Biological Process stringlengths 7 1.01k | Cellular Component stringlengths 6 867 | Molecular Function stringlengths 11 871 | Organism stringlengths 8 73 | Keywords stringlengths 1 810 | Sequence 10 stringlengths 5 10 | Sequence stringlengths 5 1.02k | Combined stringlengths 136 3.91k |
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de novo' IMP biosynthetic process glutamine metabolic process purine nucleobase biosynthetic process purine nucleotide biosynthetic process | cytoplasm; cytosol | amidophosphoribosyltransferase activity glycosyltransferase activity guanosine tetraphosphate binding identical protein binding magnesium ion binding | Escherichia coli | 3D-structure Direct protein sequencing Glutamine amidotransferase Glycosyltransferase Magnesium Metal-binding Purine biosynthesis Reference proteome Transferase | MCGIVGIAGV | MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAHNGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEADNIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDENRTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIPIPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIRFPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAENPDIQQFECSVFNGVYVTKDVDQGYLDFLDTLRNDDAKAVQRQNEVENLEMHNEG | de novo' IMP biosynthetic process glutamine metabolic process purine nucleobase biosynthetic process purine nucleotide biosynthetic process cytoplasm; cytosol amidophosphoribosyltransferase activity glycosyltransferase activity guanosine tetraphosphate binding identical protein binding magnesium ion binding Escherichia coli 3D-structure Direct protein sequencing Glutamine amidotransferase Glycosyltransferase Magnesium Metal-binding Purine biosynthesis Reference proteome Transferase MCGIVGIAGV MCGIVGIAGVMPVNQSIYDALTVLQHRGQDAAGIITIDANNCFRLRKANGLVSDVFEARHMQRLQGNMGIGHVRYPTAGSSSASEAQPFYVNSPYGITLAHNGNLTNAHELRKKLFEEKRRHINTTSDSEILLNIFASELDNFRHYPLEADNIFAAIAATNRLIRGAYACVAMIIGHGMVAFRDPNGIRPLVLGKRDIDENRTEYMVASESVALDTLGFDFLRDVAPGEAIYITEEGQLFTRQCADNPVSNPCLFEYVYFARPDSFIDKISVYSARVNMGTKLGEKIAREWEDLDIDVVIPIPETSCDIALEIARILGKPYRQGFVKNRYVGRTFIMPGQQLRRKSVRRKLNANRAEFRDKNVLLVDDSIVRGTTSEQIIEMAREAGAKKVYLASAAPEIRFPNVYGIDMPSATELIAHGREVDEIRQIIGADGLIFQDLNDLIDAVRAENPDIQQFECSVFNGVYVTKDVDQGYLDFLDTLRNDDAKAVQRQNEVENLEMHNEG |
de novo' IMP biosynthetic process | cytosol | 5-(carboxyamino)imidazole ribonucleotide mutase activity identical protein binding | Escherichia coli | 3D-structure Direct protein sequencing Isomerase Purine biosynthesis Reference proteome | MSSRNNPARV | MSSRNNPARVAIVMGSKSDWATMQFAAEIFEILNVPHHVEVVSAHRTPDKLFSFAESAEENGYQVIIAGAGGAAHLPGMIAAKTLVPVLGVPVQSAALSGVDSLYSIVQMPRGIPVGTLAIGKAGAANAALLAAQILATHDKELHQRLNDWRKAQTDEVLENPDPRGAA | de novo' IMP biosynthetic process cytosol 5-(carboxyamino)imidazole ribonucleotide mutase activity identical protein binding Escherichia coli 3D-structure Direct protein sequencing Isomerase Purine biosynthesis Reference proteome MSSRNNPARV MSSRNNPARVAIVMGSKSDWATMQFAAEIFEILNVPHHVEVVSAHRTPDKLFSFAESAEENGYQVIIAGAGGAAHLPGMIAAKTLVPVLGVPVQSAALSGVDSLYSIVQMPRGIPVGTLAIGKAGAANAALLAAQILATHDKELHQRLNDWRKAQTDEVLENPDPRGAA |
guanosine tetraphosphate biosynthetic process guanosine tetraphosphate metabolic process nucleobase-containing small molecule interconversion phosphorylation response to starvation | cytosol | GTP diphosphokinase activity guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity kinase activity | Escherichia coli | Cytoplasm Hydrolase Kinase Manganese Reference proteome Transferase | MYLFESLNQL | MYLFESLNQLIQTYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMKLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKFRDKKEAQAENFRKMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRYRVIKEVVKAARGNRKEMIQKILSEIEGRLQEAGIPCRVSGREKHLYSIYCKMVLKEQRFHSIMDIYAFRVIVNDSDTCYRVLGQMHSLYKPRPGRVKDYIAIPKANGYQSLHTSMIGPHGVPVEVQIRTEDMDQMAEMGVAAHWAYKEHGETSTTAQIRAQRWMQSLLELQQSAGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGHACVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAAWLNFVVSSKARAKIRQLLKNLKRDDSVSLGRRLLNHALGGSRKLNEIPQENIQRELDRMKLATLDDLLAEIGLGNAMSVVVAKNLQHGDASIPPATQSHGHLPIKGADGVLITFAKCCRPIPGDPIIAHVSPGKGLVIHHESCRNIRGYQKEPEKFMAVEWDKETAQEFITEIKVEMFNHQGALANLTAAINTTTSNIQSLNTEEKDGRVYSAFIRLTARDRVHLANIMRKIRVMPDVIKVTRNRN | guanosine tetraphosphate biosynthetic process guanosine tetraphosphate metabolic process nucleobase-containing small molecule interconversion phosphorylation response to starvation cytosol GTP diphosphokinase activity guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity kinase activity Escherichia coli Cytoplasm Hydrolase Kinase Manganese Reference proteome Transferase MYLFESLNQL MYLFESLNQLIQTYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMKLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKFRDKKEAQAENFRKMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRYRVIKEVVKAARGNRKEMIQKILSEIEGRLQEAGIPCRVSGREKHLYSIYCKMVLKEQRFHSIMDIYAFRVIVNDSDTCYRVLGQMHSLYKPRPGRVKDYIAIPKANGYQSLHTSMIGPHGVPVEVQIRTEDMDQMAEMGVAAHWAYKEHGETSTTAQIRAQRWMQSLLELQQSAGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGHACVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAAWLNFVVSSKARAKIRQLLKNLKRDDSVSLGRRLLNHALGGSRKLNEIPQENIQRELDRMKLATLDDLLAEIGLGNAMSVVVAKNLQHGDASIPPATQSHGHLPIKGADGVLITFAKCCRPIPGDPIIAHVSPGKGLVIHHESCRNIRGYQKEPEKFMAVEWDKETAQEFITEIKVEMFNHQGALANLTAAINTTTSNIQSLNTEEKDGRVYSAFIRLTARDRVHLANIMRKIRVMPDVIKVTRNRN |
DNA-templated transcription termination | cytosol; membrane | ATP binding ATP hydrolysis activity ATP-dependent activity, acting on RNA helicase activity identical protein binding RNA binding | Escherichia coli | 3D-structure ATP-binding Direct protein sequencing Helicase Hydrolase Nucleotide-binding Reference proteome RNA-binding Transcription Transcription regulation Transcription termination | MNLTELKNTP | MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDDFFEMMKRS | DNA-templated transcription termination cytosol; membrane ATP binding ATP hydrolysis activity ATP-dependent activity, acting on RNA helicase activity identical protein binding RNA binding Escherichia coli 3D-structure ATP-binding Direct protein sequencing Helicase Hydrolase Nucleotide-binding Reference proteome RNA-binding Transcription Transcription regulation Transcription termination MNLTELKNTP MNLTELKNTPVSELITLGENMGLENLARMRKQDIIFAILKQHAKSGEDIFGDGVLEILQDGFGFLRSADSSYLAGPDDIYVSPSQIRRFNLRTGDTISGKIRPPKEGERYFALLKVNEVNFDKPENARNKILFENLTPLHANSRLRMERGNGSTEDLTARVLDLASPIGRGQRGLIVAPPKAGKTMLLQNIAQSIAYNHPDCVLMVLLIDERPEEVTEMQRLVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVIILLDSITRLARAYNTVVPASGKVLTGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNMELHLSRKIAEKRVFPAIDYNRSGTRKEELLTTQEELQKMWILRKIIHPMGEIDAMEFLINKLAMTKTNDDFFEMMKRS |
cytoplasmic translation response to antibiotic ribosomal large subunit assembly | cytoplasm; cytosol; cytosolic large ribosomal subunit | large ribosomal subunit rRNA binding structural constituent of ribosome | Escherichia coli | 3D-structure Acetylation Antibiotic resistance Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding | MSRVAKAPVV | MSRVAKAPVVVPAGVDVKINGQVITIKGKNGELTRTLNDAVEVKHADNTLTFGPRDGYADGWAQAGTARALLNSMVIGVTEGFTKKLQLVGVGYRAAVKGNVINLSLGFSHPVDHQLPAGITAECPTQTEIVLKGADKQVIGQVAADLRAYRRPEPYKGKGVRYADEVVRTKEAKKK | cytoplasmic translation response to antibiotic ribosomal large subunit assembly cytoplasm; cytosol; cytosolic large ribosomal subunit large ribosomal subunit rRNA binding structural constituent of ribosome Escherichia coli 3D-structure Acetylation Antibiotic resistance Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding MSRVAKAPVV MSRVAKAPVVVPAGVDVKINGQVITIKGKNGELTRTLNDAVEVKHADNTLTFGPRDGYADGWAQAGTARALLNSMVIGVTEGFTKKLQLVGVGYRAAVKGNVINLSLGFSHPVDHQLPAGITAECPTQTEIVLKGADKQVIGQVAADLRAYRRPEPYKGKGVRYADEVVRTKEAKKK |
cytoplasmic translation ribosomal small subunit assembly translation | cytoplasm; cytosolic small ribosomal subunit; small ribosomal subunit | rRNA binding structural constituent of ribosome tRNA binding | Escherichia coli | 3D-structure Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein | MAKQSMKARE | MAKQSMKAREVKRVALADKYFAKRAELKAIISDVNASDEDRWNAVLKLQTLPRDSSPSRQRNRCRQTGRPHGFLRKFGLSRIKVREAAMRGEIPGLKKASW | cytoplasmic translation ribosomal small subunit assembly translation cytoplasm; cytosolic small ribosomal subunit; small ribosomal subunit rRNA binding structural constituent of ribosome tRNA binding Escherichia coli 3D-structure Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein MAKQSMKARE MAKQSMKAREVKRVALADKYFAKRAELKAIISDVNASDEDRWNAVLKLQTLPRDSSPSRQRNRCRQTGRPHGFLRKFGLSRIKVREAAMRGEIPGLKKASW |
cytoplasmic translation response to antibiotic ribosomal small subunit assembly | cytoplasm; cytosolic small ribosomal subunit | molecular adaptor activity rRNA binding small ribosomal subunit rRNA binding structural constituent of ribosome zinc ion binding | Escherichia coli | 3D-structure Antibiotic resistance Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding | MTDKIRTLQG | MTDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL | cytoplasmic translation response to antibiotic ribosomal small subunit assembly cytoplasm; cytosolic small ribosomal subunit molecular adaptor activity rRNA binding small ribosomal subunit rRNA binding structural constituent of ribosome zinc ion binding Escherichia coli 3D-structure Antibiotic resistance Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding MTDKIRTLQG MTDKIRTLQGRVVSDKMEKSIVVAIERFVKHPIYGKFIKRTTKLHVHDENNECGIGDVVEIRECRPLSKTKSWTLVRVVEKAVL |
cytoplasmic translation negative regulation of cytoplasmic translation positive regulation of cytoplasmic translation ribosomal small subunit assembly RNA secondary structure unwinding translation | cytoplasm; cytosolic small ribosomal subunit; membrane | mRNA binding RNA binding single-stranded RNA binding structural constituent of ribosome | Escherichia coli | 3D-structure Acetylation Chaperone Cytoplasm Direct protein sequencing Phosphoprotein Reference proteome Repeat Repressor Ribonucleoprotein Ribosomal protein RNA-binding | MTESFAQLFE | MTESFAQLFEESLKEIETRPGSIVRGVVVAIDKDVVLVDAGLKSESAIPAEQFKNAQGELEIQVGDEVDVALDAVEDGFGETLLSREKAKRHEAWITLEKAYEDAETVTGVINGKVKGGFTVELNGIRAFLPGSLVDVRPVRDTLHLEGKELEFKVIKLDQKRNNVVVSRRAVIESENSAERDQLLENLQEGMEVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRVKHPSEIVNVGDEITVKVLKFDRERTRVSLGLKQLGEDPWVAIAKRYPEGTKLTGRVTNLTDYGCFVEIEEGVEGLVHVSEMDWTNKNIHPSKVVNVGDVVEVMVLDIDEERRRISLGLKQCKANPWQQFAETHNKGDRVEGKIKSITDFGIFIGLDGGIDGLVHLSDISWNVAGEEAVREYKKGDEIAAVVLQVDAERERISLGVKQLAEDPFNNWVALNKKGAIVTGKVTAVDAKGATVELADGVEGYLRASEASRDRVEDATLVLSVGDEVEAKFTGVDRKNRAISLSVRAKDEADEKDAIATVNKQEDANFSNNAMAEAFKAAKGE | cytoplasmic translation negative regulation of cytoplasmic translation positive regulation of cytoplasmic translation ribosomal small subunit assembly RNA secondary structure unwinding translation cytoplasm; cytosolic small ribosomal subunit; membrane mRNA binding RNA binding single-stranded RNA binding structural constituent of ribosome Escherichia coli 3D-structure Acetylation Chaperone Cytoplasm Direct protein sequencing Phosphoprotein Reference proteome Repeat Repressor Ribonucleoprotein Ribosomal protein RNA-binding MTESFAQLFE MTESFAQLFEESLKEIETRPGSIVRGVVVAIDKDVVLVDAGLKSESAIPAEQFKNAQGELEIQVGDEVDVALDAVEDGFGETLLSREKAKRHEAWITLEKAYEDAETVTGVINGKVKGGFTVELNGIRAFLPGSLVDVRPVRDTLHLEGKELEFKVIKLDQKRNNVVVSRRAVIESENSAERDQLLENLQEGMEVKGIVKNLTDYGAFVDLGGVDGLLHITDMAWKRVKHPSEIVNVGDEITVKVLKFDRERTRVSLGLKQLGEDPWVAIAKRYPEGTKLTGRVTNLTDYGCFVEIEEGVEGLVHVSEMDWTNKNIHPSKVVNVGDVVEVMVLDIDEERRRISLGLKQCKANPWQQFAETHNKGDRVEGKIKSITDFGIFIGLDGGIDGLVHLSDISWNVAGEEAVREYKKGDEIAAVVLQVDAERERISLGVKQLAEDPFNNWVALNKKGAIVTGKVTAVDAKGATVELADGVEGYLRASEASRDRVEDATLVLSVGDEVEAKFTGVDRKNRAISLSVRAKDEADEKDAIATVNKQEDANFSNNAMAEAFKAAKGE |
localization maintenance of unfolded protein protein folding protein localization protein targeting protein tetramerization protein transport protein transport by the Sec complex | cytosol | preprotein binding unfolded protein binding | Escherichia coli | 3D-structure Chaperone Cytoplasm Protein transport Reference proteome Translocation Transport | MSEQNNTEMT | MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGAYCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA | localization maintenance of unfolded protein protein folding protein localization protein targeting protein tetramerization protein transport protein transport by the Sec complex cytosol preprotein binding unfolded protein binding Escherichia coli 3D-structure Chaperone Cytoplasm Protein transport Reference proteome Translocation Transport MSEQNNTEMT MSEQNNTEMTFQIQRIYTKDISFEAPNAPHVFQKDWQPEVKLDLDTASSQLADDVYEVVLRVTVTASLGEETAFLCEVQQGGIFSIAGIEGTQMAHCLGAYCPNILFPYARECITSMVSRGTFPQLNLAPVNFDALFMNYLQQQAGEGTEEHQDA |
intracellular protein transmembrane transport protein insertion into membrane from inner side protein targeting protein transport protein transport by the Sec complex | cell envelope Sec protein transport complex; membrane; plasma membrane | protein-transporting ATPase activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport | MLNRYPLWKY | MLNRYPLWKYVMLIVVIVIGLLYALPNLFGEDPAVQITGARGVAASEQTLIQVQKTLQEEKITAKSVALEEGAILARFDSTDTQLRAREALMGVMGDKYVVALNLAPATPRWLAAIHAEPMKLGLDLRGGVHFLMEVDMDTALGKLQEQNIDSLRSDLREKGIPYTTVRKENNYGLSITFRDAKARDEAIAYLSKRHPDLVISSQGSNQLRAVMSDARLSEAREYAVQQNINILRNRVNQLGVAEPVVQRQGADRIVVELPGIQDTARAKEILGATATLEFRLVNTNVDQAAAASGRVPGDSEVKQTREGQPVVLYKRVILTGDHITDSTSSQDEYNQPQVNISLDSAGGNIMSNFTKDNIGKPMATLFVEYKDSGKKDANGRAVLVKQEEVINIANIQSRLGNSFRITGINNPNEARQLSLLLRAGALIAPIQIVEERTIGPTLGMQNIEQGLEACLAGLLVSILFMIIFYKKFGLIATSALIANLILIVGIMSLLPGATLSMPGIAGIVLTLAVAVDANVLINERIKEELSNGRTVQQAIDEGYRGAFSSIFDANITTLIKVIILYAVGTGAIKGFAITTGIGVATSMFTAIVGTRAIVNLLYGGKRVKKLSI | intracellular protein transmembrane transport protein insertion into membrane from inner side protein targeting protein transport protein transport by the Sec complex cell envelope Sec protein transport complex; membrane; plasma membrane protein-transporting ATPase activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport MLNRYPLWKY MLNRYPLWKYVMLIVVIVIGLLYALPNLFGEDPAVQITGARGVAASEQTLIQVQKTLQEEKITAKSVALEEGAILARFDSTDTQLRAREALMGVMGDKYVVALNLAPATPRWLAAIHAEPMKLGLDLRGGVHFLMEVDMDTALGKLQEQNIDSLRSDLREKGIPYTTVRKENNYGLSITFRDAKARDEAIAYLSKRHPDLVISSQGSNQLRAVMSDARLSEAREYAVQQNINILRNRVNQLGVAEPVVQRQGADRIVVELPGIQDTARAKEILGATATLEFRLVNTNVDQAAAASGRVPGDSEVKQTREGQPVVLYKRVILTGDHITDSTSSQDEYNQPQVNISLDSAGGNIMSNFTKDNIGKPMATLFVEYKDSGKKDANGRAVLVKQEEVINIANIQSRLGNSFRITGINNPNEARQLSLLLRAGALIAPIQIVEERTIGPTLGMQNIEQGLEACLAGLLVSILFMIIFYKKFGLIATSALIANLILIVGIMSLLPGATLSMPGIAGIVLTLAVAVDANVLINERIKEELSNGRTVQQAIDEGYRGAFSSIFDANITTLIKVIILYAVGTGAIKGFAITTGIGVATSMFTAIVGTRAIVNLLYGGKRVKKLSI |
intracellular protein transmembrane transport protein insertion into membrane from inner side protein targeting protein transport protein transport by the Sec complex | cell envelope Sec protein transport complex; membrane; plasma membrane | protein-transporting ATPase activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport | MAQEYTVEQL | MAQEYTVEQLNHGRKVYDFMRWDYWAFGISGLLLIAAIVIMGVRGFNWGLDFTGGTVIEITLEKPAEIDVMRDALQKAGFEEPMLQNFGSSHDIMVRMPPAEGETGGQVLGSQVLKVINESTNQNAAVKRIEFVGPSVGADLAQTGAMALMAALLSILVYVGFRFEWRLAAGVVIALAHDVIITLGILSLFHIEIDLTIVASLMSVIGYSLNDSIVVSDRIRENFRKIRRGTPYEIFNVSLTQTLHRTLITSGTTLMVILMLYLFGGPVLEGFSLTMLIGVSIGTASSIYVASALALKLGMKREHMLQQKVEKEGADQPSILP | intracellular protein transmembrane transport protein insertion into membrane from inner side protein targeting protein transport protein transport by the Sec complex cell envelope Sec protein transport complex; membrane; plasma membrane protein-transporting ATPase activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport MAQEYTVEQL MAQEYTVEQLNHGRKVYDFMRWDYWAFGISGLLLIAAIVIMGVRGFNWGLDFTGGTVIEITLEKPAEIDVMRDALQKAGFEEPMLQNFGSSHDIMVRMPPAEGETGGQVLGSQVLKVINESTNQNAAVKRIEFVGPSVGADLAQTGAMALMAALLSILVYVGFRFEWRLAAGVVIALAHDVIITLGILSLFHIEIDLTIVASLMSVIGYSLNDSIVVSDRIRENFRKIRRGTPYEIFNVSLTQTLHRTLITSGTTLMVILMLYLFGGPVLEGFSLTMLIGVSIGTASSIYVASALALKLGMKREHMLQQKVEKEGADQPSILP |
intracellular protein transmembrane transport intracellular protein transport protein insertion into membrane from inner side protein secretion protein transport by the Sec complex SRP-dependent cotranslational protein targeting to membrane, translocation | cell envelope Sec protein transport complex; membrane; plasma membrane | protein transmembrane transporter activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport | MSANTEAQGS | MSANTEAQGSGRGLEAMKWVVVVALLLVAIVGNYLYRDIMLPLRALAVVILIAAAGGVALLTTKGKATVAFAREARTEVRKVIWPTRQETLHTTLIVAAVTAVMSLILWGLDGILVRLVSFITGLRF | intracellular protein transmembrane transport intracellular protein transport protein insertion into membrane from inner side protein secretion protein transport by the Sec complex SRP-dependent cotranslational protein targeting to membrane, translocation cell envelope Sec protein transport complex; membrane; plasma membrane protein transmembrane transporter activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport MSANTEAQGS MSANTEAQGSGRGLEAMKWVVVVALLLVAIVGNYLYRDIMLPLRALAVVILIAAAGGVALLTTKGKATVAFAREARTEVRKVIWPTRQETLHTTLIVAAVTAVMSLILWGLDGILVRLVSFITGLRF |
intracellular protein transmembrane transport intracellular protein transport protein insertion into membrane from inner side protein secretion protein transport by the Sec complex SRP-dependent cotranslational protein targeting to membrane, translocation | cell envelope Sec protein transport complex; membrane; plasma membrane | protein transmembrane transporter activity protein-transporting ATPase activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Direct protein sequencing Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport | MYEALLVVFL | MYEALLVVFLIVAIGLVGLIMLQQGKGADMGASFGAGASATLFGSSGSGNFMTRMTALLATLFFIISLVLGNINSNKTNKGSEWENLSAPAKTEQTQPAAPAKPTSDIPN | intracellular protein transmembrane transport intracellular protein transport protein insertion into membrane from inner side protein secretion protein transport by the Sec complex SRP-dependent cotranslational protein targeting to membrane, translocation cell envelope Sec protein transport complex; membrane; plasma membrane protein transmembrane transporter activity protein-transporting ATPase activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Direct protein sequencing Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport MYEALLVVFL MYEALLVVFLIVAIGLVGLIMLQQGKGADMGASFGAGASATLFGSSGSGNFMTRMTALLATLFFIISLVLGNINSNKTNKGSEWENLSAPAKTEQTQPAAPAKPTSDIPN |
intracellular protein transmembrane transport intracellular protein transport protein insertion into membrane from inner side protein transport by the Sec complex SRP-dependent cotranslational protein targeting to membrane, translocation | cell envelope Sec protein transport complex; membrane; plasma membrane | protein transmembrane transporter activity signal sequence binding | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport | MAKQPGLDFQ | MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALYITFICLIPEFMRDAMKVPFYFGGTSLLIVVVVIMDFMAQVQTLMMSSQYESALKKANLKGYGR | intracellular protein transmembrane transport intracellular protein transport protein insertion into membrane from inner side protein transport by the Sec complex SRP-dependent cotranslational protein targeting to membrane, translocation cell envelope Sec protein transport complex; membrane; plasma membrane protein transmembrane transporter activity signal sequence binding Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Protein transport Reference proteome Translocation Transmembrane Transmembrane helix Transport MAKQPGLDFQ MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALYITFICLIPEFMRDAMKVPFYFGGTSLLIVVVVIMDFMAQVQTLMMSSQYESALKKANLKGYGR |
amino acid biosynthetic process dephosphorylation L-serine biosynthetic process | cytoplasm | L-phosphoserine phosphatase activity magnesium ion binding phosphatase activity | Escherichia coli | Amino-acid biosynthesis Hydrolase Magnesium Metal-binding Reference proteome Serine biosynthesis | MPNITWCDLP | MPNITWCDLPEDVSLWPGLPLSLSGDEVMPLDYHAGRSGWLLYGRGLDKQRLTQYQSKLGAAMVIVAAWCVEDYQVIRLAGSLTARATRLAHEAQLDVAPLGKIPHLRTPGLLVMDMDSTAIQIECIDEIAKLAGTGEMVAEVTERAMRGELDFTASLRSRVATLKGADANILQQVRENLPLMPGLTQLVLKLETLGWKVAIASGGFTFFAEYLRDKLRLTAVVANELEIMDGKFTGNVIGDIVDAQYKAKTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKAEVTIRHADLMGVFCILSGSLNQK | amino acid biosynthetic process dephosphorylation L-serine biosynthetic process cytoplasm L-phosphoserine phosphatase activity magnesium ion binding phosphatase activity Escherichia coli Amino-acid biosynthesis Hydrolase Magnesium Metal-binding Reference proteome Serine biosynthesis MPNITWCDLP MPNITWCDLPEDVSLWPGLPLSLSGDEVMPLDYHAGRSGWLLYGRGLDKQRLTQYQSKLGAAMVIVAAWCVEDYQVIRLAGSLTARATRLAHEAQLDVAPLGKIPHLRTPGLLVMDMDSTAIQIECIDEIAKLAGTGEMVAEVTERAMRGELDFTASLRSRVATLKGADANILQQVRENLPLMPGLTQLVLKLETLGWKVAIASGGFTFFAEYLRDKLRLTAVVANELEIMDGKFTGNVIGDIVDAQYKAKTLTRLAQEYEIPLAQTVAIGDGANDLPMIKAAGLGIAYHAKPKVNEKAEVTIRHADLMGVFCILSGSLNQK |
DNA recombination DNA-templated transcription DNA-templated transcription initiation regulation of DNA-templated transcription regulation of DNA-templated transcription initiation regulation of gene expression response to heat | cytosol; cytosolic DNA-directed RNA polymerase complex; invertasome; plasma membrane | bacterial-type RNA polymerase core enzyme binding core promoter sequence-specific DNA binding DNA binding DNA-binding transcription activator activity sigma factor activity site-specific recombinase activity | Escherichia coli | 3D-structure Cytoplasm DNA-binding Reference proteome Sigma factor Stress response Transcription Transcription regulation | MTDKMQSLAL | MTDKMQSLALAPVGNLDSYIRAANAWPMLSADEERALAEKLHYHGDLEAAKTLILSHLRFVVHIARNYAGYGLPQADLIQEGNIGLMKAVRRFNPEVGVRLVSFAVHWIKAEIHEYVLRNWRIVKVATTKAQRKLFFNLRKTKQRLGWFNQDEVEMVARELGVTSKDVREMESRMAAQDMTFDLSSDDDSDSQPMAPVLYLQDKSSNFADGIEDDNWEEQAANRLTDAMQGLDERSQDIIRARWLDEDNKSTLQELADRYGVSAERVRQLEKNAMKKLRAAIEA | DNA recombination DNA-templated transcription DNA-templated transcription initiation regulation of DNA-templated transcription regulation of DNA-templated transcription initiation regulation of gene expression response to heat cytosol; cytosolic DNA-directed RNA polymerase complex; invertasome; plasma membrane bacterial-type RNA polymerase core enzyme binding core promoter sequence-specific DNA binding DNA binding DNA-binding transcription activator activity sigma factor activity site-specific recombinase activity Escherichia coli 3D-structure Cytoplasm DNA-binding Reference proteome Sigma factor Stress response Transcription Transcription regulation MTDKMQSLAL MTDKMQSLALAPVGNLDSYIRAANAWPMLSADEERALAEKLHYHGDLEAAKTLILSHLRFVVHIARNYAGYGLPQADLIQEGNIGLMKAVRRFNPEVGVRLVSFAVHWIKAEIHEYVLRNWRIVKVATTKAQRKLFFNLRKTKQRLGWFNQDEVEMVARELGVTSKDVREMESRMAAQDMTFDLSSDDDSDSQPMAPVLYLQDKSSNFADGIEDDNWEEQAANRLTDAMQGLDERSQDIIRARWLDEDNKSTLQELADRYGVSAERVRQLEKNAMKKLRAAIEA |
cellular response to cell envelope stress DNA-templated transcription initiation negative regulation of DNA-templated transcription regulation of DNA-templated transcription regulation of DNA-templated transcription initiation response to osmotic stress response to temperature stimulus submerged biofilm formation | cytoplasm; cytosolic DNA-directed RNA polymerase complex; plasma membrane; sigma factor antagonist complex | DNA binding sigma factor activity | Escherichia coli | 3D-structure Cytoplasm Direct protein sequencing DNA-binding Reference proteome Sigma factor Stress response Transcription Transcription regulation | MSEQLTDQVL | MSEQLTDQVLVERVQKGDQKAFNLLVVRYQHKVASLVSRYVPSGDVPDVVQEAFIKAYRALDSFRGDSAFYTWLYRIAVNTAKNYLVAQGRRPPSSDVDAIEAENFESGGALKEISNPENLMLSEELRQIVFRTIESLPEDLRMAITLRELDGLSYEEIAAIMDCPVGTVRSRIFRAREAIDNKVQPLIRR | cellular response to cell envelope stress DNA-templated transcription initiation negative regulation of DNA-templated transcription regulation of DNA-templated transcription regulation of DNA-templated transcription initiation response to osmotic stress response to temperature stimulus submerged biofilm formation cytoplasm; cytosolic DNA-directed RNA polymerase complex; plasma membrane; sigma factor antagonist complex DNA binding sigma factor activity Escherichia coli 3D-structure Cytoplasm Direct protein sequencing DNA-binding Reference proteome Sigma factor Stress response Transcription Transcription regulation MSEQLTDQVL MSEQLTDQVLVERVQKGDQKAFNLLVVRYQHKVASLVSRYVPSGDVPDVVQEAFIKAYRALDSFRGDSAFYTWLYRIAVNTAKNYLVAQGRRPPSSDVDAIEAENFESGGALKEISNPENLMLSEELRQIVFRTIESLPEDLRMAITLRELDGLSYEEIAAIMDCPVGTVRSRIFRAREAIDNKVQPLIRR |
carbohydrate transport glucose-6-phosphate transport hexose phosphate transport phosphate ion transmembrane transport | plasma membrane | glucose 6-phosphate:inorganic phosphate antiporter activity hexose-phosphate:inorganic phosphate antiporter activity | Escherichia coli | Cell inner membrane Cell membrane Membrane Phosphate transport Reference proteome Sugar transport Transmembrane Transmembrane helix Transport | MLAFLNQVRK | MLAFLNQVRKPTLDLPLEVRRKMWFKPFMQSYLVVFIGYLTMYLIRKNFNIAQNDMISTYGLSMTQLGMIGLGFSITYGVGKTLVSYYADGKNTKQFLPFMLILSAICMLGFSASMGSGSVSLFLMIAFYALSGFFQSTGGSCSYSTITKWTPRRKRGTFLGFWNISHNLGGAGAAGVALFGANYLFDGHVIGMFIFPSIIALIVGFIGLRYGSDSPESYGLGKAEELFGEEISEEDKETESTDMTKWQIFVEYVLKNKVIWLLCFANIFLYVVRIGIDQWSTVYAFQELKLSKAVAIQGFTLFEAGALVGTLLWGWLSDLANGRRGLVACIALALIIATLGVYQHASNEYIYLASLFALGFLVFGPQLLIGVAAVGFVPKKAIGAADGIKGTFAYLIGDSFAKLGLGMIADGTPVFGLTGWAGTFAALDIAAIGCICLMAIVAVMEERKIRREKKIQQLTVA | carbohydrate transport glucose-6-phosphate transport hexose phosphate transport phosphate ion transmembrane transport plasma membrane glucose 6-phosphate:inorganic phosphate antiporter activity hexose-phosphate:inorganic phosphate antiporter activity Escherichia coli Cell inner membrane Cell membrane Membrane Phosphate transport Reference proteome Sugar transport Transmembrane Transmembrane helix Transport MLAFLNQVRK MLAFLNQVRKPTLDLPLEVRRKMWFKPFMQSYLVVFIGYLTMYLIRKNFNIAQNDMISTYGLSMTQLGMIGLGFSITYGVGKTLVSYYADGKNTKQFLPFMLILSAICMLGFSASMGSGSVSLFLMIAFYALSGFFQSTGGSCSYSTITKWTPRRKRGTFLGFWNISHNLGGAGAAGVALFGANYLFDGHVIGMFIFPSIIALIVGFIGLRYGSDSPESYGLGKAEELFGEEISEEDKETESTDMTKWQIFVEYVLKNKVIWLLCFANIFLYVVRIGIDQWSTVYAFQELKLSKAVAIQGFTLFEAGALVGTLLWGWLSDLANGRRGLVACIALALIIATLGVYQHASNEYIYLASLFALGFLVFGPQLLIGVAAVGFVPKKAIGAADGIKGTFAYLIGDSFAKLGLGMIADGTPVFGLTGWAGTFAALDIAAIGCICLMAIVAVMEERKIRREKKIQQLTVA |
cell wall organization peptidoglycan catabolic process | membrane; outer membrane-bounded periplasmic space; peptidoglycan-based cell wall | hydrolase activity, hydrolyzing O-glycosyl compounds lytic endotransglycosylase activity lytic transglycosylase activity | Escherichia coli | 3D-structure Cell wall biogenesis/degradation Direct protein sequencing Disulfide bond Lyase Periplasm Reference proteome Signal | MEKAKQVTWR | MEKAKQVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQPAVTVTNFVRANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGKSQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDFTRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVRMALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQNVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAYNDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATEWGRRY | cell wall organization peptidoglycan catabolic process membrane; outer membrane-bounded periplasmic space; peptidoglycan-based cell wall hydrolase activity, hydrolyzing O-glycosyl compounds lytic endotransglycosylase activity lytic transglycosylase activity Escherichia coli 3D-structure Cell wall biogenesis/degradation Direct protein sequencing Disulfide bond Lyase Periplasm Reference proteome Signal MEKAKQVTWR MEKAKQVTWRLLAAGVCLLTVSSVARADSLDEQRSRYAQIKQAWDNRQMDVVEQMMPGLKDYPLYPYLEYRQITDDLMNQPAVTVTNFVRANPTLPPARTLQSRFVNELARREDWRGLLAFSPEKPGTTEAQCNYYYAKWNTGQSEEAWQGAKELWLTGKSQPNACDKLFSVWRASGKQDPLAYLERIRLAMKAGNTGLVTVLAGQMPADYQTIASAIISLANNPNTVLTFARTTGATDFTRQMAAVAFASVARQDAENARLMIPSLAQAQQLNEDQIQELRDIVAWRLMGNDVTDEQAKWRDDAIMRSQSTSLIERRVRMALGTGDRRGLNTWLARLPMEAKEKDEWRYWQADLLLERGREAEAKEILHQLMQQRGFYPMVAAQRIGEEYELKIDKAPQNVDSALTQGPEMARVRELMYWNLDNTARSEWANLVKSKSKTEQAQLARYAFNNQWWDLSVQATIAGKLWDHLEERFPLAYNDLFKRYTSGKEIPQSYAMAIARQESAWNPKVKSPVGASGLMQIMPGTATHTVKMFSIPGYSSPGQLLDPETNINIGTSYLQYVYQQFGNNRIFSSAAYNAGPGRVRTWLGNSAGRIDAVAFVESIPFSETRGYVKNVLAYDAYYRYFMGDKPTLMSATEWGRRY |
removal of superoxide radicals superoxide metabolic process | outer membrane-bounded periplasmic space; periplasmic space | copper ion binding superoxide dismutase activity zinc ion binding | Escherichia coli | 3D-structure Antioxidant Copper Direct protein sequencing Disulfide bond Metal-binding Oxidoreductase Periplasm Reference proteome Signal Zinc | MKRFSLAILA | MKRFSLAILALVVATGAQAASEKVEMNLVTSQGVGQSIGSVTITETDKGLEFSPDLKALPPGEHGFHIHAKGSCQPATKDGKASAAESAGGHLDPQNTGKHEGPEGAGHLGDLPALVVNNDGKATDAVIAPRLKSLDEIKDKALMVHVGGDNMSDQPKPLGGGGERYACGVIK | removal of superoxide radicals superoxide metabolic process outer membrane-bounded periplasmic space; periplasmic space copper ion binding superoxide dismutase activity zinc ion binding Escherichia coli 3D-structure Antioxidant Copper Direct protein sequencing Disulfide bond Metal-binding Oxidoreductase Periplasm Reference proteome Signal Zinc MKRFSLAILA MKRFSLAILALVVATGAQAASEKVEMNLVTSQGVGQSIGSVTITETDKGLEFSPDLKALPPGEHGFHIHAKGSCQPATKDGKASAAESAGGHLDPQNTGKHEGPEGAGHLGDLPALVVNNDGKATDAVIAPRLKSLDEIKDKALMVHVGGDNMSDQPKPLGGGGERYACGVIK |
removal of superoxide radicals response to superoxide superoxide metabolic process | cytoplasm; cytosol; membrane | iron ion binding oxidoreductase activity superoxide dismutase activity | Escherichia coli | 3D-structure Acetylation Direct protein sequencing Iron Metal-binding Oxidoreductase Reference proteome | MSFELPALPY | MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA | removal of superoxide radicals response to superoxide superoxide metabolic process cytoplasm; cytosol; membrane iron ion binding oxidoreductase activity superoxide dismutase activity Escherichia coli 3D-structure Acetylation Direct protein sequencing Iron Metal-binding Oxidoreductase Reference proteome MSFELPALPY MSFELPALPYAKDALAPHISAETIEYHYGKHHQTYVTNLNNLIKGTAFEGKSLEEIIRSSEGGVFNNAAQVWNHTFYWNCLAPNAGGEPTGKVAEAIAASFGSFADFKAQFTDAAIKNFGSGWTWLVKNSDGKLAIVSTSNAGTPLTTDATPLLTVDVWEHAYYIDYRNARPGYLEHFWALVNWEFVAKNLAA |
protein targeting to membrane SRP-dependent cotranslational protein targeting to membrane | cytosol; ribonucleoprotein complex; signal recognition particle | 7S RNA binding ATP hydrolysis activity GTP binding GTPase activity | Escherichia coli | 3D-structure Cytoplasm GTP-binding Hydrolase Nucleotide-binding Reference proteome Ribonucleoprotein RNA-binding Signal recognition particle | MFDNLTDRLS | MFDNLTDRLSRTLRNISGRGRLTEDNVKDTLREVRMALLEADVALPVVREFINRVKEKAVGHEVNKSLTPGQEFVKIVRNELVAAMGEENQTLNLAAQPPAVVLMAGLQGAGKTTSVGKLGKFLREKHKKKVLVVSADVYRPAAIKQLETLAEQVGVDFFPSDVGQKPVDIVNAALKEAKLKFYDVLLVDTAGRLHVDEAMMDEIKQVHASINPVETLFVVDAMTGQDAANTAKAFNEALPLTGVVLTKVDGDARGGAALSIRHITGKPIKFLGVGEKTEALEPFHPDRIASRILGMGDVLSLIEDIESKVDRAQAEKLASKLKKGDGFDLNDFLEQLRQMKNMGGMASLMGKLPGMGQIPDNVKSQMDDKVLVRMEAIINSMTMKERAKPEIIKGSRKRRIAAGCGMQVQDVNRLLKQFDDMQRMMKKMKKGGMAKMMRSMKGMMPPGFPGR | protein targeting to membrane SRP-dependent cotranslational protein targeting to membrane cytosol; ribonucleoprotein complex; signal recognition particle 7S RNA binding ATP hydrolysis activity GTP binding GTPase activity Escherichia coli 3D-structure Cytoplasm GTP-binding Hydrolase Nucleotide-binding Reference proteome Ribonucleoprotein RNA-binding Signal recognition particle MFDNLTDRLS MFDNLTDRLSRTLRNISGRGRLTEDNVKDTLREVRMALLEADVALPVVREFINRVKEKAVGHEVNKSLTPGQEFVKIVRNELVAAMGEENQTLNLAAQPPAVVLMAGLQGAGKTTSVGKLGKFLREKHKKKVLVVSADVYRPAAIKQLETLAEQVGVDFFPSDVGQKPVDIVNAALKEAKLKFYDVLLVDTAGRLHVDEAMMDEIKQVHASINPVETLFVVDAMTGQDAANTAKAFNEALPLTGVVLTKVDGDARGGAALSIRHITGKPIKFLGVGEKTEALEPFHPDRIASRILGMGDVLSLIEDIESKVDRAQAEKLASKLKKGDGFDLNDFLEQLRQMKNMGGMASLMGKLPGMGQIPDNVKSQMDDKVLVRMEAIINSMTMKERAKPEIIKGSRKRRIAAGCGMQVQDVNRLLKQFDDMQRMMKKMKKGGMAKMMRSMKGMMPPGFPGR |
DNA-templated DNA replication mismatch repair positive regulation of catalytic activity recombinational repair SOS response | cytosol; nucleoid; replisome; single-stranded DNA-binding protein complex | enzyme activator activity identical protein binding single-stranded DNA binding | Escherichia coli | 3D-structure Direct protein sequencing DNA damage DNA recombination DNA repair DNA replication DNA-binding Phosphoprotein Reference proteome | MASRGVNKVI | MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKATGEMKEQTEWHRVVLFGKLAEVASEYLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQMLGGRQGGGAPAGGNIGGGQPQGGWGQPQQPQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFDDDIPF | DNA-templated DNA replication mismatch repair positive regulation of catalytic activity recombinational repair SOS response cytosol; nucleoid; replisome; single-stranded DNA-binding protein complex enzyme activator activity identical protein binding single-stranded DNA binding Escherichia coli 3D-structure Direct protein sequencing DNA damage DNA recombination DNA repair DNA replication DNA-binding Phosphoprotein Reference proteome MASRGVNKVI MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKATGEMKEQTEWHRVVLFGKLAEVASEYLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQMLGGRQGGGAPAGGNIGGGQPQGGWGQPQQPQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFDDDIPF |
amino acid transport serine transport threonine transport | plasma membrane | neutral L-amino acid transmembrane transporter activity neutral L-amino acid:sodium symporter activity | Escherichia coli | Amino-acid transport Cell inner membrane Cell membrane Direct protein sequencing Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport | MTTQRSPGLF | MTTQRSPGLFRRLAHGSLVKQILVGLVLGILLAWISKPAAEAVGLLGTLFVGALKAVAPILVLMLVMASIANHQHGQKTNIRPILFLYLLGTFSAALAAVVFSFAFPSTLHLSSSAGDISPPSGIVEVMRGLVMSMVSNPIDALLKGNYIGILVWAIGLGFALRHGNETTKNLVNDMSNAVTFMVKLVIRFAPIGIFGLVSSTLATTGFSTLWGYAQLLVVLVGCMLLVALVVNPLLVWWKIRRNPFPLVLLCLRESGVYAFFTRSSAANIPVNMALCEKLNLDRDTYSVSIPLGATINMAGAAITITVLTLAAVNTLGIPVDLPTALLLSVVASLCACGASGVAGGSLLLIPLACNMFGISNDIAMQVVAVGFIIGVLQDSCETALNSSTDVLFTAAACQAEDDRLANSALRN | amino acid transport serine transport threonine transport plasma membrane neutral L-amino acid transmembrane transporter activity neutral L-amino acid:sodium symporter activity Escherichia coli Amino-acid transport Cell inner membrane Cell membrane Direct protein sequencing Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport MTTQRSPGLF MTTQRSPGLFRRLAHGSLVKQILVGLVLGILLAWISKPAAEAVGLLGTLFVGALKAVAPILVLMLVMASIANHQHGQKTNIRPILFLYLLGTFSAALAAVVFSFAFPSTLHLSSSAGDISPPSGIVEVMRGLVMSMVSNPIDALLKGNYIGILVWAIGLGFALRHGNETTKNLVNDMSNAVTFMVKLVIRFAPIGIFGLVSSTLATTGFSTLWGYAQLLVVLVGCMLLVALVVNPLLVWWKIRRNPFPLVLLCLRESGVYAFFTRSSAANIPVNMALCEKLNLDRDTYSVSIPLGATINMAGAAITITVLTLAAVNTLGIPVDLPTALLLSVVASLCACGASGVAGGSLLLIPLACNMFGISNDIAMQVVAVGFIIGVLQDSCETALNSSTDVLFTAAACQAEDDRLANSALRN |
tricarboxylic acid cycle | cytoplasm; cytosol; succinate-CoA ligase complex (ADP-forming) | nucleotide binding succinate-CoA ligase (ADP-forming) activity succinate-CoA ligase (GDP-forming) activity | Escherichia coli | 3D-structure Direct protein sequencing Ligase Nucleotide-binding Reference proteome Tricarboxylic acid cycle | MSILIDKNTK | MSILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQTEAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVLK | tricarboxylic acid cycle cytoplasm; cytosol; succinate-CoA ligase complex (ADP-forming) nucleotide binding succinate-CoA ligase (ADP-forming) activity succinate-CoA ligase (GDP-forming) activity Escherichia coli 3D-structure Direct protein sequencing Ligase Nucleotide-binding Reference proteome Tricarboxylic acid cycle MSILIDKNTK MSILIDKNTKVICQGFTGSQGTFHSEQAIAYGTKMVGGVTPGKGGTTHLGLPVFNTVREAVAATGATASVIYVPAPFCKDSILEAIDAGIKLIITITEGIPTLDMLTVKVKLDEAGVRMIGPNCPGVITPGECKIGIQPGHIHKPGKVGIVSRSGTLTYEAVKQTTDYGFGQSTCVGIGGDPIPGSNFIDILEMFEKDPQTEAIVMIGEIGGSAEEEAAAYIKEHVTKPVVGYIAGVTAPKGKRMGHAGAIIAGGKGTADEKFAALEAAGVKTVRSLADIGEALKTVLK |
D-xylose transmembrane transport transmembrane transport | membrane; plasma membrane | D-xylose:proton symporter activity transmembrane transporter activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Reference proteome Sugar transport Symport Transmembrane Transmembrane helix Transport | MNTQYNSSYI | MNTQYNSSYIFSITLVATLGGLLFGYDTAVISGTVESLNTVFVAPQNLSESAANSLLGFCVASALIGCIIGGALGGYCSNRFGRRDSLKIAAVLFFISGVGSAWPELGFTSINPDNTVPVYLAGYVPEFVIYRIIGGIGVGLASMLSPMYIAELAPAHIRGKLVSFNQFAIIFGQLLVYCVNYFIARSGDASWLNTDGWRYMFASECIPALLFLMLLYTVPESPRWLMSRGKQEQAEGILRKIMGNTLATQAVQEIKHSLDHGRKTGGRLLMFGVGVIVIGVMLSIFQQFVGINVVLYYAPEVFKTLGASTDIALLQTIIVGVINLTFTVLAIMTVDKFGRKPLQIIGALGMAIGMFSLGTAFYTQAPGIVALLSMLFYVAAFAMSWGPVCWVLLSEIFPNAIRGKALAIAVAAQWLANYFVSWTFPMMDKNSWLVAHFHNGFSYWIYGCMGVLAALFMWKFVPETKGKTLEELEALWEPETKKTQQTATL | D-xylose transmembrane transport transmembrane transport membrane; plasma membrane D-xylose:proton symporter activity transmembrane transporter activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Reference proteome Sugar transport Symport Transmembrane Transmembrane helix Transport MNTQYNSSYI MNTQYNSSYIFSITLVATLGGLLFGYDTAVISGTVESLNTVFVAPQNLSESAANSLLGFCVASALIGCIIGGALGGYCSNRFGRRDSLKIAAVLFFISGVGSAWPELGFTSINPDNTVPVYLAGYVPEFVIYRIIGGIGVGLASMLSPMYIAELAPAHIRGKLVSFNQFAIIFGQLLVYCVNYFIARSGDASWLNTDGWRYMFASECIPALLFLMLLYTVPESPRWLMSRGKQEQAEGILRKIMGNTLATQAVQEIKHSLDHGRKTGGRLLMFGVGVIVIGVMLSIFQQFVGINVVLYYAPEVFKTLGASTDIALLQTIIVGVINLTFTVLAIMTVDKFGRKPLQIIGALGMAIGMFSLGTAFYTQAPGIVALLSMLFYVAAFAMSWGPVCWVLLSEIFPNAIRGKALAIAVAAQWLANYFVSWTFPMMDKNSWLVAHFHNGFSYWIYGCMGVLAALFMWKFVPETKGKTLEELEALWEPETKKTQQTATL |
isoleucine biosynthetic process L-serine catabolic process L-threonine catabolic process to propionate threonine catabolic process | cytosol; protein-containing complex | amino acid binding L-serine ammonia-lyase activity L-threonine ammonia-lyase activity nucleotide binding pyridoxal phosphate binding threonine aldolase activity | Escherichia coli | Allosteric enzyme Direct protein sequencing Lyase Nucleotide-binding Pyridoxal phosphate Reference proteome | MHITYDLPVA | MHITYDLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRVSQITGFVDA | isoleucine biosynthetic process L-serine catabolic process L-threonine catabolic process to propionate threonine catabolic process cytosol; protein-containing complex amino acid binding L-serine ammonia-lyase activity L-threonine ammonia-lyase activity nucleotide binding pyridoxal phosphate binding threonine aldolase activity Escherichia coli Allosteric enzyme Direct protein sequencing Lyase Nucleotide-binding Pyridoxal phosphate Reference proteome MHITYDLPVA MHITYDLPVAIDDIIEAKQRLAGRIYKTGMPRSNYFSERCKGEIFLKFENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACSAGNHAQGVSLSCAMLGIDGKVVMPKGAPKSKVAATCDYSAEVVLHGDNFNDTIAKVSEIVEMEGRIFIPPYDDPKVIAGQGTIGLEIMEDLYDVDNVIVPIGGGGLIAGIAVAIKSINPTIRVIGVQSENVHGMAASFHSGEITTHRTTGTLADGCDVSRPGNLTYEIVRELVDDIVLVSEDEIRNSMIALIQRNKVVTEGAGALACAALLSGKLDQYIQNRKTVSIISGGNIDLSRVSQITGFVDA |
acyl-CoA metabolic process fatty acid catabolic process | cytosol | acyl-CoA hydrolase activity identical protein binding myristoyl-CoA hydrolase activity palmitoyl-CoA hydrolase activity protein homodimerization activity | Escherichia coli | 3D-structure Direct protein sequencing Hydrolase Lipid metabolism Reference proteome | MSQALKNLLT | MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEVRPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN | acyl-CoA metabolic process fatty acid catabolic process cytosol acyl-CoA hydrolase activity identical protein binding myristoyl-CoA hydrolase activity palmitoyl-CoA hydrolase activity protein homodimerization activity Escherichia coli 3D-structure Direct protein sequencing Hydrolase Lipid metabolism Reference proteome MSQALKNLLT MSQALKNLLTLLNLEKIEEGLFRGQSEDLGLRQVFGGQVVGQALYAAKETVPEERLVHSFHSYFLRPGDSKKPIIYDVETLRDGNSFSARRVAAIQNGKPIFYMTASFQAPEAGFEHQKTMPSAPAPDGLPSETQIAQSLAHLLPPVLKDKFICDRPLEVRPVEFHNPLKGHVAEPHRQVWIRANGSVPDDLRVHQYLLGYASDLNFLPVALQPHGIGFLEPGIQIATIDHSMWFHRPFNLNEWLLYSVESTSASSARGFVRGEFYTQDGVLVASTVQEGVMRNHN |
D-ribose transmembrane transport | ATP-binding cassette (ABC) transporter complex; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; membrane; plasma membrane | D-ribose transmembrane transporter activity | Escherichia coli | Cell inner membrane Cell membrane Membrane Reference proteome Sugar transport Transmembrane Transmembrane helix Transport | MTTQTVSGRR | MTTQTVSGRRYFTKAWLMEQKSLIALLVLIAIVSTLSPNFFTINNLFNILQQTSVNAIMAVGMTLVILTSGIDLSVGSLLALTGAVAASIVGIEVNALVAVAAALALGAAIGAVTGVIVAKGRVQAFIATLVMMLLLRGVTMVYTNGSPVNTGFTENADLFGWFGIGRPLGVPTPVWIMGIVFLAAWYMLHHTRLGRYIYALGGNEAATRLSGINVNKIKIIVYSLCGLLASLAGIIEVARLSSAQPTAGTGYELDAIAAVVLGGTSLAGGKGRIVGTLIGALILGFLNNGLNLLGVSSYYQMIVKAVVILLAVLVDNKKQ | D-ribose transmembrane transport ATP-binding cassette (ABC) transporter complex; ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; membrane; plasma membrane D-ribose transmembrane transporter activity Escherichia coli Cell inner membrane Cell membrane Membrane Reference proteome Sugar transport Transmembrane Transmembrane helix Transport MTTQTVSGRR MTTQTVSGRRYFTKAWLMEQKSLIALLVLIAIVSTLSPNFFTINNLFNILQQTSVNAIMAVGMTLVILTSGIDLSVGSLLALTGAVAASIVGIEVNALVAVAAALALGAAIGAVTGVIVAKGRVQAFIATLVMMLLLRGVTMVYTNGSPVNTGFTENADLFGWFGIGRPLGVPTPVWIMGIVFLAAWYMLHHTRLGRYIYALGGNEAATRLSGINVNKIKIIVYSLCGLLASLAGIIEVARLSSAQPTAGTGYELDAIAAVVLGGTSLAGGKGRIVGTLIGALILGFLNNGLNLLGVSSYYQMIVKAVVILLAVLVDNKKQ |
wobble position cytosine ribose methylation wobble position uridine ribose methylation | cytoplasm | protein homodimerization activity RNA binding tRNA (5-carboxymethylaminomethyluridine(34)-2'-O)-methyltransferase activity tRNA (cytidine(34)-2'-O)-methyltransferase activity tRNA (uracil-2'-O-)-methyltransferase activity | Escherichia coli | 3D-structure Cytoplasm Methyltransferase Reference proteome S-adenosyl-L-methionine Transferase tRNA processing | MLNIVLYEPE | MLNIVLYEPEIPPNTGNIIRLCANTGFRLHIIEPMGFAWDDKRLRRAGLDYHEFTAVTRHHDYRAFLEAENPQRLFALTTKGTPAHSAVSYQDGDYLMFGPETRGLPASILDALPAEQKIRIPMVPDSRSMNLSNAVSVVVYEAWRQLGYPGAVLRD | wobble position cytosine ribose methylation wobble position uridine ribose methylation cytoplasm protein homodimerization activity RNA binding tRNA (5-carboxymethylaminomethyluridine(34)-2'-O)-methyltransferase activity tRNA (cytidine(34)-2'-O)-methyltransferase activity tRNA (uracil-2'-O-)-methyltransferase activity Escherichia coli 3D-structure Cytoplasm Methyltransferase Reference proteome S-adenosyl-L-methionine Transferase tRNA processing MLNIVLYEPE MLNIVLYEPEIPPNTGNIIRLCANTGFRLHIIEPMGFAWDDKRLRRAGLDYHEFTAVTRHHDYRAFLEAENPQRLFALTTKGTPAHSAVSYQDGDYLMFGPETRGLPASILDALPAEQKIRIPMVPDSRSMNLSNAVSVVVYEAWRQLGYPGAVLRD |
tRNA aminoacylation tyrosyl-tRNA aminoacylation | cytosol; membrane | ATP binding protein homodimerization activity RNA binding tyrosine-tRNA ligase activity | Escherichia coli | 3D-structure Acetylation Aminoacyl-tRNA synthetase ATP-binding Cytoplasm Direct protein sequencing Ligase Nucleotide-binding Protein biosynthesis Reference proteome RNA-binding | MASSNLIKQL | MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLQAAKRITECLFSGSLSALSEADFEQLAQDGVPMVEMEKGADLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYFFKEEDRLFGRFTLLRRGKKNYCLICWK | tRNA aminoacylation tyrosyl-tRNA aminoacylation cytosol; membrane ATP binding protein homodimerization activity RNA binding tyrosine-tRNA ligase activity Escherichia coli 3D-structure Acetylation Aminoacyl-tRNA synthetase ATP-binding Cytoplasm Direct protein sequencing Ligase Nucleotide-binding Protein biosynthesis Reference proteome RNA-binding MASSNLIKQL MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLQAAKRITECLFSGSLSALSEADFEQLAQDGVPMVEMEKGADLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYFFKEEDRLFGRFTLLRRGKKNYCLICWK |
uracil import across plasma membrane uracil transport | membrane; plasma membrane | protein homodimerization activity uracil transmembrane transporter activity uracil:monoatomic cation symporter activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport | MTRRAIGVSE | MTRRAIGVSERPPLLQTIPLSLQHLFAMFGATVLVPVLFHINPATVLLFNGIGTLLYLFICKGKIPAYLGSSFAFISPVLLLLPLGYEVALGGFIMCGVLFCLVSFIVKKAGTGWLDVLFPPAAMGAIVAVIGLELAGVAAGMAGLLPAEGQTPDSKTIIISITTLAVTVLGSVLFRGFLAIIPILIGVLVGYALSFAMGIVDTTPIINAHWFALPTLYTPRFEWFAILTILPAALVVIAEHVGHLVVTANIVKKDLLRDPGLHRSMFANGLSTVISGFFGSTPNTTYGENIGVMAITRVYSTWVIGGAAIFAILLSCVGKLAAAIQMIPLPVMGGVSLLLYGVIGASGIRVLIESKVDYNKAQNLILTSVILIIGVSGAKVNIGAAELKGMALATIVGIGLSLIFKLISVLRPEEVVLDAEDADITDK | uracil import across plasma membrane uracil transport membrane; plasma membrane protein homodimerization activity uracil transmembrane transporter activity uracil:monoatomic cation symporter activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport MTRRAIGVSE MTRRAIGVSERPPLLQTIPLSLQHLFAMFGATVLVPVLFHINPATVLLFNGIGTLLYLFICKGKIPAYLGSSFAFISPVLLLLPLGYEVALGGFIMCGVLFCLVSFIVKKAGTGWLDVLFPPAAMGAIVAVIGLELAGVAAGMAGLLPAEGQTPDSKTIIISITTLAVTVLGSVLFRGFLAIIPILIGVLVGYALSFAMGIVDTTPIINAHWFALPTLYTPRFEWFAILTILPAALVVIAEHVGHLVVTANIVKKDLLRDPGLHRSMFANGLSTVISGFFGSTPNTTYGENIGVMAITRVYSTWVIGGAAIFAILLSCVGKLAAAIQMIPLPVMGGVSLLLYGVIGASGIRVLIESKVDYNKAQNLILTSVILIIGVSGAKVNIGAAELKGMALATIVGIGLSLIFKLISVLRPEEVVLDAEDADITDK |
cytoplasmic translation | cytoplasm; cytosol; cytosolic large ribosomal subunit | 5S rRNA binding structural constituent of ribosome | Escherichia coli | 3D-structure Direct protein sequencing Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding | MDKKSARIRR | MDKKSARIRRATRARRKLQELGATRLVVHRTPRHIYAQVIAPNGSEVLVAASTVEKAIAEQLKYTGNKDAAAAVGKAVAERALEKGIKDVSFDRSGFQYHGRVQALADAAREAGLQF | cytoplasmic translation cytoplasm; cytosol; cytosolic large ribosomal subunit 5S rRNA binding structural constituent of ribosome Escherichia coli 3D-structure Direct protein sequencing Phosphoprotein Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding MDKKSARIRR MDKKSARIRRATRARRKLQELGATRLVVHRTPRHIYAQVIAPNGSEVLVAASTVEKAIAEQLKYTGNKDAAAAVGKAVAERALEKGIKDVSFDRSGFQYHGRVQALADAAREAGLQF |
defense response to bacterium killing of cells of another organism | extracellular region | toxin activity | Myrmecia pilosula | Allergen Amidation Antibiotic Antimicrobial Cytolysis Direct protein sequencing Disulfide bond Hemolysis Secreted Toxin | LIGLVSKGTC | LIGLVSKGTCVLVKTVCKKVLKQ | defense response to bacterium killing of cells of another organism extracellular region toxin activity Myrmecia pilosula Allergen Amidation Antibiotic Antimicrobial Cytolysis Direct protein sequencing Disulfide bond Hemolysis Secreted Toxin LIGLVSKGTC LIGLVSKGTCVLVKTVCKKVLKQ |
acetyl-CoA catabolic process brown fat cell differentiation butyryl-CoA catabolic process coenzyme A catabolic process malonyl-CoA catabolic process medium-chain fatty-acyl-CoA catabolic process nucleoside diphosphate metabolic process propionyl-CoA catabolic process propionyl-CoA metabolic process succinyl-CoA catabolic process | cytosol; peroxisomal matrix; peroxisome | coenzyme A diphosphatase activity magnesium ion binding manganese ion binding snoRNA binding | Homo sapiens | 3D-structure Alternative splicing Hydrolase Magnesium Manganese Metal-binding Peroxisome Reference proteome RNA-binding | MSRLGLPEEP | MSRLGLPEEPVRNSLLDDAKARLRKYDIGGKYSHLPYNKYSVLLPLVAKEGKLHLLFTVRSEKLRRAPGEVCFPGGKRDPTDMDDAATALREAQEEVGLRPHQVEVVCCLVPCLIDTDTLITPFVGLIDHNFQAQPNPAEVKDVFLVPLAYFLHPQVHDQHYVTRLGHRFINHIFEYTNPEDGVTYQIKGMTANLAVLVAFIILEKKPTFEVQFNLNDVLASSEELFLKVHKKATSRL | acetyl-CoA catabolic process brown fat cell differentiation butyryl-CoA catabolic process coenzyme A catabolic process malonyl-CoA catabolic process medium-chain fatty-acyl-CoA catabolic process nucleoside diphosphate metabolic process propionyl-CoA catabolic process propionyl-CoA metabolic process succinyl-CoA catabolic process cytosol; peroxisomal matrix; peroxisome coenzyme A diphosphatase activity magnesium ion binding manganese ion binding snoRNA binding Homo sapiens 3D-structure Alternative splicing Hydrolase Magnesium Manganese Metal-binding Peroxisome Reference proteome RNA-binding MSRLGLPEEP MSRLGLPEEPVRNSLLDDAKARLRKYDIGGKYSHLPYNKYSVLLPLVAKEGKLHLLFTVRSEKLRRAPGEVCFPGGKRDPTDMDDAATALREAQEEVGLRPHQVEVVCCLVPCLIDTDTLITPFVGLIDHNFQAQPNPAEVKDVFLVPLAYFLHPQVHDQHYVTRLGHRFINHIFEYTNPEDGVTYQIKGMTANLAVLVAFIILEKKPTFEVQFNLNDVLASSEELFLKVHKKATSRL |
adenosine 5'-(hexahydrogen pentaphosphate) catabolic process diadenosine hexaphosphate catabolic process diadenosine pentaphosphate catabolic process diphosphoinositol polyphosphate metabolic process | cytoplasm; cytosol; nucleus | bis(5'-adenosyl)-hexaphosphatase activity bis(5'-adenosyl)-pentaphosphatase activity diphosphoinositol-polyphosphate diphosphatase activity endopolyphosphatase activity metal ion binding | Mus musculus | Cytoplasm Hydrolase Magnesium Manganese Metal-binding Reference proteome | MKCKPNQTRT | MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPDGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVFVLTVTELLEDWEDSVSIGRKREWFKIEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSAAPSPPESEP | adenosine 5'-(hexahydrogen pentaphosphate) catabolic process diadenosine hexaphosphate catabolic process diadenosine pentaphosphate catabolic process diphosphoinositol polyphosphate metabolic process cytoplasm; cytosol; nucleus bis(5'-adenosyl)-hexaphosphatase activity bis(5'-adenosyl)-pentaphosphatase activity diphosphoinositol-polyphosphate diphosphatase activity endopolyphosphatase activity metal ion binding Mus musculus Cytoplasm Hydrolase Magnesium Manganese Metal-binding Reference proteome MKCKPNQTRT MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPDGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVFVLTVTELLEDWEDSVSIGRKREWFKIEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSAAPSPPESEP |
adenosine 5'-(hexahydrogen pentaphosphate) catabolic process diadenosine hexaphosphate catabolic process diadenosine pentaphosphate catabolic process diphosphoinositol polyphosphate metabolic process | cytoplasm; cytosol; nucleus | bis(5'-adenosyl)-hexaphosphatase activity bis(5'-adenosyl)-pentaphosphatase activity diphosphoinositol-polyphosphate diphosphatase activity endopolyphosphatase activity metal ion binding | Mus musculus | Cytoplasm Hydrolase Magnesium Manganese Metal-binding Reference proteome | MKCKPNQTRT | MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPDGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVFVLTVTELLEDWEDSVSIGRKREWFKIEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSAAPSPPESEP | adenosine 5'-(hexahydrogen pentaphosphate) catabolic process diadenosine hexaphosphate catabolic process diadenosine pentaphosphate catabolic process diphosphoinositol polyphosphate metabolic process cytoplasm; cytosol; nucleus bis(5'-adenosyl)-hexaphosphatase activity bis(5'-adenosyl)-pentaphosphatase activity diphosphoinositol-polyphosphate diphosphatase activity endopolyphosphatase activity metal ion binding Mus musculus Cytoplasm Hydrolase Magnesium Manganese Metal-binding Reference proteome MKCKPNQTRT MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPDGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVFVLTVTELLEDWEDSVSIGRKREWFKIEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSAAPSPPESEP |
negative regulation of cytoskeleton organization suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity | host cell nucleus; host cell perinuclear region of cytoplasm; viral capsid | complement binding enzyme binding serpin family protein binding small GTPase binding structural molecule activity zymogen binding | Hepatitis C virus genotype 1a | Host cytoplasm Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host RIG-I by virus Inhibition of host RLR pathway by virus Reference proteome Ribosomal frameshifting Viral immunoevasion | MSTNPKPQRK | MSTNPKPQRKKPNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRGRLPSGRNLEVDVSLSPRHVGPRAGPGLSPGTLGPSMAMRVAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWKTA | negative regulation of cytoskeleton organization suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity host cell nucleus; host cell perinuclear region of cytoplasm; viral capsid complement binding enzyme binding serpin family protein binding small GTPase binding structural molecule activity zymogen binding Hepatitis C virus genotype 1a Host cytoplasm Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host RIG-I by virus Inhibition of host RLR pathway by virus Reference proteome Ribosomal frameshifting Viral immunoevasion MSTNPKPQRK MSTNPKPQRKKPNVTPTVAHRTSSSRVAVRSLVEFTCCRAGALDWVCARRGRLPSGRNLEVDVSLSPRHVGPRAGPGLSPGTLGPSMAMRVAGGRDGSCLPVALGLAGAPQTPGVGRAIWVRSSIPLRAASPTSWGTYRSSAPLLEALPGPWRMASGFWKTA |
negative regulation of translation protein stabilization response to heat | cytosol | identical protein binding mRNA 5'-UTR binding protein homodimerization activity | Escherichia coli | Chaperone Cytoplasm Direct protein sequencing Reference proteome Stress response | MRNFDLSPLY | MRNFDLSPLYRSAIGFDRLFNHLENNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQKERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN | negative regulation of translation protein stabilization response to heat cytosol identical protein binding mRNA 5'-UTR binding protein homodimerization activity Escherichia coli Chaperone Cytoplasm Direct protein sequencing Reference proteome Stress response MRNFDLSPLY MRNFDLSPLYRSAIGFDRLFNHLENNQSQSNGGYPPYNVELVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQKERTYLYQGIAERNFERKFQLAENIHVRGANLVNGLLYIDLERVIPEAKKPRRIEIN |
protein stabilization response to heat stress response to copper ion | cytoplasm | identical protein binding | Escherichia coli | Chaperone Cytoplasm Direct protein sequencing Reference proteome Stress response | MRNFDLSPLM | MRNFDLSPLMRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLEIQLEGTRLSVKGTPEQPKEEKKWLHQGLMNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEPIAAQRIAISERPALNS | protein stabilization response to heat stress response to copper ion cytoplasm identical protein binding Escherichia coli Chaperone Cytoplasm Direct protein sequencing Reference proteome Stress response MRNFDLSPLM MRNFDLSPLMRQWIGFDKLANALQNAGESQSFPPYNIEKSDDNHYRITLALAGFRQEDLEIQLEGTRLSVKGTPEQPKEEKKWLHQGLMNQPFSLSFTLAENMEVSGATFVNGLLHIDLIRNEPEPIAAQRIAISERPALNS |
cellular response to amino acid starvation mRNA catabolic process negative regulation of translation regulation of DNA-templated transcription regulation of growth response to antibiotic single-species biofilm formation | protein-DNA complex; toxin-antitoxin complex | DNA-binding transcription repressor activity ribosome binding RNA endonuclease activity rRNA binding toxin sequestering activity transcription cis-regulatory region binding | Escherichia coli | 3D-structure Antibiotic resistance Endonuclease Hydrolase Nuclease Reference proteome Repressor RNA-binding rRNA-binding Stress response Toxin-antitoxin system Transcription Transcription regulation | MAYFLDFDER | MAYFLDFDERALKEWRKLGSTVREQLKKKLVEVLESPRIEANKLRGMPDCYKIKLRSSGYRLVYQVIDEKVVVFVISVGKRERSEVYSEAVKRIL | cellular response to amino acid starvation mRNA catabolic process negative regulation of translation regulation of DNA-templated transcription regulation of growth response to antibiotic single-species biofilm formation protein-DNA complex; toxin-antitoxin complex DNA-binding transcription repressor activity ribosome binding RNA endonuclease activity rRNA binding toxin sequestering activity transcription cis-regulatory region binding Escherichia coli 3D-structure Antibiotic resistance Endonuclease Hydrolase Nuclease Reference proteome Repressor RNA-binding rRNA-binding Stress response Toxin-antitoxin system Transcription Transcription regulation MAYFLDFDER MAYFLDFDERALKEWRKLGSTVREQLKKKLVEVLESPRIEANKLRGMPDCYKIKLRSSGYRLVYQVIDEKVVVFVISVGKRERSEVYSEAVKRIL |
DNA-templated transcription regulation of DNA-templated transcription regulation of growth single-species biofilm formation | protein-DNA complex; toxin-antitoxin complex | DNA-binding transcription repressor activity toxin sequestering activity transcription cis-regulatory region binding | Escherichia coli | 3D-structure DNA-binding Reference proteome Repressor Stress response Toxin-antitoxin system Transcription Transcription regulation | MGSINLRIDD | MGSINLRIDDELKARSYAALEKMGVTPSEALRLMLEYIADNERLPFKQTLLSDEDAELVEIVKERLRNPKPVRVTLDEL | DNA-templated transcription regulation of DNA-templated transcription regulation of growth single-species biofilm formation protein-DNA complex; toxin-antitoxin complex DNA-binding transcription repressor activity toxin sequestering activity transcription cis-regulatory region binding Escherichia coli 3D-structure DNA-binding Reference proteome Repressor Stress response Toxin-antitoxin system Transcription Transcription regulation MGSINLRIDD MGSINLRIDDELKARSYAALEKMGVTPSEALRLMLEYIADNERLPFKQTLLSDEDAELVEIVKERLRNPKPVRVTLDEL |
cardiolipin biosynthetic process dephosphorylation negative regulation of insulin secretion involved in cellular response to glucose stimulus regulation of intrinsic apoptotic signaling pathway | mitochondrial inner membrane; mitochondrion | myosin phosphatase activity phosphatidylglycerophosphatase activity phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity protein tyrosine phosphatase activity protein tyrosine/serine/threonine phosphatase activity | Rattus norvegicus | Hydrolase Lipid biosynthesis Lipid metabolism Membrane Mitochondrion Mitochondrion inner membrane Phospholipid biosynthesis Phospholipid metabolism Protein phosphatase Reference proteome Transit peptide | MAASAWLEAG | MAASAWLEAGLARVLFYPTLLYTVFRGRVGGPAHRDWYHRIDHTVLLGALPLRSMTRRLVLDENVRGVITMNEEYETRFLCNTSKEWKNVGVEQLRLSTVDMTGVPTLANLHRGVQFALKYQSLGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEILKEFHKEIAARAAKN | cardiolipin biosynthetic process dephosphorylation negative regulation of insulin secretion involved in cellular response to glucose stimulus regulation of intrinsic apoptotic signaling pathway mitochondrial inner membrane; mitochondrion myosin phosphatase activity phosphatidylglycerophosphatase activity phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity protein tyrosine phosphatase activity protein tyrosine/serine/threonine phosphatase activity Rattus norvegicus Hydrolase Lipid biosynthesis Lipid metabolism Membrane Mitochondrion Mitochondrion inner membrane Phospholipid biosynthesis Phospholipid metabolism Protein phosphatase Reference proteome Transit peptide MAASAWLEAG MAASAWLEAGLARVLFYPTLLYTVFRGRVGGPAHRDWYHRIDHTVLLGALPLRSMTRRLVLDENVRGVITMNEEYETRFLCNTSKEWKNVGVEQLRLSTVDMTGVPTLANLHRGVQFALKYQSLGQCVYVHCKAGRSRSATMVAAYLIQVHNWSPEEAIEAIAKIRSHISIRPSQLEILKEFHKEIAARAAKN |
behavioral response to pain intracellular protein transport negative regulation of DNA-templated transcription negative regulation of transcription by RNA polymerase II potassium ion transport regulation of neuron apoptotic process regulation of potassium ion transmembrane transport response to pain sensory perception of pain | axon; axon terminus; cytosol; dendrite; nucleoplasm; nucleus; protein-DNA complex; voltage-gated potassium channel complex | calcium ion binding calcium-dependent protein binding DNA binding DNA-binding transcription repressor activity, RNA polymerase II-specific potassium channel regulator activity RNA polymerase II cis-regulatory region sequence-specific DNA binding sequence-specific DNA binding transmembrane transporter binding | Mus musculus | Alternative splicing Reference proteome | MRQLPAGPSS | MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIGWQPPGRSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRL | behavioral response to pain intracellular protein transport negative regulation of DNA-templated transcription negative regulation of transcription by RNA polymerase II potassium ion transport regulation of neuron apoptotic process regulation of potassium ion transmembrane transport response to pain sensory perception of pain axon; axon terminus; cytosol; dendrite; nucleoplasm; nucleus; protein-DNA complex; voltage-gated potassium channel complex calcium ion binding calcium-dependent protein binding DNA binding DNA-binding transcription repressor activity, RNA polymerase II-specific potassium channel regulator activity RNA polymerase II cis-regulatory region sequence-specific DNA binding sequence-specific DNA binding transmembrane transporter binding Mus musculus Alternative splicing Reference proteome MRQLPAGPSS MRQLPAGPSSLACSGCKAGRLVTVPFSSRDAEDQGSREGIGWQPPGRSWAHTTEQEGKHQVAKATVHPPGPDALLLNQVDPVQCCPTRL |
division septum site selection negative regulation of division septum assembly negative regulation of protein polymerization regulation of DNA-templated transcription | bacterial nucleoid; cytoplasm | DNA binding DNA-binding transcription factor activity identical protein binding protein homodimerization activity sequence-specific DNA binding transcription cis-regulatory region binding | Escherichia coli | 3D-structure Cell cycle Cell division Coiled coil Cytoplasm DNA-binding Reference proteome | MAEKQTAKRN | MAEKQTAKRNRREEILQSLALMLESSDGSQRITTAKLAASVGVSEAALYRHFPSKTRMFDSLIEFIEDSLITRINLILKDEKDTTARLRLIVLLLLGFGERNPGLTRILTGHALMFEQDRLQGRINQLFERIEAQLRQVLREKRMREGEGYTTDETLLASQILAFCEGMLSRFVRSEFKYRPTDDFDARWPLIAAQLQ | division septum site selection negative regulation of division septum assembly negative regulation of protein polymerization regulation of DNA-templated transcription bacterial nucleoid; cytoplasm DNA binding DNA-binding transcription factor activity identical protein binding protein homodimerization activity sequence-specific DNA binding transcription cis-regulatory region binding Escherichia coli 3D-structure Cell cycle Cell division Coiled coil Cytoplasm DNA-binding Reference proteome MAEKQTAKRN MAEKQTAKRNRREEILQSLALMLESSDGSQRITTAKLAASVGVSEAALYRHFPSKTRMFDSLIEFIEDSLITRINLILKDEKDTTARLRLIVLLLLGFGERNPGLTRILTGHALMFEQDRLQGRINQLFERIEAQLRQVLREKRMREGEGYTTDETLLASQILAFCEGMLSRFVRSEFKYRPTDDFDARWPLIAAQLQ |
autophagosome maturation autophagy late endosome to lysosome transport late endosome to vacuole transport via multivesicular body sorting pathway membrane fission midbody abscission mitotic metaphase chromosome alignment multivesicular body assembly multivesicular body sorting pathway multivesicular body-lysosome fusion nuclear membrane reassembly nucleus organization plasma membrane repair protein transport regulation of mitotic spindle assembly regulation of protein catabolic process ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway vesicle budding from membrane vesicle fusion with vacuole viral budding from plasma membrane viral budding via host ESCRT complex | amphisome membrane; autophagosome membrane; endosome membrane; ESCRT III complex; kinetochore; kinetochore microtubule; lysosomal membrane; midbody; multivesicular body; multivesicular body membrane; nuclear pore; plasma membrane | protein-containing complex binding | Mus musculus | Coiled coil Endosome Lipoprotein Membrane Myristate Phosphoprotein Protein transport Reference proteome Transport Ubl conjugation | MGNLFGRKKQ | MGNLFGRKKQSRVTEQDRAILQLKQQRDKLRQYQKRVTQQLERERALARQLLRDGRKERAKLLLKKKRYREQLLDRTENQISSLEAMVQSIEFTQIEMKVMEGLQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGNFTQEDEDAILEELNAITQEQMELPEVPSEPLPDRNPEAPAKARSRQAELVAAS | autophagosome maturation autophagy late endosome to lysosome transport late endosome to vacuole transport via multivesicular body sorting pathway membrane fission midbody abscission mitotic metaphase chromosome alignment multivesicular body assembly multivesicular body sorting pathway multivesicular body-lysosome fusion nuclear membrane reassembly nucleus organization plasma membrane repair protein transport regulation of mitotic spindle assembly regulation of protein catabolic process ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway vesicle budding from membrane vesicle fusion with vacuole viral budding from plasma membrane viral budding via host ESCRT complex amphisome membrane; autophagosome membrane; endosome membrane; ESCRT III complex; kinetochore; kinetochore microtubule; lysosomal membrane; midbody; multivesicular body; multivesicular body membrane; nuclear pore; plasma membrane protein-containing complex binding Mus musculus Coiled coil Endosome Lipoprotein Membrane Myristate Phosphoprotein Protein transport Reference proteome Transport Ubl conjugation MGNLFGRKKQ MGNLFGRKKQSRVTEQDRAILQLKQQRDKLRQYQKRVTQQLERERALARQLLRDGRKERAKLLLKKKRYREQLLDRTENQISSLEAMVQSIEFTQIEMKVMEGLQVGNECLNKMHQVMSIEEVERILDETQEAVEYQRQIDELLAGNFTQEDEDAILEELNAITQEQMELPEVPSEPLPDRNPEAPAKARSRQAELVAAS |
negative regulation of ER-associated ubiquitin-dependent protein catabolic process negative regulation of ERAD pathway negative regulation of protein-containing complex assembly negative regulation of retrograde protein transport, ER to cytosol negative regulation of ubiquitin-dependent protein catabolic process negative regulation of VCP-NPL4-UFD1 AAA ATPase complex assembly positive regulation of autophagy positive regulation of protein lipidation | endoplasmic reticulum membrane; Golgi membrane; membrane; plasma membrane; smooth endoplasmic reticulum membrane | ATPase binding protein self-association | Rattus norvegicus | Cell membrane Endoplasmic reticulum Golgi apparatus Lipoprotein Membrane Myristate Phosphoprotein Reference proteome | MGLCFPCPAE | MGLCFPCPAESAPPSPSPEEKRAKLAEAAERRQKEAASRGILDIQSVEAKKKKKEQLEKQMETSGPPAGGLRWTVS | negative regulation of ER-associated ubiquitin-dependent protein catabolic process negative regulation of ERAD pathway negative regulation of protein-containing complex assembly negative regulation of retrograde protein transport, ER to cytosol negative regulation of ubiquitin-dependent protein catabolic process negative regulation of VCP-NPL4-UFD1 AAA ATPase complex assembly positive regulation of autophagy positive regulation of protein lipidation endoplasmic reticulum membrane; Golgi membrane; membrane; plasma membrane; smooth endoplasmic reticulum membrane ATPase binding protein self-association Rattus norvegicus Cell membrane Endoplasmic reticulum Golgi apparatus Lipoprotein Membrane Myristate Phosphoprotein Reference proteome MGLCFPCPAE MGLCFPCPAESAPPSPSPEEKRAKLAEAAERRQKEAASRGILDIQSVEAKKKKKEQLEKQMETSGPPAGGLRWTVS |
glucose metabolic process glycolytic process NADH regeneration | cytoplasm | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity NAD binding NADP binding protease binding | Streptococcus pyogenes | 3D-structure Cytoplasm Direct protein sequencing Glycolysis NAD Nucleotide-binding Oxidoreductase | MVVKVGINGF | MVVKVGINGFGRIGRLAFRRIQNIEGVEVTRINDLTDPNMLAHLLKYDTTQGRFDGTVEVKEGGFEVNGNFIKVSAERDPENIDWATDGVEIVLEATGFFAKKEAAEKHLHANGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGASCTTNCLAPMAKALHDAFGIQKGLMTTIHAYTGDQMILDGPHRGGDLRRARAGAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVVTLDKNVSVDEINSAMKAASNDSFGYTEDPIVSSDIVGVSYGSLFDATQTKVMEVDGSQLVKVVSWYDNEMSYTAQLVRTLEYFAKIAK | glucose metabolic process glycolytic process NADH regeneration cytoplasm glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity NAD binding NADP binding protease binding Streptococcus pyogenes3D-structure Cytoplasm Direct protein sequencing Glycolysis NAD Nucleotide-binding Oxidoreductase MVVKVGINGF MVVKVGINGFGRIGRLAFRRIQNIEGVEVTRINDLTDPNMLAHLLKYDTTQGRFDGTVEVKEGGFEVNGNFIKVSAERDPENIDWATDGVEIVLEATGFFAKKEAAEKHLHANGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGASCTTNCLAPMAKALHDAFGIQKGLMTTIHAYTGDQMILDGPHRGGDLRRARAGAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVVTLDKNVSVDEINSAMKAASNDSFGYTEDPIVSSDIVGVSYGSLFDATQTKVMEVDGSQLVKVVSWYDNEMSYTAQLVRTLEYFAKIAK |
evasion of host immune response programmed cell death induced by symbiont proteolysis symbiont-mediated suppression of host autophagy | extracellular region; host cell cytosol; host extracellular space | cysteine-type endopeptidase activity cysteine-type peptidase activity toxin activity | Streptococcus pyogenes | 3D-structure Autocatalytic cleavage Direct protein sequencing Host cytoplasm Hydrolase Methylation Protease Secreted Signal Thiol protease Toxin Virulence Zymogen | MNKKKLGIRL | MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP | evasion of host immune response programmed cell death induced by symbiont proteolysis symbiont-mediated suppression of host autophagy extracellular region; host cell cytosol; host extracellular space cysteine-type endopeptidase activity cysteine-type peptidase activity toxin activity Streptococcus pyogenes3D-structure Autocatalytic cleavage Direct protein sequencing Host cytoplasm Hydrolase Methylation Protease Secreted Signal Thiol protease Toxin Virulence Zymogen MNKKKLGIRL MNKKKLGIRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRSDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP |
evasion of host immune response programmed cell death induced by symbiont protein maturation proteolysis symbiont-mediated suppression of host autophagy | cytosol; extracellular region; host cell cytosol; host extracellular space | cysteine-type endopeptidase activity toxin activity | Streptococcus pyogenes serotype M1 | 3D-structure Autocatalytic cleavage Direct protein sequencing Host cytoplasm Hydrolase Methylation Protease Reference proteome Secreted Signal Thiol protease Toxin Virulence Zymogen | MNKKKLGVRL | MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP | evasion of host immune response programmed cell death induced by symbiont protein maturation proteolysis symbiont-mediated suppression of host autophagy cytosol; extracellular region; host cell cytosol; host extracellular space cysteine-type endopeptidase activity toxin activity Streptococcus pyogenes serotype M13D-structure Autocatalytic cleavage Direct protein sequencing Host cytoplasm Hydrolase Methylation Protease Reference proteome Secreted Signal Thiol protease Toxin Virulence Zymogen MNKKKLGVRL MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQIDKELSQNQPVYYQGVGKVGGHAFVIDGADGRNFYHVNWGWGGVSDGFFRLDALNPSALGTGGGAGGFNGYQSAVVGIKP |
phosphorylation | cytoplasm | ATP binding magnesium ion binding protein serine kinase activity protein serine/threonine kinase activity | Escherichia coli | 3D-structure ATP-binding Cytoplasm Kinase Magnesium Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Serine/threonine-protein kinase Stress response Transferase | MNNSAFTFQT | MNNSAFTFQTLHPDTIMDALFEHGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVNDEVPVAAPVAFNGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKQLFIHRPTIGLNEYLIEPRKLFEDATLIPSGLKAAFLKATDELIAAVTAHWREDFTVLRLHGDCHAGNILWRDGPMFVDLDDARNGPAVQDLWMLLNGDKAEQRMQLETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWADPAFPKNFPWLTGEDYWLRQTATFIEQAKVLQEPPLQLTPMY | phosphorylation cytoplasm ATP binding magnesium ion binding protein serine kinase activity protein serine/threonine kinase activity Escherichia coli 3D-structure ATP-binding Cytoplasm Kinase Magnesium Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Serine/threonine-protein kinase Stress response Transferase MNNSAFTFQT MNNSAFTFQTLHPDTIMDALFEHGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWTADQILEEHQFALQLVNDEVPVAAPVAFNGQTLLNHQGFYFAVFPSVGGRQFEADNIDQMEAVGRYLGRMHQTGRKQLFIHRPTIGLNEYLIEPRKLFEDATLIPSGLKAAFLKATDELIAAVTAHWREDFTVLRLHGDCHAGNILWRDGPMFVDLDDARNGPAVQDLWMLLNGDKAEQRMQLETIIEAYEEFSEFDTAEIGLIEPLRAMRLVYYLAWLMRRWADPAFPKNFPWLTGEDYWLRQTATFIEQAKVLQEPPLQLTPMY |
hyperosmotic response response to hydroperoxide response to oxidative stress | cytosol | peroxidase activity peroxiredoxin activity protein homodimerization activity | Escherichia coli | 3D-structure Acetylation Antioxidant Cytoplasm Direct protein sequencing Oxidoreductase Peroxidase Reference proteome | MTIHKKGQAH | MTIHKKGQAHWEGDIKRGKGTVSTESGVLNQQPYGFNTRFEGEKGTNPEELIGAAHAACFSMALSLMLGEAGFTPTSIDTTADVSLDKVDAGFAITKIALKSEVAVPGIDASTFDGIIQKAKAGCPVSQVLKAEITLDYQLKS | hyperosmotic response response to hydroperoxide response to oxidative stress cytosol peroxidase activity peroxiredoxin activity protein homodimerization activity Escherichia coli 3D-structure Acetylation Antioxidant Cytoplasm Direct protein sequencing Oxidoreductase Peroxidase Reference proteome MTIHKKGQAH MTIHKKGQAHWEGDIKRGKGTVSTESGVLNQQPYGFNTRFEGEKGTNPEELIGAAHAACFSMALSLMLGEAGFTPTSIDTTADVSLDKVDAGFAITKIALKSEVAVPGIDASTFDGIIQKAKAGCPVSQVLKAEITLDYQLKS |
amino acid transport cellular hyperosmotic response cellular hyperosmotic salinity response glycine betaine transport osmosensory signaling pathway proline import across plasma membrane | plasma membrane | proline:proton symporter activity protein homodimerization activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Coiled coil Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport | MLKRKKVKPI | MLKRKKVKPITLRDVTIIDDGKLRKAITAASLGNAMEWFDFGVYGFVAYALGKVFFPGADPSVQMVAALATFSVPFLIRPLGGLFFGMLGDKYGRQKILAITIVIMSISTFCIGLIPSYDTIGIWAPILLLICKMAQGFSVGGEYTGASIFVAEYSPDRKRGFMGSWLDFGSIAGFVLGAGVVVLISTIVGEANFLDWGWRIPFFIALPLGIIGLYLRHALEETPAFQQHVDKLEQGDREGLQDGPKVSFKEIATKYWRSLLTCIGLVIATNVTYYMLLTYMPSYLSHNLHYSEDHGVLIIIAIMIGMLFVQPVMGLLSDRFGRRPFVLLGSVALFVLAIPAFILINSNVIGLIFAGLLMLAVILNCFTGVMASTLPAMFPTHIRYSALAAAFNISVLVAGLTPTLAAWLVESSQNLMMPAYYLMVVAVVGLITGVTMKETANRPLKGATPAASDIQEAKEILVEHYDNIEQKIDDIDHEIADLQAKRTRLVQQHPRIDE | amino acid transport cellular hyperosmotic response cellular hyperosmotic salinity response glycine betaine transport osmosensory signaling pathway proline import across plasma membrane plasma membrane proline:proton symporter activity protein homodimerization activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Coiled coil Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport MLKRKKVKPI MLKRKKVKPITLRDVTIIDDGKLRKAITAASLGNAMEWFDFGVYGFVAYALGKVFFPGADPSVQMVAALATFSVPFLIRPLGGLFFGMLGDKYGRQKILAITIVIMSISTFCIGLIPSYDTIGIWAPILLLICKMAQGFSVGGEYTGASIFVAEYSPDRKRGFMGSWLDFGSIAGFVLGAGVVVLISTIVGEANFLDWGWRIPFFIALPLGIIGLYLRHALEETPAFQQHVDKLEQGDREGLQDGPKVSFKEIATKYWRSLLTCIGLVIATNVTYYMLLTYMPSYLSHNLHYSEDHGVLIIIAIMIGMLFVQPVMGLLSDRFGRRPFVLLGSVALFVLAIPAFILINSNVIGLIFAGLLMLAVILNCFTGVMASTLPAMFPTHIRYSALAAAFNISVLVAGLTPTLAAWLVESSQNLMMPAYYLMVVAVVGLITGVTMKETANRPLKGATPAASDIQEAKEILVEHYDNIEQKIDDIDHEIADLQAKRTRLVQQHPRIDE |
RNA methylation | cytosol | rRNA (uridine-2'-O-)-methyltransferase activity | Escherichia coli | 3D-structure Cytoplasm Methyltransferase Reference proteome rRNA processing S-adenosyl-L-methionine Stress response Transferase | MTGKKRSASS | MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYVVTQIGGKGRIIACDLLPMDPIVGVDFLQGDFRDELVMKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALEMCRDVLAPGGSFVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKP | RNA methylation cytosol rRNA (uridine-2'-O-)-methyltransferase activity Escherichia coli 3D-structure Cytoplasm Methyltransferase Reference proteome rRNA processing S-adenosyl-L-methionine Stress response Transferase MTGKKRSASS MTGKKRSASSSRWLQEHFSDKYVQQAQKKGLRSRAWFKLDEIQQSDKLFKPGMTVVDLGAAPGGWSQYVVTQIGGKGRIIACDLLPMDPIVGVDFLQGDFRDELVMKALLERVGDSKVQVVMSDMAPNMSGTPAVDIPRAMYLVELALEMCRDVLAPGGSFVVKVFQGEGFDEYLREIRSLFTKVKVRKPDSSRARSREVYIVATGRKP |
intracellular water homeostasis monoatomic ion transmembrane transport protein homooligomerization | membrane; plasma membrane | identical protein binding mechanosensitive monoatomic ion channel activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Ion channel Ion transport Membrane Reference proteome Transmembrane Transmembrane helix Transport | MEDLNVVDSI | MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRKIDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSREPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVWSNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA | intracellular water homeostasis monoatomic ion transmembrane transport protein homooligomerization membrane; plasma membrane identical protein binding mechanosensitive monoatomic ion channel activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Ion channel Ion transport Membrane Reference proteome Transmembrane Transmembrane helix Transport MEDLNVVDSI MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRKIDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSREPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVWSNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA |
cellular response to estradiol stimulus positive regulation of transcription by RNA polymerase II | euchromatin; heterochromatin; nucleosome; nucleus | DNA binding nucleosomal DNA binding protein heterodimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding structural constituent of chromatin | Bos taurus | Acetylation Chromosome Direct protein sequencing DNA-binding Isopeptide bond Methylation Nucleosome core Nucleus Reference proteome Ubl conjugation | MAGGKAGKDS | MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | cellular response to estradiol stimulus positive regulation of transcription by RNA polymerase II euchromatin; heterochromatin; nucleosome; nucleus DNA binding nucleosomal DNA binding protein heterodimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding structural constituent of chromatin Bos taurus Acetylation Chromosome Direct protein sequencing DNA-binding Isopeptide bond Methylation Nucleosome core Nucleus Reference proteome Ubl conjugation MAGGKAGKDS MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV |
cellular response to estradiol stimulus chromatin organization positive regulation of transcription by RNA polymerase II | euchromatin; extracellular exosome; heterochromatin; nucleosome; nucleus | chromatin DNA binding DNA binding nucleosomal DNA binding protein heterodimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding structural constituent of chromatin | Homo sapiens | 3D-structure Acetylation Chromosome DNA-binding Isopeptide bond Methylation Nucleosome core Nucleus Reference proteome Ubl conjugation | MAGGKAGKDS | MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | cellular response to estradiol stimulus chromatin organization positive regulation of transcription by RNA polymerase II euchromatin; extracellular exosome; heterochromatin; nucleosome; nucleus chromatin DNA binding DNA binding nucleosomal DNA binding protein heterodimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding structural constituent of chromatin Homo sapiens 3D-structure Acetylation Chromosome DNA-binding Isopeptide bond Methylation Nucleosome core Nucleus Reference proteome Ubl conjugation MAGGKAGKDS MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV |
cellular response to estradiol stimulus cellular response to insulin stimulus chromatin organization positive regulation of transcription by RNA polymerase II | euchromatin; heterochromatin; nucleosome; nucleus | chromatin DNA binding DNA binding nucleosomal DNA binding protein heterodimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding structural constituent of chromatin | Mus musculus | 3D-structure Acetylation Chromosome Developmental protein DNA-binding Isopeptide bond Methylation Nucleosome core Nucleus Reference proteome Ubl conjugation | MAGGKAGKDS | MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | cellular response to estradiol stimulus cellular response to insulin stimulus chromatin organization positive regulation of transcription by RNA polymerase II euchromatin; heterochromatin; nucleosome; nucleus chromatin DNA binding DNA binding nucleosomal DNA binding protein heterodimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding structural constituent of chromatin Mus musculus 3D-structure Acetylation Chromosome Developmental protein DNA-binding Isopeptide bond Methylation Nucleosome core Nucleus Reference proteome Ubl conjugation MAGGKAGKDS MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV |
cellular response to estradiol stimulus cellular response to insulin stimulus positive regulation of transcription by RNA polymerase II | euchromatin; heterochromatin; nucleosome; nucleus | chromatin DNA binding DNA binding nucleosomal DNA binding protein heterodimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding structural constituent of chromatin | Rattus norvegicus | Acetylation Chromosome DNA-binding Isopeptide bond Methylation Nucleosome core Nucleus Reference proteome Ubl conjugation | MAGGKAGKDS | MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | cellular response to estradiol stimulus cellular response to insulin stimulus positive regulation of transcription by RNA polymerase II euchromatin; heterochromatin; nucleosome; nucleus chromatin DNA binding DNA binding nucleosomal DNA binding protein heterodimerization activity RNA polymerase II cis-regulatory region sequence-specific DNA binding RNA polymerase II core promoter sequence-specific DNA binding structural constituent of chromatin Rattus norvegicus Acetylation Chromosome DNA-binding Isopeptide bond Methylation Nucleosome core Nucleus Reference proteome Ubl conjugation MAGGKAGKDS MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV |
cellular response to lipopolysaccharide negative regulation of non-canonical NF-kappaB signal transduction positive regulation of canonical NF-kappaB signal transduction positive regulation of transcription by RNA polymerase II regulation of cytokine production regulation of macrophage cytokine production response to lipopolysaccharide | cytoplasmic side of early endosome membrane; cytoplasmic side of late endosome membrane; cytoplasmic side of lysosomal membrane; cytoplasmic side of plasma membrane; extracellular region; Golgi apparatus; Golgi membrane; lysosomal membrane; nucleus; plasma membrane | DNA-binding transcription activator activity, RNA polymerase II-specific identical protein binding RNA polymerase II cis-regulatory region sequence-specific DNA binding WW domain binding zinc ion binding | Rattus norvegicus | Cell membrane Cytoplasm DNA-binding Endosome Golgi apparatus Lysosome Membrane Metal-binding Nucleus Reference proteome Transcription Transcription regulation Zinc | MSAPGPYQAA | MSAPGPYQAAAGPSVMPTAPPTYEETVGVNSYYPTPPAPQPGPATGLITGPDGKGMNPPSYYTQPVPVPNANAIAVQTVYVQQPISFYDRPIQMCCPSCNKMIVTQLSYNAGALTWLSCGSLCLLGCVAGCCFIPFCVDALQDVDHYCPNCKALLGTYKRL | cellular response to lipopolysaccharide negative regulation of non-canonical NF-kappaB signal transduction positive regulation of canonical NF-kappaB signal transduction positive regulation of transcription by RNA polymerase II regulation of cytokine production regulation of macrophage cytokine production response to lipopolysaccharide cytoplasmic side of early endosome membrane; cytoplasmic side of late endosome membrane; cytoplasmic side of lysosomal membrane; cytoplasmic side of plasma membrane; extracellular region; Golgi apparatus; Golgi membrane; lysosomal membrane; nucleus; plasma membrane DNA-binding transcription activator activity, RNA polymerase II-specific identical protein binding RNA polymerase II cis-regulatory region sequence-specific DNA binding WW domain binding zinc ion binding Rattus norvegicus Cell membrane Cytoplasm DNA-binding Endosome Golgi apparatus Lysosome Membrane Metal-binding Nucleus Reference proteome Transcription Transcription regulation Zinc MSAPGPYQAA MSAPGPYQAAAGPSVMPTAPPTYEETVGVNSYYPTPPAPQPGPATGLITGPDGKGMNPPSYYTQPVPVPNANAIAVQTVYVQQPISFYDRPIQMCCPSCNKMIVTQLSYNAGALTWLSCGSLCLLGCVAGCCFIPFCVDALQDVDHYCPNCKALLGTYKRL |
inositol trisphosphate metabolic process necroptotic process neural tube development phosphorylation | apical plasma membrane | ATP binding hydrolase activity inositol tetrakisphosphate 1-kinase activity inositol tetrakisphosphate 6-kinase activity inositol-1,3,4-trisphosphate 5-kinase activity inositol-1,3,4-trisphosphate 6-kinase activity inositol-3,4,6-trisphosphate 1-kinase activity isomerase activity magnesium ion binding | Bos taurus | Acetylation ATP-binding Direct protein sequencing Hydrolase Isomerase Kinase Magnesium Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Transferase | MQTFLKGKRV | MQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGIEVVQLNLSRPIEEQGPLDVIIHKLTDVILEADQNDSQALELVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYMKDDRICSPPFMELTSLCGDDTMRLLEENGLAFPFICKTRVAHGTNSHEMAIVFNQEGLSAIQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVSKPESSSVLTALDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFPGYEGVSEFFTDLLNHIASVLQGQSSGVAGAGDVAPLKHSRLLAEQAGGLAAERTCSASPGCCSSMMGQEPPWTPEADMGGVGAGSTAKLPHQRLGCTAGVSPSFQQHCVASLATKASSQ | inositol trisphosphate metabolic process necroptotic process neural tube development phosphorylation apical plasma membrane ATP binding hydrolase activity inositol tetrakisphosphate 1-kinase activity inositol tetrakisphosphate 6-kinase activity inositol-1,3,4-trisphosphate 5-kinase activity inositol-1,3,4-trisphosphate 6-kinase activity inositol-3,4,6-trisphosphate 1-kinase activity isomerase activity magnesium ion binding Bos taurus Acetylation ATP-binding Direct protein sequencing Hydrolase Isomerase Kinase Magnesium Metal-binding Nucleotide-binding Phosphoprotein Reference proteome Transferase MQTFLKGKRV MQTFLKGKRVGYWLSEKKIKKLNFQAFAELCRKRGIEVVQLNLSRPIEEQGPLDVIIHKLTDVILEADQNDSQALELVHRFQEYIDAHPETIVLDPLPAIRTLLDRSKSYELIRKIEAYMKDDRICSPPFMELTSLCGDDTMRLLEENGLAFPFICKTRVAHGTNSHEMAIVFNQEGLSAIQPPCVVQNFINHNAVLYKVFVVGESYTVVQRPSLKNFSAGTSDRESIFFNSHNVSKPESSSVLTALDKIEGVFERPSDEVIRELSRALRQALGVSLFGIDIIINNQTGQHAVIDINAFPGYEGVSEFFTDLLNHIASVLQGQSSGVAGAGDVAPLKHSRLLAEQAGGLAAERTCSASPGCCSSMMGQEPPWTPEADMGGVGAGSTAKLPHQRLGCTAGVSPSFQQHCVASLATKASSQ |
determination of left/right symmetry heart development in utero embryonic development innate immune response kidney development | ciliary inversin compartment; cytoplasm | identical protein binding | Rattus norvegicus | ANK repeat Cell projection Cilium Cytoplasm Disease variant Hydroxylation Phosphoprotein Reference proteome Repeat | MGEGALAPGL | MGEGALAPGLQLLLRACEQGDTDTARRLLEPGGEPVAGSEAGAEPAGPEAARAVEAGTPVPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGESTASGGSRDELLGITALMAAVQHGHEAVVRLLMEWGADPNHTARTVGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYLDPLTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIADEDPNHVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADMNKQDSVHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVRLLASVCMQVNKDRGGRPSHRPPLPHSKARQPWSIPMLPDDKGGLKSWWSRMSNRFRKLKLMQTLPRGLAANQPLPFSDEPELALDSTMRAPPQDRTNHLGPPEAAHAAKDSGPGNPRREKDDVLLTTMLRNGAPFPRLPSDKLKAVIPPFLPPSSFELWSSDRSRTCPNGKADPMKTVLPPRASRAHPVGCVGTDGAAGRPVKFPSISRSPTSPASSGNFNHSPHSSGGASGVGSMSRLGGELHNRSGGSVDSVLSQIAAQRKKAAGLCEQKPPCQQSSPVGPATGSSPPELPASLLGSGSGSSNVTSSSKKLDPGKRPPSGTSATSKSTSPTLTPSPSPKGHTAESSVSSSSSHRQSKSSGGSSSGTITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNAGKGRERQILQETIHNFHSSFESSASNTRAPGNSPCMAGWVRPEETVSSRR | determination of left/right symmetry heart development in utero embryonic development innate immune response kidney development ciliary inversin compartment; cytoplasm identical protein binding Rattus norvegicus ANK repeat Cell projection Cilium Cytoplasm Disease variant Hydroxylation Phosphoprotein Reference proteome Repeat MGEGALAPGL MGEGALAPGLQLLLRACEQGDTDTARRLLEPGGEPVAGSEAGAEPAGPEAARAVEAGTPVPVDCSDEAGNSALQLAAAGGHEPLVRFLLRRGASVNSRNHYGWSALMQAARCGHASVAHLLLDHGADVNAQNRLGASVLTVASRGGHLGVVKLLLEAGATVDHRNPSGESTASGGSRDELLGITALMAAVQHGHEAVVRLLMEWGADPNHTARTVGWSPLMLAALLGKLSVVQQLVEKGANPDHLGVLEKTAFEVALDRKHRDLADYLDPLTTVRPKTDEEKRRPDIFHALKMGNFQLVKEIADEDPNHVNLVNGDGATPLMLAAVTGQLPLVQLLVEKHADMNKQDSVHGWTALMQATYHGNKEIVKYLLNQGADVTLRAKNGYTAFDLVMLLNDPDTELVRLLASVCMQVNKDRGGRPSHRPPLPHSKARQPWSIPMLPDDKGGLKSWWSRMSNRFRKLKLMQTLPRGLAANQPLPFSDEPELALDSTMRAPPQDRTNHLGPPEAAHAAKDSGPGNPRREKDDVLLTTMLRNGAPFPRLPSDKLKAVIPPFLPPSSFELWSSDRSRTCPNGKADPMKTVLPPRASRAHPVGCVGTDGAAGRPVKFPSISRSPTSPASSGNFNHSPHSSGGASGVGSMSRLGGELHNRSGGSVDSVLSQIAAQRKKAAGLCEQKPPCQQSSPVGPATGSSPPELPASLLGSGSGSSNVTSSSKKLDPGKRPPSGTSATSKSTSPTLTPSPSPKGHTAESSVSSSSSHRQSKSSGGSSSGTITDEDELTGILKKLSLEKYQPIFEEQEVDMEAFLTLTDGDLQELGIKTDGSRQQILAAISELNAGKGRERQILQETIHNFHSSFESSASNTRAPGNSPCMAGWVRPEETVSSRR |
cytoplasmic translation | cytosol; cytosolic small ribosomal subunit | structural constituent of ribosome | Saccharomyces cerevisiae | Cytoplasm Direct protein sequencing Methylation Reference proteome Ribonucleoprotein Ribosomal protein | MPPKQQLSKA | MPPKQQLSKAAKAAAALAGGKKSKKKWSKKSMKDRAQHAVILDQEKYDRILKEVPTYRYVSVSVLVDRLKIGGSLARIALRHLEKEGIIKPISKHSKQAIYTRAAASE | cytoplasmic translation cytosol; cytosolic small ribosomal subunit structural constituent of ribosome Saccharomyces cerevisiae Cytoplasm Direct protein sequencing Methylation Reference proteome Ribonucleoprotein Ribosomal protein MPPKQQLSKA MPPKQQLSKAAKAAAALAGGKKSKKKWSKKSMKDRAQHAVILDQEKYDRILKEVPTYRYVSVSVLVDRLKIGGSLARIALRHLEKEGIIKPISKHSKQAIYTRAAASE |
peptidoglycan biosynthetic process peptidoglycan metabolic process proteolysis response to xenobiotic stimulus | outer membrane-bounded periplasmic space | endopeptidase activity metal ion binding metalloendopeptidase activity peptidase activity serine-type endopeptidase activity | Escherichia coli | 3D-structure Direct protein sequencing Disulfide bond Hydrolase Metal-binding Metalloprotease Periplasm Protease Reference proteome Signal Zinc | MNKTAIALLA | MNKTAIALLALLASSASLAATPWQKITQPVPGSAQSIGSFSNGCIVGADTLPIQSEHYQVMRTDQRRYFGHPDLVMFIQRLSSQVSNLGMGTVLIGDMGMPAGGRFNGGHASHQTGLDVDIFLQLPKTRWTSAQLLRPQALDLVSRDGKHVVSTLWKPEIFSLIKLAAQDKDVTRIFVNPAIKQQLCLDAGTDRDWLRKVRPWFQHRAHMHVRLRCPADSLECEDQPLPPSGDGCGAELQSWFEPPKPGTTKPEKKTPPPLPPSCQALLDEHVI | peptidoglycan biosynthetic process peptidoglycan metabolic process proteolysis response to xenobiotic stimulus outer membrane-bounded periplasmic space endopeptidase activity metal ion binding metalloendopeptidase activity peptidase activity serine-type endopeptidase activity Escherichia coli 3D-structure Direct protein sequencing Disulfide bond Hydrolase Metal-binding Metalloprotease Periplasm Protease Reference proteome Signal Zinc MNKTAIALLA MNKTAIALLALLASSASLAATPWQKITQPVPGSAQSIGSFSNGCIVGADTLPIQSEHYQVMRTDQRRYFGHPDLVMFIQRLSSQVSNLGMGTVLIGDMGMPAGGRFNGGHASHQTGLDVDIFLQLPKTRWTSAQLLRPQALDLVSRDGKHVVSTLWKPEIFSLIKLAAQDKDVTRIFVNPAIKQQLCLDAGTDRDWLRKVRPWFQHRAHMHVRLRCPADSLECEDQPLPPSGDGCGAELQSWFEPPKPGTTKPEKKTPPPLPPSCQALLDEHVI |
chaperone-mediated protein folding protein folding protein quality control for misfolded or incompletely synthesized proteins proteolysis response to heat response to oxidative stress response to temperature stimulus | outer membrane-bounded periplasmic space; periplasmic space; plasma membrane | identical protein binding peptidase activity serine-type endopeptidase activity serine-type peptidase activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Direct protein sequencing Disulfide bond Hydrolase Membrane Protease Reference proteome Repeat Serine protease Signal Stress response | MKKTTLALSA | MKKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ | chaperone-mediated protein folding protein folding protein quality control for misfolded or incompletely synthesized proteins proteolysis response to heat response to oxidative stress response to temperature stimulus outer membrane-bounded periplasmic space; periplasmic space; plasma membrane identical protein binding peptidase activity serine-type endopeptidase activity serine-type peptidase activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Direct protein sequencing Disulfide bond Hydrolase Membrane Protease Reference proteome Repeat Serine protease Signal Stress response MKKTTLALSA MKKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ |
endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) translation | cytosol; cytosolic small ribosomal subunit | structural constituent of ribosome | Saccharomyces cerevisiae | 3D-structure Acetylation Cytoplasm Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein rRNA processing | MENDKGQLVE | MENDKGQLVELYVPRKCSATNRIIKADDHASVQINVAKVDEEGRAIPGEYVTYALSGYVRSRGESDDSLNRLAQNDGLLKNVWSYSR | endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) translation cytosol; cytosolic small ribosomal subunit structural constituent of ribosome Saccharomyces cerevisiae 3D-structure Acetylation Cytoplasm Direct protein sequencing Reference proteome Ribonucleoprotein Ribosomal protein rRNA processing MENDKGQLVE MENDKGQLVELYVPRKCSATNRIIKADDHASVQINVAKVDEEGRAIPGEYVTYALSGYVRSRGESDDSLNRLAQNDGLLKNVWSYSR |
fusion of virus membrane with host plasma membrane | host cell plasma membrane; membrane; viral envelope; virion membrane | carbohydrate binding host cell surface receptor binding sialate 4-O-acetylesterase activity sialate 9-O-acetylesterase activity sialate O-acetylesterase activity | Breda virus 1 | 3D-structure Disulfide bond Glycoprotein Hemagglutinin Host cell membrane Host membrane Hydrolase Membrane Reference proteome Signal Transmembrane Transmembrane helix Viral envelope protein Virion | MLSLILFFPS | MLSLILFFPSFAFAATPVTPYYGPGHITFDWCGFGDSRSDCTNPQSPMSLDIPQQLCPKFSSKSSSSMFLSLHWNNHSSFVSYDYFNCGVEKVFYEGVNFSPRKQYSCWDEGVDGWIELKTRFYTKLYQMATTSRCIKLIQLQAPSSLPTLQAGVCRTNKQLPDNPRLALLSDTVPTSVQFVLPGSSGTTICTKHLVPFCYLNHGCFTTGGSCLPFGVSYVSDSFYYGYYDATPQIGSTESHDYVCDYLFMEPGTYNASTVGKFLVYPTKSYCMDTMNITVPVQAVQSIWSEQYASDDAIGQACKAPYCIFYNKTTPYTVTNGSDANHGDDEVRMMMQGLLRNSSCISPQGSTPLALYSTEMIYEPNYGSCPQFYKLFDTSGNENIDVISSSYFVATWVLLVVVVILIFVIISFFC | fusion of virus membrane with host plasma membrane host cell plasma membrane; membrane; viral envelope; virion membrane carbohydrate binding host cell surface receptor binding sialate 4-O-acetylesterase activity sialate 9-O-acetylesterase activity sialate O-acetylesterase activity Breda virus 1 3D-structure Disulfide bond Glycoprotein Hemagglutinin Host cell membrane Host membrane Hydrolase Membrane Reference proteome Signal Transmembrane Transmembrane helix Viral envelope protein Virion MLSLILFFPS MLSLILFFPSFAFAATPVTPYYGPGHITFDWCGFGDSRSDCTNPQSPMSLDIPQQLCPKFSSKSSSSMFLSLHWNNHSSFVSYDYFNCGVEKVFYEGVNFSPRKQYSCWDEGVDGWIELKTRFYTKLYQMATTSRCIKLIQLQAPSSLPTLQAGVCRTNKQLPDNPRLALLSDTVPTSVQFVLPGSSGTTICTKHLVPFCYLNHGCFTTGGSCLPFGVSYVSDSFYYGYYDATPQIGSTESHDYVCDYLFMEPGTYNASTVGKFLVYPTKSYCMDTMNITVPVQAVQSIWSEQYASDDAIGQACKAPYCIFYNKTTPYTVTNGSDANHGDDEVRMMMQGLLRNSSCISPQGSTPLALYSTEMIYEPNYGSCPQFYKLFDTSGNENIDVISSSYFVATWVLLVVVVILIFVIISFFC |
cytoplasmic translation ribosomal large subunit assembly | cytosol; cytosolic large ribosomal subunit; nucleus | RNA binding rRNA binding structural constituent of ribosome | Saccharomyces cerevisiae | 3D-structure Acetylation Cytoplasm Direct protein sequencing Methylation Nucleus Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding | MSAKAQNPMR | MSAKAQNPMRDLKIEKLVLNISVGESGDRLTRASKVLEQLSGQTPVQSKARYTVRTFGIRRNEKIAVHVTVRGPKAEEILERGLKVKEYQLRDRNFSATGNFGFGIDEHIDLGIKYDPSIGIFGMDFYVVMNRPGARVTRRKRCKGTVGNSHKTTKEDTVSWFKQKYDADVLDK | cytoplasmic translation ribosomal large subunit assembly cytosol; cytosolic large ribosomal subunit; nucleus RNA binding rRNA binding structural constituent of ribosome Saccharomyces cerevisiae 3D-structure Acetylation Cytoplasm Direct protein sequencing Methylation Nucleus Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding MSAKAQNPMR MSAKAQNPMRDLKIEKLVLNISVGESGDRLTRASKVLEQLSGQTPVQSKARYTVRTFGIRRNEKIAVHVTVRGPKAEEILERGLKVKEYQLRDRNFSATGNFGFGIDEHIDLGIKYDPSIGIFGMDFYVVMNRPGARVTRRKRCKGTVGNSHKTTKEDTVSWFKQKYDADVLDK |
cytoplasmic translation maturation of SSU-rRNA positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay ribosomal small subunit assembly rRNA export from nucleus | cytosol; cytosolic small ribosomal subunit | structural constituent of ribosome | Saccharomyces cerevisiae | 3D-structure Acetylation Cytoplasm Reference proteome Ribonucleoprotein Ribosomal protein | MDSKTPVTLA | MDSKTPVTLAKVIKVLGRTGSRGGVTQVRVEFLEDTSRTIVRNVKGPVRENDILVLMESEREARRLR | cytoplasmic translation maturation of SSU-rRNA positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay ribosomal small subunit assembly rRNA export from nucleus cytosol; cytosolic small ribosomal subunit structural constituent of ribosome Saccharomyces cerevisiae 3D-structure Acetylation Cytoplasm Reference proteome Ribonucleoprotein Ribosomal protein MDSKTPVTLA MDSKTPVTLAKVIKVLGRTGSRGGVTQVRVEFLEDTSRTIVRNVKGPVRENDILVLMESEREARRLR |
chaperone cofactor-dependent protein refolding protein refolding response to heat | GroEL-GroES complex | ATP binding ATP-dependent protein folding chaperone isomerase activity unfolded protein binding | Chlamydia trachomatis | ATP-binding Chaperone Cytoplasm Direct protein sequencing Isomerase Nucleotide-binding Reference proteome Stress response | MVAKNIKYNE | MVAKNIKYNEEARKKIQKGVKTLAEAVKVTLGPKGRHVVIDKSFGSPQVTKDGVTVAKEVELADKHENMGAQMVKEVASKTADKAGDGTTTATVLAEAIYTEGLRNVTAGANPMDLKRGIDKAVKVVVDQIRKISKPVQHHKEIAQVATISANNDAEIGNLIAEAMEKVGKNGSITVEEAKGFETVLDIVEGMNFNRGYLSSYFATNPETQECVLEDALVLIYDKKISGIKDFLPVLQQVAESGRPLLIIAEDIEGEALATLVVNRIRGGFRVCAVKAPGFGDRRKAMLEDIAILTGGQLISEELGMKLENANLAMLGKAKKVIVSKEDTTIVEGMGEKEALEARCESIKKQIEDSSSDYDKEKLQERLAKLSGGVAVIRVGAATEIEMKEKKDRVDDAQHATIAAVEEGILPGGGTALIRCIPTLEAFLPMLTNEDEQIGARIVLKALSAPLKQIAANAGKEGAIIFQQVMSRSANEGYDALRDAYTDMLEAGILDPAKVTRSALESAASVAGLLLTTEALIAEIPEEKPAAAPAMPGAGMDY | chaperone cofactor-dependent protein refolding protein refolding response to heat GroEL-GroES complex ATP binding ATP-dependent protein folding chaperone isomerase activity unfolded protein binding Chlamydia trachomatis ATP-binding Chaperone Cytoplasm Direct protein sequencing Isomerase Nucleotide-binding Reference proteome Stress response MVAKNIKYNE MVAKNIKYNEEARKKIQKGVKTLAEAVKVTLGPKGRHVVIDKSFGSPQVTKDGVTVAKEVELADKHENMGAQMVKEVASKTADKAGDGTTTATVLAEAIYTEGLRNVTAGANPMDLKRGIDKAVKVVVDQIRKISKPVQHHKEIAQVATISANNDAEIGNLIAEAMEKVGKNGSITVEEAKGFETVLDIVEGMNFNRGYLSSYFATNPETQECVLEDALVLIYDKKISGIKDFLPVLQQVAESGRPLLIIAEDIEGEALATLVVNRIRGGFRVCAVKAPGFGDRRKAMLEDIAILTGGQLISEELGMKLENANLAMLGKAKKVIVSKEDTTIVEGMGEKEALEARCESIKKQIEDSSSDYDKEKLQERLAKLSGGVAVIRVGAATEIEMKEKKDRVDDAQHATIAAVEEGILPGGGTALIRCIPTLEAFLPMLTNEDEQIGARIVLKALSAPLKQIAANAGKEGAIIFQQVMSRSANEGYDALRDAYTDMLEAGILDPAKVTRSALESAASVAGLLLTTEALIAEIPEEKPAAAPAMPGAGMDY |
branching morphogenesis of an epithelial tube cilium assembly determination of left/right symmetry epithelial tube branching involved in lung morphogenesis head development heart development kidney development negative regulation of centrosome duplication non-canonical Wnt signaling pathway photoreceptor cell outer segment organization positive regulation of ERAD pathway positive regulation of non-motile cilium assembly ubiquitin-dependent ERAD pathway | centrosome; ciliary membrane; ciliary transition zone; cytoplasmic vesicle membrane; endoplasmic reticulum membrane; MKS complex | filamin binding misfolded protein binding unfolded protein binding | Rattus norvegicus | Cell membrane Cell projection Cilium Cilium biogenesis/degradation Cytoplasm Cytoskeleton Disease variant Disulfide bond Endoplasmic reticulum Glycoprotein Membrane Reference proteome Signal Transmembrane Transmembrane helix | MVMRTRPLAA | MVMRTRPLAAMAVRSCFSALTGTVYLLLVLCEVSWAQIFSFPFQRPETCDLNQYFDISALSCAPCGANQRRDALGTSCICLPGYHMISNNGGPSIICKKCPENMKGVTKDGWDCISCPNGLTAEGKCHCPSGHILVERNVSGSLLSQATCELCDGNENSFTKPNALGTRCVRCEPTFVNTSRSCSCSEPHISTGGLCFSNTGNFPQRLISTERYGELGMSSNSEWFTKYLQATAAACWTHSNLTSCQALGNMCVMNMNSYDSTTFDACRLFHYVFEGAAGLTGVHSVPFWRQNLPWLFYGDQPGLASQVLSTTPLPTNFSFKGQNQLKFVAASYDIRGNFIRWQTVKGGVLQLCPDTERRLDAAYSFGTTYQQNCEISLSKLLADFPSPVFYDIYLEYTDEVQHHYLWAIPVLNLNLQHNKLFVNQDSSSSKWLLTRRIFLVDAVSGRENDLGNQPRVIRVATQISLSIRLVPNTKNGNIYTPLLTIAYSDIDIKNAYSQSVKISFSVKYEMNQGDAFVQTDIALGVLGGLAVLSSLLKTAGWKRRIGSPMIDLQTVMKFLLYYAGDLANVFFIITVGTGLYWLIFFKAQKSVSVLLPMPVQEERFVTYVGCAFAMKALQFLHKLISQITIDIFFIDWERPKGKVLKAVEGEGGVRSATVPVSIWRTYFVANEWNEIQTVRKINPLFQVLTTLFFLEVVGFKNLALMDPSSSLSRSLSDYAAPYSRILRYAVATTIWLVIGIVQVVFFAAFYERFIEDKIRQFVDLCSMSNVSVFLLSHRCFGYYIHGRSVHGHADTNMEDMNMNLRREAENLCSQRGLVPNTDGQTFQIAVSSQMRQHYDRIHETLTRRNGPARLLSSSGSTLEQSIKAYHAMNKFLGSFIDHVHKEMDYFIKDKLLLEKILGMEFMEPLEKSIFYNDESHSFSSVLYYGNEATLLIFDLLFFCVVDLACQNFVLASFLTYLQQEIFRFIRNTVGQKNLATKTLVDERFLI | branching morphogenesis of an epithelial tube cilium assembly determination of left/right symmetry epithelial tube branching involved in lung morphogenesis head development heart development kidney development negative regulation of centrosome duplication non-canonical Wnt signaling pathway photoreceptor cell outer segment organization positive regulation of ERAD pathway positive regulation of non-motile cilium assembly ubiquitin-dependent ERAD pathway centrosome; ciliary membrane; ciliary transition zone; cytoplasmic vesicle membrane; endoplasmic reticulum membrane; MKS complex filamin binding misfolded protein binding unfolded protein binding Rattus norvegicus Cell membrane Cell projection Cilium Cilium biogenesis/degradation Cytoplasm Cytoskeleton Disease variant Disulfide bond Endoplasmic reticulum Glycoprotein Membrane Reference proteome Signal Transmembrane Transmembrane helix MVMRTRPLAA MVMRTRPLAAMAVRSCFSALTGTVYLLLVLCEVSWAQIFSFPFQRPETCDLNQYFDISALSCAPCGANQRRDALGTSCICLPGYHMISNNGGPSIICKKCPENMKGVTKDGWDCISCPNGLTAEGKCHCPSGHILVERNVSGSLLSQATCELCDGNENSFTKPNALGTRCVRCEPTFVNTSRSCSCSEPHISTGGLCFSNTGNFPQRLISTERYGELGMSSNSEWFTKYLQATAAACWTHSNLTSCQALGNMCVMNMNSYDSTTFDACRLFHYVFEGAAGLTGVHSVPFWRQNLPWLFYGDQPGLASQVLSTTPLPTNFSFKGQNQLKFVAASYDIRGNFIRWQTVKGGVLQLCPDTERRLDAAYSFGTTYQQNCEISLSKLLADFPSPVFYDIYLEYTDEVQHHYLWAIPVLNLNLQHNKLFVNQDSSSSKWLLTRRIFLVDAVSGRENDLGNQPRVIRVATQISLSIRLVPNTKNGNIYTPLLTIAYSDIDIKNAYSQSVKISFSVKYEMNQGDAFVQTDIALGVLGGLAVLSSLLKTAGWKRRIGSPMIDLQTVMKFLLYYAGDLANVFFIITVGTGLYWLIFFKAQKSVSVLLPMPVQEERFVTYVGCAFAMKALQFLHKLISQITIDIFFIDWERPKGKVLKAVEGEGGVRSATVPVSIWRTYFVANEWNEIQTVRKINPLFQVLTTLFFLEVVGFKNLALMDPSSSLSRSLSDYAAPYSRILRYAVATTIWLVIGIVQVVFFAAFYERFIEDKIRQFVDLCSMSNVSVFLLSHRCFGYYIHGRSVHGHADTNMEDMNMNLRREAENLCSQRGLVPNTDGQTFQIAVSSQMRQHYDRIHETLTRRNGPARLLSSSGSTLEQSIKAYHAMNKFLGSFIDHVHKEMDYFIKDKLLLEKILGMEFMEPLEKSIFYNDESHSFSSVLYYGNEATLLIFDLLFFCVVDLACQNFVLASFLTYLQQEIFRFIRNTVGQKNLATKTLVDERFLI |
collagen-activated signaling pathway collagen-activated tyrosine kinase receptor signaling pathway platelet aggregation | cell surface; membrane raft; plasma membrane; tetraspanin-enriched microdomain | collagen binding collagen receptor activity protein tyrosine kinase binding | Mus musculus | Blood coagulation Cell membrane Disulfide bond Glycoprotein Hemostasis Immunoglobulin domain Membrane Receptor Reference proteome Repeat Signal Transmembrane Transmembrane helix | MSPASPTFFC | MSPASPTFFCIGLCVLQVIQTQSGPLPKPSLQAQPSSLVPLGQSVILRCQGPPDVDLYRLEKLKPEKYEDQDFLFIPTMERSNAGRYRCSYQNGSHWSLPSDQLELIATGVYAKPSLSAHPSSAVPQGRDVTLKCQSPYSFDEFVLYKEGDTGSYKRPEKWYRANFPIITVTAAHSGTYRCYSFSSSSPYLWSAPSDPLVLVVTGLSATPSQVPTEESFPVTESSRRPSILPTNKISTTEKPMNITASPEGLSPPFGFAHQHYAKGNLVRICLGATIIIILLGLLAEDWHSRKKCLQHRMRALQRPLPPLPLA | collagen-activated signaling pathway collagen-activated tyrosine kinase receptor signaling pathway platelet aggregation cell surface; membrane raft; plasma membrane; tetraspanin-enriched microdomain collagen binding collagen receptor activity protein tyrosine kinase binding Mus musculus Blood coagulation Cell membrane Disulfide bond Glycoprotein Hemostasis Immunoglobulin domain Membrane Receptor Reference proteome Repeat Signal Transmembrane Transmembrane helix MSPASPTFFC MSPASPTFFCIGLCVLQVIQTQSGPLPKPSLQAQPSSLVPLGQSVILRCQGPPDVDLYRLEKLKPEKYEDQDFLFIPTMERSNAGRYRCSYQNGSHWSLPSDQLELIATGVYAKPSLSAHPSSAVPQGRDVTLKCQSPYSFDEFVLYKEGDTGSYKRPEKWYRANFPIITVTAAHSGTYRCYSFSSSSPYLWSAPSDPLVLVVTGLSATPSQVPTEESFPVTESSRRPSILPTNKISTTEKPMNITASPEGLSPPFGFAHQHYAKGNLVRICLGATIIIILLGLLAEDWHSRKKCLQHRMRALQRPLPPLPLA |
positive regulation of synapse assembly regulation of postsynaptic density assembly regulation of presynapse assembly synaptic membrane adhesion | cerebellar mossy fiber; glutamatergic synapse; plasma membrane; postsynaptic density membrane; presynaptic membrane | signaling receptor binding | Mus musculus | 3D-structure Cell membrane Cell projection Disulfide bond Glycoprotein Immunoglobulin domain Leucine-rich repeat Membrane Phosphoprotein Reference proteome Repeat Signal Synapse Transmembrane Transmembrane helix | MAQAHIRGSP | MAQAHIRGSPCPLLPPGRMSWPHGALLLLWLFSPPLRAGGGGVAVTSAAGGGSPPATSCPAACSCSNQASRVICTRRELAEVPASIPVNTRYLNLQENSIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDLGELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCDVLWLSWWLKETVPSNTTCCARCHAPAGLKGRYIGELDQSHFTCYAPVIVEPPTDLNVTEGMAAELKCRTGTSMTSVNWLTPNGTLMTHGSYRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNVSAVDPVAAGGPGGGGPGGGGGAGGAGGYTYFTTVTVETLETQPGEEAQQPRGTEKEPPGPTTDGAWGGGRPDAAAPASASTTAPAPRSSRPTEKAFTVPITDVTENALKDLDDVMKTTKIIIGCFVAITFMAAVMLVAFYKLRKQHQLHKHHGPTRTVEIINVEDELPAASAVSVAAAAAVAGGAGVGGDSHLALPALERDHLNHHHYVAAAFKAHYGGNPGGGCGAKGPGLNSIHEPLLFKSGSKENVQETQI | positive regulation of synapse assembly regulation of postsynaptic density assembly regulation of presynapse assembly synaptic membrane adhesion cerebellar mossy fiber; glutamatergic synapse; plasma membrane; postsynaptic density membrane; presynaptic membrane signaling receptor binding Mus musculus 3D-structure Cell membrane Cell projection Disulfide bond Glycoprotein Immunoglobulin domain Leucine-rich repeat Membrane Phosphoprotein Reference proteome Repeat Signal Synapse Transmembrane Transmembrane helix MAQAHIRGSP MAQAHIRGSPCPLLPPGRMSWPHGALLLLWLFSPPLRAGGGGVAVTSAAGGGSPPATSCPAACSCSNQASRVICTRRELAEVPASIPVNTRYLNLQENSIQVIRTDTFKHLRHLEILQLSKNLVRKIEVGAFNGLPSLNTLELFDNRLTTVPTQAFEYLSKLRELWLRNNPIESIPSYAFNRVPSLRRLDLGELKRLEYISEAAFEGLVNLRYLNLGMCNLKDIPNLTALVRLEELELSGNRLDLIRPGSFQGLTSLRKLWLMHAQVATIERNAFDDLKSLEELNLSHNNLMSLPHDLFTPLHRLERVHLNHNPWHCNCDVLWLSWWLKETVPSNTTCCARCHAPAGLKGRYIGELDQSHFTCYAPVIVEPPTDLNVTEGMAAELKCRTGTSMTSVNWLTPNGTLMTHGSYRVRISVLHDGTLNFTNVTVQDTGQYTCMVTNSAGNTTASATLNVSAVDPVAAGGPGGGGPGGGGGAGGAGGYTYFTTVTVETLETQPGEEAQQPRGTEKEPPGPTTDGAWGGGRPDAAAPASASTTAPAPRSSRPTEKAFTVPITDVTENALKDLDDVMKTTKIIIGCFVAITFMAAVMLVAFYKLRKQHQLHKHHGPTRTVEIINVEDELPAASAVSVAAAAAVAGGAGVGGDSHLALPALERDHLNHHHYVAAAFKAHYGGNPGGGCGAKGPGLNSIHEPLLFKSGSKENVQETQI |
pectin catabolic process symbiont-mediated disruption of host cell wall | extracellular region | metal ion binding pectate lyase activity | Dickeya dadantii ) | 3D-structure Calcium Disulfide bond Lyase Metal-binding Reference proteome Secreted Signal Virulence | MKYLNCFIST | MKYLNCFISTGLAAFFLVNSTSVLAADCSSDLTSGISTKRIYYVAPNGNSSNNGSSFNAPMSFSAAMAAVNPGELILLKPGTYTIPYTQGKGNTITFNKSGKDGAPIYVAAANCGRAVFDFSFPDSQWVQASYGFYVTGDYWYFKGVEVTRAGYQGAYVIGSHNTFENTAFHHNRNTGLEINNGGSYNTVINSDAYRNYDPKKNGSMADGFGPKQKQGPGNRFVGCRAWENSDDGFDLFDSPQKVVIENSWAFRNGINYWNDSAFAGNGNGFKLGGNQAVGNHRITRSVAFGNVSKGFDQNNNAGGVTVINNTSYKNGINYGFGSNVQSGQKHYFRNNVSLSASVTVSNADAKSNSWDTGPAASASDFVSLDTSLATVSRDNDGTLPETSLFRLSANSKLINAGTKESNISYSGSAPDLGAFERN | pectin catabolic process symbiont-mediated disruption of host cell wall extracellular region metal ion binding pectate lyase activity Dickeya dadantii )3D-structure Calcium Disulfide bond Lyase Metal-binding Reference proteome Secreted Signal Virulence MKYLNCFIST MKYLNCFISTGLAAFFLVNSTSVLAADCSSDLTSGISTKRIYYVAPNGNSSNNGSSFNAPMSFSAAMAAVNPGELILLKPGTYTIPYTQGKGNTITFNKSGKDGAPIYVAAANCGRAVFDFSFPDSQWVQASYGFYVTGDYWYFKGVEVTRAGYQGAYVIGSHNTFENTAFHHNRNTGLEINNGGSYNTVINSDAYRNYDPKKNGSMADGFGPKQKQGPGNRFVGCRAWENSDDGFDLFDSPQKVVIENSWAFRNGINYWNDSAFAGNGNGFKLGGNQAVGNHRITRSVAFGNVSKGFDQNNNAGGVTVINNTSYKNGINYGFGSNVQSGQKHYFRNNVSLSASVTVSNADAKSNSWDTGPAASASDFVSLDTSLATVSRDNDGTLPETSLFRLSANSKLINAGTKESNISYSGSAPDLGAFERN |
cell wall modification pectin catabolic process | extracellular space | aspartyl esterase activity pectinesterase activity | Dickeya dadantii ) | 3D-structure Aspartyl esterase Cell wall biogenesis/degradation Direct protein sequencing Disulfide bond Hydrolase Reference proteome Secreted Signal | MLKTISGTLA | MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNPEDSRFFEYKSYGAGATVSKDRRQLTDAQAAEYTQSKVLGDWTPTLP | cell wall modification pectin catabolic process extracellular space aspartyl esterase activity pectinesterase activity Dickeya dadantii )3D-structure Aspartyl esterase Cell wall biogenesis/degradation Direct protein sequencing Disulfide bond Hydrolase Reference proteome Secreted Signal MLKTISGTLA MLKTISGTLALSLIIAASVHQAQAATTYNAVVSKSSSDGKTFKTIADAIASAPAGSTPFVILIKNGVYNERLTITRNNLHLKGESRNGAVIAAATAAGTLKSDGSKWGTAGSSTITISAKDFSAQSLTIRNDFDFPANQAKSDSDSSKIKDTQAVALYVTKSGDRAYFKDVSLVGYQDTLYVSGGRSFFSDCRISGTVDFIFGDGTALFNNCDLVSRYRADVKSGNVSGYLTAPSTNINQKYGLVITNSRVIRESDSVPAKSYGLGRPWHPTTTFSDGRYADPNAIGQTVFLNTSMDNHIYGWDKMSGKDKNGNTIWFNPEDSRFFEYKSYGAGATVSKDRRQLTDAQAAEYTQSKVLGDWTPTLP |
carbohydrate catabolic process | cell septum; cell wall-bounded periplasmic space; extracellular region; fungal-type cell wall; hyphal septin band; spitzenkorper | alpha-amylase activity calcium ion binding | Aspergillus oryzae | 3D-structure Calcium Carbohydrate metabolism Direct protein sequencing Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Reference proteome Secreted Signal | MMVAWWSLFL | MMVAWWSLFLYGLQVAAPALAATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCFIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLSGYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGTDGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICSSS | carbohydrate catabolic process cell septum; cell wall-bounded periplasmic space; extracellular region; fungal-type cell wall; hyphal septin band; spitzenkorper alpha-amylase activity calcium ion binding Aspergillus oryzae 3D-structure Calcium Carbohydrate metabolism Direct protein sequencing Disulfide bond Glycoprotein Glycosidase Hydrolase Metal-binding Reference proteome Secreted Signal MMVAWWSLFL MMVAWWSLFLYGLQVAAPALAATPADWRSQSIYFLLTDRFARTDGSTTATCNTADQKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCFIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLSGYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGTDGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICSSS |
defense response to bacterium | nucleosome; nucleus | DNA binding protein heterodimerization activity structural constituent of chromatin | Gallus gallus | 3D-structure Acetylation Antibiotic Antimicrobial Chromosome Direct protein sequencing DNA-binding Isopeptide bond Nucleosome core Nucleus Phosphoprotein Reference proteome Ubl conjugation | MPEPAKSAPA | MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | defense response to bacterium nucleosome; nucleus DNA binding protein heterodimerization activity structural constituent of chromatin Gallus gallus 3D-structure Acetylation Antibiotic Antimicrobial Chromosome Direct protein sequencing DNA-binding Isopeptide bond Nucleosome core Nucleus Phosphoprotein Reference proteome Ubl conjugation MPEPAKSAPA MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK |
DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway | extracellular region; host cell cytoplasm; host cell nucleolus | actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding | Human immunodeficiency virus type 1 group M subtype F2 | Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc | MEVVDPKIDP | MEVVDPKIDPWNHPGSQPETPCNNCYCKKCCFHCPLCFMKKGLGISYGRKKRRQRRRTPQGSKIHQDPVPKQPLSQTRGDPTGPEESKKKVESQTETDP | DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway extracellular region; host cell cytoplasm; host cell nucleolus actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding Human immunodeficiency virus type 1 group M subtype F2 Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc MEVVDPKIDP MEVVDPKIDPWNHPGSQPETPCNNCYCKKCCFHCPLCFMKKGLGISYGRKKRRQRRRTPQGSKIHQDPVPKQPLSQTRGDPTGPEESKKKVESQTETDP |
DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway | extracellular region; host cell cytoplasm; host cell nucleolus | actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding | Human immunodeficiency virus type 1 group M subtype F2 | Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc | MEVVDPNLDP | MEVVDPNLDPWKHPGSQPETPCNKCYCKKCCFHCQLCFTRKGLGISYGRKKRRQRRRTPQSGEVHQDPVSKQPLSQTRGDPKGPEESKKKVESKTKTDPSD | DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway extracellular region; host cell cytoplasm; host cell nucleolus actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding Human immunodeficiency virus type 1 group M subtype F2 Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc MEVVDPNLDP MEVVDPNLDPWKHPGSQPETPCNKCYCKKCCFHCQLCFTRKGLGISYGRKKRRQRRRTPQSGEVHQDPVSKQPLSQTRGDPKGPEESKKKVESKTKTDPSD |
DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway | extracellular region; host cell cytoplasm; host cell nucleolus | actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding | Human immunodeficiency virus type 1 group O | Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein Reference proteome RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc | MDPVDPEVPP | MDPVDPEVPPWHHPGSQPQIPCNNCYCKRCCYHCYVCFVRKGLGISYGRKKRGRPAAASHPDHKDPVPKQSPTITKRKQERQEEQEEEVEKKAGPGGYPRRKGSCHCCTRTSEQ | DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway extracellular region; host cell cytoplasm; host cell nucleolus actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding Human immunodeficiency virus type 1 group O Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein Reference proteome RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc MDPVDPEVPP MDPVDPEVPPWHHPGSQPQIPCNNCYCKRCCYHCYVCFVRKGLGISYGRKKRGRPAAASHPDHKDPVPKQSPTITKRKQERQEEQEEEVEKKAGPGGYPRRKGSCHCCTRTSEQ |
DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway | extracellular region; host cell cytoplasm; host cell nucleolus | actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding | Human immunodeficiency virus type 1 group O | Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein Reference proteome RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc | MDPVDPEMPP | MDPVDPEMPPWHHPGSKPQTPCNNCYCKRCCYHCYVCFTKKGLGISHGRKKRRRPAAAASYPDNKDPVPEQHTGRKQKRQEEQEKKVEKETGPSGQPCHQDSCNSCTRISGQ | DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway extracellular region; host cell cytoplasm; host cell nucleolus actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding Human immunodeficiency virus type 1 group O Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein Reference proteome RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc MDPVDPEMPP MDPVDPEMPPWHHPGSKPQTPCNNCYCKRCCYHCYVCFTKKGLGISHGRKKRRRPAAAASYPDNKDPVPEQHTGRKQKRQEEQEKKVEKETGPSGQPCHQDSCNSCTRISGQ |
DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway | extracellular region; host cell cytoplasm; host cell nucleolus | actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding | Human immunodeficiency virus type 1 group M subtype K | Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc | MEPVDPNIEP | MEPVDPNIEPWNQPGSQPKTACNQCYCKKCCYHCQLCFLQKGLGICYGREKRRQRTTTPYASKNHKDPIPKQPLPQARGDPTGPKESKKEVESKTKTDP | DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway extracellular region; host cell cytoplasm; host cell nucleolus actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding Human immunodeficiency virus type 1 group M subtype K Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc MEPVDPNIEP MEPVDPNIEPWNQPGSQPKTACNQCYCKKCCYHCQLCFLQKGLGICYGREKRRQRTTTPYASKNHKDPIPKQPLPQARGDPTGPKESKKEVESKTKTDP |
DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway | extracellular region; host cell cytoplasm; host cell nucleolus | actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding | Human immunodeficiency virus type 1 group M subtype K | Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc | MDPVDPNIEP | MDPVDPNIEPWNQPGSQPKTACNQCYCKRCCYHCQICFLKKGLGISNGRKKRRPRRTTPYNSENHQDPLRKQPLSQPRGEQTDPKESKKKVESKTKTDQFD | DNA-templated transcription modulation by virus of host chromatin organization negative regulation of peptidyl-threonine phosphorylation positive regulation of transcription elongation by RNA polymerase II positive regulation of viral transcription suppression by virus of host translation initiation suppression by virus of host type I interferon-mediated signaling pathway extracellular region; host cell cytoplasm; host cell nucleolus actinin binding cyclin binding metal ion binding protein domain specific binding protein serine/threonine phosphatase inhibitor activity RNA-binding transcription regulator activity trans-activation response element binding Human immunodeficiency virus type 1 group M subtype K Acetylation Activator AIDS Alternative splicing Apoptosis Host cytoplasm Host nucleus Host-virus interaction Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Isopeptide bond Metal-binding Methylation Modulation of host chromatin by virus Modulation of host PP1 activity by virus Phosphoprotein RNA-binding Secreted Transcription Transcription regulation Ubl conjugation Viral immunoevasion Zinc MDPVDPNIEP MDPVDPNIEPWNQPGSQPKTACNQCYCKRCCYHCQICFLKKGLGISNGRKKRRPRRTTPYNSENHQDPLRKQPLSQPRGEQTDPKESKKKVESKTKTDQFD |
viral budding via host ESCRT complex | host cell nucleus; host cell plasma membrane; host multivesicular body; membrane; viral nucleocapsid; virion membrane | RNA binding structural molecule activity zinc ion binding | Human immunodeficiency virus type 1 group M subtype G | AIDS Capsid protein Host cell membrane Host cytoplasm Host endosome Host membrane Host nucleus Host-virus interaction Lipoprotein Membrane Metal-binding Methylation Myristate Phosphoprotein Repeat Ribosomal frameshifting RNA-binding Viral budding Viral budding via the host ESCRT complexes Viral nucleoprotein Viral release from host cell Virion Zinc Zinc-finger | MGARASVLSG | MGARASVLSGGKLDSWEKIRLRPGGRKKYKLKHIVWASRELGRFALNRDLLETAEGCVQIMKQLQPALTGTEELRSLFNTVATLYCVHQKIEVKDTKEAPEEVEKIQKNSQQEIQQAAKNEGNSNPVSQNYPIVQNAQGQMIHQAISPWTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINDEAAEWDRIHPQQAGPIPPGQIREPSGSDIAGTTSTLQEQIRWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVKGWMTDTLLVQNANPDCKTILRALGPGATLEEMMTACQGVGGPSHKARVLAEAMSQASGAAAAAIMMQKSNFKGPRRIIKCFNCGKEGHLARNCRAPRKKGCWKCGKEGHQMKECTERQANFLGKIWPSNKGRPGNFLQNRTEPTAPPAESFGFGEEIAPSPKQEPKEKELYPLTSLKSLFGSDP | viral budding via host ESCRT complex host cell nucleus; host cell plasma membrane; host multivesicular body; membrane; viral nucleocapsid; virion membrane RNA binding structural molecule activity zinc ion binding Human immunodeficiency virus type 1 group M subtype G AIDS Capsid protein Host cell membrane Host cytoplasm Host endosome Host membrane Host nucleus Host-virus interaction Lipoprotein Membrane Metal-binding Methylation Myristate Phosphoprotein Repeat Ribosomal frameshifting RNA-binding Viral budding Viral budding via the host ESCRT complexes Viral nucleoprotein Viral release from host cell Virion Zinc Zinc-finger MGARASVLSG MGARASVLSGGKLDSWEKIRLRPGGRKKYKLKHIVWASRELGRFALNRDLLETAEGCVQIMKQLQPALTGTEELRSLFNTVATLYCVHQKIEVKDTKEAPEEVEKIQKNSQQEIQQAAKNEGNSNPVSQNYPIVQNAQGQMIHQAISPWTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKDTINDEAAEWDRIHPQQAGPIPPGQIREPSGSDIAGTTSTLQEQIRWMTSNPPIPVGEIYKRWIILGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVKGWMTDTLLVQNANPDCKTILRALGPGATLEEMMTACQGVGGPSHKARVLAEAMSQASGAAAAAIMMQKSNFKGPRRIIKCFNCGKEGHLARNCRAPRKKGCWKCGKEGHQMKECTERQANFLGKIWPSNKGRPGNFLQNRTEPTAPPAESFGFGEEIAPSPKQEPKEKELYPLTSLKSLFGSDP |
metabolic process negative regulation of cAMP-mediated signaling negative regulation of cGMP-mediated signaling signal transduction | cytosol; perikaryon | 3',5'-cyclic-AMP phosphodiesterase activity 3',5'-cyclic-GMP phosphodiesterase activity cGMP binding cGMP-stimulated cyclic-nucleotide phosphodiesterase activity cyclic-nucleotide phosphodiesterase activity metal ion binding | Mus musculus | Allosteric enzyme cAMP cGMP Cytoplasm Hydrolase Metal-binding Phosphoprotein Reference proteome Repeat | MAASRLDFGE | MAASRLDFGEVETFLDRHPELFEDYLMRKGKQELVDKWLQRHTSGQGASSLRPALAGASSLAQSNAKGSPGIGGGAGPQGSAHSHPTPGGGESAGVPLSPSWASGSRGDGSLQRRASQKELRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRVNLPQYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAAAGKKTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNDEIDKLTGYKTKSLLCMPIRNSDGEIIGVAQAINKVPEGAPFTEDDEKVMQMYLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKESVEKSSYSDWLINNSIAELVASTGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKAEVDKFKAANIPLVSELAIDDIHFDDFSLDVDAMITAALRMFMELGMVQKFKIDYETLCRWLLTVRKNYRMVLYHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAVMILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVRKGDYDWSITSHRDVFRSMLMTACDLGAVTKPWEISRQVAELVTSEFFEQGDRERSELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSVAANRRKWEELHQKRLQVSAASPDPASPMVAGEDRL | metabolic process negative regulation of cAMP-mediated signaling negative regulation of cGMP-mediated signaling signal transduction cytosol; perikaryon 3',5'-cyclic-AMP phosphodiesterase activity 3',5'-cyclic-GMP phosphodiesterase activity cGMP binding cGMP-stimulated cyclic-nucleotide phosphodiesterase activity cyclic-nucleotide phosphodiesterase activity metal ion binding Mus musculus Allosteric enzyme cAMP cGMP Cytoplasm Hydrolase Metal-binding Phosphoprotein Reference proteome Repeat MAASRLDFGE MAASRLDFGEVETFLDRHPELFEDYLMRKGKQELVDKWLQRHTSGQGASSLRPALAGASSLAQSNAKGSPGIGGGAGPQGSAHSHPTPGGGESAGVPLSPSWASGSRGDGSLQRRASQKELRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRVNLPQYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAAAGKKTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNDEIDKLTGYKTKSLLCMPIRNSDGEIIGVAQAINKVPEGAPFTEDDEKVMQMYLPFCGIAISNAQLFAASRKEYERSRALLEVVNDLFEEQTDLEKIVKKIMHRAQTLLKCERCSVLLLEDIESPVVKFTKSFELMSPKCSADAENSFKESVEKSSYSDWLINNSIAELVASTGLPVNVSDAYQDPRFDAEADQISGFHIRSVLCVPIWNSNHQIIGVAQVLNRLDGKPFDDADQRLFEAFVIFCGLGINNTIMYDQVKKSWAKQSVALDVLSYHATCSKAEVDKFKAANIPLVSELAIDDIHFDDFSLDVDAMITAALRMFMELGMVQKFKIDYETLCRWLLTVRKNYRMVLYHNWRHAFNVCQLMFAMLTTAGFQEILTEVEILAVIVGCLCHDLDHRGTNNAFQAKSDSALAQLYGTSATLEHHHFNHAVMILQSEGHNIFANLSSKEYSDLMQLLKQSILATDLTLYFERRTEFFELVRKGDYDWSITSHRDVFRSMLMTACDLGAVTKPWEISRQVAELVTSEFFEQGDRERSELKLTPSAIFDRNRKDELPRLQLEWIDSICMPLYQALVKVNAKLKPMLDSVAANRRKWEELHQKRLQVSAASPDPASPMVAGEDRL |
membrane organization phosphatidylcholine acyl-chain remodeling platelet activating factor biosynthetic process | endoplasmic reticulum; endoplasmic reticulum membrane; Golgi membrane; Golgi stack; lipid droplet; membrane; plasma membrane | 1-acylglycerol-3-phosphate O-acyltransferase activity 1-acylglycerophosphocholine O-acyltransferase activity 1-alkenylglycerophosphocholine O-acyltransferase activity 1-alkylglycerophosphocholine O-acetyltransferase activity calcium ion binding lysophosphatidic acid acyltransferase activity plasmalogen synthase activity | Rattus norvegicus | Acyltransferase Calcium Cell membrane Endoplasmic reticulum Golgi apparatus Lipid biosynthesis Lipid droplet Lipid metabolism Membrane Metal-binding Phospholipid biosynthesis Phospholipid metabolism Reference proteome Repeat Signal-anchor Transferase Transmembrane Transmembrane helix | MNRCAEAAAV | MNRCAEAAAVAATVPGSGVGDSGLRPPMVPRQASFFPPPVPNPFVQQTRISAARRLQMILLGIILLPVRALLVGLVLLLAWPFAVISTVCCPKKLTHPISDWRRKITQPALKFLGRAMFFSMGFRVTVKGKVASPLEAPIFVVAPHSTFFDGIACVVAGLPSLVSRNENAQTPLVGRLLRALQPVLVSRVDPDSRKNTINEIKKRAMSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYTFIQLCVLTFCQLFTKVEVEFMPVQAPSEEERNDPVLFASRVRNLMAEALEIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGIRKHLDEYASIASSAKGGRIGASSAKGGRIGPVSDVLRQLFALFDRNNDGSIDFREYVIGLAVLCNPANTEDIIQVAFKLFDVDEDGYITEEEFCTILQASLGVPDLNVSGLFREIAQGDSVSYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPEDVQTAPSVASNKVSPESHEEGTSGKKVD | membrane organization phosphatidylcholine acyl-chain remodeling platelet activating factor biosynthetic process endoplasmic reticulum; endoplasmic reticulum membrane; Golgi membrane; Golgi stack; lipid droplet; membrane; plasma membrane 1-acylglycerol-3-phosphate O-acyltransferase activity 1-acylglycerophosphocholine O-acyltransferase activity 1-alkenylglycerophosphocholine O-acyltransferase activity 1-alkylglycerophosphocholine O-acetyltransferase activity calcium ion binding lysophosphatidic acid acyltransferase activity plasmalogen synthase activity Rattus norvegicus Acyltransferase Calcium Cell membrane Endoplasmic reticulum Golgi apparatus Lipid biosynthesis Lipid droplet Lipid metabolism Membrane Metal-binding Phospholipid biosynthesis Phospholipid metabolism Reference proteome Repeat Signal-anchor Transferase Transmembrane Transmembrane helix MNRCAEAAAV MNRCAEAAAVAATVPGSGVGDSGLRPPMVPRQASFFPPPVPNPFVQQTRISAARRLQMILLGIILLPVRALLVGLVLLLAWPFAVISTVCCPKKLTHPISDWRRKITQPALKFLGRAMFFSMGFRVTVKGKVASPLEAPIFVVAPHSTFFDGIACVVAGLPSLVSRNENAQTPLVGRLLRALQPVLVSRVDPDSRKNTINEIKKRAMSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYTFIQLCVLTFCQLFTKVEVEFMPVQAPSEEERNDPVLFASRVRNLMAEALEIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGIRKHLDEYASIASSAKGGRIGASSAKGGRIGPVSDVLRQLFALFDRNNDGSIDFREYVIGLAVLCNPANTEDIIQVAFKLFDVDEDGYITEEEFCTILQASLGVPDLNVSGLFREIAQGDSVSYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPEDVQTAPSVASNKVSPESHEEGTSGKKVD |
female meiotic nuclear division female pronucleus assembly mitotic cell cycle negative regulation of oocyte maturation phosphorylation positive regulation of phosphorylation regulation of fertilization regulation of meiosis I | cytoplasm; cytosol; nucleoplasm; nucleus; plasma membrane | ATP binding magnesium ion binding non-membrane spanning protein tyrosine kinase activity protein tyrosine kinase activity | Homo sapiens | 3D-structure ATP-binding Coiled coil Disease variant Kinase Magnesium Meiosis Metal-binding Nucleotide-binding Nucleus Phosphoprotein Reference proteome Transferase Tyrosine-protein kinase | MDDKDIDKEL | MDDKDIDKELRQKLNFSYCEETEIEGQKKVEESREASSQTPEKGEVQDSEAKGTPPWTPLSNVHELDTSSEKDKESPDQILRTPVSHPLKCPETPAQPDSRSKLLPSDSPSTPKTMLSRLVISPTGKLPSRGPKHLKLTPAPLKDEMTSLALVNINPFTPESYKKLFLQSGGKRKIRGDLEEAGPEEGKGGLPAKRCVLRETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSMKTFTELSNENSALHEVYAHAVLGHHPHVVRYYSSWAEDDHMIIQNEYCNGGSLQAAISENTKSGNHFEEPKLKDILLQISLGLNYIHNSSMVHLDIKPSNIFICHKMQSESSGVIEEVENEADWFLSANVMYKIGDLGHATSINKPKVEEGDSRFLANEILQEDYRHLPKADIFALGLTIAVAAGAESLPTNGAAWHHIRKGNFPDVPQELSESFSSLLKNMIQPDAEQRPSAAALARNTVLRPSLGKTEELQQQLNLEKFKTATLERELREAQQAQSPQGYTHHGDTGVSGTHTGSRSTKRLVGGKSARSSSFTSGEREPLH | female meiotic nuclear division female pronucleus assembly mitotic cell cycle negative regulation of oocyte maturation phosphorylation positive regulation of phosphorylation regulation of fertilization regulation of meiosis I cytoplasm; cytosol; nucleoplasm; nucleus; plasma membrane ATP binding magnesium ion binding non-membrane spanning protein tyrosine kinase activity protein tyrosine kinase activity Homo sapiens 3D-structure ATP-binding Coiled coil Disease variant Kinase Magnesium Meiosis Metal-binding Nucleotide-binding Nucleus Phosphoprotein Reference proteome Transferase Tyrosine-protein kinase MDDKDIDKEL MDDKDIDKELRQKLNFSYCEETEIEGQKKVEESREASSQTPEKGEVQDSEAKGTPPWTPLSNVHELDTSSEKDKESPDQILRTPVSHPLKCPETPAQPDSRSKLLPSDSPSTPKTMLSRLVISPTGKLPSRGPKHLKLTPAPLKDEMTSLALVNINPFTPESYKKLFLQSGGKRKIRGDLEEAGPEEGKGGLPAKRCVLRETNMASRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSMKTFTELSNENSALHEVYAHAVLGHHPHVVRYYSSWAEDDHMIIQNEYCNGGSLQAAISENTKSGNHFEEPKLKDILLQISLGLNYIHNSSMVHLDIKPSNIFICHKMQSESSGVIEEVENEADWFLSANVMYKIGDLGHATSINKPKVEEGDSRFLANEILQEDYRHLPKADIFALGLTIAVAAGAESLPTNGAAWHHIRKGNFPDVPQELSESFSSLLKNMIQPDAEQRPSAAALARNTVLRPSLGKTEELQQQLNLEKFKTATLERELREAQQAQSPQGYTHHGDTGVSGTHTGSRSTKRLVGGKSARSSSFTSGEREPLH |
arachidonic acid metabolic process cannabinoid biosynthetic process diacylglycerol catabolic process icosanoid metabolic process monoacylglycerol biosynthetic process neuroblast proliferation neurogenesis positive regulation of triglyceride catabolic process prostaglandin biosynthetic process regulation of inflammatory response | plasma membrane | acylglycerol lipase activity lipase activity metal ion binding triglyceride lipase activity | Rattus norvegicus | Calcium Cell membrane Hydrolase Lipid degradation Lipid metabolism Membrane Metal-binding Phosphoprotein Reference proteome Transmembrane Transmembrane helix | MPGMVLFGRR | MPGMVLFGRRWSLASDDLVFPGSFELFLRVLWWIASLTLYLMHRRKLDCPGGVLLSTYLIVLLVLLAVIIGIVLAIVCVSMRGTICNPGPRKSMSKLLYIRLALFLPEMVWASLGAAWVAKGIQCDRTVVIGIIATVIVSWIVIAATMVTIVFVFDPLGGKMAPYPPCIPEHLDSNSSNHLLTGLRTAAKSVWETRVQCCCCCIGQDDNTRVAFSSTADLFSTYFSDTDLVPSDIAAGFTLLHQQQDKISHSREPSEVVTHTPGQPQETELDAEVENCHHYMPFSPVCSPWPVCVLNSSRVELCRTGNNFCRGRDIEYDAVEGDEHHCHFASILKTTGLQYRDFIHVSFHDKVYELPFIVVLDHRKESVVVAVRGTMSLQDVLTDLSAESENLELDIELQDCVAHKGIAQAARYIYRRLVNDGILSQAFSVAPEYRLVVVGHSLGAGAAALLAIMLRGAYPQVRAYAFSPPRGLLSKSLFEYSKDFVVSLILGMDVIPRLSVANMEDLKRRILRVIANCNKPKYKILLHGCWYSVFGGSPDNFPTELDEGNQGALTQPLLGEQTLLTRCSPGYCSGDSPLDSPKYPTLYPPGRIIHLEEEGGSGRFGCCSAAQYRARWAHETEFSKILIGPKMLIDHMPDVMIRALDRVVADRTACVSCPGQGGSNVP | arachidonic acid metabolic process cannabinoid biosynthetic process diacylglycerol catabolic process icosanoid metabolic process monoacylglycerol biosynthetic process neuroblast proliferation neurogenesis positive regulation of triglyceride catabolic process prostaglandin biosynthetic process regulation of inflammatory response plasma membrane acylglycerol lipase activity lipase activity metal ion binding triglyceride lipase activity Rattus norvegicus Calcium Cell membrane Hydrolase Lipid degradation Lipid metabolism Membrane Metal-binding Phosphoprotein Reference proteome Transmembrane Transmembrane helix MPGMVLFGRR MPGMVLFGRRWSLASDDLVFPGSFELFLRVLWWIASLTLYLMHRRKLDCPGGVLLSTYLIVLLVLLAVIIGIVLAIVCVSMRGTICNPGPRKSMSKLLYIRLALFLPEMVWASLGAAWVAKGIQCDRTVVIGIIATVIVSWIVIAATMVTIVFVFDPLGGKMAPYPPCIPEHLDSNSSNHLLTGLRTAAKSVWETRVQCCCCCIGQDDNTRVAFSSTADLFSTYFSDTDLVPSDIAAGFTLLHQQQDKISHSREPSEVVTHTPGQPQETELDAEVENCHHYMPFSPVCSPWPVCVLNSSRVELCRTGNNFCRGRDIEYDAVEGDEHHCHFASILKTTGLQYRDFIHVSFHDKVYELPFIVVLDHRKESVVVAVRGTMSLQDVLTDLSAESENLELDIELQDCVAHKGIAQAARYIYRRLVNDGILSQAFSVAPEYRLVVVGHSLGAGAAALLAIMLRGAYPQVRAYAFSPPRGLLSKSLFEYSKDFVVSLILGMDVIPRLSVANMEDLKRRILRVIANCNKPKYKILLHGCWYSVFGGSPDNFPTELDEGNQGALTQPLLGEQTLLTRCSPGYCSGDSPLDSPKYPTLYPPGRIIHLEEEGGSGRFGCCSAAQYRARWAHETEFSKILIGPKMLIDHMPDVMIRALDRVVADRTACVSCPGQGGSNVP |
protein processing proteolysis | endoplasmic reticulum; extracellular space; Golgi apparatus; membrane; plasma membrane | endopeptidase activity metalloendopeptidase activity zinc ion binding | Rattus norvegicus | Alternative splicing Coiled coil Disulfide bond Glycoprotein Hydrolase Membrane Metal-binding Metalloprotease Protease Reference proteome Secreted Signal-anchor Transmembrane Transmembrane helix Zinc | MGKSESSVGM | MGKSESSVGMMERADNCGRRRLGFVECGLLVLLTLLLMGAIVTLGVFYSIGKQLPLLNSLLHVSRHERTVVKRVLRDSSQKSDICTTPSCVIAAARILQNMDQSKKPCDNFYQYACGGWLRHHVIPETNSRYSVFDILRDELEVILKGVLEDSSVQHRPAVEKAKTLYRSCMNQSVIEKRDSEPLLNVLDMIGGWPVAMDKWNETMGPKWELERQLAVLNSQFNRRVLIDLFIWNDDQNSSRHVIYIDQPTLGMPSREYYFKEDSHRVREAYLQFMTSVATMLRRDLNLPGETDLVQEEMAQVLHLETHLANATVPQEKRHDVTALYHRMGLEELQERFGLKGFNWTLFIQNVLSSVQVELLPNEEVVVYGIPYLENLEEIIDVFPAQTLQNYLVWRLVLDRIGSLSQRFKEARVDYRKALYGTTMEEVRWRECVSYVNSNMESAVGSLYIKRAFSKDSKSIVSELIEKIRSVFVDNLDELNWMDEESKKKAQEKALNIREQIGYPDYILEDNNRHLDEEYSSLTFSEDLYFENGLQNLKNNAQRSLKKLREKVDQNLWIIGAAVVNAFYSPNRNLIVFPAGILQPPFFSKDQPQALNFGGIGMVIGHEITHGFDDNGRNFDKNGNMLDWWSNFSARHFRQQSQCMIYQYSNFSWELADNQNVNGFSTLGENIADNGGVRQAYKAYLQWLAEGGRDQRLPGLNLTYAQLFFINYAQVWCGSYRPEFAIQSIKTDVHSPLNAQVLGSLQNLPGFSEAFHCPRGSPMHPMNRCRIW | protein processing proteolysis endoplasmic reticulum; extracellular space; Golgi apparatus; membrane; plasma membrane endopeptidase activity metalloendopeptidase activity zinc ion binding Rattus norvegicus Alternative splicing Coiled coil Disulfide bond Glycoprotein Hydrolase Membrane Metal-binding Metalloprotease Protease Reference proteome Secreted Signal-anchor Transmembrane Transmembrane helix Zinc MGKSESSVGM MGKSESSVGMMERADNCGRRRLGFVECGLLVLLTLLLMGAIVTLGVFYSIGKQLPLLNSLLHVSRHERTVVKRVLRDSSQKSDICTTPSCVIAAARILQNMDQSKKPCDNFYQYACGGWLRHHVIPETNSRYSVFDILRDELEVILKGVLEDSSVQHRPAVEKAKTLYRSCMNQSVIEKRDSEPLLNVLDMIGGWPVAMDKWNETMGPKWELERQLAVLNSQFNRRVLIDLFIWNDDQNSSRHVIYIDQPTLGMPSREYYFKEDSHRVREAYLQFMTSVATMLRRDLNLPGETDLVQEEMAQVLHLETHLANATVPQEKRHDVTALYHRMGLEELQERFGLKGFNWTLFIQNVLSSVQVELLPNEEVVVYGIPYLENLEEIIDVFPAQTLQNYLVWRLVLDRIGSLSQRFKEARVDYRKALYGTTMEEVRWRECVSYVNSNMESAVGSLYIKRAFSKDSKSIVSELIEKIRSVFVDNLDELNWMDEESKKKAQEKALNIREQIGYPDYILEDNNRHLDEEYSSLTFSEDLYFENGLQNLKNNAQRSLKKLREKVDQNLWIIGAAVVNAFYSPNRNLIVFPAGILQPPFFSKDQPQALNFGGIGMVIGHEITHGFDDNGRNFDKNGNMLDWWSNFSARHFRQQSQCMIYQYSNFSWELADNQNVNGFSTLGENIADNGGVRQAYKAYLQWLAEGGRDQRLPGLNLTYAQLFFINYAQVWCGSYRPEFAIQSIKTDVHSPLNAQVLGSLQNLPGFSEAFHCPRGSPMHPMNRCRIW |
anterior/posterior pattern specification dorsal/ventral pattern formation embryonic skeletal system morphogenesis facial nerve structural organization morphogenesis of an epithelial sheet neural nucleus development positive regulation of transcription by RNA polymerase II rhombomere 3 development rhombomere 4 development skeletal system morphogenesis | nucleoplasm | DNA-binding transcription activator activity, RNA polymerase II-specific sequence-specific DNA binding sequence-specific double-stranded DNA binding | Mus musculus | Developmental protein DNA-binding Homeobox Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation | MNFEFEREIG | MNFEFEREIGFINSQPSLAECLTSFPAVLETFQTSSIKESTLIPPPPPLEQTFPSLQLGASTLQRPGSQKQAGDGPALRSPPPLPVAPPAPEFPWMKEKKSTKKPSQSAASPSPAASSVRASEVGSPSDGPGLPECGGSGSRRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQHREPPEGEPGGPSAQDDAGEPAEEPTVSPGDVATHRLREACFHPAEAAQGPRGAPPSALPATTLESVGASSPGCTMLRAGGRQSEPLPEDACPERQDSPFLPDLNFFAADSCLQMSGGLSPSLQGSLDSPVPFSEEELDFFTSTLCAIDLQFP | anterior/posterior pattern specification dorsal/ventral pattern formation embryonic skeletal system morphogenesis facial nerve structural organization morphogenesis of an epithelial sheet neural nucleus development positive regulation of transcription by RNA polymerase II rhombomere 3 development rhombomere 4 development skeletal system morphogenesis nucleoplasm DNA-binding transcription activator activity, RNA polymerase II-specific sequence-specific DNA binding sequence-specific double-stranded DNA binding Mus musculus Developmental protein DNA-binding Homeobox Nucleus Phosphoprotein Reference proteome Transcription Transcription regulation MNFEFEREIG MNFEFEREIGFINSQPSLAECLTSFPAVLETFQTSSIKESTLIPPPPPLEQTFPSLQLGASTLQRPGSQKQAGDGPALRSPPPLPVAPPAPEFPWMKEKKSTKKPSQSAASPSPAASSVRASEVGSPSDGPGLPECGGSGSRRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQHREPPEGEPGGPSAQDDAGEPAEEPTVSPGDVATHRLREACFHPAEAAQGPRGAPPSALPATTLESVGASSPGCTMLRAGGRQSEPLPEDACPERQDSPFLPDLNFFAADSCLQMSGGLSPSLQGSLDSPVPFSEEELDFFTSTLCAIDLQFP |
proteolysis | extracellular region | serine-type endopeptidase activity | Staphylococcus aureus | 3D-structure Direct protein sequencing Hydrolase Protease Repeat Secreted Serine protease Signal Virulence Zymogen | MKGKFLKVSS | MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA | proteolysis extracellular region serine-type endopeptidase activity Staphylococcus aureus3D-structure Direct protein sequencing Hydrolase Protease Repeat Secreted Serine protease Signal Virulence Zymogen MKGKFLKVSS MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPDNPDNGDNNNSDNPDAA |
phosphorylation positive regulation of Notch signaling pathway presynaptic endocytosis protein stabilization regulation of clathrin-dependent endocytosis regulation of protein localization | calyx of Held; cell leading edge; clathrin complex; clathrin-coated pit; presynapse; synapse; terminal bouton | AP-2 adaptor complex binding ATP binding Notch binding protein serine kinase activity protein serine/threonine kinase activity | Rattus norvegicus | Acetylation ATP-binding Cell membrane Cell projection Coated pit Endocytosis Kinase Membrane Methylation Nucleotide-binding Phosphoprotein Reference proteome Serine/threonine-protein kinase Synapse Transferase | MKKFFDSRRE | MKKFFDSRREQGSSGLGSGSSGGGGSSSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFALVFLVRTSNGVKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQAEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGSFTIPDNSRYSQDMHCLIYMLEPDPDKRPDIYQVSYFSFKLLKKECPVPNVQNSPIPTKLPEPVKASEAAVKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPLPQATGPSNQPSLLASVSQPKAQATPSQPLQSSQPKQPQAPPTPQQTPAPQTQGLPTQAQATPQHQQQLLLKQQQQQQQQQQQQQPQQPTAPPQPSGTFYQQQQPQQQQAQTQQQFQAVHPAAQQSVTAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQLMAQQAALQQKTAVVVPQPQAQPATAPQAAAAQEPQIQAPARQQPKVQTTPPPTIQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLHAAAAEASLSKSKSATTTPSGSPRTSQQNVSNASEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKLPEKLGGSAESLIPGFQATQGDAFATSSFSAGTAEKRKGGQAVDSGIPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADAAVESLIPGLEPPVAQRLPSHTESVTSNRTDSLTGEDSLLDCSLLSNPTADLLDEFAPIALSASTHKAAEDSNLISGFGVAEGSEKVAEDEFDPIPVLITKNTQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL | phosphorylation positive regulation of Notch signaling pathway presynaptic endocytosis protein stabilization regulation of clathrin-dependent endocytosis regulation of protein localization calyx of Held; cell leading edge; clathrin complex; clathrin-coated pit; presynapse; synapse; terminal bouton AP-2 adaptor complex binding ATP binding Notch binding protein serine kinase activity protein serine/threonine kinase activity Rattus norvegicus Acetylation ATP-binding Cell membrane Cell projection Coated pit Endocytosis Kinase Membrane Methylation Nucleotide-binding Phosphoprotein Reference proteome Serine/threonine-protein kinase Synapse Transferase MKKFFDSRRE MKKFFDSRREQGSSGLGSGSSGGGGSSSGLGSGYIGRVFGIGRQQVTVDEVLAEGGFALVFLVRTSNGVKCALKRMFVNNEHDLQVCKREIQIMRDLSGHKNIVGYIDSSINNVSSGDVWEVLILMDFCRGGQVVNLMNQRLQTGFTENEVLQIFCDTCEAVARLHQCKTPIIHRDLKVENILLHDRGHYVLCDFGSATNKFQNPQAEGVNAVEDEIKKYTTLSYRAPEMVNLYSGKIITTKADIWALGCLLYKLCYFTLPFGESQVAICDGSFTIPDNSRYSQDMHCLIYMLEPDPDKRPDIYQVSYFSFKLLKKECPVPNVQNSPIPTKLPEPVKASEAAVKKTQPKARLTDPIPTTETSIAPRQRPKAGQTQPNPGILPIQPALTPRKRATVQPLPQATGPSNQPSLLASVSQPKAQATPSQPLQSSQPKQPQAPPTPQQTPAPQTQGLPTQAQATPQHQQQLLLKQQQQQQQQQQQQQPQQPTAPPQPSGTFYQQQQPQQQQAQTQQQFQAVHPAAQQSVTAQFPVVSQGGSQQQLMQNFYQQQQQQQQQQQQLMAQQAALQQKTAVVVPQPQAQPATAPQAAAAQEPQIQAPARQQPKVQTTPPPTIQGQKVGSLTPPSSPKTQRAGHRRILSDVTHSAVFGVPASKSTQLLHAAAAEASLSKSKSATTTPSGSPRTSQQNVSNASEGSTWNPFDDDNFSKLTAEELLNKDFAKLGEGKLPEKLGGSAESLIPGFQATQGDAFATSSFSAGTAEKRKGGQAVDSGIPLLSVSDPFIPLQVPDAPEKLIEGLKSPDTSLLLPDLLPMTDPFGSTSDAVIEKADAAVESLIPGLEPPVAQRLPSHTESVTSNRTDSLTGEDSLLDCSLLSNPTADLLDEFAPIALSASTHKAAEDSNLISGFGVAEGSEKVAEDEFDPIPVLITKNTQGGHSRNSSGSSESSLPNLARSLLLVDQLIDL |
apoptotic signaling pathway chromatin remodeling DNA recombination DNA repair male gonad development positive regulation of apoptotic process positive regulation of DNA repair positive regulation of DNA-templated transcription positive regulation of telomere maintenance in response to DNA damage regulation of cell cycle regulation of chromosome organization regulation of DNA repair regulation of DNA replication regulation of DNA strand elongation regulation of embryonic development telomere maintenance | actin filament; cytoplasm; Ino80 complex; nucleoplasm; nucleus | DNA binding protein kinase binding protein-containing complex binding | Homo sapiens | Alternative splicing Apoptosis Chromosomal rearrangement DNA damage DNA recombination DNA repair Isopeptide bond Nucleus Phosphoprotein Proto-oncogene Reference proteome Transcription Transcription regulation Ubl conjugation | MELEQREGTM | MELEQREGTMAAVGFEEFSAPPGSELALPPLFGGHILESELETEVEFVSGGLGGSGLRERDEEEEAARGRRRRQRELNRRKYQALGRRCREIEQVNERVLNRLHQVQRITRRLQQERRFLMRVLDSYGDDYRASQFTIVLEDEGSQGTDAPTPGNAENEPPEKETLSPPRRTPAPPEPGSPAPGEGPSGRKRRRVPRDGRRAGNALTPELAPVQIKVEEDFGFEADEALDSSWVSRGPDKLLPYPTLASPASD | apoptotic signaling pathway chromatin remodeling DNA recombination DNA repair male gonad development positive regulation of apoptotic process positive regulation of DNA repair positive regulation of DNA-templated transcription positive regulation of telomere maintenance in response to DNA damage regulation of cell cycle regulation of chromosome organization regulation of DNA repair regulation of DNA replication regulation of DNA strand elongation regulation of embryonic development telomere maintenance actin filament; cytoplasm; Ino80 complex; nucleoplasm; nucleus DNA binding protein kinase binding protein-containing complex binding Homo sapiens Alternative splicing Apoptosis Chromosomal rearrangement DNA damage DNA recombination DNA repair Isopeptide bond Nucleus Phosphoprotein Proto-oncogene Reference proteome Transcription Transcription regulation Ubl conjugation MELEQREGTM MELEQREGTMAAVGFEEFSAPPGSELALPPLFGGHILESELETEVEFVSGGLGGSGLRERDEEEEAARGRRRRQRELNRRKYQALGRRCREIEQVNERVLNRLHQVQRITRRLQQERRFLMRVLDSYGDDYRASQFTIVLEDEGSQGTDAPTPGNAENEPPEKETLSPPRRTPAPPEPGSPAPGEGPSGRKRRRVPRDGRRAGNALTPELAPVQIKVEEDFGFEADEALDSSWVSRGPDKLLPYPTLASPASD |
mRNA transport | host cell cytoplasm; host cell nucleolus | RNA binding | Human T-cell leukemia virus 1 | Alternative splicing Host cytoplasm Host nucleus Host-virus interaction mRNA transport Phosphoprotein RNA-binding Transport | MPKTRRRPRR | MPKTRRRPRRSQRKRPPTPWPTSQGLDRVFFSDTQSTCLETVYKATGAPSLGDYVRPAYIVTPYWPPVQSIRSPGTPSMDALSAQLYSSLSLDSPPSPPREPLRPSRSLPRQSLIQPPTFHPPSSRPCANTPPSEMDTWNPPLGSTSQPCLFQTPDSGPKTCTPSGEAPLSACTSTSFPPPSPGPSCPT | mRNA transport host cell cytoplasm; host cell nucleolus RNA binding Human T-cell leukemia virus 1 Alternative splicing Host cytoplasm Host nucleus Host-virus interaction mRNA transport Phosphoprotein RNA-binding Transport MPKTRRRPRR MPKTRRRPRRSQRKRPPTPWPTSQGLDRVFFSDTQSTCLETVYKATGAPSLGDYVRPAYIVTPYWPPVQSIRSPGTPSMDALSAQLYSSLSLDSPPSPPREPLRPSRSLPRQSLIQPPTFHPPSSRPCANTPPSEMDTWNPPLGSTSQPCLFQTPDSGPKTCTPSGEAPLSACTSTSFPPPSPGPSCPT |
mRNA transport | host cell cytoplasm; host cell nucleolus | RNA binding | Human T-cell leukemia virus 1 | 3D-structure Alternative splicing Host cytoplasm Host nucleus Host-virus interaction mRNA transport Phosphoprotein Reference proteome RNA-binding Transport | MPKTRRRPRR | MPKTRRRPRRSQRKRPPTPWPTSQGLDRVFFSDTQSTCLETVYKATGAPSLGDYVRPAYIVTPYWPPVQSIRSPGTPSMDALSAQLYSSLSLDSPPSPPREPLRPLRSLPRQSLIQPPTFHPPSSRPCANTPPSEMDTWNPPLGSTSQPCLFQTPDSGPKTCTPSGEAPLSACTSTSFPPPSPGPSCPM | mRNA transport host cell cytoplasm; host cell nucleolus RNA binding Human T-cell leukemia virus 1 3D-structure Alternative splicing Host cytoplasm Host nucleus Host-virus interaction mRNA transport Phosphoprotein Reference proteome RNA-binding Transport MPKTRRRPRR MPKTRRRPRRSQRKRPPTPWPTSQGLDRVFFSDTQSTCLETVYKATGAPSLGDYVRPAYIVTPYWPPVQSIRSPGTPSMDALSAQLYSSLSLDSPPSPPREPLRPLRSLPRQSLIQPPTFHPPSSRPCANTPPSEMDTWNPPLGSTSQPCLFQTPDSGPKTCTPSGEAPLSACTSTSFPPPSPGPSCPM |
viral process | viral nucleocapsid | nucleic acid binding structural molecule activity zinc ion binding | Human T-cell leukemia virus 1 | Capsid protein Disulfide bond Host-virus interaction Lipoprotein Metal-binding Myristate Phosphoprotein Repeat Ribosomal frameshifting Ubl conjugation Viral nucleoprotein Virion Zinc Zinc-finger | MGQIFPRSAN | MGQIFPRSANPIPRPPRGLATHHWLNFLQAAYRLEPGPSSYDFHQLKTVLKMALETPVWMCPINYSLLASLLPKGYPGQVNEILQVLIQTQTQIPSHPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGVPPTHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLTAFAALPGSAKDPSWASILQGLEEPYHTFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGHTNSPLGDMLRACQAWTPRDKTKVLVVQPKKPPPNQPCFRCGKAGHWSRDCAQPRPPPGPCPLCQDPTHWKRDCPRLKPAIPEPEPEEDALLLDLPADIPHPKNSIGGEV | viral process viral nucleocapsid nucleic acid binding structural molecule activity zinc ion binding Human T-cell leukemia virus 1 Capsid protein Disulfide bond Host-virus interaction Lipoprotein Metal-binding Myristate Phosphoprotein Repeat Ribosomal frameshifting Ubl conjugation Viral nucleoprotein Virion Zinc Zinc-finger MGQIFPRSAN MGQIFPRSANPIPRPPRGLATHHWLNFLQAAYRLEPGPSSYDFHQLKTVLKMALETPVWMCPINYSLLASLLPKGYPGQVNEILQVLIQTQTQIPSHPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGVPPTHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLTAFAALPGSAKDPSWASILQGLEEPYHTFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGHTNSPLGDMLRACQAWTPRDKTKVLVVQPKKPPPNQPCFRCGKAGHWSRDCAQPRPPPGPCPLCQDPTHWKRDCPRLKPAIPEPEPEEDALLLDLPADIPHPKNSIGGEV |
proteolysis suppression by virus of host gene expression | viral nucleocapsid | aspartic-type endopeptidase activity nucleic acid binding structural molecule activity zinc ion binding | Human T-cell leukemia virus 1 | 3D-structure Aspartyl protease Capsid protein Eukaryotic host gene expression shutoff by virus Eukaryotic host translation shutoff by virus Host gene expression shutoff by virus Host-virus interaction Hydrolase Lipoprotein Metal-binding Myristate Phosphoprotein Protease Repeat Ribosomal frameshifting Viral nucleoprotein Virion Zinc Zinc-finger | MGQIFPRSAN | MGQIFPRSANPIPRPPRGLATHHWLNFLQAAYRLEPGPSSYDFHQLKTVLKMALETPVWMCPINYSLLASLLPKGYPGQVNEILQVLIQTQTQIPSHPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGVPPTHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLTAFAALPGSAKDPSWASILQGLEEPYHTFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGHTNSPLGDMLRACQAWTPRDKTKVLVVQPKKPPPNQPCFRCGKAGHWSRDCAQPRPPPGPCPLCQDPTHWKRDCPRLKPAIPEPEPEEDALLLDLPADIPHPKNLHRGGGLTSPPTLRQVHPNKDPASILPVIPLDPARRPLIKAQVDTQTSHPRTIEALLDTGADMTVLPIALFSSDTPLKDTSVLGAGGQTQDHFKLTSLPVLIRLPFRTTPIVLTSCLVDTKNNWAIIGRDALQQCQGVLYLPEAKRPPVILPIQAPAVLGLEHLPRPPEISQFPLNQNASRPCNTWSGRPWRQAISNRTPGQEITQYSQLKRPMEPGDSSTTCGPLIL | proteolysis suppression by virus of host gene expression viral nucleocapsid aspartic-type endopeptidase activity nucleic acid binding structural molecule activity zinc ion binding Human T-cell leukemia virus 1 3D-structure Aspartyl protease Capsid protein Eukaryotic host gene expression shutoff by virus Eukaryotic host translation shutoff by virus Host gene expression shutoff by virus Host-virus interaction Hydrolase Lipoprotein Metal-binding Myristate Phosphoprotein Protease Repeat Ribosomal frameshifting Viral nucleoprotein Virion Zinc Zinc-finger MGQIFPRSAN MGQIFPRSANPIPRPPRGLATHHWLNFLQAAYRLEPGPSSYDFHQLKTVLKMALETPVWMCPINYSLLASLLPKGYPGQVNEILQVLIQTQTQIPSHPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGVPPTHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLTAFAALPGSAKDPSWASILQGLEEPYHTFVERLNVALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGHTNSPLGDMLRACQAWTPRDKTKVLVVQPKKPPPNQPCFRCGKAGHWSRDCAQPRPPPGPCPLCQDPTHWKRDCPRLKPAIPEPEPEEDALLLDLPADIPHPKNLHRGGGLTSPPTLRQVHPNKDPASILPVIPLDPARRPLIKAQVDTQTSHPRTIEALLDTGADMTVLPIALFSSDTPLKDTSVLGAGGQTQDHFKLTSLPVLIRLPFRTTPIVLTSCLVDTKNNWAIIGRDALQQCQGVLYLPEAKRPPVILPIQAPAVLGLEHLPRPPEISQFPLNQNASRPCNTWSGRPWRQAISNRTPGQEITQYSQLKRPMEPGDSSTTCGPLIL |
killing of cells of another organism | extracellular region | calcium-dependent phospholipase C activity phosphatidylcholine phospholipase C activity toxin activity zinc ion binding | Clostridium perfringens | 3D-structure Calcium Cytolysis Hemolysis Hydrolase Metal-binding Reference proteome Secreted Signal Toxin Virulence Zinc | MKRKICKALI | MKRKICKALICATLATSLWAGASTKVYAWDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRKFSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFAEERKEQYKINTAGCKTNEDFYADILKNKDFNAWSKEYARGFAKTGKSIYYSHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDFMTGSKDTYTFKLKDENLKIDDIQNMWIRKRKYTAFPDAYKPENIKIIANGKVVVDKDINEWISGNSTYNIK | killing of cells of another organism extracellular region calcium-dependent phospholipase C activity phosphatidylcholine phospholipase C activity toxin activity zinc ion binding Clostridium perfringens 3D-structure Calcium Cytolysis Hemolysis Hydrolase Metal-binding Reference proteome Secreted Signal Toxin Virulence Zinc MKRKICKALI MKRKICKALICATLATSLWAGASTKVYAWDGKIDGTGTHAMIVTQGVSILENDLSKNEPESVRKNLEILKENMHELQLGSTYPDYDKNAYDLYQDHFWDPDTDNNFSKDNSWYLAYSIPDTGESQIRKFSALARYEWQRGNYKQATFYLGEAMHYFGDIDTPYHPANVTAVDSAGHVKFETFAEERKEQYKINTAGCKTNEDFYADILKNKDFNAWSKEYARGFAKTGKSIYYSHASMSHSWDDWDYAAKVTLANSQKGTAGYIYRFLHDVSEGNDPSVGKNVKELVAYISTSGEKDAGTDDYMYFGIKTKDGKTQEWEMDNPGNDFMTGSKDTYTFKLKDENLKIDDIQNMWIRKRKYTAFPDAYKPENIKIIANGKVVVDKDINEWISGNSTYNIK |
biomineral tissue development bone development brain development cellular response to insulin stimulus cognition glucose homeostasis learning or memory negative regulation of bone development positive regulation of neurotransmitter secretion regulation of bone mineralization regulation of cellular response to insulin stimulus regulation of testosterone biosynthetic process response to vitamin K type B pancreatic cell proliferation | cytoplasm; extracellular region | calcium ion binding hormone activity structural constituent of bone | Capra hircus | Biomineralization Calcium Direct protein sequencing Disulfide bond Gamma-carboxyglutamic acid Hormone Hydroxylation Metal-binding Reference proteome Secreted | YLDPGLGAPA | YLDPGLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGIA | biomineral tissue development bone development brain development cellular response to insulin stimulus cognition glucose homeostasis learning or memory negative regulation of bone development positive regulation of neurotransmitter secretion regulation of bone mineralization regulation of cellular response to insulin stimulus regulation of testosterone biosynthetic process response to vitamin K type B pancreatic cell proliferation cytoplasm; extracellular region calcium ion binding hormone activity structural constituent of bone Capra hircus Biomineralization Calcium Direct protein sequencing Disulfide bond Gamma-carboxyglutamic acid Hormone Hydroxylation Metal-binding Reference proteome Secreted YLDPGLGAPA YLDPGLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGIA |
biomineral tissue development bone development brain development cellular response to insulin stimulus cognition glucose homeostasis learning or memory negative regulation of bone development positive regulation of neurotransmitter secretion regulation of bone mineralization regulation of cellular response to insulin stimulus regulation of testosterone biosynthetic process response to vitamin K type B pancreatic cell proliferation | cytoplasm; extracellular region | calcium ion binding hormone activity structural constituent of bone | Notamacropus eugenii | Biomineralization Calcium Direct protein sequencing Disulfide bond Gamma-carboxyglutamic acid Hormone Hydroxylation Metal-binding Secreted | YLYQTLGFPA | YLYQTLGFPAPYPDPQENKREVCELNPDCDELADHIGFQEAYRRFYGTA | biomineral tissue development bone development brain development cellular response to insulin stimulus cognition glucose homeostasis learning or memory negative regulation of bone development positive regulation of neurotransmitter secretion regulation of bone mineralization regulation of cellular response to insulin stimulus regulation of testosterone biosynthetic process response to vitamin K type B pancreatic cell proliferation cytoplasm; extracellular region calcium ion binding hormone activity structural constituent of bone Notamacropus eugenii Biomineralization Calcium Direct protein sequencing Disulfide bond Gamma-carboxyglutamic acid Hormone Hydroxylation Metal-binding Secreted YLYQTLGFPA YLYQTLGFPAPYPDPQENKREVCELNPDCDELADHIGFQEAYRRFYGTA |
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