRRLPGEGRRLRTCDHCSKCATDTV | clathrin-dependent endocytosis of virus by host cell fusion of virus membrane with host endosome membrane proteolysis suppression by virus of host toll-like receptor signaling pathway virion attachment to host cell host cell cytoplasm; host cell nucleus; host cell plasma membrane; membrane; T=4 icosahedral viral capsid; viral envelope; virion membrane serine-type endopeptidase activity structural molecule activity Sindbis virus Capsid protein Clathrin-mediated endocytosis of virus by host Cleavage on pair of basic residues Disulfide bond Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Glycoprotein Host cell membrane Host cytoplasm Host membrane Host nucleus Host-virus interaction Hydrolase Lipoprotein Membrane Palmitate Protease Reference proteome Ribosomal frameshifting Serine protease T=4 icosahedral capsid protein Transmembrane Transmembrane helix Viral attachment to host cell Viral envelope protein Viral penetration into host cytoplasm Virion Virus endocytosis by host Virus entry into host cell MNRGFFNMLG MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQPPRPRPPPRQKKQAPKQPPKPKKPKTQEKKKKQPAKPKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEWSAAPLVTAMCLLGNVSFPCDRPPTCYTREPSRALDILEENVNHEAYDTLLNAILRCGSSGRSKRSVIDDFTLTSPYLGTCSYCHHTVPCFSPVKIEQVWDEADDNTIRIQTSAQFGYDQSGAASANKYRYMSLKQDHTVKEGTMDDIKISTSGPCRRLSYKGYFLLAKCPPGDSVTVSIVSSNSATSCTLARKIKPKFVGREKYDLPPVHGKKIPCTVYDRLKETTAGYITMHRPRPHAYTSYLEESSGKVYAKPPSGKNITYECKCGDYKTGTVSTRTEITGCTAIKQCVAYKSDQTKWVFNSPDLIRHDDHTAQGKLHLPFKLIPSTCMVPVAHAPNVIHGFKHISLQLDTDHLTLLTTRRLGANPEPTTEWIVGKTVRNFTVDRDGLEYIWGNHEPVRVYAQESAPGDPHGWPHEIVQHYYHRHPVYTILAVASATVAMMIGVTVAVLCACKARRECLTPYALAPNAVIPTSLALLCCVRSANAETFTETMSYLWSNSQPFFWVQLCIPLAAFIVLMRCCSCCLPFLSGCRRLPGEGRRLRTCDHCSKCATDTV |
fusion of virus membrane with host endosome membrane proteolysis suppression by virus of host toll-like receptor signaling pathway viral entry into host cell virion attachment to host cell | host cell cytoplasm; host cell nucleus; host cell plasma membrane; membrane; T=4 icosahedral viral capsid; virion membrane | serine-type endopeptidase activity structural molecule activity | Chikungunya virus | 3D-structure Capsid protein Cleavage on pair of basic residues Disulfide bond Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Glycoprotein Host cell membrane Host cytoplasm Host membrane Host nucleus Host-virus interaction Hydrolase Lipoprotein Membrane Palmitate Protease Reference proteome Ribosomal frameshifting Serine protease T=4 icosahedral capsid protein Transmembrane Transmembrane helix Viral attachment to host cell Viral penetration into host cytoplasm Virion Virus entry into host cell | MEFIPTQTFY | MEFIPTQTFYNRRYQPRPWTPRPTIQVIRPRPRPQRQAGQLAQLISAVNKLTMRAVPQQKPRKNRKNKKQKQKQQAPQNNTNQKKQPPKKKPAQKKKKPGRRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGTIDNADLAKLAFKRSSKYDLECAQIPVHMKSDASKFTHEKPEGYYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGARTALSVVTWNKDIVTKITPEGAEEWSLAIPVMCLLANTTFPCSQPPCIPCCYEKEPEETLRMLEDNVMRPGYYQLLQASLTCSPHRQRRSTKDNFNVYKATRPYLAHCPDCGEGHSCHSPVALERIRNEATDGTLKIQVSLQIGIGTDDSHDWTKLRYMDNHIPADAGRAGLFVRTSAPCTITGTMGHFILARCPKGETLTVGFTDSRKISHSCTHPFHHDPPVIGREKFHSRPQHGKELPCSTYVQSNAATAEEIEVHMPPDTPDRTLLSQQSGNVKITVNSQTVRYKCNCGGSNEGLITTDKVINNCKVDQCHAAVTNHKKWQYNSPLVPRNAELGDRKGKIHIPFPLANVTCMVPKARNPTVTYGKNQVIMLLYPDHPTLLSYRSMGEEPNYQEEWVTHKKEVVLTVPTEGLEVTWGNNEPYKYWPQLSANGTAHGHPHEIILYYYELYPTMTVVVVSVASFILLSMVGMAVGMCMCARRRCITPYELTPGATVPFLLSLICCIRTAKAATYQEAAVYLWNEQQPLFWLQALIPLAALIVLCNCLRLLPCCCKTLAFLSRNEHRCPHCERVRTRNSDPEHGGSTV | fusion of virus membrane with host endosome membrane proteolysis suppression by virus of host toll-like receptor signaling pathway viral entry into host cell virion attachment to host cell host cell cytoplasm; host cell nucleus; host cell plasma membrane; membrane; T=4 icosahedral viral capsid; virion membrane serine-type endopeptidase activity structural molecule activity Chikungunya virus 3D-structure Capsid protein Cleavage on pair of basic residues Disulfide bond Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Glycoprotein Host cell membrane Host cytoplasm Host membrane Host nucleus Host-virus interaction Hydrolase Lipoprotein Membrane Palmitate Protease Reference proteome Ribosomal frameshifting Serine protease T=4 icosahedral capsid protein Transmembrane Transmembrane helix Viral attachment to host cell Viral penetration into host cytoplasm Virion Virus entry into host cell MEFIPTQTFY MEFIPTQTFYNRRYQPRPWTPRPTIQVIRPRPRPQRQAGQLAQLISAVNKLTMRAVPQQKPRKNRKNKKQKQKQQAPQNNTNQKKQPPKKKPAQKKKKPGRRERMCMKIENDCIFEVKHEGKVTGYACLVGDKVMKPAHVKGTIDNADLAKLAFKRSSKYDLECAQIPVHMKSDASKFTHEKPEGYYNWHHGAVQYSGGRFTIPTGAGKPGDSGRPIFDNKGRVVAIVLGGANEGARTALSVVTWNKDIVTKITPEGAEEWSLAIPVMCLLANTTFPCSQPPCIPCCYEKEPEETLRMLEDNVMRPGYYQLLQASLTCSPHRQRRSTKDNFNVYKATRPYLAHCPDCGEGHSCHSPVALERIRNEATDGTLKIQVSLQIGIGTDDSHDWTKLRYMDNHIPADAGRAGLFVRTSAPCTITGTMGHFILARCPKGETLTVGFTDSRKISHSCTHPFHHDPPVIGREKFHSRPQHGKELPCSTYVQSNAATAEEIEVHMPPDTPDRTLLSQQSGNVKITVNSQTVRYKCNCGGSNEGLITTDKVINNCKVDQCHAAVTNHKKWQYNSPLVPRNAELGDRKGKIHIPFPLANVTCMVPKARNPTVTYGKNQVIMLLYPDHPTLLSYRSMGEEPNYQEEWVTHKKEVVLTVPTEGLEVTWGNNEPYKYWPQLSANGTAHGHPHEIILYYYELYPTMTVVVVSVASFILLSMVGMAVGMCMCARRRCITPYELTPGATVPFLLSLICCIRTAKAATYQEAAVYLWNEQQPLFWLQALIPLAALIVLCNCLRLLPCCCKTLAFLSRNEHRCPHCERVRTRNSDPEHGGSTV |
activation of innate immune response cellular response to glucose starvation cellular response to interferon-beta cellular response to ionizing radiation defense response to virus intrinsic apoptotic signaling pathway by p53 class mediator monocyte differentiation negative regulation of AIM2 inflammasome complex assembly negative regulation of DNA-templated transcription negative regulation of gene expression, epigenetic negative regulation of innate immune response negative regulation of transcription by RNA polymerase II negative regulation of viral genome replication positive regulation of interleukin-1 beta production positive regulation of transcription by RNA polymerase II | cytoplasm; cytosol; intracellular membrane-bounded organelle; nuclear periphery; nuclear speck; nucleolus; nucleoplasm; nucleus; protein-containing complex | double-stranded DNA binding identical protein binding ubiquitin protein ligase binding | Mus musculus | 3D-structure Alternative splicing Nucleus Reference proteome Repeat Transcription Transcription regulation | MVNEYKRIVL | MVNEYKRIVLLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIEFCEEVPALRKRAEILKKERSEVTGETSLEKNGQEAGPATPTSTTSHMLASERGETSATQEETSTAQAGTSTAQAGTSTAQAGTSTAQKRKSMREEETGVKKSKAAKEPDQPPCCEEPTAMCQSPILHSSSSASSNILSAKNQKSQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMFHATVATVSQYFHVKVFNIDLKEKFTKNNFITISNYFESKGILEINETSSVLEAAPKQMIEVPNCITRNANASPKICDIQKGTSGTVFYGVFTLHKKKVKTQNTSYEIKDGSGSIEVVGSGQWHNINCKEGDKLHLFCFHLKRERGQPKLVCGDHSFVKVTKAGKKKEASTVQ | activation of innate immune response cellular response to glucose starvation cellular response to interferon-beta cellular response to ionizing radiation defense response to virus intrinsic apoptotic signaling pathway by p53 class mediator monocyte differentiation negative regulation of AIM2 inflammasome complex assembly negative regulation of DNA-templated transcription negative regulation of gene expression, epigenetic negative regulation of innate immune response negative regulation of transcription by RNA polymerase II negative regulation of viral genome replication positive regulation of interleukin-1 beta production positive regulation of transcription by RNA polymerase II cytoplasm; cytosol; intracellular membrane-bounded organelle; nuclear periphery; nuclear speck; nucleolus; nucleoplasm; nucleus; protein-containing complex double-stranded DNA binding identical protein binding ubiquitin protein ligase binding Mus musculus 3D-structure Alternative splicing Nucleus Reference proteome Repeat Transcription Transcription regulation MVNEYKRIVL MVNEYKRIVLLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIEFCEEVPALRKRAEILKKERSEVTGETSLEKNGQEAGPATPTSTTSHMLASERGETSATQEETSTAQAGTSTAQAGTSTAQAGTSTAQKRKSMREEETGVKKSKAAKEPDQPPCCEEPTAMCQSPILHSSSSASSNILSAKNQKSQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMFHATVATVSQYFHVKVFNIDLKEKFTKNNFITISNYFESKGILEINETSSVLEAAPKQMIEVPNCITRNANASPKICDIQKGTSGTVFYGVFTLHKKKVKTQNTSYEIKDGSGSIEVVGSGQWHNINCKEGDKLHLFCFHLKRERGQPKLVCGDHSFVKVTKAGKKKEASTVQ |
activation of innate immune response cellular response to glucose starvation cellular response to interferon-alpha cellular response to interferon-beta cellular response to ionizing radiation defense response to virus innate immune response inner ear development intrinsic apoptotic signaling pathway by p53 class mediator intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator monocyte differentiation negative regulation of AIM2 inflammasome complex assembly negative regulation of DNA-templated transcription negative regulation of gene expression, epigenetic negative regulation of innate immune response negative regulation of transcription by RNA polymerase II negative regulation of viral genome replication positive regulation of interleukin-1 beta production positive regulation of osteoblast differentiation positive regulation of transcription by RNA polymerase II regulation of transcription by RNA polymerase II response to bacterium | cytoplasm; cytosol; intracellular membrane-bounded organelle; nuclear inclusion body; nuclear speck; nucleolus; nucleoplasm; nucleus; protein-containing complex | double-stranded DNA binding identical protein binding transcription coregulator activity ubiquitin protein ligase binding | Mus musculus | 3D-structure Acetylation Activator Cytoplasm Developmental protein DNA-binding Immunity Innate immunity Nucleus Reference proteome Repeat Repressor Transcription Transcription regulation | MVNEYKRIVL | MVNEYKRIVLLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIAFCEEVPALRKRAEILKKERSEVTGETSLEKNGQEAGPATPTSTTSHMLASERGETSATQEETSTAQAGTSTAQARTSTAQAGTSTAQKRKIMREEETGVKKSKAAKEPDQPPCCEEPTARCQSPILHSSSSASSNIPSAKNQKSQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMLHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVLEAAPDQMIEVPNSIIRNANASPKICDIQKGTSGAVFYGVFTLHKKTVNRKNTIYEIKDGSGSIEVVGSGKWHNINCKEGDKLHLFCFHLKTIDRQPKLVCGEHSFIKISKRGNVPKEPAKEEDHHHGPKQVMVLKVTEPFTYDLKEDKRMFHATVATETEFFRVKVFDTALKSKFIPRNIIAISDYFGCNGFLEIYRASCVSDVNVNPTMVISNTLRQRANATPKISYLFSQARGTFVSGEYLVNKKTERNKFIYYGIGDDTGKMEVVVYGRLTNVRCEPGSKLRLVCFELTSTEDGWQLRSVRHSYMQVINARK | activation of innate immune response cellular response to glucose starvation cellular response to interferon-alpha cellular response to interferon-beta cellular response to ionizing radiation defense response to virus innate immune response inner ear development intrinsic apoptotic signaling pathway by p53 class mediator intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator monocyte differentiation negative regulation of AIM2 inflammasome complex assembly negative regulation of DNA-templated transcription negative regulation of gene expression, epigenetic negative regulation of innate immune response negative regulation of transcription by RNA polymerase II negative regulation of viral genome replication positive regulation of interleukin-1 beta production positive regulation of osteoblast differentiation positive regulation of transcription by RNA polymerase II regulation of transcription by RNA polymerase II response to bacterium cytoplasm; cytosol; intracellular membrane-bounded organelle; nuclear inclusion body; nuclear speck; nucleolus; nucleoplasm; nucleus; protein-containing complex double-stranded DNA binding identical protein binding transcription coregulator activity ubiquitin protein ligase binding Mus musculus 3D-structure Acetylation Activator Cytoplasm Developmental protein DNA-binding Immunity Innate immunity Nucleus Reference proteome Repeat Repressor Transcription Transcription regulation MVNEYKRIVL MVNEYKRIVLLRGLECINKHYFSLFKSLLARDLNLERDNQEQYTTIQIANMMEEKFPADSGLGKLIAFCEEVPALRKRAEILKKERSEVTGETSLEKNGQEAGPATPTSTTSHMLASERGETSATQEETSTAQAGTSTAQARTSTAQAGTSTAQKRKIMREEETGVKKSKAAKEPDQPPCCEEPTARCQSPILHSSSSASSNIPSAKNQKSQPQNQNIPRGAVLHSEPLTVMVLTATDPFEYESPEHEVKNMLHATVATVSQYFHVKVFNINLKEKFTKKNFIIISNYFESKGILEINETSSVLEAAPDQMIEVPNSIIRNANASPKICDIQKGTSGAVFYGVFTLHKKTVNRKNTIYEIKDGSGSIEVVGSGKWHNINCKEGDKLHLFCFHLKTIDRQPKLVCGEHSFIKISKRGNVPKEPAKEEDHHHGPKQVMVLKVTEPFTYDLKEDKRMFHATVATETEFFRVKVFDTALKSKFIPRNIIAISDYFGCNGFLEIYRASCVSDVNVNPTMVISNTLRQRANATPKISYLFSQARGTFVSGEYLVNKKTERNKFIYYGIGDDTGKMEVVVYGRLTNVRCEPGSKLRLVCFELTSTEDGWQLRSVRHSYMQVINARK |
C-5 methylation of cytosine cell differentiation homologous chromosome pairing at meiosis male meiosis I negative regulation of transcription by RNA polymerase II piRNA-mediated retrotransposon silencing by heterochromatin formation retrotransposon silencing by heterochromatin formation spermatogenesis | nucleus | DNA (cytosine-5-)-methyltransferase activity DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates DNA binding metal ion binding | Mus musculus | Differentiation DNA-binding Metal-binding Methyltransferase Nucleus Reference proteome Repressor S-adenosyl-L-methionine Spermatogenesis Transferase Zinc Zinc-finger | MRGGSRHLSN | MRGGSRHLSNEEDVSGCEDCIIISGTCSDQSSDPKTVPLTQVLEAVCTVENRGCRTSSQPSKRKASSLISYVQDLTGDGDEDRDGEVGGSSGSGTPVMPQLFCETRIPSKTPAPLSWQANTSASTPWLSPASPYPIIDLTDEDVIPQSISTPSVDWSQDSHQEGMDTTQVDAESRDGGNIEYQVSADKLLLSQSCILAAFYKLVPYRESIYRTLEKARVRAGKACPSSPGESLEDQLKPMLEWAHGGFKPTGIEGLKPNKKQPENKSRRRTTNDPAASESSPPKRLKTNSYGGKDRGEDEESREQMASDVTNNKGNLEDHCLSCGRKDPVSFHPLFEGGLCQSCRDRFLELFYMYDEDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGAGTAEDVKLQEPWSCYMCLPQRCHGVLRRRKDWNMRLQDFFTTDPDLEEFEPPKLYPAIPAAKRRPIRVLSLFDGIATGYLVLKELGIKVEKYIASEVCAESIAVGTVKHEGQIKYVDDIRNITKEHIDEWGPFDLVIGGSPCNDLSCVNPVRKGLFEGTGRLFFEFYRLLNYSCPEEEDDRPFFWMFENVVAMEVGDKRDISRFLECNPVMIDAIKVSAAHRARYFWGNLPGMNRPVMASKNDKLELQDCLEFSRTAKLKKVQTITTKSNSIRQGKNQLFPVVMNGKDDVLWCTELERIFGFPEHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDHFACE | C-5 methylation of cytosine cell differentiation homologous chromosome pairing at meiosis male meiosis I negative regulation of transcription by RNA polymerase II piRNA-mediated retrotransposon silencing by heterochromatin formation retrotransposon silencing by heterochromatin formation spermatogenesis nucleus DNA (cytosine-5-)-methyltransferase activity DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates DNA binding metal ion binding Mus musculus Differentiation DNA-binding Metal-binding Methyltransferase Nucleus Reference proteome Repressor S-adenosyl-L-methionine Spermatogenesis Transferase Zinc Zinc-finger MRGGSRHLSN MRGGSRHLSNEEDVSGCEDCIIISGTCSDQSSDPKTVPLTQVLEAVCTVENRGCRTSSQPSKRKASSLISYVQDLTGDGDEDRDGEVGGSSGSGTPVMPQLFCETRIPSKTPAPLSWQANTSASTPWLSPASPYPIIDLTDEDVIPQSISTPSVDWSQDSHQEGMDTTQVDAESRDGGNIEYQVSADKLLLSQSCILAAFYKLVPYRESIYRTLEKARVRAGKACPSSPGESLEDQLKPMLEWAHGGFKPTGIEGLKPNKKQPENKSRRRTTNDPAASESSPPKRLKTNSYGGKDRGEDEESREQMASDVTNNKGNLEDHCLSCGRKDPVSFHPLFEGGLCQSCRDRFLELFYMYDEDGYQSYCTVCCEGRELLLCSNTSCCRCFCVECLEVLVGAGTAEDVKLQEPWSCYMCLPQRCHGVLRRRKDWNMRLQDFFTTDPDLEEFEPPKLYPAIPAAKRRPIRVLSLFDGIATGYLVLKELGIKVEKYIASEVCAESIAVGTVKHEGQIKYVDDIRNITKEHIDEWGPFDLVIGGSPCNDLSCVNPVRKGLFEGTGRLFFEFYRLLNYSCPEEEDDRPFFWMFENVVAMEVGDKRDISRFLECNPVMIDAIKVSAAHRARYFWGNLPGMNRPVMASKNDKLELQDCLEFSRTAKLKKVQTITTKSNSIRQGKNQLFPVVMNGKDDVLWCTELERIFGFPEHYTDVSNMGRGARQKLLGRSWSVPVIRHLFAPLKDHFACE |
immunoglobulin mediated immune response | blood microparticle; extracellular exosome; extracellular region; extracellular space; IgG immunoglobulin complex; plasma membrane | antigen binding | Homo sapiens | 3D-structure Adaptive immunity Bence-Jones protein Cell membrane Direct protein sequencing Disulfide bond Immunity Immunoglobulin Immunoglobulin domain Membrane Reference proteome Secreted | GQPKAAPSVT | GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS | immunoglobulin mediated immune response blood microparticle; extracellular exosome; extracellular region; extracellular space; IgG immunoglobulin complex; plasma membrane antigen binding Homo sapiens 3D-structure Adaptive immunity Bence-Jones protein Cell membrane Direct protein sequencing Disulfide bond Immunity Immunoglobulin Immunoglobulin domain Membrane Reference proteome Secreted GQPKAAPSVT GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS |
adaptive immune response B cell receptor signaling pathway immunoglobulin mediated immune response | blood microparticle; extracellular exosome; extracellular region; extracellular space; IgA immunoglobulin complex; IgD immunoglobulin complex; IgE immunoglobulin complex; IgG immunoglobulin complex; IgM immunoglobulin complex; plasma membrane | antigen binding | Homo sapiens | 3D-structure Adaptive immunity Bence-Jones protein Cell membrane Direct protein sequencing Disulfide bond Immunity Immunoglobulin Immunoglobulin domain Membrane Reference proteome Secreted | GQPKAAPSVT | GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS | adaptive immune response B cell receptor signaling pathway immunoglobulin mediated immune response blood microparticle; extracellular exosome; extracellular region; extracellular space; IgA immunoglobulin complex; IgD immunoglobulin complex; IgE immunoglobulin complex; IgG immunoglobulin complex; IgM immunoglobulin complex; plasma membrane antigen binding Homo sapiens 3D-structure Adaptive immunity Bence-Jones protein Cell membrane Direct protein sequencing Disulfide bond Immunity Immunoglobulin Immunoglobulin domain Membrane Reference proteome Secreted GQPKAAPSVT GQPKAAPSVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADSSPVKAGVETTTPSKQSNNKYAASSYLSLTPEQWKSHKSYSCQVTHEGSTVEKTVAPTECS |
autophagosome membrane docking cellular response to interferon-beta cellular response to type II interferon detection of calcium ion G2/M transition of mitotic cell cycle mitochondrion-endoplasmic reticulum membrane tethering negative regulation of ryanodine-sensitive calcium-release channel activity organelle localization by membrane tethering positive regulation of protein dephosphorylation positive regulation of receptor signaling pathway via JAK-STAT regulation of cardiac muscle cell action potential regulation of cardiac muscle contraction regulation of cytokinesis regulation of heart rate regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum regulation of ryanodine-sensitive calcium-release channel activity response to calcium ion | calcium channel complex; catalytic complex; centrosome; cytoplasm; cytosol; growth cone; myelin sheath; nucleoplasm; protein-containing complex; sarcomere; sperm midpiece; spindle microtubule; spindle pole; voltage-gated potassium channel complex | adenylate cyclase activator activity adenylate cyclase binding calcium channel inhibitor activity calcium ion binding calcium-dependent protein binding nitric-oxide synthase binding nitric-oxide synthase regulator activity phosphatidylinositol 3-kinase binding protein domain specific binding protein kinase binding protein phosphatase activator activity protein serine/threonine kinase activator activity titin binding transmembrane transporter binding type 3 metabotropic glutamate receptor binding | Mus musculus | 3D-structure Acetylation Calcium Cell projection Cilium Cytoplasm Cytoskeleton Direct protein sequencing Flagellum Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation | MADQLTEEQI | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | autophagosome membrane docking cellular response to interferon-beta cellular response to type II interferon detection of calcium ion G2/M transition of mitotic cell cycle mitochondrion-endoplasmic reticulum membrane tethering negative regulation of ryanodine-sensitive calcium-release channel activity organelle localization by membrane tethering positive regulation of protein dephosphorylation positive regulation of receptor signaling pathway via JAK-STAT regulation of cardiac muscle cell action potential regulation of cardiac muscle contraction regulation of cytokinesis regulation of heart rate regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum regulation of ryanodine-sensitive calcium-release channel activity response to calcium ion calcium channel complex; catalytic complex; centrosome; cytoplasm; cytosol; growth cone; myelin sheath; nucleoplasm; protein-containing complex; sarcomere; sperm midpiece; spindle microtubule; spindle pole; voltage-gated potassium channel complex adenylate cyclase activator activity adenylate cyclase binding calcium channel inhibitor activity calcium ion binding calcium-dependent protein binding nitric-oxide synthase binding nitric-oxide synthase regulator activity phosphatidylinositol 3-kinase binding protein domain specific binding protein kinase binding protein phosphatase activator activity protein serine/threonine kinase activator activity titin binding transmembrane transporter binding type 3 metabotropic glutamate receptor binding Mus musculus 3D-structure Acetylation Calcium Cell projection Cilium Cytoplasm Cytoskeleton Direct protein sequencing Flagellum Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation MADQLTEEQI MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK |
autophagosome membrane docking cellular response to interferon-beta cellular response to type II interferon detection of calcium ion G2/M transition of mitotic cell cycle mitochondrion-endoplasmic reticulum membrane tethering negative regulation of calcium ion export across plasma membrane negative regulation of calcium ion transmembrane transporter activity negative regulation of ryanodine-sensitive calcium-release channel activity positive regulation of protein dephosphorylation positive regulation of receptor signaling pathway via JAK-STAT regulation of calcium-mediated signaling regulation of cardiac muscle cell action potential regulation of cardiac muscle contraction regulation of cytokinesis regulation of heart rate regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum response to calcium ion | calcium channel complex; catalytic complex; centrosome; cytoplasm; growth cone; membrane; myelin sheath; protein-containing complex; sarcomere; spindle microtubule; spindle pole; vesicle; voltage-gated potassium channel complex | adenylate cyclase activator activity adenylate cyclase binding calcium channel inhibitor activity calcium ion binding calcium-dependent protein binding nitric-oxide synthase binding nitric-oxide synthase regulator activity phosphatidylinositol 3-kinase binding protein domain specific binding protein kinase binding protein phosphatase activator activity protein serine/threonine kinase activator activity titin binding transmembrane transporter binding type 3 metabotropic glutamate receptor binding | Mus musculus | Acetylation Calcium Cytoplasm Cytoskeleton Direct protein sequencing Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation | MADQLTEEQI | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | autophagosome membrane docking cellular response to interferon-beta cellular response to type II interferon detection of calcium ion G2/M transition of mitotic cell cycle mitochondrion-endoplasmic reticulum membrane tethering negative regulation of calcium ion export across plasma membrane negative regulation of calcium ion transmembrane transporter activity negative regulation of ryanodine-sensitive calcium-release channel activity positive regulation of protein dephosphorylation positive regulation of receptor signaling pathway via JAK-STAT regulation of calcium-mediated signaling regulation of cardiac muscle cell action potential regulation of cardiac muscle contraction regulation of cytokinesis regulation of heart rate regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum response to calcium ion calcium channel complex; catalytic complex; centrosome; cytoplasm; growth cone; membrane; myelin sheath; protein-containing complex; sarcomere; spindle microtubule; spindle pole; vesicle; voltage-gated potassium channel complex adenylate cyclase activator activity adenylate cyclase binding calcium channel inhibitor activity calcium ion binding calcium-dependent protein binding nitric-oxide synthase binding nitric-oxide synthase regulator activity phosphatidylinositol 3-kinase binding protein domain specific binding protein kinase binding protein phosphatase activator activity protein serine/threonine kinase activator activity titin binding transmembrane transporter binding type 3 metabotropic glutamate receptor binding Mus musculus Acetylation Calcium Cytoplasm Cytoskeleton Direct protein sequencing Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation MADQLTEEQI MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK |
autophagosome membrane docking cellular response to interferon-beta cellular response to type II interferon detection of calcium ion G2/M transition of mitotic cell cycle mitochondrion-endoplasmic reticulum membrane tethering negative regulation of high voltage-gated calcium channel activity positive regulation of protein dephosphorylation positive regulation of receptor signaling pathway via JAK-STAT regulation of cardiac muscle cell action potential regulation of cardiac muscle contraction regulation of cytokinesis regulation of heart rate regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum response to calcium ion | calcium channel complex; catalytic complex; centrosome; growth cone; myelin sheath; protein-containing complex; sarcomere; spindle microtubule; spindle pole; voltage-gated potassium channel complex | adenylate cyclase activator activity adenylate cyclase binding calcium channel inhibitor activity calcium ion binding calcium-dependent protein binding nitric-oxide synthase binding nitric-oxide synthase regulator activity phosphatidylinositol 3-kinase binding protein domain specific binding protein kinase binding protein phosphatase activator activity protein serine/threonine kinase activator activity titin binding transmembrane transporter binding type 3 metabotropic glutamate receptor binding | Mus musculus | Acetylation Calcium Cytoplasm Cytoskeleton Direct protein sequencing Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation | MADQLTEEQI | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | autophagosome membrane docking cellular response to interferon-beta cellular response to type II interferon detection of calcium ion G2/M transition of mitotic cell cycle mitochondrion-endoplasmic reticulum membrane tethering negative regulation of high voltage-gated calcium channel activity positive regulation of protein dephosphorylation positive regulation of receptor signaling pathway via JAK-STAT regulation of cardiac muscle cell action potential regulation of cardiac muscle contraction regulation of cytokinesis regulation of heart rate regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum response to calcium ion calcium channel complex; catalytic complex; centrosome; growth cone; myelin sheath; protein-containing complex; sarcomere; spindle microtubule; spindle pole; voltage-gated potassium channel complex adenylate cyclase activator activity adenylate cyclase binding calcium channel inhibitor activity calcium ion binding calcium-dependent protein binding nitric-oxide synthase binding nitric-oxide synthase regulator activity phosphatidylinositol 3-kinase binding protein domain specific binding protein kinase binding protein phosphatase activator activity protein serine/threonine kinase activator activity titin binding transmembrane transporter binding type 3 metabotropic glutamate receptor binding Mus musculus Acetylation Calcium Cytoplasm Cytoskeleton Direct protein sequencing Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation MADQLTEEQI MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK |
autophagosome membrane docking calcium-mediated signaling cellular response to interferon-beta cellular response to type II interferon detection of calcium ion establishment of protein localization to membrane establishment of protein localization to mitochondrial membrane G2/M transition of mitotic cell cycle mitochondrion-endoplasmic reticulum membrane tethering negative regulation of high voltage-gated calcium channel activity organelle localization by membrane tethering positive regulation of protein dephosphorylation positive regulation of receptor signaling pathway via JAK-STAT regulation of cardiac muscle cell action potential regulation of cardiac muscle contraction regulation of cytokinesis regulation of heart rate regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum regulation of synaptic vesicle endocytosis regulation of synaptic vesicle exocytosis response to amphetamine response to calcium ion | calcium channel complex; catalytic complex; centrosome; cytoplasm; growth cone; mitochondrion; myelin sheath; protein-containing complex; sarcomere; spindle microtubule; spindle pole; voltage-gated potassium channel complex | adenylate cyclase activator activity adenylate cyclase binding calcium channel inhibitor activity calcium ion binding nitric-oxide synthase binding nitric-oxide synthase regulator activity protein kinase binding protein phosphatase activator activity protein serine/threonine kinase activator activity titin binding transmembrane transporter binding | Rattus norvegicus | 3D-structure Acetylation Calcium Cytoplasm Cytoskeleton Direct protein sequencing Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation | MADQLTEEQI | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK | autophagosome membrane docking calcium-mediated signaling cellular response to interferon-beta cellular response to type II interferon detection of calcium ion establishment of protein localization to membrane establishment of protein localization to mitochondrial membrane G2/M transition of mitotic cell cycle mitochondrion-endoplasmic reticulum membrane tethering negative regulation of high voltage-gated calcium channel activity organelle localization by membrane tethering positive regulation of protein dephosphorylation positive regulation of receptor signaling pathway via JAK-STAT regulation of cardiac muscle cell action potential regulation of cardiac muscle contraction regulation of cytokinesis regulation of heart rate regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum regulation of synaptic vesicle endocytosis regulation of synaptic vesicle exocytosis response to amphetamine response to calcium ion calcium channel complex; catalytic complex; centrosome; cytoplasm; growth cone; mitochondrion; myelin sheath; protein-containing complex; sarcomere; spindle microtubule; spindle pole; voltage-gated potassium channel complex adenylate cyclase activator activity adenylate cyclase binding calcium channel inhibitor activity calcium ion binding nitric-oxide synthase binding nitric-oxide synthase regulator activity protein kinase binding protein phosphatase activator activity protein serine/threonine kinase activator activity titin binding transmembrane transporter binding Rattus norvegicus 3D-structure Acetylation Calcium Cytoplasm Cytoskeleton Direct protein sequencing Isopeptide bond Metal-binding Methylation Phosphoprotein Reference proteome Repeat Ubl conjugation MADQLTEEQI MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK |
acetylcholine receptor signaling pathway regulation of neurotransmitter receptor activity | extracellular space; plasma membrane; synapse | acetylcholine receptor binding acetylcholine receptor regulator activity | Homo sapiens | 3D-structure Disulfide bond Reference proteome Secreted Signal | MQLGTGLLLA | MQLGTGLLLAAVLSLQLAAAEAIWCHQCTGFGGCSHGSRCLRDSTHCVTTATRVLSNTEDLPLVTKMCHIGCPDIPSLGLGPYVSIACCQTSLCNHD | acetylcholine receptor signaling pathway regulation of neurotransmitter receptor activity extracellular space; plasma membrane; synapse acetylcholine receptor binding acetylcholine receptor regulator activity Homo sapiens 3D-structure Disulfide bond Reference proteome Secreted Signal MQLGTGLLLA MQLGTGLLLAAVLSLQLAAAEAIWCHQCTGFGGCSHGSRCLRDSTHCVTTATRVLSNTEDLPLVTKMCHIGCPDIPSLGLGPYVSIACCQTSLCNHD |
regulation of neurotransmitter receptor activity synaptic transmission, cholinergic | dendrite; endoplasmic reticulum; plasma membrane; side of membrane; synapse | acetylcholine receptor binding acetylcholine receptor inhibitor activity acetylcholine receptor regulator activity ion channel inhibitor activity | Homo sapiens | 3D-structure Alternative splicing Cell membrane Cell projection Disulfide bond Endoplasmic reticulum Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Signal | MTPLLTLILV | MTPLLTLILVVLMGLPLAQALDCHVCAYNGDNCFNPMRCPAMVAYCMTTRTYYTPTRMKVSKSCVPRCFETVYDGYSKHASTTSCCQYDLCNGTGLATPATLALAPILLATLWGLL | regulation of neurotransmitter receptor activity synaptic transmission, cholinergic dendrite; endoplasmic reticulum; plasma membrane; side of membrane; synapse acetylcholine receptor binding acetylcholine receptor inhibitor activity acetylcholine receptor regulator activity ion channel inhibitor activity Homo sapiens 3D-structure Alternative splicing Cell membrane Cell projection Disulfide bond Endoplasmic reticulum Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Signal MTPLLTLILV MTPLLTLILVVLMGLPLAQALDCHVCAYNGDNCFNPMRCPAMVAYCMTTRTYYTPTRMKVSKSCVPRCFETVYDGYSKHASTTSCCQYDLCNGTGLATPATLALAPILLATLWGLL |
regulation of neurotransmitter receptor activity synaptic transmission, cholinergic | dendrite; endoplasmic reticulum; membrane; plasma membrane; side of membrane; synapse | acetylcholine receptor binding acetylcholine receptor inhibitor activity acetylcholine receptor regulator activity ion channel inhibitor activity | Mus musculus | Cell membrane Cell projection Disulfide bond Endoplasmic reticulum Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Signal | MTHLLTVFLV | MTHLLTVFLVALMGLPVAQALECHVCAYNGDNCFKPMRCPAMATYCMTTRTYFTPYRMKVRKSCVPSCFETVYDGYSKHASATSCCQYYLCNGAGFATPVTLALVPALLATFWSLL | regulation of neurotransmitter receptor activity synaptic transmission, cholinergic dendrite; endoplasmic reticulum; membrane; plasma membrane; side of membrane; synapse acetylcholine receptor binding acetylcholine receptor inhibitor activity acetylcholine receptor regulator activity ion channel inhibitor activity Mus musculus Cell membrane Cell projection Disulfide bond Endoplasmic reticulum Glycoprotein GPI-anchor Lipoprotein Membrane Reference proteome Signal MTHLLTVFLV MTHLLTVFLVALMGLPVAQALECHVCAYNGDNCFKPMRCPAMATYCMTTRTYFTPYRMKVRKSCVPSCFETVYDGYSKHASATSCCQYYLCNGAGFATPVTLALVPALLATFWSLL |
adult heart development angiogenesis apelin receptor signaling pathway coronary vasculature development embryonic heart tube development mesoderm migration involved in gastrulation placenta blood vessel development positive regulation of angiogenesis positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade positive regulation of G protein-coupled receptor internalization positive regulation of heart contraction positive regulation of trophoblast cell migration regulation of blood pressure vasculogenesis | extracellular region; extracellular space | apelin receptor binding hormone activity | Rattus norvegicus | Angiogenesis Developmental protein Differentiation Gastrulation Hormone Reference proteome Secreted Signal | MRFQPLFWVF | MRFQPLFWVFFIFAMSLLFITEEKSVNFPRRRKLYRHNCFRRRCISLHSRVPFP | adult heart development angiogenesis apelin receptor signaling pathway coronary vasculature development embryonic heart tube development mesoderm migration involved in gastrulation placenta blood vessel development positive regulation of angiogenesis positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis positive regulation of ERK1 and ERK2 cascade positive regulation of G protein-coupled receptor internalization positive regulation of heart contraction positive regulation of trophoblast cell migration regulation of blood pressure vasculogenesis extracellular region; extracellular space apelin receptor binding hormone activity Rattus norvegicus Angiogenesis Developmental protein Differentiation Gastrulation Hormone Reference proteome Secreted Signal MRFQPLFWVF MRFQPLFWVFFIFAMSLLFITEEKSVNFPRRRKLYRHNCFRRRCISLHSRVPFP |
cholesterol efflux cholesterol homeostasis cholesterol metabolic process diacylglycerol catabolic process high-density lipoprotein particle assembly high-density lipoprotein particle clearance high-density lipoprotein particle remodeling lipoprotein metabolic process low-density lipoprotein particle remodeling negative regulation of cholesterol import negative regulation of cytokine production involved in immune response negative regulation of lipid catabolic process negative regulation of very-low-density lipoprotein particle remodeling phosphatidylcholine biosynthetic process phospholipid catabolic process phospholipid efflux positive regulation of interleukin-8 production positive regulation of lipid catabolic process positive regulation of phagocytosis protein stabilization regulation of intestinal cholesterol absorption response to glucose reverse cholesterol transport triglyceride-rich lipoprotein particle remodeling | chylomicron; spherical high-density lipoprotein particle; very-low-density lipoprotein particle | apolipoprotein receptor binding cholesterol binding cholesterol transfer activity enzyme binding heat shock protein binding high-density lipoprotein particle binding high-density lipoprotein particle receptor binding lipase inhibitor activity phosphatidylcholine binding phosphatidylcholine-sterol O-acyltransferase activator activity protein heterodimerization activity protein homodimerization activity | Chlorocebus sabaeus | Cleavage on pair of basic residues HDL Lipid transport Oxidation Phosphoprotein Reference proteome Secreted Signal Transport | MKLLAATVLL | MKLLAATVLLLTVCSLEGALVRRQAEEPSVESLVSQYFQTVTDYGKDLMEKVKSPELQAQAKAYFEKSKEQLTPLVKKAGTDLVNFLSYFVELRTQPATQ | cholesterol efflux cholesterol homeostasis cholesterol metabolic process diacylglycerol catabolic process high-density lipoprotein particle assembly high-density lipoprotein particle clearance high-density lipoprotein particle remodeling lipoprotein metabolic process low-density lipoprotein particle remodeling negative regulation of cholesterol import negative regulation of cytokine production involved in immune response negative regulation of lipid catabolic process negative regulation of very-low-density lipoprotein particle remodeling phosphatidylcholine biosynthetic process phospholipid catabolic process phospholipid efflux positive regulation of interleukin-8 production positive regulation of lipid catabolic process positive regulation of phagocytosis protein stabilization regulation of intestinal cholesterol absorption response to glucose reverse cholesterol transport triglyceride-rich lipoprotein particle remodeling chylomicron; spherical high-density lipoprotein particle; very-low-density lipoprotein particle apolipoprotein receptor binding cholesterol binding cholesterol transfer activity enzyme binding heat shock protein binding high-density lipoprotein particle binding high-density lipoprotein particle receptor binding lipase inhibitor activity phosphatidylcholine binding phosphatidylcholine-sterol O-acyltransferase activator activity protein heterodimerization activity protein homodimerization activity Chlorocebus sabaeus Cleavage on pair of basic residues HDL Lipid transport Oxidation Phosphoprotein Reference proteome Secreted Signal Transport MKLLAATVLL MKLLAATVLLLTVCSLEGALVRRQAEEPSVESLVSQYFQTVTDYGKDLMEKVKSPELQAQAKAYFEKSKEQLTPLVKKAGTDLVNFLSYFVELRTQPATQ |
branched-chain amino acid biosynthetic process isoleucine biosynthetic process valine biosynthetic process | acetolactate synthase complex | acetolactate synthase activity flavin adenine dinucleotide binding magnesium ion binding thiamine pyrophosphate binding | Escherichia coli | Amino-acid biosynthesis Branched-chain amino acid biosynthesis Direct protein sequencing FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate Transferase | MNGAQWVVHA | MNGAQWVVHALRAQGVNTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALLDSIPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLEELPRIMAEAFDVACSGRPGPVLVDIPKDIQLASGDLEPWFTTVENEVTFPHAEVEQARQMLAKAQKPMLYVGGGVGMAQAVPALREFLAATKMPATCTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPHASVIHMDIDPAEMNKLRQAHVALQGDLNALLPALQQPLNQYDWQQHCAQLRDEHSWRYDHPGDAIYAPLLLKQLSDRKPADCVVTTDVGQHQMWAAQHIAHTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVVCISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIHGQHITRKDQVEAALDTMLNSDGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS | branched-chain amino acid biosynthetic process isoleucine biosynthetic process valine biosynthetic process acetolactate synthase complex acetolactate synthase activity flavin adenine dinucleotide binding magnesium ion binding thiamine pyrophosphate binding Escherichia coli Amino-acid biosynthesis Branched-chain amino acid biosynthesis Direct protein sequencing FAD Flavoprotein Magnesium Metal-binding Thiamine pyrophosphate Transferase MNGAQWVVHA MNGAQWVVHALRAQGVNTVFGYPGGAIMPVYDALYDGGVEHLLCRHEQGAAMAAIGYARATGKTGVCIATSGPGATNLITGLADALLDSIPVVAITGQVSAPFIGTDAFQEVDVLGLSLACTKHSFLVQSLEELPRIMAEAFDVACSGRPGPVLVDIPKDIQLASGDLEPWFTTVENEVTFPHAEVEQARQMLAKAQKPMLYVGGGVGMAQAVPALREFLAATKMPATCTLKGLGAVEADYPYYLGMLGMHGTKAANFAVQECDLLIAVGARFDDRVTGKLNTFAPHASVIHMDIDPAEMNKLRQAHVALQGDLNALLPALQQPLNQYDWQQHCAQLRDEHSWRYDHPGDAIYAPLLLKQLSDRKPADCVVTTDVGQHQMWAAQHIAHTRPENFITSSGLGTMGFGLPAAVGAQVARPNDTVVCISGDGSFMMNVQELGTVKRKQLPLKIVLLDNQRLGMVRQWQQLFFQERYSETTLTDNPDFLMLASAFGIHGQHITRKDQVEAALDTMLNSDGPYLLHVSIDELENVWPLVPPGASNSEMLEKLS |
positive regulation of hippo signaling | cell junction; cytoplasm; plasma membrane | identical protein binding | Homo sapiens | Alternative splicing Coiled coil Cytoplasm Phosphoprotein Reference proteome | MERSGQRVTT | MERSGQRVTTWDCDQGKHSDSDYREDGMDLGSDAGSSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDERDQRGYRDDRSPAREPGDVSARTRSGGGGGRSATTAMPPPVPNGNLHQHDPQDLRHNGNVVVAGRPSCSRGPRRAIQKPQPAGGRRSGRGPAAGGLCLQPPDGGTCVPEEPPVPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSSRLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK | positive regulation of hippo signaling cell junction; cytoplasm; plasma membrane identical protein binding Homo sapiens Alternative splicing Coiled coil Cytoplasm Phosphoprotein Reference proteome MERSGQRVTT MERSGQRVTTWDCDQGKHSDSDYREDGMDLGSDAGSSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDERDQRGYRDDRSPAREPGDVSARTRSGGGGGRSATTAMPPPVPNGNLHQHDPQDLRHNGNVVVAGRPSCSRGPRRAIQKPQPAGGRRSGRGPAAGGLCLQPPDGGTCVPEEPPVPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSSRLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK |
estrogen metabolic process face morphogenesis female gonad development fibroblast migration kidney development luteinization nitrogen compound metabolic process platelet-derived growth factor receptor signaling pathway positive regulation of hippo signaling post-embryonic development roof of mouth development skeletal system morphogenesis smooth muscle tissue development | cell junction; cytoplasm; plasma membrane | identical protein binding protein homodimerization activity | Mus musculus | Alternative splicing Coiled coil Reference proteome | MERSEQRVRA | MERSEQRVRAAWDCDPGKQADRDYREDGMDLGSDAGSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDDRGYRDDGCPAREPGDVSARIGSSGSGSRSAATTMPSPMPNGNLHPHDPQDLRHNGNVVVAGRPNASRVPRRPIQKTQPPGSRRGGRNRASGGLCLQPPDGGTRVPEEPPAPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSARLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK | estrogen metabolic process face morphogenesis female gonad development fibroblast migration kidney development luteinization nitrogen compound metabolic process platelet-derived growth factor receptor signaling pathway positive regulation of hippo signaling post-embryonic development roof of mouth development skeletal system morphogenesis smooth muscle tissue development cell junction; cytoplasm; plasma membrane identical protein binding protein homodimerization activity Mus musculus Alternative splicing Coiled coil Reference proteome MERSEQRVRA MERSEQRVRAAWDCDPGKQADRDYREDGMDLGSDAGSSSSSRASSQSNSTKVTPCSECKSSSSPGGSLDLVSALEDYEEPFPVYQKKVIDEWAPEEDGEEEEEEDDRGYRDDGCPAREPGDVSARIGSSGSGSRSAATTMPSPMPNGNLHPHDPQDLRHNGNVVVAGRPNASRVPRRPIQKTQPPGSRRGGRNRASGGLCLQPPDGGTRVPEEPPAPPMDWEALEKHLAGLQFREQEVRNQGQARTNSTSAQKNERESIRQKLALGSFFDDGPGIYTSCSKSGKPSLSARLQSGMNLQICFVNDSGSDKDSDADDSKTETSLDTPLSPMSKQSSSYSDRDTTEEESESLDDMDFLTRQKKLQAEAKMALAMAKPMAKMQVEVEKQNRKKSPVADLLPHMPHISECLMKRSLKPTDLRDMTIGQLQVIVNDLHSQIESLNEELVQLLLIRDELHTEQDAMLVDIEDLTRHAESQQKHMAEKMPAK |
transcription by RNA polymerase I transcription by RNA polymerase III | RNA polymerase I complex; RNA polymerase III complex | DNA binding DNA-directed 5'-3' RNA polymerase activity protein dimerization activity | Homo sapiens | 3D-structure Acetylation Alternative splicing Direct protein sequencing Disease variant DNA-directed RNA polymerase Nucleus Reference proteome Transcription | MEEDQELERK | MEEDQELERKISGLKTSMAEGERKTALEMVQAAGTDRHCVTFVLHEEDHTLGNSLRYMIMKNPEVEFCGYTTTHPSESKINLRIQTRGTLPAVEPFQRGLNELMNVCQHVLDKFEASIKDYKDQKASRNESTF | transcription by RNA polymerase I transcription by RNA polymerase III RNA polymerase I complex; RNA polymerase III complex DNA binding DNA-directed 5'-3' RNA polymerase activity protein dimerization activity Homo sapiens 3D-structure Acetylation Alternative splicing Direct protein sequencing Disease variant DNA-directed RNA polymerase Nucleus Reference proteome Transcription MEEDQELERK MEEDQELERKISGLKTSMAEGERKTALEMVQAAGTDRHCVTFVLHEEDHTLGNSLRYMIMKNPEVEFCGYTTTHPSESKINLRIQTRGTLPAVEPFQRGLNELMNVCQHVLDKFEASIKDYKDQKASRNESTF |
mRNA catabolic process negative regulation of translational initiation positive regulation of translational initiation regulation of carbohydrate metabolic process | cytoplasm | mRNA 5'-UTR binding | Pseudomonas protegens | 3D-structure Activator Cytoplasm Repressor RNA-binding Translation regulation | MLILTRKVGE | MLILTRKVGESINIGDDITITILGVSGQQVRIGINAPKDVAVHREEIYQRIQAGLTAPDKRETP | mRNA catabolic process negative regulation of translational initiation positive regulation of translational initiation regulation of carbohydrate metabolic process cytoplasm mRNA 5'-UTR binding Pseudomonas protegens 3D-structure Activator Cytoplasm Repressor RNA-binding Translation regulation MLILTRKVGE MLILTRKVGESINIGDDITITILGVSGQQVRIGINAPKDVAVHREEIYQRIQAGLTAPDKRETP |
cell-cell signaling G protein-coupled receptor signaling pathway methylation peptide hormone processing protein processing | cytoplasmic vesicle membrane; Golgi membrane; plasma membrane; transport vesicle membrane | metal ion binding metalloendopeptidase activity methyltransferase activity | Homo sapiens | Alternative splicing Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Methyltransferase Multifunctional enzyme Protease Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix Zinc | MNVALQELGA | MNVALQELGAGSNMVEYKRATLRDEDAPETPVEGGASPDAMEVGKGASPFSPGPSPGMTPGTPRSSGLFWRVTCPHLRSISGLCSRTMVGFQKGTRQLLGSRTQLELVLAGASLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAEQKTQRFYLSCLQVERIEELGAQPLRDLIEKIGGWNITGPWDQDNFMEVLKAVAGTYRATPFFTVYISADSKSSNSNVIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGRPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPSMDWLEFLSFLLSPLELSDSEPVVVYGMDYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDRRFESAQEKLLETLYGTKKSCVPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRTAFEEALGQLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEISEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYARNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACMEEQYNQYQVNGERLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW | cell-cell signaling G protein-coupled receptor signaling pathway methylation peptide hormone processing protein processing cytoplasmic vesicle membrane; Golgi membrane; plasma membrane; transport vesicle membrane metal ion binding metalloendopeptidase activity methyltransferase activity Homo sapiens Alternative splicing Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Methyltransferase Multifunctional enzyme Protease Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix Zinc MNVALQELGA MNVALQELGAGSNMVEYKRATLRDEDAPETPVEGGASPDAMEVGKGASPFSPGPSPGMTPGTPRSSGLFWRVTCPHLRSISGLCSRTMVGFQKGTRQLLGSRTQLELVLAGASLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAEQKTQRFYLSCLQVERIEELGAQPLRDLIEKIGGWNITGPWDQDNFMEVLKAVAGTYRATPFFTVYISADSKSSNSNVIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGRPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPSMDWLEFLSFLLSPLELSDSEPVVVYGMDYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDRRFESAQEKLLETLYGTKKSCVPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRTAFEEALGQLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEISEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYARNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACMEEQYNQYQVNGERLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW |
brain development cardioblast differentiation heart development methylation protein processing | Golgi membrane; plasma membrane; transport vesicle membrane | metal ion binding metalloendopeptidase activity methyltransferase activity | Homo sapiens | Alternative splicing Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Methyltransferase Multifunctional enzyme Phosphoprotein Protease Reference proteome Transferase Transmembrane Transmembrane helix Zinc | MASPGAGRAP | MASPGAGRAPPELPERNCGYREVEYWDQRYQGAADSAPYDWFGDFSSFRALLEPELRPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSSVVVAAMQARHAHVPQLRWETMDVRKLDFPSASFDVVLEKGTLDALLAGERDPWTVSSEGVHTVDQVLSEVGFQKGTRQLLGSRTQLELVLAGASLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAEQKTQRFYLSCLQVERIEELGAQPLRDLIEKIGGWNITGPWDQDNFMEVLKAVAGTYRATPFFTVYISADSKSSNSNVIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGRPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPSMDWLEFLSFLLSPLELSDSEPVVVYGMDYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDRRFESAQEKLLETLYGTKKSCVPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRTAFEEALGQLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEISEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYARNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACMEEQYNQYQVNGERLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW | brain development cardioblast differentiation heart development methylation protein processing Golgi membrane; plasma membrane; transport vesicle membrane metal ion binding metalloendopeptidase activity methyltransferase activity Homo sapiens Alternative splicing Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Methyltransferase Multifunctional enzyme Phosphoprotein Protease Reference proteome Transferase Transmembrane Transmembrane helix Zinc MASPGAGRAP MASPGAGRAPPELPERNCGYREVEYWDQRYQGAADSAPYDWFGDFSSFRALLEPELRPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSSVVVAAMQARHAHVPQLRWETMDVRKLDFPSASFDVVLEKGTLDALLAGERDPWTVSSEGVHTVDQVLSEVGFQKGTRQLLGSRTQLELVLAGASLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAEQKTQRFYLSCLQVERIEELGAQPLRDLIEKIGGWNITGPWDQDNFMEVLKAVAGTYRATPFFTVYISADSKSSNSNVIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGRPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPSMDWLEFLSFLLSPLELSDSEPVVVYGMDYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDRRFESAQEKLLETLYGTKKSCVPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRTAFEEALGQLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEISEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYARNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACMEEQYNQYQVNGERLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW |
brain development cardioblast differentiation heart development methylation peptide hormone processing protein processing | cytoplasmic vesicle membrane; Golgi membrane; plasma membrane; trans-Golgi network; transport vesicle membrane | metal ion binding metalloendopeptidase activity methyltransferase activity | Mus musculus | Alternative splicing Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Methyltransferase Multifunctional enzyme Phosphoprotein Protease Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix Zinc | MASPRTPVSP | MASPRTPVSPPELPEKNFQYRQVQYWDQRYKDAADSGPYEWFGDFASFRALLEPELCPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSPVVVAAMQVRYAHVPSLRWETMDVRALDFPSGSFDVVLEKGTLDAMLAGEPDPWNVSSEGVHTVDQVLSEVGFQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCLQSERIEKLGAKPLRDLIDKIGGWNITGPWDEDSFMDVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMVELGVLLGGQPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPAVDWLEFLSFLLSPLELGDSEPVVVYGTEYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDQRFETAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMINEIRSAFEETLGDLVWMDEKTRLAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYAHNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLTAFQNHTACMEEQYSQYQVNGERLNGLQTLGENIADNGGLKAAYNAYKAWLRKHGEEQPLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW | brain development cardioblast differentiation heart development methylation peptide hormone processing protein processing cytoplasmic vesicle membrane; Golgi membrane; plasma membrane; trans-Golgi network; transport vesicle membrane metal ion binding metalloendopeptidase activity methyltransferase activity Mus musculus Alternative splicing Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Methyltransferase Multifunctional enzyme Phosphoprotein Protease Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix Zinc MASPRTPVSP MASPRTPVSPPELPEKNFQYRQVQYWDQRYKDAADSGPYEWFGDFASFRALLEPELCPEDRILVLGCGNSALSYELFLGGFPNVTSVDYSPVVVAAMQVRYAHVPSLRWETMDVRALDFPSGSFDVVLEKGTLDAMLAGEPDPWNVSSEGVHTVDQVLSEVGFQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHRDPAHSTCVTEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPNGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTRSFYLSCLQSERIEKLGAKPLRDLIDKIGGWNITGPWDEDSFMDVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMVELGVLLGGQPTSTREQMQQVLELEIQLANITVPQDQRRDEEKIYHKMSISELQALAPAVDWLEFLSFLLSPLELGDSEPVVVYGTEYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDQRFETAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMINEIRSAFEETLGDLVWMDEKTRLAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYAHNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLTAFQNHTACMEEQYSQYQVNGERLNGLQTLGENIADNGGLKAAYNAYKAWLRKHGEEQPLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW |
brain development cardioblast differentiation heart development methylation peptide hormone processing protein processing | Golgi membrane; plasma membrane; transport vesicle membrane | metal ion binding metalloendopeptidase activity methyltransferase activity | Bos taurus | Alternative splicing Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Methyltransferase Multifunctional enzyme Phosphoprotein Protease Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix Zinc | MACLGPSAQV | MACLGPSAQVPELPEKNCGYREVQYWDQRYQGAADSAPYEWFGDFSCFRDLLEPELRPLDRILVLGCGNSALSYEIFLGGFPDVTSVDYSSVVVAAMRARYAHVPTLRWETMDVRALGFPSGSFDVVLEKGTLDALLTGEQDPWTVSSEGVHTVDQVLNEAGFRKRTSRLLGLHTQLELVLAGVSLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTQRFYLSCLQVERIEELGAQPLRDLIDKIGGWNVTGPWDQDNFMEVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGQPTSTREQMRQVLELEIQLANITVPQDQRRDEEKIYHKMSIAELQALAPSMDWLEFLSFLLSPLELGDSEPVVVYGTDYLQQVSELINRTEPSVLNNYLIWNLVQKTTSSLDHRFESAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRAAFEEALGHLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYTCNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACIEEQYSQYQVNGEKLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNSGQLCEVW | brain development cardioblast differentiation heart development methylation peptide hormone processing protein processing Golgi membrane; plasma membrane; transport vesicle membrane metal ion binding metalloendopeptidase activity methyltransferase activity Bos taurus Alternative splicing Cytoplasmic vesicle Disulfide bond Glycoprotein Golgi apparatus Hydrolase Membrane Metal-binding Metalloprotease Methyltransferase Multifunctional enzyme Phosphoprotein Protease Reference proteome Signal-anchor Transferase Transmembrane Transmembrane helix Zinc MACLGPSAQV MACLGPSAQVPELPEKNCGYREVQYWDQRYQGAADSAPYEWFGDFSCFRDLLEPELRPLDRILVLGCGNSALSYEIFLGGFPDVTSVDYSSVVVAAMRARYAHVPTLRWETMDVRALGFPSGSFDVVLEKGTLDALLTGEQDPWTVSSEGVHTVDQVLNEAGFRKRTSRLLGLHTQLELVLAGVSLLLAALLLGCLVALGVQYHRDPSHSTCLTEACIRVAGKILESLDRGVSPCEDFYQFSCGGWIRRNPLPDGRSRWNTFNSLWDQNQAILKHLLENTTFNSSSEAERKTQRFYLSCLQVERIEELGAQPLRDLIDKIGGWNVTGPWDQDNFMEVLKAVAGTYRATPFFTVYVSADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLTAYLDYMEELGMLLGGQPTSTREQMRQVLELEIQLANITVPQDQRRDEEKIYHKMSIAELQALAPSMDWLEFLSFLLSPLELGDSEPVVVYGTDYLQQVSELINRTEPSVLNNYLIWNLVQKTTSSLDHRFESAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRAAFEEALGHLVWMDEKTRQAAKEKADAIYDMIGFPDFILEPKELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYTCNHPKALNFGGIGVVMGHELTHAFDDQGREYDKEGNLRPWWQNESLAAFRNHTACIEEQYSQYQVNGEKLNGRQTLGENIADNGGLKAAYNAYKAWLRKHGEEQQLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNSGQLCEVW |
male germ-line stem cell population maintenance microtubule cytoskeleton organization mitotic cell cycle | ciliary basal body; cytoplasm; microtubule; microtubule cytoskeleton; nucleus | GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton | Homo sapiens | Acetylation Alternative splicing Cytoplasm Cytoskeleton GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome | MRECISIHVG | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY | male germ-line stem cell population maintenance microtubule cytoskeleton organization mitotic cell cycle ciliary basal body; cytoplasm; microtubule; microtubule cytoskeleton; nucleus GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton Homo sapiens Acetylation Alternative splicing Cytoplasm Cytoskeleton GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome MRECISIHVG MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY |
microtubule cytoskeleton organization mitotic cell cycle | cytoplasm; microtubule; microtubule cytoskeleton | GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton | Homo sapiens | Acetylation Cytoplasm Cytoskeleton Disease variant GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome | MRECISIHVG | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY | microtubule cytoskeleton organization mitotic cell cycle cytoplasm; microtubule; microtubule cytoskeleton GTP binding hydrolase activity metal ion binding structural constituent of cytoskeleton Homo sapiens Acetylation Cytoplasm Cytoskeleton Disease variant GTP-binding Hydrolase Isopeptide bond Magnesium Metal-binding Methylation Microtubule Nitration Nucleotide-binding Phosphoprotein Reference proteome MRECISIHVG MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY |
cerebral cortex development Notch signaling pathway positive regulation of Notch signaling pathway | extracellular region | calcium ion binding Notch binding | Homo sapiens | Alternative splicing Calcium Disulfide bond EGF-like domain Glycoprotein Notch signaling pathway Reference proteome Repeat Secreted Signal | MPALRPALLW | MPALRPALLWALLALWLCCATPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGICLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN | cerebral cortex development Notch signaling pathway positive regulation of Notch signaling pathway extracellular region calcium ion binding Notch binding Homo sapiens Alternative splicing Calcium Disulfide bond EGF-like domain Glycoprotein Notch signaling pathway Reference proteome Repeat Secreted Signal MPALRPALLW MPALRPALLWALLALWLCCATPAHALQCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGICLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN |
cerebral cortex development Notch signaling pathway positive regulation of Notch signaling pathway | extracellular region | calcium ion binding | Homo sapiens | Alternative splicing Calcium Disulfide bond EGF-like domain Glycoprotein Neurodegeneration Notch signaling pathway Reference proteome Repeat Secreted Triplet repeat expansion | MWICPGGGGG | MWICPGGGGGGGGGGGGGDREDARPAPLCCGRCWRSGCAARPPRMCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN | cerebral cortex development Notch signaling pathway positive regulation of Notch signaling pathway extracellular region calcium ion binding Homo sapiens Alternative splicing Calcium Disulfide bond EGF-like domain Glycoprotein Neurodegeneration Notch signaling pathway Reference proteome Repeat Secreted Triplet repeat expansion MWICPGGGGG MWICPGGGGGGGGGGGGGDREDARPAPLCCGRCWRSGCAARPPRMCRDGYEPCVNEGMCVTYHNGTGYCKCPEGFLGEYCQHRDPCEKNRCQNGGTCVAQAMLGKATCRCASGFTGEDCQYSTSHPCFVSRPCLNGGTCHMLSRDTYECTCQVGFTGKECQWTDACLSHPCANGSTCTTVANQFSCKCLTGFTGQKCETDVNECDIPGHCQHGGTCLNLPGSYQCQCLQGFTGQYCDSLYVPCAPSPCVNGGTCRQTGDFTFECNCLPETVRRGTELWERDREVWNGKEHDEN |
protein ubiquitination Wnt signaling pathway | endoplasmic reticulum membrane; nuclear envelope; plasma membrane | metal ion binding transferase activity | Xenopus tropicalis | Cell membrane Developmental protein Disulfide bond Endoplasmic reticulum Glycoprotein Membrane Metal-binding Nucleus Reference proteome Signal Transferase Transmembrane Transmembrane helix Ubl conjugation pathway Wnt signaling pathway Zinc Zinc-finger | MNRARLQLAS | MNRARLQLASLWLLLTVTLQAVASAMGTTEREMDVKALIRVTPLQAEESGGVGQGNLTLEGLFARVAEISPAEGRLLQFHPLSLCNTSEDDQTKPGFISIVKLETPDRDTQPCLSLANKARLAGERGAHAVLFDITNDRGALQQLQQPAGINQPVVLIWGPDAEKLMDVVNKNKEALVKIEVQEQPKWLHHDIWILLTVAGTVMFFVLYAVARLLCRQPPPQDSIQQQTLLAISRLGTRRYQQRMLKDQRASGGWVETASTSSSVPVCAICLEEFTDGQELRILPCCHEYHLGCVDPWLRQNHTCPLCMYDILDSGTPPRPLAHRAPSQTQLWGRYPGSARLMSHLPPHGTPMVFPTPNNSLFLPRAPYYLDHTHHWQMPEQMAMQMRTHRRGAEGTRELGISPGCQDSSGYLPDDPGSDSSSGPCHGSSSENCTDISLHCLHGTSSSSVHSSQSNQEDSSPPALASYLLPQGELPALNPLLSTQASYASHVHFHQHRHHHYRRNQPSMSHSHPHRSKRRTKVSRADPSYYREHRHTTGANGELRSLMVRREPRPSCSRTCFDPRTNREHPRHQQSMPQAASVVQGSSEPDVATSLRGSRTDPPSRTYRKKKSSAPSHLPLLYSPRHCHPANSVQMSESSHPRWAEEVRLLHSRVNSHRENTAMMHLYHPPHHNQGATEEIEAVCEHAV | protein ubiquitination Wnt signaling pathway endoplasmic reticulum membrane; nuclear envelope; plasma membrane metal ion binding transferase activity Xenopus tropicalis Cell membrane Developmental protein Disulfide bond Endoplasmic reticulum Glycoprotein Membrane Metal-binding Nucleus Reference proteome Signal Transferase Transmembrane Transmembrane helix Ubl conjugation pathway Wnt signaling pathway Zinc Zinc-finger MNRARLQLAS MNRARLQLASLWLLLTVTLQAVASAMGTTEREMDVKALIRVTPLQAEESGGVGQGNLTLEGLFARVAEISPAEGRLLQFHPLSLCNTSEDDQTKPGFISIVKLETPDRDTQPCLSLANKARLAGERGAHAVLFDITNDRGALQQLQQPAGINQPVVLIWGPDAEKLMDVVNKNKEALVKIEVQEQPKWLHHDIWILLTVAGTVMFFVLYAVARLLCRQPPPQDSIQQQTLLAISRLGTRRYQQRMLKDQRASGGWVETASTSSSVPVCAICLEEFTDGQELRILPCCHEYHLGCVDPWLRQNHTCPLCMYDILDSGTPPRPLAHRAPSQTQLWGRYPGSARLMSHLPPHGTPMVFPTPNNSLFLPRAPYYLDHTHHWQMPEQMAMQMRTHRRGAEGTRELGISPGCQDSSGYLPDDPGSDSSSGPCHGSSSENCTDISLHCLHGTSSSSVHSSQSNQEDSSPPALASYLLPQGELPALNPLLSTQASYASHVHFHQHRHHHYRRNQPSMSHSHPHRSKRRTKVSRADPSYYREHRHTTGANGELRSLMVRREPRPSCSRTCFDPRTNREHPRHQQSMPQAASVVQGSSEPDVATSLRGSRTDPPSRTYRKKKSSAPSHLPLLYSPRHCHPANSVQMSESSHPRWAEEVRLLHSRVNSHRENTAMMHLYHPPHHNQGATEEIEAVCEHAV |
proteolysis | extracellular region | serine-type endopeptidase activity toxin activity | Vipera ammodytes ammodytes | Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Secreted Toxin | VIGGDECNIN | VIGGDECNINEHPFLVALHTARXXRFYCAGTLINQEWVLTAARCDRXXXXXILGVHSKXXXXXXXXXXXXXXXXXXXXXXTYTRWDKDIMLIRLKRXXXXXXXXXXXXXXXXXXXXXXXXXIMGWGTITTTKVTYPDVPHCADINMFDYSVCQKXXXKLPEKSRTLCAGILQGGIDSCKGISGGPLICNGEIQGIVSYGK | proteolysis extracellular region serine-type endopeptidase activity toxin activity Vipera ammodytes ammodytes Direct protein sequencing Disulfide bond Glycoprotein Hemostasis impairing toxin Secreted Toxin VIGGDECNIN VIGGDECNINEHPFLVALHTARXXRFYCAGTLINQEWVLTAARCDRXXXXXILGVHSKXXXXXXXXXXXXXXXXXXXXXXTYTRWDKDIMLIRLKRXXXXXXXXXXXXXXXXXXXXXXXXXIMGWGTITTTKVTYPDVPHCADINMFDYSVCQKXXXKLPEKSRTLCAGILQGGIDSCKGISGGPLICNGEIQGIVSYGK |
arachidonic acid secretion killing of cells of another organism lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity toxin activity | Cerastes cerastes | Blood coagulation cascade inhibiting toxin Calcium Cytolysis Direct protein sequencing Disulfide bond Hemolysis Hemostasis impairing toxin Hydrolase Metal-binding Platelet aggregation inhibiting toxin Secreted Toxin | NLYQFGKMIN | NLYQFGKMINHMVGKSPIFSYGDYGCYCGWGGKGTPVDATDRCCFVHDCCYGRANGCDPKLSTYSYNFQNGNIVCGNKYGCLRHICECDRVAAICFGENVNTYDKKFLSSSRCRQTSEQC | arachidonic acid secretion killing of cells of another organism lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Cerastes cerastes Blood coagulation cascade inhibiting toxin Calcium Cytolysis Direct protein sequencing Disulfide bond Hemolysis Hemostasis impairing toxin Hydrolase Metal-binding Platelet aggregation inhibiting toxin Secreted Toxin NLYQFGKMIN NLYQFGKMINHMVGKSPIFSYGDYGCYCGWGGKGTPVDATDRCCFVHDCCYGRANGCDPKLSTYSYNFQNGNIVCGNKYGCLRHICECDRVAAICFGENVNTYDKKFLSSSRCRQTSEQC |
arachidonic acid secretion defense response to bacterium killing of cells of another organism lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity | Walterinnesia aegyptia | Antibiotic Antimicrobial Calcium Cytolysis Direct protein sequencing Disulfide bond Glycoprotein Hemolysis Hydrolase Lipid degradation Lipid metabolism Metal-binding Secreted | NLYQFKNMVQ | NLYQFKNMVQCVGTQLCVAYVKYGCYCGPG | arachidonic acid secretion defense response to bacterium killing of cells of another organism lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity Walterinnesia aegyptia Antibiotic Antimicrobial Calcium Cytolysis Direct protein sequencing Disulfide bond Glycoprotein Hemolysis Hydrolase Lipid degradation Lipid metabolism Metal-binding Secreted NLYQFKNMVQ NLYQFKNMVQCVGTQLCVAYVKYGCYCGPG |
entry of bacterium into host cell | cell surface; extracellular region; peptidoglycan-based cell wall; plasma membrane | heparin binding lipid binding metal ion binding | Listeria monocytogenes serotype 1/2a | 3D-structure Calcium Cell membrane Heparin-binding Leucine-rich repeat Lipid-binding Membrane Metal-binding Repeat Secreted Signal Virulence | MKEKHNPRRK | MKEKHNPRRKYCLISGLAIIFSLWIIIGNGAKVQAETITVSTPIKQIFPDDAFAETIKDNLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVTKLFLNGNKLTDIKPLTNLKNLGWLFLDENKIKDLSSLKDLKKLKSLSLEHNGISDINGLVHLPQLESLYLGNNKITDITVLSRLTKLDTLSLEDNQISDIVPLAGLTKLQNLYLSKNHISDLRALAGLKNLDVLELFSQECLNKPINHQSNLVVPNTVKNTDGSLVTPEIISDDGDYEKPNVKWHLPEFTNEVSFIFYQPVTIGKAKARFHGRVTQPLKEVYTVSYDVDGTVIKTKVEAGTRITAPKPPTKQGYVFKGWYTEKNGGHEWNFNTDYMSGNDFTLYAVFKAETTEKTVNLTRYVKYIRGNAGIYKLPREDNSLKQGTLASHRCKALTVDREARNGGKLWYRLKNIGWTKAENLSLDRYDKMEYDKGVTAYARVRNASGNSVWTKPYNTAGAKHVNKLSVYQGKNMRILREAKTPITTWYQFSIGGKVIGWVDTRALNTFYKQSMEKPTRLTRYVSANKAGESYYKVPVADNPVKRGTLAKYKNQKLIVDCQATIEGQLWYRIRTSSTFIGWTKAANLRAQK | entry of bacterium into host cell cell surface; extracellular region; peptidoglycan-based cell wall; plasma membrane heparin binding lipid binding metal ion binding Listeria monocytogenes serotype 1/2a 3D-structure Calcium Cell membrane Heparin-binding Leucine-rich repeat Lipid-binding Membrane Metal-binding Repeat Secreted Signal Virulence MKEKHNPRRK MKEKHNPRRKYCLISGLAIIFSLWIIIGNGAKVQAETITVSTPIKQIFPDDAFAETIKDNLKKKSVTDAVTQNELNSIDQIIANNSDIKSVQGIQYLPNVTKLFLNGNKLTDIKPLTNLKNLGWLFLDENKIKDLSSLKDLKKLKSLSLEHNGISDINGLVHLPQLESLYLGNNKITDITVLSRLTKLDTLSLEDNQISDIVPLAGLTKLQNLYLSKNHISDLRALAGLKNLDVLELFSQECLNKPINHQSNLVVPNTVKNTDGSLVTPEIISDDGDYEKPNVKWHLPEFTNEVSFIFYQPVTIGKAKARFHGRVTQPLKEVYTVSYDVDGTVIKTKVEAGTRITAPKPPTKQGYVFKGWYTEKNGGHEWNFNTDYMSGNDFTLYAVFKAETTEKTVNLTRYVKYIRGNAGIYKLPREDNSLKQGTLASHRCKALTVDREARNGGKLWYRLKNIGWTKAENLSLDRYDKMEYDKGVTAYARVRNASGNSVWTKPYNTAGAKHVNKLSVYQGKNMRILREAKTPITTWYQFSIGGKVIGWVDTRALNTFYKQSMEKPTRLTRYVSANKAGESYYKVPVADNPVKRGTLAKYKNQKLIVDCQATIEGQLWYRIRTSSTFIGWTKAANLRAQK |
defense response to bacterium killing of cells of another organism | extracellular region | L-phenylalaine oxidase activity toxin activity | Cerastes cerastes | Antibiotic Antimicrobial Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Platelet aggregation inhibiting toxin Secreted Toxin | ADDKNPLEEC | ADDKNPLEECFREADYEEFLEIAKVTVLEASERNDKEDWYANLGPMRLPEKLNEFVQETENGWYFIKYPVKPSEEGKSAGQLYEESLRKSAGQLYQESLGKAHDDIFAYEKRFDEIVDGMDKLPTSMYQAIQERINFKPPLPPKKYAMGAITTFTPYQFQHFSEALTAPVGR | defense response to bacterium killing of cells of another organism extracellular region L-phenylalaine oxidase activity toxin activity Cerastes cerastes Antibiotic Antimicrobial Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Oxidoreductase Platelet aggregation inhibiting toxin Secreted Toxin ADDKNPLEEC ADDKNPLEECFREADYEEFLEIAKVTVLEASERNDKEDWYANLGPMRLPEKLNEFVQETENGWYFIKYPVKPSEEGKSAGQLYEESLRKSAGQLYQESLGKAHDDIFAYEKRFDEIVDGMDKLPTSMYQAIQERINFKPPLPPKKYAMGAITTFTPYQFQHFSEALTAPVGR |
magnetosome assembly | cytoplasm; cytoskeleton | ATP binding ATP hydrolysis activity | Magnetospirillum magneticum | ATP-binding Biomineralization Cytoplasm Cytoskeleton Hydrolase Nucleotide-binding Reference proteome | MIVNDNQNIL | MIVNDNQNILYVGIDFGYSKTVIMTSRGKSLSLKSLVGYPKDFVGLARLGRPYLVGDEAFEMRSYLHLRNPLLDGLLNPISEQDIDVTRHFISHIIKCAEPAAGEKVFAVIGVTPRFTAANKKLLLKLAQEYCQNVLLMSAPFLAGNSIGKASGSIIIDIGAWTTDICAMKGRIPRPEDQSSIAKAGSYIDERLKNSILERYPALQINANIARMVKEQFAFVGRPQLVAACEFRSAGKAVRCDVTEQVRAACESPFAEIAERIGAVLCVVPPEDQALVLKNIVITGAGAQIRGLPEYVKSMLAPYGDARVSIANEPLMEACKGALSMAQEIPPHFWGQL | magnetosome assembly cytoplasm; cytoskeleton ATP binding ATP hydrolysis activity Magnetospirillum magneticum ATP-binding Biomineralization Cytoplasm Cytoskeleton Hydrolase Nucleotide-binding Reference proteome MIVNDNQNIL MIVNDNQNILYVGIDFGYSKTVIMTSRGKSLSLKSLVGYPKDFVGLARLGRPYLVGDEAFEMRSYLHLRNPLLDGLLNPISEQDIDVTRHFISHIIKCAEPAAGEKVFAVIGVTPRFTAANKKLLLKLAQEYCQNVLLMSAPFLAGNSIGKASGSIIIDIGAWTTDICAMKGRIPRPEDQSSIAKAGSYIDERLKNSILERYPALQINANIARMVKEQFAFVGRPQLVAACEFRSAGKAVRCDVTEQVRAACESPFAEIAERIGAVLCVVPPEDQALVLKNIVITGAGAQIRGLPEYVKSMLAPYGDARVSIANEPLMEACKGALSMAQEIPPHFWGQL |
short-chain fatty acid catabolic process | mitochondrial matrix; mitochondrion | ATP binding metal ion binding propionyl-CoA carboxylase activity | Sus scrofa | Acetylation ATP-binding Biotin Ligase Lipid degradation Lipid metabolism Magnesium Manganese Metal-binding Mitochondrion Nucleotide-binding Phosphoprotein Reference proteome Transit peptide | MAGLWVGGSV | MAGLWVGGSVLVAAGRRGSRSPRPLMRSVALWTLKHVPQYSRQRLLVSRSLCLAGYDSNEKTFDKILIANRGEIACRVIKTCKKMGIKTVAVHSDVDASSVHVTMADEAVCVGPAPTSKSYLNMDAIMEAVRTTRAQAVHPGYGFLSENKEFAKCLAAEGVIFIGPDTHAIQAMGDKIESKLLAKKAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDSETRRAMGEQAVALAKAVNYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHRQADIPINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPIHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSNRMEALKRMENALDNYVIRGVTHNIALLREVIINSRFVEGDINTKFLSDVYPDGFKGHKLTEDERNQLLAIASSLFVASQLRAQRFQEPENSRVPIIKPQVANWELSIRLHDEVHTVTASNSGPTFSVEVDGSKLNVTSTWNLASPLLSVSIDGTQRTIQCLSRDAGGNMSIQFLGTVYKVHILTKLAAELNKFMLEKAAEDTSSILHSPMPGVVVAVSVKPGDLVAEGQEICVIEAMKMQNSMTAGKTGKVKSVHCKAGDTVGEGDLLVELE | short-chain fatty acid catabolic process mitochondrial matrix; mitochondrion ATP binding metal ion binding propionyl-CoA carboxylase activity Sus scrofa Acetylation ATP-binding Biotin Ligase Lipid degradation Lipid metabolism Magnesium Manganese Metal-binding Mitochondrion Nucleotide-binding Phosphoprotein Reference proteome Transit peptide MAGLWVGGSV MAGLWVGGSVLVAAGRRGSRSPRPLMRSVALWTLKHVPQYSRQRLLVSRSLCLAGYDSNEKTFDKILIANRGEIACRVIKTCKKMGIKTVAVHSDVDASSVHVTMADEAVCVGPAPTSKSYLNMDAIMEAVRTTRAQAVHPGYGFLSENKEFAKCLAAEGVIFIGPDTHAIQAMGDKIESKLLAKKAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDSETRRAMGEQAVALAKAVNYSSAGTVEFLVDSKKNFYFLEMNTRLQVEHPVTECITGLDLVQEMIRVAKGYPLRHRQADIPINGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPIHLPGVRVDSGIQPGSDISIYYDPMISKLITYGSNRMEALKRMENALDNYVIRGVTHNIALLREVIINSRFVEGDINTKFLSDVYPDGFKGHKLTEDERNQLLAIASSLFVASQLRAQRFQEPENSRVPIIKPQVANWELSIRLHDEVHTVTASNSGPTFSVEVDGSKLNVTSTWNLASPLLSVSIDGTQRTIQCLSRDAGGNMSIQFLGTVYKVHILTKLAAELNKFMLEKAAEDTSSILHSPMPGVVVAVSVKPGDLVAEGQEICVIEAMKMQNSMTAGKTGKVKSVHCKAGDTVGEGDLLVELE |
induction by virus of host reticulophagy inorganic cation transmembrane transport protein complex oligomerization virus-mediated pore formation in host cell membrane | extracellular region; host cell endoplasmic reticulum; host cell endoplasmic reticulum membrane; host cell endosome; host cell lysosome; host cell plasma membrane; plasma membrane; virion membrane; voltage-gated calcium channel complex; voltage-gated potassium channel complex | identical protein binding molecular function activator activity monoatomic ion channel activity | Severe acute respiratory syndrome coronavirus 2 | 3D-structure Activation of host autophagy by virus Glycoprotein Host cell membrane Host cytoplasm Host endoplasmic reticulum Host endosome Host lysosome Host membrane Host-virus interaction Ion channel Ion transport Membrane Reference proteome Secreted Transmembrane Transmembrane helix Transport Viral ion channel Virion | MDLFMRIFTI | MDLFMRIFTIGTVTLKQGEIKDATPSDFVRATATIPIQASLPFGWLIVGVALLAVFQSASKIITLKKRWQLALSKGVHFVCNLLLLFVTVYSHLLLVAAGLEAPFLYLYALVYFLQSINFVRIIMRLWLCWKCRSKNPLLYDANYFLCWHTNCYDYCIPYNSVTSSIVITSGDGTTSPISEHDYQIGGYTEKWESGVKDCVVLHSYFTSDYYQLYSTQLSTDTGVEHVTFFIYNKIVDEPEEHVQIHTIDGSSGVVNPVMEPIYDEPTTTTSVPL | induction by virus of host reticulophagy inorganic cation transmembrane transport protein complex oligomerization virus-mediated pore formation in host cell membrane extracellular region; host cell endoplasmic reticulum; host cell endoplasmic reticulum membrane; host cell endosome; host cell lysosome; host cell plasma membrane; plasma membrane; virion membrane; voltage-gated calcium channel complex; voltage-gated potassium channel complex identical protein binding molecular function activator activity monoatomic ion channel activity Severe acute respiratory syndrome coronavirus 2 3D-structure Activation of host autophagy by virus Glycoprotein Host cell membrane Host cytoplasm Host endoplasmic reticulum Host endosome Host lysosome Host membrane Host-virus interaction Ion channel Ion transport Membrane Reference proteome Secreted Transmembrane Transmembrane helix Transport Viral ion channel Virion MDLFMRIFTI MDLFMRIFTIGTVTLKQGEIKDATPSDFVRATATIPIQASLPFGWLIVGVALLAVFQSASKIITLKKRWQLALSKGVHFVCNLLLLFVTVYSHLLLVAAGLEAPFLYLYALVYFLQSINFVRIIMRLWLCWKCRSKNPLLYDANYFLCWHTNCYDYCIPYNSVTSSIVITSGDGTTSPISEHDYQIGGYTEKWESGVKDCVVLHSYFTSDYYQLYSTQLSTDTGVEHVTFFIYNKIVDEPEEHVQIHTIDGSSGVVNPVMEPIYDEPTTTTSVPL |
cytoplasmic capsid assembly viral budding from Golgi membrane virus-mediated pore formation in host cell membrane | endoplasmic reticulum-Golgi intermediate compartment; host cell Golgi membrane; membrane; virion membrane | identical protein binding monoatomic ion channel activity structural constituent of virion | Severe acute respiratory syndrome coronavirus 2 | 3D-structure Apoptosis Host Golgi apparatus Host membrane Membrane Reference proteome Transmembrane Transmembrane helix | MYSFVSEETG | MYSFVSEETGTLIVNSVLLFLAFVVFLLVTLAILTALRLCAYCCNIVNVSLVKPSFYVYSRVKNLNSSRVPDLLV | cytoplasmic capsid assembly viral budding from Golgi membrane virus-mediated pore formation in host cell membrane endoplasmic reticulum-Golgi intermediate compartment; host cell Golgi membrane; membrane; virion membrane identical protein binding monoatomic ion channel activity structural constituent of virion Severe acute respiratory syndrome coronavirus 2 3D-structure Apoptosis Host Golgi apparatus Host membrane Membrane Reference proteome Transmembrane Transmembrane helix MYSFVSEETG MYSFVSEETGTLIVNSVLLFLAFVVFLLVTLAILTALRLCAYCCNIVNVSLVKPSFYVYSRVKNLNSSRVPDLLV |
cytoplasmic capsid assembly suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity | endoplasmic reticulum-Golgi intermediate compartment; host cell Golgi membrane; plasma membrane; viral envelope; virion membrane | identical protein binding protein sequestering activity structural constituent of virion | Severe acute respiratory syndrome coronavirus 2 | 3D-structure Glycoprotein Host Golgi apparatus Host membrane Host-virus interaction Membrane Reference proteome Transmembrane Transmembrane helix Viral envelope protein Viral immunoevasion Viral matrix protein Virion | MADSNGTITV | MADSNGTITVEELKKLLEQWNLVIGFLFLTWICLLQFAYANRNRFLYIIKLIFLWLLWPVTLACFVLAAVYRINWITGGIAIAMACLVGLMWLSYFIASFRLFARTRSMWSFNPETNILLNVPLHGTILTRPLLESELVIGAVILRGHLRIAGHHLGRCDIKDLPKEITVATSRTLSYYKLGASQRVAGDSGFAAYSRYRIGNYKLNTDHSSSSDNIALLVQ | cytoplasmic capsid assembly suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity endoplasmic reticulum-Golgi intermediate compartment; host cell Golgi membrane; plasma membrane; viral envelope; virion membrane identical protein binding protein sequestering activity structural constituent of virion Severe acute respiratory syndrome coronavirus 2 3D-structure Glycoprotein Host Golgi apparatus Host membrane Host-virus interaction Membrane Reference proteome Transmembrane Transmembrane helix Viral envelope protein Viral immunoevasion Viral matrix protein Virion MADSNGTITV MADSNGTITVEELKKLLEQWNLVIGFLFLTWICLLQFAYANRNRFLYIIKLIFLWLLWPVTLACFVLAAVYRINWITGGIAIAMACLVGLMWLSYFIASFRLFARTRSMWSFNPETNILLNVPLHGTILTRPLLESELVIGAVILRGHLRIAGHHLGRCDIKDLPKEITVATSRTLSYYKLGASQRVAGDSGFAAYSRYRIGNYKLNTDHSSSSDNIALLVQ |
disruption by virus of host JAK-STAT cascade via inhibition of STAT1 activity disruption by virus of host JAK-STAT cascade via inhibition of STAT2 activity suppression by virus of host type I interferon-mediated signaling pathway suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity | host cell endoplasmic reticulum membrane; host cell Golgi membrane; membrane; nuclear pore | protein sequestering activity | Severe acute respiratory syndrome coronavirus 2 | 3D-structure Host endoplasmic reticulum Host Golgi apparatus Host membrane Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Inhibition of host STAT1 by virus Inhibition of host STAT2 by virus Membrane Reference proteome Viral immunoevasion Virulence | MFHLVDFQVT | MFHLVDFQVTIAEILLIIMRTFKVSIWNLDYIINLIIKNLSKSLTENKYSQLDEEQPMEID | disruption by virus of host JAK-STAT cascade via inhibition of STAT1 activity disruption by virus of host JAK-STAT cascade via inhibition of STAT2 activity suppression by virus of host type I interferon-mediated signaling pathway suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity host cell endoplasmic reticulum membrane; host cell Golgi membrane; membrane; nuclear pore protein sequestering activity Severe acute respiratory syndrome coronavirus 2 3D-structure Host endoplasmic reticulum Host Golgi apparatus Host membrane Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Inhibition of host STAT1 by virus Inhibition of host STAT2 by virus Membrane Reference proteome Viral immunoevasion Virulence MFHLVDFQVT MFHLVDFQVTIAEILLIIMRTFKVSIWNLDYIINLIIKNLSKSLTENKYSQLDEEQPMEID |
negative regulation of interferon-beta production positive regulation of immunoglobulin mediated immune response suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I virus-mediated perturbation of host defense response | endoplasmic reticulum; extracellular region; extracellular space; lysosome | cytokine activity identical protein binding | Severe acute respiratory syndrome coronavirus 2 | 3D-structure Disulfide bond Evasion of host immunity by viral interleukin-like protein Glycoprotein Host-virus interaction Reference proteome Secreted Signal Viral immunoevasion | MKFLVFLGII | MKFLVFLGIITTVAAFHQECSLQSCTQHQPYVVDDPCPIHFYSKWYIRVGARKSAPLIELCVDEAGSKSPIQYIDIGNYTVSCLPFTINCQEPKLGSLVVRCSFYEDFLEYHDVRVVLDFI | negative regulation of interferon-beta production positive regulation of immunoglobulin mediated immune response suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I virus-mediated perturbation of host defense response endoplasmic reticulum; extracellular region; extracellular space; lysosome cytokine activity identical protein binding Severe acute respiratory syndrome coronavirus 2 3D-structure Disulfide bond Evasion of host immunity by viral interleukin-like protein Glycoprotein Host-virus interaction Reference proteome Secreted Signal Viral immunoevasion MKFLVFLGII MKFLVFLGIITTVAAFHQECSLQSCTQHQPYVVDDPCPIHFYSKWYIRVGARKSAPLIELCVDEAGSKSPIQYIDIGNYTVSCLPFTINCQEPKLGSLVVRCSFYEDFLEYHDVRVVLDFI |
cytoplasmic capsid assembly negative regulation of interferon-beta production positive regulation of NLRP3 inflammasome complex assembly response to host immune response viral RNA genome packaging | cytoplasm; extracellular region; host cell endoplasmic reticulum-Golgi intermediate compartment; host cell Golgi apparatus; host cell perinuclear region of cytoplasm; host extracellular space; intracellular non-membrane-bounded organelle; MHC class I protein complex; ribonucleoprotein complex; viral capsid; viral nucleocapsid | identical protein binding MHC class I protein binding molecular condensate scaffold activity protein homodimerization activity protein sequestering activity RNA binding RNA stem-loop binding | Severe acute respiratory syndrome coronavirus 2 | 3D-structure ADP-ribosylation Host cytoplasm Phosphoprotein Reference proteome Ribonucleoprotein RNA-binding Secreted Transcription Transcription regulation Viral nucleoprotein Virion | MSDNGPQNQR | MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQRQKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQA | cytoplasmic capsid assembly negative regulation of interferon-beta production positive regulation of NLRP3 inflammasome complex assembly response to host immune response viral RNA genome packaging cytoplasm; extracellular region; host cell endoplasmic reticulum-Golgi intermediate compartment; host cell Golgi apparatus; host cell perinuclear region of cytoplasm; host extracellular space; intracellular non-membrane-bounded organelle; MHC class I protein complex; ribonucleoprotein complex; viral capsid; viral nucleocapsid identical protein binding MHC class I protein binding molecular condensate scaffold activity protein homodimerization activity protein sequestering activity RNA binding RNA stem-loop binding Severe acute respiratory syndrome coronavirus 2 3D-structure ADP-ribosylation Host cytoplasm Phosphoprotein Reference proteome Ribonucleoprotein RNA-binding Secreted Transcription Transcription regulation Viral nucleoprotein Virion MSDNGPQNQR MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKEDLKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANKDGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRNSSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEASKKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSRIGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQRQKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQA |
negative regulation of defense response to virus negative regulation of mitochondrial fission positive regulation of autophagosome assembly suppression by virus of host type I interferon-mediated signaling pathway suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity | host cell mitochondrion; mitochondrial membrane; mitochondrial outer membrane; outer mitochondrial membrane protein complex | identical protein binding protein sequestering activity | Severe acute respiratory syndrome coronavirus 2 | 3D-structure Host cytoplasm Host mitochondrion Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host MAVS by virus Inhibition of host RLR pathway by virus Reference proteome Viral immunoevasion | MDPKISEMHP | MDPKISEMHPALRLVDPQIQLAVTRMENAVGRDQNNVGPKVYPIILRLGSPLSLNMARKTLNSLEDKAFQLTPIAVQMTKLATTEELPDEFVVVTVK | negative regulation of defense response to virus negative regulation of mitochondrial fission positive regulation of autophagosome assembly suppression by virus of host type I interferon-mediated signaling pathway suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity host cell mitochondrion; mitochondrial membrane; mitochondrial outer membrane; outer mitochondrial membrane protein complex identical protein binding protein sequestering activity Severe acute respiratory syndrome coronavirus 2 3D-structure Host cytoplasm Host mitochondrion Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host MAVS by virus Inhibition of host RLR pathway by virus Reference proteome Viral immunoevasion MDPKISEMHP MDPKISEMHPALRLVDPQIQLAVTRMENAVGRDQNNVGPKVYPIILRLGSPLSLNMARKTLNSLEDKAFQLTPIAVQMTKLATTEELPDEFVVVTVK |
bile acid metabolic process cellular glucuronidation response to stimulus sensory perception of chemical stimulus sensory perception of smell | endoplasmic reticulum membrane | glucuronosyltransferase activity | Homo sapiens | Alternative splicing Endoplasmic reticulum Glycoprotein Glycosyltransferase Lipid metabolism Membrane Olfaction Reference proteome Sensory transduction Signal Transferase Transmembrane Transmembrane helix | MLNNLLLFSL | MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALFITPTSNPSLTFEIYKVPFGKERIEGVIKDFVLTWLENRPSPSTIWRFYQEMAKVIKDFHMVSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVEKHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGGLLLCCPGWSAVADLGSLQPLLPGFKRFSRLSLHCSWDYRLPAGRPTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKVLWRYKGKKPATLGNNTQLFDWIPQNDLLGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTSVDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE | bile acid metabolic process cellular glucuronidation response to stimulus sensory perception of chemical stimulus sensory perception of smell endoplasmic reticulum membrane glucuronosyltransferase activity Homo sapiens Alternative splicing Endoplasmic reticulum Glycoprotein Glycosyltransferase Lipid metabolism Membrane Olfaction Reference proteome Sensory transduction Signal Transferase Transmembrane Transmembrane helix MLNNLLLFSL MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALFITPTSNPSLTFEIYKVPFGKERIEGVIKDFVLTWLENRPSPSTIWRFYQEMAKVIKDFHMVSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVEKHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGGLLLCCPGWSAVADLGSLQPLLPGFKRFSRLSLHCSWDYRLPAGRPTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKVLWRYKGKKPATLGNNTQLFDWIPQNDLLGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTSVDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE |
bile acid metabolic process cellular glucuronidation | endoplasmic reticulum membrane | glucuronosyltransferase activity | Homo sapiens | Alternative splicing Endoplasmic reticulum Glycoprotein Glycosyltransferase Lipid metabolism Membrane Reference proteome Transferase Transmembrane Transmembrane helix | MVSIRDFTMP | MVSIRDFTMPKKFVQMLVFNLTLTEVVLSGNVLIWPTDGSHWLNIKIILEELIQRNHNVTVLASSATLFINSNPDSPVNFEVIPVSYKKSNIDSLIEHMIMLWIDHRPTPLTIWAFYKELGKLLDTFFQINIQLCDGVLKNPKLMARLQKGGFDVLVADPVTICGDLVALKLGIPFMYTLRFSPASTVERHCGKIPAPVSYVPAALSELTDQMTFGERIKNTISYSLQDYIFQSYWGEWNSYYSKILGRPTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKNGVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDLLGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTSVDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE | bile acid metabolic process cellular glucuronidation endoplasmic reticulum membrane glucuronosyltransferase activity Homo sapiens Alternative splicing Endoplasmic reticulum Glycoprotein Glycosyltransferase Lipid metabolism Membrane Reference proteome Transferase Transmembrane Transmembrane helix MVSIRDFTMP MVSIRDFTMPKKFVQMLVFNLTLTEVVLSGNVLIWPTDGSHWLNIKIILEELIQRNHNVTVLASSATLFINSNPDSPVNFEVIPVSYKKSNIDSLIEHMIMLWIDHRPTPLTIWAFYKELGKLLDTFFQINIQLCDGVLKNPKLMARLQKGGFDVLVADPVTICGDLVALKLGIPFMYTLRFSPASTVERHCGKIPAPVSYVPAALSELTDQMTFGERIKNTISYSLQDYIFQSYWGEWNSYYSKILGRPTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKNGVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDLLGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTSVDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHDLTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE |
carbohydrate metabolic process oligosaccharide metabolic process | extracellular exosome; extracellular space | alpha-amylase activity calcium ion binding chloride ion binding | Homo sapiens | Calcium Carbohydrate metabolism Chloride Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal | MKLFWLLFTI | MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL | carbohydrate metabolic process oligosaccharide metabolic process extracellular exosome; extracellular space alpha-amylase activity calcium ion binding chloride ion binding Homo sapiens Calcium Carbohydrate metabolism Chloride Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal MKLFWLLFTI MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL |
carbohydrate metabolic process oligosaccharide metabolic process | extracellular exosome; extracellular space | alpha-amylase activity calcium ion binding chloride ion binding | Homo sapiens | Calcium Carbohydrate metabolism Chloride Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal | MKLFWLLFTI | MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL | carbohydrate metabolic process oligosaccharide metabolic process extracellular exosome; extracellular space alpha-amylase activity calcium ion binding chloride ion binding Homo sapiens Calcium Carbohydrate metabolism Chloride Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal MKLFWLLFTI MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL |
ribosome biogenesis | cytosol; ribonucleoprotein complex | GTP binding GTPase activity guanosine tetraphosphate binding ribosome binding rRNA binding tRNA binding | Escherichia coli | 3D-structure Chaperone Cytoplasm Direct protein sequencing GTP-binding Hydrolase Nucleotide-binding Reference proteome Ribosome biogenesis RNA-binding rRNA-binding tRNA-binding | MIEKLRNIAI | MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPIRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPKDD | ribosome biogenesis cytosol; ribonucleoprotein complex GTP binding GTPase activity guanosine tetraphosphate binding ribosome binding rRNA binding tRNA binding Escherichia coli 3D-structure Chaperone Cytoplasm Direct protein sequencing GTP-binding Hydrolase Nucleotide-binding Reference proteome Ribosome biogenesis RNA-binding rRNA-binding tRNA-binding MIEKLRNIAI MIEKLRNIAIIAHVDHGKTTLVDKLLQQSGTFDSRAETQERVMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGGEVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVVINKVDRPGARPDWVVDQVFDLFVNLDATDEQLDFPIVYASALNGIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNAKVGKVLGHLGLERIETDLAEAGDIVAITGLGELNISDTVCDTQNVEALPALSVDEPTVSMFFCVNTSPFCGKEGKFVTSRQILDRLNKELVHNVALRVEETEDADAFRVSGRGELHLSVLIENMRREGFELAVSRPKVIFREIDGRKQEPYENVTLDVEEQHQGSVMQALGERKGDLKNMNPDGKGRVRLDYVIPSRGLIGFRSEFMTMTSGTGLLYSTFSHYDDVRPGEVGQRQNGVLISNGQGKAVAFALFGLQDRGKLFLGHGAEVYEGQIIGIHSRSNDLTVNCLTGKKLTNMRASGTDEAVVLVPPIRMTLEQALEFIDDDELVEVTPTSIRIRKRHLTENDRRRANRAPKDD |
detection of tumor cell response to bacterium T cell mediated cytotoxicity directed against tumor cell target | alpha-beta T cell receptor complex | signaling receptor activity | Homo sapiens | Adaptive immunity Cell membrane Disulfide bond Glycoprotein Immunity Membrane Reference proteome Signal Transmembrane Transmembrane helix | MACPGFLWAL | MACPGFLWALVISTCLEFSMAQTVTQSQPEMSVQEAETVTLSCTYDTSESDYYLFWYKQPPSRQMILVIRQEAYKQQNATENRFSVNFQKAAKSFSLKISDSQLGDAAMYFCAYRSAVNARLMFGDGTQLVVKPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTNLNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS | detection of tumor cell response to bacterium T cell mediated cytotoxicity directed against tumor cell target alpha-beta T cell receptor complex signaling receptor activity Homo sapiens Adaptive immunity Cell membrane Disulfide bond Glycoprotein Immunity Membrane Reference proteome Signal Transmembrane Transmembrane helix MACPGFLWAL MACPGFLWALVISTCLEFSMAQTVTQSQPEMSVQEAETVTLSCTYDTSESDYYLFWYKQPPSRQMILVIRQEAYKQQNATENRFSVNFQKAAKSFSLKISDSQLGDAAMYFCAYRSAVNARLMFGDGTQLVVKPNIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTNLNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS |
cell surface receptor signaling pathway detection of tumor cell T cell mediated cytotoxicity directed against tumor cell target | alpha-beta T cell receptor complex; plasma membrane | signaling receptor activity | Homo sapiens | Cell membrane Disulfide bond Glycoprotein Immunity Membrane Reference proteome Signal Transmembrane Transmembrane helix | MTIRLLCYMG | MTIRLLCYMGFYFLGAGLMEADIYQTPRYLVIGTGKKITLECSQTMGHDKMYWYQQDPGMELHLIHYSYGVNSTEKGDLSSESTVSRIRTEHFPLTLESARPSHTSQYLCASSEARGLAEFTDTQYFGPGTRLTVLEDLKNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDSRG | cell surface receptor signaling pathway detection of tumor cell T cell mediated cytotoxicity directed against tumor cell target alpha-beta T cell receptor complex; plasma membrane signaling receptor activity Homo sapiens Cell membrane Disulfide bond Glycoprotein Immunity Membrane Reference proteome Signal Transmembrane Transmembrane helix MTIRLLCYMG MTIRLLCYMGFYFLGAGLMEADIYQTPRYLVIGTGKKITLECSQTMGHDKMYWYQQDPGMELHLIHYSYGVNSTEKGDLSSESTVSRIRTEHFPLTLESARPSHTSQYLCASSEARGLAEFTDTQYFGPGTRLTVLEDLKNVFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVSTDPQPLKEQPALNDSRYCLSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRADCGFTSESYQQGVLSATILYEILLGKATLYAVLVSALVLMAMVKRKDSRG |
carbohydrate metabolic process oligosaccharide metabolic process | extracellular exosome; extracellular space | alpha-amylase activity calcium ion binding chloride ion binding | Homo sapiens | 3D-structure Calcium Carbohydrate metabolism Chloride Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal | MKLFWLLFTI | MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL | carbohydrate metabolic process oligosaccharide metabolic process extracellular exosome; extracellular space alpha-amylase activity calcium ion binding chloride ion binding Homo sapiens 3D-structure Calcium Carbohydrate metabolism Chloride Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Pyrrolidone carboxylic acid Reference proteome Secreted Signal MKLFWLLFTI MKLFWLLFTIGFCWAQYSSNTQQGRTSIVHLFEWRWVDIALECERYLAPKGFGGVQVSPPNENVAIHNPFRPWWERYQPVSYKLCTRSGNEDEFRNMVTRCNNVGVRIYVDAVINHMCGNAVSAGTSSTCGSYFNPGSRDFPAVPYSGWDFNDGKCKTGSGDIENYNDATQVRDCRLSGLLDLALGKDYVRSKIAEYMNHLIDIGVAGFRIDASKHMWPGDIKAILDKLHNLNSNWFPEGSKPFIYQEVIDLGGEPIKSSDYFGNGRVTEFKYGAKLGTVIRKWNGEKMSYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYRWPRYFENGKDVNDWVGPPNDNGVTKEVTINPDTTCGNDWVCEHRWRQIRNMVNFRNVVDGQPFTNWYDNGSNQVAFGRGNRGFIVFNNDDWTFSLTLQTGLPAGTYCDVISGDKINGNCTGIKIYVSDDGKAHFSISNSAEDPFIAIHAESKL |
lipid catabolic process | extracellular region | metal ion binding triglyceride lipase activity | Burkholderia plantarii | 3D-structure Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Secreted Signal | MVRSMRSRVA | MVRSMRSRVAARAVAWALAVMPLAGAAGLTMAASPAAVAADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV | lipid catabolic process extracellular region metal ion binding triglyceride lipase activity Burkholderia plantarii3D-structure Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Secreted Signal MVRSMRSRVA MVRSMRSRVAARAVAWALAVMPLAGAAGLTMAASPAAVAADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV |
lipid catabolic process | extracellular region | metal ion binding triglyceride lipase activity | Pseudarthrobacter phenanthrenivorans | 3D-structure Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Secreted | ADTYAATRYP | ADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV | lipid catabolic process extracellular region metal ion binding triglyceride lipase activity Pseudarthrobacter phenanthrenivorans 3D-structure Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Secreted ADTYAATRYP ADTYAATRYPVILVHGLAGTDKFANVVDYWYGIQSDLQSHGAKVYVANLSGFQSDDGPNGRGEQLLAYVKQVLAATGATKVNLIGHSQGGLTSRYVAAVAPQLVASVTTIGTPHRGSEFADFVQDVLKTDPTGLSSTVIAAFVNVFGTLVSSSHNTDQDALAALRTLTTAQTATYNRNFPSAGLGAPGSCQTGAATETVGGSQHLLYSWGGTAIQPTSTVLGVTGATDTSTGTLDVANVTDPSTLALLATGAVMINRASGQNDGLVSRCSSLFGQVISTSYHWNHLDEINQLLGVRGANAEDPVAVIRTHVNRLKLQGV |
peptidyl-serine O-acetylation peptidyl-threonine O-acetylation regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway symbiont-mediated activation of host programmed cell death | extracellular region | O-acetyltransferase activity toxin activity | Yersinia pseudotuberculosis serotype O:3 | Acyltransferase Allosteric enzyme Direct protein sequencing Plasmid Secreted Transferase Virulence | MIGPISQINI | MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV | peptidyl-serine O-acetylation peptidyl-threonine O-acetylation regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway symbiont-mediated activation of host programmed cell death extracellular region O-acetyltransferase activity toxin activity Yersinia pseudotuberculosis serotype O:3 Acyltransferase Allosteric enzyme Direct protein sequencing Plasmid Secreted Transferase Virulence MIGPISQINI MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV |
arachidonic acid secretion phospholipid metabolic process | extracellular region | metal ion binding phospholipase A2 activity toxin activity | Naja haje haje | Blood coagulation cascade inhibiting toxin Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Metal-binding Platelet aggregation inhibiting toxin Secreted Toxin | NVYQYRKMLQ | NVYQYRKMLQCAMPNGGPFECCQTHDNCYGEAEKLKACTSTHSSPYFK | arachidonic acid secretion phospholipid metabolic process extracellular region metal ion binding phospholipase A2 activity toxin activity Naja haje haje Blood coagulation cascade inhibiting toxin Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Metal-binding Platelet aggregation inhibiting toxin Secreted Toxin NVYQYRKMLQ NVYQYRKMLQCAMPNGGPFECCQTHDNCYGEAEKLKACTSTHSSPYFK |
symbiont-mediated perturbation of host defense-related programmed cell death | extracellular region; host cell; host cell Golgi apparatus | lipid binding manganese ion binding protein-arginine N-acetylglucosaminyltransferase activity toxin activity | Salmonella typhimurium | 3D-structure Glycoprotein Glycosyltransferase Host Golgi apparatus Lipid-binding Manganese Metal-binding Secreted Toxin Transferase Virulence | MFSRVRGFLS | MFSRVRGFLSCQNYSHTATPAITLPSSGSANFAGVEYPLLPLDQHTPLLFQWFERNPSRFGENQIPIINTQQNPYLNNIINAAIIEKERTIGVLVDGNFSAGQKKALAKLEKQYENIKVIYNSDLDYSMYDKKLSDIYLENIAKIEAQPANVRDEYLLGEIKKSLNEVLKNNPEESLVSSHDKRLGHVRFDFYRNLFLLKGSNAFLEAGKHGCHHLQPGGGCIYLDADMLLTGKLGTLYLPDGIAVHVSRKGNSMSLENGIIAVNRSEHPALKKGLEIMHSKPYGDPYIDGVCGGLRHYFNCSIRHNYEEFCNFIEFKHEHIFMDTSSLTISSWR | symbiont-mediated perturbation of host defense-related programmed cell death extracellular region; host cell; host cell Golgi apparatus lipid binding manganese ion binding protein-arginine N-acetylglucosaminyltransferase activity toxin activity Salmonella typhimurium 3D-structure Glycoprotein Glycosyltransferase Host Golgi apparatus Lipid-binding Manganese Metal-binding Secreted Toxin Transferase Virulence MFSRVRGFLS MFSRVRGFLSCQNYSHTATPAITLPSSGSANFAGVEYPLLPLDQHTPLLFQWFERNPSRFGENQIPIINTQQNPYLNNIINAAIIEKERTIGVLVDGNFSAGQKKALAKLEKQYENIKVIYNSDLDYSMYDKKLSDIYLENIAKIEAQPANVRDEYLLGEIKKSLNEVLKNNPEESLVSSHDKRLGHVRFDFYRNLFLLKGSNAFLEAGKHGCHHLQPGGGCIYLDADMLLTGKLGTLYLPDGIAVHVSRKGNSMSLENGIIAVNRSEHPALKKGLEIMHSKPYGDPYIDGVCGGLRHYFNCSIRHNYEEFCNFIEFKHEHIFMDTSSLTISSWR |
regulation of cell shape | plasma membrane | lipid binding | Helicobacter pylori | 3D-structure Cell inner membrane Cell membrane Cell shape Lipid-binding Membrane Reference proteome Stress response Toxin-antitoxin system | MATKHGKNSW | MATKHGKNSWKTLYLKISFLGCKVVVLLKR | regulation of cell shape plasma membrane lipid binding Helicobacter pylori 3D-structure Cell inner membrane Cell membrane Cell shape Lipid-binding Membrane Reference proteome Stress response Toxin-antitoxin system MATKHGKNSW MATKHGKNSWKTLYLKISFLGCKVVVLLKR |
arachidonic acid secretion lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity | Bothrocophias hyoprora | Calcium Direct protein sequencing Disulfide bond Hydrolase Metal-binding Secreted | DLMQFETLIM | DLMQFETLIMKSGVWYYGSYGCYCGSGGQFRPQDASDRCCFVHDCCYGKNGDIVCGGDDPCKKQICECDRVAATCFRDNKVTYDNKYWFFPAKFPPQNCKEESEPC | arachidonic acid secretion lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity Bothrocophias hyoprora Calcium Direct protein sequencing Disulfide bond Hydrolase Metal-binding Secreted DLMQFETLIM DLMQFETLIMKSGVWYYGSYGCYCGSGGQFRPQDASDRCCFVHDCCYGKNGDIVCGGDDPCKKQICECDRVAATCFRDNKVTYDNKYWFFPAKFPPQNCKEESEPC |
arachidonic acid secretion lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity toxin activity | Bothrocophias hyoprora | Calcium Direct protein sequencing Disulfide bond Hydrolase Metal-binding Myotoxin Secreted Toxin | NLLQFNKMIL | NLLQFNKMILKETGKNAIPFYAFYGCYCGWGGRGKPKDKTDDRCCFVHDCCYGKLTGCPKWDIYPYSLKSGYITCGKGTWCEEQICECDRAAAICFRENLDTYNKYGYMFYPDSRCKGPSEQC | arachidonic acid secretion lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Bothrocophias hyoprora Calcium Direct protein sequencing Disulfide bond Hydrolase Metal-binding Myotoxin Secreted Toxin NLLQFNKMIL NLLQFNKMILKETGKNAIPFYAFYGCYCGWGGRGKPKDKTDDRCCFVHDCCYGKLTGCPKWDIYPYSLKSGYITCGKGTWCEEQICECDRAAAICFRENLDTYNKYGYMFYPDSRCKGPSEQC |
arachidonic acid secretion lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity toxin activity | Bothrocophias hyoprora | Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Myotoxin Secreted Toxin | DLWEFGKMIL | DLWEFGKMILKETGKNPFPYYGAYGCYCGWGGRGKPKDKTDDRCCFVHDCCRYKKLTGCPKTNDRYSYSWKDLTIVCGEDDPCKELCECDKAAAVCFRENLGTYNKKYRYHLRSLCKKADKPC | arachidonic acid secretion lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Bothrocophias hyoprora Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Myotoxin Secreted Toxin DLWEFGKMIL DLWEFGKMILKETGKNPFPYYGAYGCYCGWGGRGKPKDKTDDRCCFVHDCCRYKKLTGCPKTNDRYSYSWKDLTIVCGEDDPCKELCECDKAAAVCFRENLGTYNKKYRYHLRSLCKKADKPC |
arachidonic acid secretion lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity toxin activity | Bothrops brazili | Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Lipid degradation Lipid metabolism Metal-binding Platelet aggregation inhibiting toxin Secreted Toxin | NLWQFEMLIM | NLWQFEMLIMKIALTSGFMFYSSYGCYCGWGGHGRPKDASDRCCFVHDCCYGKVTTCNPKFGVVVCGGDDPCKKQICECDRVAATCFRDNKYWFYGAKXCQEESDPC | arachidonic acid secretion lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Bothrops brazili Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Lipid degradation Lipid metabolism Metal-binding Platelet aggregation inhibiting toxin Secreted Toxin NLWQFEMLIM NLWQFEMLIMKIALTSGFMFYSSYGCYCGWGGHGRPKDASDRCCFVHDCCYGKVTTCNPKFGVVVCGGDDPCKKQICECDRVAATCFRDNKYWFYGAKXCQEESDPC |
arachidonic acid secretion lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity toxin activity | Bothrops brazili | Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Lipid degradation Lipid metabolism Metal-binding Platelet aggregation inhibiting toxin Secreted Toxin | NLWQFEMLIM | NLWQFEMLIMKIAKTSGFMFYSSYGCYCGWGGHGRPQDASDRCCFVHDCCYGKVTGVVVCGGDDPCKXQICECDRVAATCFRDNKYWFFPAK | arachidonic acid secretion lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Bothrops brazili Calcium Direct protein sequencing Disulfide bond Hemostasis impairing toxin Hydrolase Lipid degradation Lipid metabolism Metal-binding Platelet aggregation inhibiting toxin Secreted Toxin NLWQFEMLIM NLWQFEMLIMKIAKTSGFMFYSSYGCYCGWGGHGRPQDASDRCCFVHDCCYGKVTGVVVCGGDDPCKXQICECDRVAATCFRDNKYWFFPAK |
arachidonic acid secretion lipid catabolic process phospholipid metabolic process | extracellular region | calcium ion binding phospholipase A2 activity toxin activity | Bothrops bilineatus smaragdinus | Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Myotoxin Neurotoxin Presynaptic neurotoxin Secreted Toxin | HLLQFNKNAI | HLLQFNKNAIPFYAFYGCYCGWGGRCCFVHDCCYGKWDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC | arachidonic acid secretion lipid catabolic process phospholipid metabolic process extracellular region calcium ion binding phospholipase A2 activity toxin activity Bothrops bilineatus smaragdinus Calcium Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Metal-binding Myotoxin Neurotoxin Presynaptic neurotoxin Secreted Toxin HLLQFNKNAI HLLQFNKNAIPFYAFYGCYCGWGGRCCFVHDCCYGKWDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSETC |
propanediol catabolic process | bacterial microcompartment | 4 iron, 4 sulfur cluster binding metal ion binding | Citrobacter freundii | 3D-structure 4Fe-4S Bacterial microcompartment Iron Iron-sulfur Metal-binding Transport | MSQAIGILEL | MSQAIGILELTSIAKGMEAGDAMLKSANVNLLVSKTICPGKFLLMLGGDVGAVQQAIATGTSLAGDMLVDSLVLPNIHASVLPAISGLNSVDKRQAVGIVETWSVAACICAADRAVKASNVTLVRVHMAFGIGGKCYMVVAGDVSDVNNAVTVASESAGEKGLLVYRSVIPRPHESMWRQMVEG | propanediol catabolic process bacterial microcompartment 4 iron, 4 sulfur cluster binding metal ion binding Citrobacter freundii3D-structure 4Fe-4S Bacterial microcompartment Iron Iron-sulfur Metal-binding Transport MSQAIGILEL MSQAIGILELTSIAKGMEAGDAMLKSANVNLLVSKTICPGKFLLMLGGDVGAVQQAIATGTSLAGDMLVDSLVLPNIHASVLPAISGLNSVDKRQAVGIVETWSVAACICAADRAVKASNVTLVRVHMAFGIGGKCYMVVAGDVSDVNNAVTVASESAGEKGLLVYRSVIPRPHESMWRQMVEG |
perturbation of host cell cycle progression | extracellular region; host cell nucleus | protein-glutamine glutaminase activity toxin activity | Escherichia coli | 3D-structure Host nucleus Hydrolase Plasmid Secreted Toxin Virulence | MKDITLPPPT | MKDITLPPPTSASCLTGAISVNTEAVLSPMQHTSALHVRDFASLCSQNLKANVLLNSDDHEVPIHQKNPAAIMQNIDSNIKQMATDWGMSIEEVEVIIGREKGIVEPSCGVTANAIMKLFLDKDGFSYCFENEQTLSLEQLQERLSCMPECKSFVLRVNDGALGHAYIVDIPKGENSCRPAFLYQSDLGEGVTRKLRFEDWMTHKALTPILLDDICNYFSCMSQNKTDLEQIATLFDIDGNVKMLRKENIQYQKHDNFSFQLFEYDTDNIEKNIEIIKSLCS | perturbation of host cell cycle progression extracellular region; host cell nucleus protein-glutamine glutaminase activity toxin activity Escherichia coli3D-structure Host nucleus Hydrolase Plasmid Secreted Toxin Virulence MKDITLPPPT MKDITLPPPTSASCLTGAISVNTEAVLSPMQHTSALHVRDFASLCSQNLKANVLLNSDDHEVPIHQKNPAAIMQNIDSNIKQMATDWGMSIEEVEVIIGREKGIVEPSCGVTANAIMKLFLDKDGFSYCFENEQTLSLEQLQERLSCMPECKSFVLRVNDGALGHAYIVDIPKGENSCRPAFLYQSDLGEGVTRKLRFEDWMTHKALTPILLDDICNYFSCMSQNKTDLEQIATLFDIDGNVKMLRKENIQYQKHDNFSFQLFEYDTDNIEKNIEIIKSLCS |
establishment of competence for transformation isoprenoid biosynthetic process | plasma membrane | metal ion binding prenyltransferase activity | Bacillus spizizenii | Cell membrane Competence Magnesium Membrane Metal-binding Prenyltransferase Transferase | MKEIVHEKIQ | MKEIVHEKIQNLDLKEYLINFIDEKNHFSFGILSFKHYVALSGNRSSHILTLAGGIELLILAFDIFDDLEDEDNIEIKWMKIDPSLALNAATTLYTLGLETICSISNSAEFHRLTLKYALNAMQGQHEDLRNSPETEEECIQMMKQKAGSLTAMSAVLAAMLANGEFNQTIEDYAYKIGIIKQLENDYYGLVNDQRSDIRKKRKTLIYLFLNRKFNEASEKILKLINSHTSYHSFISDSSKFDELLFEAGLNQYVSMLIKLYEEEITASMNQLNINIKL | establishment of competence for transformation isoprenoid biosynthetic process plasma membrane metal ion binding prenyltransferase activity Bacillus spizizenii Cell membrane Competence Magnesium Membrane Metal-binding Prenyltransferase Transferase MKEIVHEKIQ MKEIVHEKIQNLDLKEYLINFIDEKNHFSFGILSFKHYVALSGNRSSHILTLAGGIELLILAFDIFDDLEDEDNIEIKWMKIDPSLALNAATTLYTLGLETICSISNSAEFHRLTLKYALNAMQGQHEDLRNSPETEEECIQMMKQKAGSLTAMSAVLAAMLANGEFNQTIEDYAYKIGIIKQLENDYYGLVNDQRSDIRKKRKTLIYLFLNRKFNEASEKILKLINSHTSYHSFISDSSKFDELLFEAGLNQYVSMLIKLYEEEITASMNQLNINIKL |
activation of innate immune response defense response to virus innate immune response positive regulation of peptidoglycan recognition protein signaling pathway positive regulation of type I interferon production | endoplasmic reticulum membrane | 3',2'-cyclic GMP-AMP binding cyclic-di-GMP binding | Drosophila eugracilis | 3D-structure Antiviral defense Endoplasmic reticulum Glycoprotein Immunity Innate immunity Membrane Nucleotide-binding Transmembrane Transmembrane helix | MIKEMAIANN | MIKEMAIANNADEVDNEVRAEKGRKCFYLKKMIGDYIGNTVRIVATVVLADFLQRLYRSVVEYVHCSKYYLPEDRLWTILRRSCTYSNKSRYLVMGFILIGFLRISVSGNYKDVVPTFKFLAYMPLYWIFSNLGHSTLTYSSWVRDSHGLDYAAGMASNYFHGYLKLSLPERKADGLLHRMNVYEDKYNVTFGIKRLIILIPDEMFINGVIQSRILEKATPLETQFINRAGVNRPFKHAVYRLAEKVNGKTYYFAMEGATPMLSFFEAMHSNFSATWQMKELKREIWLKFYTHLNELIKTWPETRNLVELIIYNSHDTKGDLVDVGEMLKSHMELKTKNIDEMIG | activation of innate immune response defense response to virus innate immune response positive regulation of peptidoglycan recognition protein signaling pathway positive regulation of type I interferon production endoplasmic reticulum membrane 3',2'-cyclic GMP-AMP binding cyclic-di-GMP binding Drosophila eugracilis 3D-structure Antiviral defense Endoplasmic reticulum Glycoprotein Immunity Innate immunity Membrane Nucleotide-binding Transmembrane Transmembrane helix MIKEMAIANN MIKEMAIANNADEVDNEVRAEKGRKCFYLKKMIGDYIGNTVRIVATVVLADFLQRLYRSVVEYVHCSKYYLPEDRLWTILRRSCTYSNKSRYLVMGFILIGFLRISVSGNYKDVVPTFKFLAYMPLYWIFSNLGHSTLTYSSWVRDSHGLDYAAGMASNYFHGYLKLSLPERKADGLLHRMNVYEDKYNVTFGIKRLIILIPDEMFINGVIQSRILEKATPLETQFINRAGVNRPFKHAVYRLAEKVNGKTYYFAMEGATPMLSFFEAMHSNFSATWQMKELKREIWLKFYTHLNELIKTWPETRNLVELIIYNSHDTKGDLVDVGEMLKSHMELKTKNIDEMIG |
defense response to bacterium | extracellular region; membrane; other organism cell membrane | toxin activity | Neoponera commutata | Antibiotic Antimicrobial Direct protein sequencing Membrane Secreted Target cell membrane Target membrane Toxin | AGTKEWLNKA | AGTKEWLNKAKDFIKEKGLGMLSAAANAALN | defense response to bacterium extracellular region; membrane; other organism cell membrane toxin activity Neoponera commutata Antibiotic Antimicrobial Direct protein sequencing Membrane Secreted Target cell membrane Target membrane Toxin AGTKEWLNKA AGTKEWLNKAKDFIKEKGLGMLSAAANAALN |
cyclic nucleotide biosynthetic process defense response to virus intracellular signal transduction | cytoplasm | adenylate cyclase activity metal ion binding nucleotide binding | Escherichia coli | Antiviral defense Cytoplasm Lyase Manganese Metal-binding Nucleotide-binding | MSFKDVTAKN | MSFKDVTAKNFKGLKNVSLKKSMAMEGHTLVGTEARLGDAFELCESFSTSPSNIIEYEYQEEIRPFFQKAGLNKHSIGTHPELTGLGVGMIYNQYTVTMFVDIRKSSRLSLLLPLEQVYVVKNRILQACIDIVRALDGYPHRLMGDALMAFFGRSDVSKEDAIADAINAASTLRLILMDYIFPSLNEDIGEQIDLGVRIGLDYGAEDEVVWGNFGLGSFCEVTALGLPVDMTAKLQQLADKNTAMLGQGILDYIDFPEEYTKPKVKSGEELKYIIPNITNKEGQPINRRIRLLNMARYQELLPFKLNDKKMASAILYPNQFNFECFVIEDNKEVLYNSVSRFLPKKRRLTFKLSIYPGPGIGDLKIIFCKRNHGQEAKDDLSEDYSISIEDNKLIRVKNADNLSLLRKDGCYVLTVPEETLFRGLHTMEVIVRGNHETLFYRNIIGVYIK | cyclic nucleotide biosynthetic process defense response to virus intracellular signal transduction cytoplasm adenylate cyclase activity metal ion binding nucleotide binding Escherichia coliAntiviral defense Cytoplasm Lyase Manganese Metal-binding Nucleotide-binding MSFKDVTAKN MSFKDVTAKNFKGLKNVSLKKSMAMEGHTLVGTEARLGDAFELCESFSTSPSNIIEYEYQEEIRPFFQKAGLNKHSIGTHPELTGLGVGMIYNQYTVTMFVDIRKSSRLSLLLPLEQVYVVKNRILQACIDIVRALDGYPHRLMGDALMAFFGRSDVSKEDAIADAINAASTLRLILMDYIFPSLNEDIGEQIDLGVRIGLDYGAEDEVVWGNFGLGSFCEVTALGLPVDMTAKLQQLADKNTAMLGQGILDYIDFPEEYTKPKVKSGEELKYIIPNITNKEGQPINRRIRLLNMARYQELLPFKLNDKKMASAILYPNQFNFECFVIEDNKEVLYNSVSRFLPKKRRLTFKLSIYPGPGIGDLKIIFCKRNHGQEAKDDLSEDYSISIEDNKLIRVKNADNLSLLRKDGCYVLTVPEETLFRGLHTMEVIVRGNHETLFYRNIIGVYIK |
apoptotic process defense response to bacterium killing of cells of another organism | extracellular region | nucleotide binding oxidoreductase activity toxin activity | Bothrops jararacussu | Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Nucleotide-binding Oxidoreductase Secreted Toxin | ADDRNPLEEC | ADDRNPLEECFRETDYEEFLEIARNGLSDTDNPKEGWYANLGPMRLNEFSQENENAWYFIKDPGVLDYPVKPSEVGKHDDIFAYEKRFDEIVGGMDKEVTVTYQTSEKFEPPLPPK | apoptotic process defense response to bacterium killing of cells of another organism extracellular region nucleotide binding oxidoreductase activity toxin activity Bothrops jararacussu Antibiotic Antimicrobial Apoptosis Cytolysis Direct protein sequencing Disulfide bond FAD Flavoprotein Glycoprotein Hemolysis Hemostasis impairing toxin Nucleotide-binding Oxidoreductase Secreted Toxin ADDRNPLEEC ADDRNPLEECFRETDYEEFLEIARNGLSDTDNPKEGWYANLGPMRLNEFSQENENAWYFIKDPGVLDYPVKPSEVGKHDDIFAYEKRFDEIVGGMDKEVTVTYQTSEKFEPPLPPK |
3'-UTR-mediated mRNA stabilization mRNA splicing, via spliceosome mRNA stabilization negative regulation of cell growth involved in cardiac muscle cell development negative regulation of cell population proliferation negative regulation of mRNA splicing, via spliceosome negative regulation of ribosomal large subunit export from nucleus negative regulation of transcription by RNA polymerase II negative regulation of vascular associated smooth muscle cell proliferation positive regulation of execution phase of apoptosis positive regulation of vascular associated smooth muscle cell apoptotic process regulation of vascular associated smooth muscle cell apoptotic process vascular associated smooth muscle cell apoptotic process vascular associated smooth muscle cell proliferation | nuclear speck; nucleolus; nucleus; protein-containing complex | identical protein binding miRNA binding RNA binding single-stranded RNA binding | Mus musculus | Alternative initiation Alternative splicing Nucleus Reference proteome | MKDEVVVVTG | MKDEVVVVTGLAAMEPLIVHRMIVERTAAGTMIIETWTTAHTHESMAVRRASMSMTTHLKSKVQRIPTRPPRAPRLSVGGGGGTGTVPLARQASPETATIGTRTIGPSKGRRRRRRMRRRRRRRPVTSSC | 3'-UTR-mediated mRNA stabilization mRNA splicing, via spliceosome mRNA stabilization negative regulation of cell growth involved in cardiac muscle cell development negative regulation of cell population proliferation negative regulation of mRNA splicing, via spliceosome negative regulation of ribosomal large subunit export from nucleus negative regulation of transcription by RNA polymerase II negative regulation of vascular associated smooth muscle cell proliferation positive regulation of execution phase of apoptosis positive regulation of vascular associated smooth muscle cell apoptotic process regulation of vascular associated smooth muscle cell apoptotic process vascular associated smooth muscle cell apoptotic process vascular associated smooth muscle cell proliferation nuclear speck; nucleolus; nucleus; protein-containing complex identical protein binding miRNA binding RNA binding single-stranded RNA binding Mus musculus Alternative initiation Alternative splicing Nucleus Reference proteome MKDEVVVVTG MKDEVVVVTGLAAMEPLIVHRMIVERTAAGTMIIETWTTAHTHESMAVRRASMSMTTHLKSKVQRIPTRPPRAPRLSVGGGGGTGTVPLARQASPETATIGTRTIGPSKGRRRRRRMRRRRRRRPVTSSC |
medium-chain fatty acid catabolic process triglyceride catabolic process | extracellular region | carboxylesterase activity cutinase activity triglyceride lipase activity | Amycolatopsis mediterranei | Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Secreted Serine esterase Signal | MSALTSQPTS | MSALTSQPTSSGSSEKIPRLRGWRAKAAGVVLAALALTTGVAAPAPAAANPYERGPDPTTASIEATSGSFATSTVTVSRLAVSGFGGGTIYYPTTTTAGTFGALSIAPGFTATQSSIAWLGPRLASQGFVVFTIDTLTTSDQPDSRGRQLLASLDYLTQQSSVRSRIDSTRLGVVGHSMGGGGTLEAARSRPTLQAAVPLTAWDLTKNWSTLQVPTLVVGAQSDTVAPVASHSIPFYTSLPSTLDRAYLELRGASHFAPNSPNTTIAKYTLSWLKRFIDNDTRYEQFLCPIPSTSLSISDYRGNCPHNG | medium-chain fatty acid catabolic process triglyceride catabolic process extracellular region carboxylesterase activity cutinase activity triglyceride lipase activity Amycolatopsis mediterranei Direct protein sequencing Disulfide bond Hydrolase Lipid degradation Lipid metabolism Secreted Serine esterase Signal MSALTSQPTS MSALTSQPTSSGSSEKIPRLRGWRAKAAGVVLAALALTTGVAAPAPAAANPYERGPDPTTASIEATSGSFATSTVTVSRLAVSGFGGGTIYYPTTTTAGTFGALSIAPGFTATQSSIAWLGPRLASQGFVVFTIDTLTTSDQPDSRGRQLLASLDYLTQQSSVRSRIDSTRLGVVGHSMGGGGTLEAARSRPTLQAAVPLTAWDLTKNWSTLQVPTLVVGAQSDTVAPVASHSIPFYTSLPSTLDRAYLELRGASHFAPNSPNTTIAKYTLSWLKRFIDNDTRYEQFLCPIPSTSLSISDYRGNCPHNG |
neuropeptide signaling pathway | extracellular region | hormone activity | Oncorhynchus keta | Acetylation Cleavage on pair of basic residues Direct protein sequencing Endorphin Hormone Secreted Signal | MVCAPWLLAV | MVCAPWLLAVVVVCVCNPGVGGQCWDSSHCKDLPSEDKILECTHLFRSGLQDESPEPRSAAQQSTEESLSLGILLAALTSGERALDADPEPHSDKRHSYSMEHFRWGKPIGHKRRPIKVYASSLEGGDSSEGTFPLQARRQLGSWEDEMVGALGNQGAKAQTKVVPRTLTVTGLQDKKDGSYRMGHFRWGSPTAIKRYGGFMKPYTKQSHKPLITLLKHITLKNEQ | neuropeptide signaling pathway extracellular region hormone activity Oncorhynchus keta Acetylation Cleavage on pair of basic residues Direct protein sequencing Endorphin Hormone Secreted Signal MVCAPWLLAV MVCAPWLLAVVVVCVCNPGVGGQCWDSSHCKDLPSEDKILECTHLFRSGLQDESPEPRSAAQQSTEESLSLGILLAALTSGERALDADPEPHSDKRHSYSMEHFRWGKPIGHKRRPIKVYASSLEGGDSSEGTFPLQARRQLGSWEDEMVGALGNQGAKAQTKVVPRTLTVTGLQDKKDGSYRMGHFRWGSPTAIKRYGGFMKPYTKQSHKPLITLLKHITLKNEQ |
adenohypophysis development B cell differentiation cell fate specification cell population proliferation determination of adult lifespan inositol trisphosphate biosynthetic process negative regulation of transcription by RNA polymerase II pituitary gland development positive regulation of cell population proliferation positive regulation of DNA-templated transcription positive regulation of inositol trisphosphate biosynthetic process positive regulation of multicellular organism growth positive regulation of transcription by RNA polymerase II regulation of DNA-templated transcription regulation of insulin-like growth factor receptor signaling pathway regulation of transcription by RNA polymerase II somatotropin secreting cell development somatotropin secreting cell differentiation | chromatin; cytosol; nucleoplasm; nucleus | chromatin binding DNA binding DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific lncRNA binding RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II-specific DNA-binding transcription factor binding sequence-specific DNA binding sequence-specific double-stranded DNA binding | Rattus norvegicus | 3D-structure Activator Alternative splicing DNA-binding Homeobox Nucleus Reference proteome Transcription Transcription regulation | MSCQPFTSAD | MSCQPFTSADTFIPLNSDASAALPLRMHHSAAEGLPASNHATNVMSTATGLHYSVPSCHYGNQPSTYGVMAGTLTPCLYKFPDHTLSHGFPPLHQPLLAEDPTASEFKQELRRKSKLVEEPIDMDSPEIRELEQFANEFKVRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACKLKAILSKWLEEAEQVGALYNEKVGANERKRKRRTTISIAAKDALERHFGEHSKPSSQEIMRMAEELNLEKEVVRVWFCNRRQREKRVKTSLNQSLFSISKEHLECR | adenohypophysis development B cell differentiation cell fate specification cell population proliferation determination of adult lifespan inositol trisphosphate biosynthetic process negative regulation of transcription by RNA polymerase II pituitary gland development positive regulation of cell population proliferation positive regulation of DNA-templated transcription positive regulation of inositol trisphosphate biosynthetic process positive regulation of multicellular organism growth positive regulation of transcription by RNA polymerase II regulation of DNA-templated transcription regulation of insulin-like growth factor receptor signaling pathway regulation of transcription by RNA polymerase II somatotropin secreting cell development somatotropin secreting cell differentiation chromatin; cytosol; nucleoplasm; nucleus chromatin binding DNA binding DNA-binding transcription activator activity, RNA polymerase II-specific DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific lncRNA binding RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II-specific DNA-binding transcription factor binding sequence-specific DNA binding sequence-specific double-stranded DNA binding Rattus norvegicus 3D-structure Activator Alternative splicing DNA-binding Homeobox Nucleus Reference proteome Transcription Transcription regulation MSCQPFTSAD MSCQPFTSADTFIPLNSDASAALPLRMHHSAAEGLPASNHATNVMSTATGLHYSVPSCHYGNQPSTYGVMAGTLTPCLYKFPDHTLSHGFPPLHQPLLAEDPTASEFKQELRRKSKLVEEPIDMDSPEIRELEQFANEFKVRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACKLKAILSKWLEEAEQVGALYNEKVGANERKRKRRTTISIAAKDALERHFGEHSKPSSQEIMRMAEELNLEKEVVRVWFCNRRQREKRVKTSLNQSLFSISKEHLECR |
anterior/posterior pattern specification negative regulation of transcription by RNA polymerase II nematode male tail mating organ morphogenesis neuroblast migration positive regulation of epithelial cell proliferation positive regulation of mesodermal cell fate specification positive regulation of transcription by RNA polymerase II regulation of cell fate specification regulation of cell migration | nucleoplasm; nucleus; RNA polymerase II transcription regulator complex | DNA-binding transcription factor activity, RNA polymerase II-specific RNA polymerase II cis-regulatory region sequence-specific DNA binding | Caenorhabditis elegans | Developmental protein DNA-binding Homeobox Nucleus Reference proteome Repressor Transcription Transcription regulation | MSMYPGWTGD | MSMYPGWTGDDSYWAGAGTTASSQSASSGTSASASSSAAAAAAANNLKTYELYNHTYMNNMKHMLAAGWMDNSSNPFAYNPLQATSANFGETRTSMPAISQPVFPWMKMGGAKGGESKRTRQTYSRSQTLELEKEFHYHKYLTRKRRQEISETLHLTERQVKIWFQNRRMKHKKEAKGEGGSNESDEESNQDEQNEQHSS | anterior/posterior pattern specification negative regulation of transcription by RNA polymerase II nematode male tail mating organ morphogenesis neuroblast migration positive regulation of epithelial cell proliferation positive regulation of mesodermal cell fate specification positive regulation of transcription by RNA polymerase II regulation of cell fate specification regulation of cell migration nucleoplasm; nucleus; RNA polymerase II transcription regulator complex DNA-binding transcription factor activity, RNA polymerase II-specific RNA polymerase II cis-regulatory region sequence-specific DNA binding Caenorhabditis elegansDevelopmental protein DNA-binding Homeobox Nucleus Reference proteome Repressor Transcription Transcription regulation MSMYPGWTGD MSMYPGWTGDDSYWAGAGTTASSQSASSGTSASASSSAAAAAAANNLKTYELYNHTYMNNMKHMLAAGWMDNSSNPFAYNPLQATSANFGETRTSMPAISQPVFPWMKMGGAKGGESKRTRQTYSRSQTLELEKEFHYHKYLTRKRRQEISETLHLTERQVKIWFQNRRMKHKKEAKGEGGSNESDEESNQDEQNEQHSS |
chloride transmembrane transport gamma-aminobutyric acid signaling pathway inhibitory synapse assembly regulation of postsynaptic membrane potential synaptic transmission, GABAergic | chloride channel complex; cytoplasmic vesicle membrane; dendrite membrane; GABA-A receptor complex; neuron projection; postsynapse; postsynaptic membrane; synapse | GABA-A receptor activity GABA-gated chloride ion channel activity inhibitory extracellular ligand-gated monoatomic ion channel activity | Bos taurus | Cell membrane Cell projection Chloride Chloride channel Cytoplasmic vesicle Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport | MKTKLNSSNM | MKTKLNSSNMQLLLFVFLAWDPARLVLANIQEDEAKNNITIFTRILDRLLDGYDNRLRPGLGDSITEVFTNIYVTSFGPVSDTDMEYTIDVFFRQKWKDERLKFKGPMNILRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRIQDDGTLLYTMRLTVQAECPMHLEDFPMDAHSCPLKFGSYAYTTSEVTYIWTYNASDSVQVAPDGSRLNQYDLPGQSIGKETIKSSTGEYTVMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKSVVNDKKKEKASVMIQNNAYAVAVANYAPNLSKDPVLSTISKSATTPEPNKKPENKPAEAKKTFNSVSKIDRMSRIVFPVLFGTFNLVYWATYLNREPVLGVSP | chloride transmembrane transport gamma-aminobutyric acid signaling pathway inhibitory synapse assembly regulation of postsynaptic membrane potential synaptic transmission, GABAergic chloride channel complex; cytoplasmic vesicle membrane; dendrite membrane; GABA-A receptor complex; neuron projection; postsynapse; postsynaptic membrane; synapse GABA-A receptor activity GABA-gated chloride ion channel activity inhibitory extracellular ligand-gated monoatomic ion channel activity Bos taurus Cell membrane Cell projection Chloride Chloride channel Cytoplasmic vesicle Disulfide bond Glycoprotein Ion channel Ion transport Ligand-gated ion channel Membrane Postsynaptic cell membrane Receptor Reference proteome Signal Synapse Transmembrane Transmembrane helix Transport MKTKLNSSNM MKTKLNSSNMQLLLFVFLAWDPARLVLANIQEDEAKNNITIFTRILDRLLDGYDNRLRPGLGDSITEVFTNIYVTSFGPVSDTDMEYTIDVFFRQKWKDERLKFKGPMNILRLNNLMASKIWTPDTFFHNGKKSVAHNMTMPNKLLRIQDDGTLLYTMRLTVQAECPMHLEDFPMDAHSCPLKFGSYAYTTSEVTYIWTYNASDSVQVAPDGSRLNQYDLPGQSIGKETIKSSTGEYTVMTAHFHLKRKIGYFVIQTYLPCIMTVILSQVSFWLNRESVPARTVFGVTTVLTMTTLSISARNSLPKVAYATAMDWFIAVCYAFVFSALIEFATVNYFTKRGWAWDGKSVVNDKKKEKASVMIQNNAYAVAVANYAPNLSKDPVLSTISKSATTPEPNKKPENKPAEAKKTFNSVSKIDRMSRIVFPVLFGTFNLVYWATYLNREPVLGVSP |
autolysis conidium formation positive regulation of conidium formation regulation of secondary metabolite biosynthetic process regulation of sterigmatocystin biosynthetic process regulation of transcription by RNA polymerase II response to starvation sporocarp development involved in asexual reproduction sporulation resulting in formation of a cellular spore sterigmatocystin biosynthetic process | nucleus | cis-regulatory region sequence-specific DNA binding DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific metal ion binding | Emericella nidulans | Activator Conidiation DNA-binding Metal-binding Nucleus Reference proteome Repeat Sporulation Transcription Transcription regulation Zinc Zinc-finger | MRNQSSLSDR | MRNQSSLSDRLTVEVDCSSLGSNECPSMTSSFSPLESPTPTPTSIYSQGSLESPGWHGAGSLPNNTYERTPGSASMRSAFRLAGMASTESLGLPYGSMEGQERMPMPDFLSGYDENIEQLWMPSEAPKSYDHVAQGLAYHQGMHQYPTMARNTNNNYRHQAAAYLPESTTNPCLSRSIFHQPERVPSSMSSSMSMNNMLPWMNLGDSIAPQTIAPSQVGPVTPPPSYTDFPTSLSAFKQHSPTTPIRSCSLGTGSGADTPLSRLSGGPCEYMDDFQPSPVYRDGFQRPHRVASRKMLRRQTSKQNLMLENLPQVIKQVQFKCKEPGCNGRFKRQEHLKRHMKSHSKEKPHVCWVPGCHRAFSRSDNLNAHYTKTHSKRGGRNRYVATLDENSPDYDPEFRGQLTPDGRPIYGSKLDDPIPGAGDMSLDGWDE | autolysis conidium formation positive regulation of conidium formation regulation of secondary metabolite biosynthetic process regulation of sterigmatocystin biosynthetic process regulation of transcription by RNA polymerase II response to starvation sporocarp development involved in asexual reproduction sporulation resulting in formation of a cellular spore sterigmatocystin biosynthetic process nucleus cis-regulatory region sequence-specific DNA binding DNA-binding transcription factor activity DNA-binding transcription factor activity, RNA polymerase II-specific metal ion binding Emericella nidulans Activator Conidiation DNA-binding Metal-binding Nucleus Reference proteome Repeat Sporulation Transcription Transcription regulation Zinc Zinc-finger MRNQSSLSDR MRNQSSLSDRLTVEVDCSSLGSNECPSMTSSFSPLESPTPTPTSIYSQGSLESPGWHGAGSLPNNTYERTPGSASMRSAFRLAGMASTESLGLPYGSMEGQERMPMPDFLSGYDENIEQLWMPSEAPKSYDHVAQGLAYHQGMHQYPTMARNTNNNYRHQAAAYLPESTTNPCLSRSIFHQPERVPSSMSSSMSMNNMLPWMNLGDSIAPQTIAPSQVGPVTPPPSYTDFPTSLSAFKQHSPTTPIRSCSLGTGSGADTPLSRLSGGPCEYMDDFQPSPVYRDGFQRPHRVASRKMLRRQTSKQNLMLENLPQVIKQVQFKCKEPGCNGRFKRQEHLKRHMKSHSKEKPHVCWVPGCHRAFSRSDNLNAHYTKTHSKRGGRNRYVATLDENSPDYDPEFRGQLTPDGRPIYGSKLDDPIPGAGDMSLDGWDE |
regulation of transcription by RNA polymerase II | nucleus | DNA-binding transcription factor activity, RNA polymerase II-specific metal ion binding RNA polymerase II cis-regulatory region sequence-specific DNA binding | Homo sapiens | DNA-binding Isopeptide bond Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Transcription Transcription regulation Ubl conjugation Zinc Zinc-finger | MAIPKHSLSP | MAIPKHSLSPVPWEEDSFLQVKVEEEEEASLSQGGESSHDHIAHSEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLVEDLTQVLDKRGWDPGAEPTEASCKQSDLGESEPSNVTETLMGGVSLGPAFVKACEPEGSSERSGLSGEIWTKSVTQQIHFKKTSGPYKDVPTDQRGRESGASRNSSSAWPNLTSQEKPPSEDKFDLVDAYGTEPPYTYSGKRSSKCRECRKMFQSASALEAHQKTHSRKTPYACSECGKAFSRSTHLAQHQVVHTGAKPHECKECGKAFSRVTHLTQHQRIHTGEKPYKCGECGKTFSRSTHLTQHQRVHTGERPYECDACGKAFSQSTHLTQHQRIHTGEKPYKCDACGRAFSDCSALIRHLRIHSGEKPYQCKVCPKAFAQSSSLIEHQRIHTGEKPYKCSDCGKAFSRSSALMVHLRIHITVLQ | regulation of transcription by RNA polymerase II nucleus DNA-binding transcription factor activity, RNA polymerase II-specific metal ion binding RNA polymerase II cis-regulatory region sequence-specific DNA binding Homo sapiens DNA-binding Isopeptide bond Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Transcription Transcription regulation Ubl conjugation Zinc Zinc-finger MAIPKHSLSP MAIPKHSLSPVPWEEDSFLQVKVEEEEEASLSQGGESSHDHIAHSEAARLRFRHFRYEEASGPHEALAHLRALCCQWLQPEAHSKEQILELLVLEQFLGALPPEIQAWVGAQSPKSGEEAAVLVEDLTQVLDKRGWDPGAEPTEASCKQSDLGESEPSNVTETLMGGVSLGPAFVKACEPEGSSERSGLSGEIWTKSVTQQIHFKKTSGPYKDVPTDQRGRESGASRNSSSAWPNLTSQEKPPSEDKFDLVDAYGTEPPYTYSGKRSSKCRECRKMFQSASALEAHQKTHSRKTPYACSECGKAFSRSTHLAQHQVVHTGAKPHECKECGKAFSRVTHLTQHQRIHTGEKPYKCGECGKTFSRSTHLTQHQRVHTGERPYECDACGKAFSQSTHLTQHQRIHTGEKPYKCDACGRAFSDCSALIRHLRIHSGEKPYQCKVCPKAFAQSSSLIEHQRIHTGEKPYKCSDCGKAFSRSSALMVHLRIHITVLQ |
positive regulation of DNA-templated transcription regulation of transcription by RNA polymerase II telomere maintenance via telomere lengthening | chromosome, telomeric region; nucleus | DNA-binding transcription factor activity double-stranded telomeric DNA binding identical protein binding metal ion binding RNA polymerase II cis-regulatory region sequence-specific DNA binding transcription cis-regulatory region binding | Homo sapiens | 3D-structure Activator Chromosome DNA-binding Isopeptide bond Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Telomere Transcription Transcription regulation Ubl conjugation Zinc Zinc-finger | MDGSFVQHSV | MDGSFVQHSVRVLQELNKQREKGQYCDATLDVGGLVFKAHWSVLACCSHFFQSLYGDGSGGSVVLPAGFAEIFGLLLDFFYTGHLALTSGNRDQVLLAARELRVPEAVELCQSFKPKTSVGQAAGGQSGLGPPASQNVNSHVKEPAGLEEEEVSRTLGLVPRDQEPRGSHSPQRPQLHSPAQSEGPSSLCGKLKQALKPCPLEDKKPEDCKVPPRPLEAEGAQLQGGSNEWEVVVQVEDDGDGDYMSEPEAVLTRRKSNVIRKPCAAEPALSAGSLAAEPAENRKGTAVPVECPTCHKKFLSKYYLKVHNRKHTGEKPFECPKCGKCYFRKENLLEHEARNCMNRSEQVFTCSVCQETFRRRMELRVHMVSHTGEMPYKCSSCSQQFMQKKDLQSHMIKLHGAPKPHACPTCAKCFLSRTELQLHEAFKHRGEKLFVCEECGHRASSRNGLQMHIKAKHRNERPHVCEFCSHAFTQKANLNMHLRTHTGEKPFQCHLCGKTFRTQASLDKHNRTHTGERPFSCEFCEQRFTEKGPLLRHVASRHQEGRPHFCQICGKTFKAVEQLRVHVRRHKGVRKFECTECGYKFTRQAHLRRHMEIHDRVENYNPRQRKLRNLIIEDEKMVVVALQPPAELEVGSAEVIVESLAQGGLASQLPGQRLCAEESFTGPGVLEPSLIITAAVPEDCDT | positive regulation of DNA-templated transcription regulation of transcription by RNA polymerase II telomere maintenance via telomere lengthening chromosome, telomeric region; nucleus DNA-binding transcription factor activity double-stranded telomeric DNA binding identical protein binding metal ion binding RNA polymerase II cis-regulatory region sequence-specific DNA binding transcription cis-regulatory region binding Homo sapiens 3D-structure Activator Chromosome DNA-binding Isopeptide bond Metal-binding Nucleus Phosphoprotein Reference proteome Repeat Telomere Transcription Transcription regulation Ubl conjugation Zinc Zinc-finger MDGSFVQHSV MDGSFVQHSVRVLQELNKQREKGQYCDATLDVGGLVFKAHWSVLACCSHFFQSLYGDGSGGSVVLPAGFAEIFGLLLDFFYTGHLALTSGNRDQVLLAARELRVPEAVELCQSFKPKTSVGQAAGGQSGLGPPASQNVNSHVKEPAGLEEEEVSRTLGLVPRDQEPRGSHSPQRPQLHSPAQSEGPSSLCGKLKQALKPCPLEDKKPEDCKVPPRPLEAEGAQLQGGSNEWEVVVQVEDDGDGDYMSEPEAVLTRRKSNVIRKPCAAEPALSAGSLAAEPAENRKGTAVPVECPTCHKKFLSKYYLKVHNRKHTGEKPFECPKCGKCYFRKENLLEHEARNCMNRSEQVFTCSVCQETFRRRMELRVHMVSHTGEMPYKCSSCSQQFMQKKDLQSHMIKLHGAPKPHACPTCAKCFLSRTELQLHEAFKHRGEKLFVCEECGHRASSRNGLQMHIKAKHRNERPHVCEFCSHAFTQKANLNMHLRTHTGEKPFQCHLCGKTFRTQASLDKHNRTHTGERPFSCEFCEQRFTEKGPLLRHVASRHQEGRPHFCQICGKTFKAVEQLRVHVRRHKGVRKFECTECGYKFTRQAHLRRHMEIHDRVENYNPRQRKLRNLIIEDEKMVVVALQPPAELEVGSAEVIVESLAQGGLASQLPGQRLCAEESFTGPGVLEPSLIITAAVPEDCDT |
negative regulation of translation negative regulation of translation in response to stress | cytoplasm; cytoplasmic stress granule; nucleolus; nucleus; P-body; ribonucleoprotein complex | eukaryotic initiation factor 4G binding mRNA binding | Saccharomyces cerevisiae | Acetylation Cytoplasm Methylation Nucleus Phosphoprotein Reference proteome Repeat RNA-binding Stress response | MSAEIEEATN | MSAEIEEATNAVNNLSINDSEQQPRAPTHKTVIDPEDTIFIGNVAHECTEDDLKQLFVEEFGDEVSVEIPIKEHTDGHIPASKHALVKFPTKIDFDNIKENYDTKVVKDREIHIKRARTPGQMQRGGFRGRGGFRGRGGFRGGFRGGYRGGFRGRGNFRGRGGARGGFNGQKREKIPLDQMERSKDTLYINNVPFKATKEEVAEFFGTDADSISLPMRKMRDQHTGRIFTSDSANRGMAFVTFSGENVDIEAKAEEFKGKVFGDRELTVDVAVIRPENDEEEIEQETGSEEKQE | negative regulation of translation negative regulation of translation in response to stress cytoplasm; cytoplasmic stress granule; nucleolus; nucleus; P-body; ribonucleoprotein complex eukaryotic initiation factor 4G binding mRNA binding Saccharomyces cerevisiae Acetylation Cytoplasm Methylation Nucleus Phosphoprotein Reference proteome Repeat RNA-binding Stress response MSAEIEEATN MSAEIEEATNAVNNLSINDSEQQPRAPTHKTVIDPEDTIFIGNVAHECTEDDLKQLFVEEFGDEVSVEIPIKEHTDGHIPASKHALVKFPTKIDFDNIKENYDTKVVKDREIHIKRARTPGQMQRGGFRGRGGFRGRGGFRGGFRGGYRGGFRGRGNFRGRGGARGGFNGQKREKIPLDQMERSKDTLYINNVPFKATKEEVAEFFGTDADSISLPMRKMRDQHTGRIFTSDSANRGMAFVTFSGENVDIEAKAEEFKGKVFGDRELTVDVAVIRPENDEEEIEQETGSEEKQE |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.