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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cell wall macromolecule catabolic process defense response to Gram-positive bacterium killing of cells of another organism | cytoplasm; extracellular space | glycosaminoglycan binding identical protein binding lysozyme activity | Meleagris gallopavo | 3D-structure Antimicrobial Bacteriolytic enzyme Direct protein sequencing Disulfide bond Glycosidase Hydrolase Reference proteome Secreted Signal | MRSLLILVLC | MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL | cell wall macromolecule catabolic process defense response to Gram-positive bacterium killing of cells of another organism cytoplasm; extracellular space glycosaminoglycan binding identical protein binding lysozyme activity Meleagris gallopavo 3D-structure Antimicrobial Bacteriolytic enzyme Direct protein sequencing Disulfide bond Glycosidase Hydrolase Reference proteome Secreted Signal MRSLLILVLC MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDITASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHAWIRGCRL |
apoptotic process cell-cell signaling defense response to bacterium lactose biosynthetic process signal transduction | extracellular space; Golgi lumen; Golgi membrane; protein-containing complex | calcium ion binding lactose synthase activity lysozyme activity | Homo sapiens | 3D-structure Calcium Direct protein sequencing Disulfide bond Glycoprotein Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal Zinc | MRFFVPLFLV | MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL | apoptotic process cell-cell signaling defense response to bacterium lactose biosynthetic process signal transduction extracellular space; Golgi lumen; Golgi membrane; protein-containing complex calcium ion binding lactose synthase activity lysozyme activity Homo sapiens 3D-structure Calcium Direct protein sequencing Disulfide bond Glycoprotein Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal Zinc MRFFVPLFLV MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAIVENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGIDYWLAHKALCTEKLEQWLCEKL |
lactose biosynthetic process response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to progesterone | extracellular space | calcium ion binding identical protein binding lactose synthase activity lysozyme activity | Bos taurus | 3D-structure Allergen Calcium Direct protein sequencing Disulfide bond Glycoprotein Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal | MMSFVSLLLV | MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL | lactose biosynthetic process response to 11-deoxycorticosterone response to dehydroepiandrosterone response to estradiol response to progesterone extracellular space calcium ion binding identical protein binding lactose synthase activity lysozyme activity Bos taurus 3D-structure Allergen Calcium Direct protein sequencing Disulfide bond Glycoprotein Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal MMSFVSLLLV MMSFVSLLLVGILFHATQAEQLTKCEVFRELKDLKGYGGVSLPEWVCTTFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSSNICNISCDKFLDDDLTDDIMCVKKILDKVGINYWLAHKALCSEKLDQWLCEKL |
lactose biosynthetic process | extracellular region; protein-containing complex | calcium ion binding lactose synthase activity | Capra hircus | 3D-structure Calcium Direct protein sequencing Disulfide bond Glycoprotein Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal | MMSFVSLLLV | MMSFVSLLLVGILFHATQAEQLTKCEVFQKLKDLKDYGGVSLPEWVCTAFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSRNICNISCDKFLDDDLTDDIVCAKKILDKVGINYWLAHKALCSEKLDQWLCEKL | lactose biosynthetic process extracellular region; protein-containing complex calcium ion binding lactose synthase activity Capra hircus 3D-structure Calcium Direct protein sequencing Disulfide bond Glycoprotein Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal MMSFVSLLLV MMSFVSLLLVGILFHATQAEQLTKCEVFQKLKDLKDYGGVSLPEWVCTAFHTSGYDTQAIVQNNDSTEYGLFQINNKIWCKDDQNPHSRNICNISCDKFLDDDLTDDIVCAKKILDKVGINYWLAHKALCSEKLDQWLCEKL |
lactose biosynthetic process | extracellular region; protein-containing complex | calcium ion binding lactose synthase activity | Cavia porcellus | 3D-structure Calcium Direct protein sequencing Disulfide bond Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal | MMSFFPLLLV | MMSFFPLLLVGILFPAVQAKQLTKCALSHELNDLAGYRDITLPEWLCIIFHISGYDTQAIVKNSDHKEYGLFQINDKDFCESSTTVQSRNICDISCDKLLDDDLTDDIMCVKKILDIKGIDYWLAHKPLCSDKLEQWYCEAQ | lactose biosynthetic process extracellular region; protein-containing complex calcium ion binding lactose synthase activity Cavia porcellus 3D-structure Calcium Direct protein sequencing Disulfide bond Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal MMSFFPLLLV MMSFFPLLLVGILFPAVQAKQLTKCALSHELNDLAGYRDITLPEWLCIIFHISGYDTQAIVKNSDHKEYGLFQINDKDFCESSTTVQSRNICDISCDKLLDDDLTDDIMCVKKILDIKGIDYWLAHKPLCSDKLEQWYCEAQ |
lactose biosynthetic process | extracellular region; protein-containing complex | calcium ion binding lactose synthase activity lysozyme activity | Rattus norvegicus | Calcium Direct protein sequencing Disulfide bond Glycoprotein Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal | MMRFVPLFLA | MMRFVPLFLACISLPAFQATEFTKCEVSHAIEDMDGYQGISLLEWTCVLFHTSGYDSQAIVKNNGSTEYGLFQISNRNWCKSSEFPESENICDISCDKFLDDELADDIVCAKKIVAIKGIDYWKAHKPMCSEKLEQWRCEKPGAPALVVPALNSETPVP | lactose biosynthetic process extracellular region; protein-containing complex calcium ion binding lactose synthase activity lysozyme activity Rattus norvegicus Calcium Direct protein sequencing Disulfide bond Glycoprotein Lactose biosynthesis Metal-binding Milk protein Reference proteome Secreted Signal MMRFVPLFLA MMRFVPLFLACISLPAFQATEFTKCEVSHAIEDMDGYQGISLLEWTCVLFHTSGYDSQAIVKNNGSTEYGLFQISNRNWCKSSEFPESENICDISCDKFLDDELADDIVCAKKIVAIKGIDYWKAHKPMCSEKLEQWRCEKPGAPALVVPALNSETPVP |
cell wall macromolecule catabolic process defense response to bacterium peptidoglycan catabolic process viral release from host cell by cytolysis | host cell cytoplasm | lysozyme activity | Enterobacteria phage T4 | 3D-structure Antimicrobial Bacteriolytic enzyme Cytolysis Direct protein sequencing Glycosidase Host cell lysis by virus Host cytoplasm Hydrolase Reference proteome Viral release from host cell | MNIFEMLRID | MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDAYKNL | cell wall macromolecule catabolic process defense response to bacterium peptidoglycan catabolic process viral release from host cell by cytolysis host cell cytoplasm lysozyme activity Enterobacteria phage T4 3D-structure Antimicrobial Bacteriolytic enzyme Cytolysis Direct protein sequencing Glycosidase Host cell lysis by virus Host cytoplasm Hydrolase Reference proteome Viral release from host cell MNIFEMLRID MNIFEMLRIDERLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSIWYNQTPNRAKRVITTFRTGTWDAYKNL |
lactose catabolic process | beta-galactosidase complex | alkali metal ion binding beta-galactosidase activity carbohydrate binding identical protein binding magnesium ion binding | Escherichia coli | 3D-structure Direct protein sequencing Glycosidase Hydrolase Magnesium Manganese Metal-binding Reference proteome Sodium | MTMITDSLAV | MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLVWCQK | lactose catabolic process beta-galactosidase complex alkali metal ion binding beta-galactosidase activity carbohydrate binding identical protein binding magnesium ion binding Escherichia coli 3D-structure Direct protein sequencing Glycosidase Hydrolase Magnesium Manganese Metal-binding Reference proteome Sodium MTMITDSLAV MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWRFAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENPTGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRAGENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAVLEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPKLWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEHHPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHGMVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVDPSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYAHAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDRQFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALDGKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQWRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTPLRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTAHAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLGLGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNISRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLVWCQK |
fructan catabolic process inulin catabolic process raffinose catabolic process sucrose catabolic process | cell periphery; cytoplasm; extracellular region; fungal-type vacuole; mitochondrion | beta-fructofuranosidase activity inulinase activity sucrose alpha-glucosidase activity | Saccharomyces cerevisiae | 3D-structure Alternative initiation Cytoplasm Direct protein sequencing Glycoprotein Glycosidase Hydrolase Reference proteome Secreted Signal | MLLQAFLFLL | MLLQAFLFLLAGFAAKISASMTNETSDRPLVHFTPNKGWMNDPNGLWYDEKDAKWHLYFQYNPNDTVWGTPLFWGHATSDDLTNWEDQPIAIAPKRNDSGAFSGSMVVDYNNTSGFFNDTIDPRQRCVAIWTYNTPESEEQYISYSLDGGYTFTEYQKNPVLAANSTQFRDPKVFWYEPSQKWIMTAAKSQDYKIEIYSSDDLKSWKLESAFANEGFLGYQYECPGLIEVPTEQDPSKSYWVMFISINPGAPAGGSFNQYFVGSFNGTHFEAFDNQSRVVDFGKDYYALQTFFNTDPTYGSALGIAWASNWEYSAFVPTNPWRSSMSLVRKFSLNTEYQANPETELINLKAEPILNISNAGPWSRFATNTTLTKANSYNVDLSNSTGTLEFELVYAVNTTQTISKSVFADLSLWFKGLEDPEEYLRMGFEVSASSFFLDRGNSKVKFVKENPYFTNRMSVNNQPFKSENDLSYYKVYGLLDQNILELYFNDGDVVSTNTYFMTTGNALGSVNMTTGVDNLFYIDKFQVREVK | fructan catabolic process inulin catabolic process raffinose catabolic process sucrose catabolic process cell periphery; cytoplasm; extracellular region; fungal-type vacuole; mitochondrion beta-fructofuranosidase activity inulinase activity sucrose alpha-glucosidase activity Saccharomyces cerevisiae 3D-structure Alternative initiation Cytoplasm Direct protein sequencing Glycoprotein Glycosidase Hydrolase Reference proteome Secreted Signal MLLQAFLFLL MLLQAFLFLLAGFAAKISASMTNETSDRPLVHFTPNKGWMNDPNGLWYDEKDAKWHLYFQYNPNDTVWGTPLFWGHATSDDLTNWEDQPIAIAPKRNDSGAFSGSMVVDYNNTSGFFNDTIDPRQRCVAIWTYNTPESEEQYISYSLDGGYTFTEYQKNPVLAANSTQFRDPKVFWYEPSQKWIMTAAKSQDYKIEIYSSDDLKSWKLESAFANEGFLGYQYECPGLIEVPTEQDPSKSYWVMFISINPGAPAGGSFNQYFVGSFNGTHFEAFDNQSRVVDFGKDYYALQTFFNTDPTYGSALGIAWASNWEYSAFVPTNPWRSSMSLVRKFSLNTEYQANPETELINLKAEPILNISNAGPWSRFATNTTLTKANSYNVDLSNSTGTLEFELVYAVNTTQTISKSVFADLSLWFKGLEDPEEYLRMGFEVSASSFFLDRGNSKVKFVKENPYFTNRMSVNNQPFKSENDLSYYKVYGLLDQNILELYFNDGDVVSTNTYFMTTGNALGSVNMTTGVDNLFYIDKFQVREVK |
proteolysis | cytoplasm; mitochondrion | carboxypeptidase activity dipeptidase activity disordered domain specific binding manganese ion binding metalloaminopeptidase activity peptidase activity | Bos taurus | 3D-structure Acetylation Alternative initiation Aminopeptidase Cobalt Cytoplasm Dipeptidase Direct protein sequencing Hydrolase Magnesium Manganese Metal-binding Phosphoprotein Protease Reference proteome Zinc | MFLLPLPAAA | MFLLPLPAAARVAVRHLSVKRLWAPGPAAADMTKGLVLGIYSKEKEEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGKTRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQIQDLEIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSEDQEAWQRGVLFASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDVFIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGKGITFDSGGISIKAAANMDLMRADMGGAATICSAIVSAAKLDLPINIVGLAPLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGAMDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLFEHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDIAGVMTNKDEVPYLRKGMAGRPTRTLIEFLFRFSQDSA | proteolysis cytoplasm; mitochondrion carboxypeptidase activity dipeptidase activity disordered domain specific binding manganese ion binding metalloaminopeptidase activity peptidase activity Bos taurus 3D-structure Acetylation Alternative initiation Aminopeptidase Cobalt Cytoplasm Dipeptidase Direct protein sequencing Hydrolase Magnesium Manganese Metal-binding Phosphoprotein Protease Reference proteome Zinc MFLLPLPAAA MFLLPLPAAARVAVRHLSVKRLWAPGPAAADMTKGLVLGIYSKEKEEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGKTRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQIQDLEIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSEDQEAWQRGVLFASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDVFIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGKGITFDSGGISIKAAANMDLMRADMGGAATICSAIVSAAKLDLPINIVGLAPLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGAMDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLFEHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDIAGVMTNKDEVPYLRKGMAGRPTRTLIEFLFRFSQDSA |
macroautophagy phytochelatin biosynthetic process zymogen activation | cytoplasm; endoplasmic reticulum; extracellular region; fungal-type vacuole; fungal-type vacuole lumen | serine-type carboxypeptidase activity | Saccharomyces cerevisiae | 3D-structure Carboxypeptidase Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Protease Reference proteome Signal Vacuole Zymogen | MKAFTSLLCG | MKAFTSLLCGLGLSTTLAKAISLQRPLGLDKDVLLQAAEKFGLDLDLDHLLKELDSNVLDAWAQIEHLYPNQVMSLETSTKPKFPEAIKTKKDWDFVVKNDAIENYQLRVNKIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYCNNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAVTDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVPFDVPENALSMVNEWIHGGFSL | macroautophagy phytochelatin biosynthetic process zymogen activation cytoplasm; endoplasmic reticulum; extracellular region; fungal-type vacuole; fungal-type vacuole lumen serine-type carboxypeptidase activity Saccharomyces cerevisiae 3D-structure Carboxypeptidase Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Protease Reference proteome Signal Vacuole Zymogen MKAFTSLLCG MKAFTSLLCGLGLSTTLAKAISLQRPLGLDKDVLLQAAEKFGLDLDLDHLLKELDSNVLDAWAQIEHLYPNQVMSLETSTKPKFPEAIKTKKDWDFVVKNDAIENYQLRVNKIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYCNNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAVTDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVPFDVPENALSMVNEWIHGGFSL |
leukotriene metabolic process proteolysis | extracellular space | metallocarboxypeptidase activity zinc ion binding | Bos taurus | 3D-structure Carboxypeptidase Direct protein sequencing Disulfide bond Hydrolase Metal-binding Metalloprotease Protease Reference proteome Secreted Signal Zinc Zymogen | MQGLLILSVL | MQGLLILSVLLGAALGKEDFVGHQVLRITAADEAEVQTVKELEDLEHLQLDFWRGPGQPGSPIDVRVPFPSLQAVKVFLEAHGIRYRIMIEDVQSLLDEEQEQMFASQSRARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKYGSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTLNNLY | leukotriene metabolic process proteolysis extracellular space metallocarboxypeptidase activity zinc ion binding Bos taurus 3D-structure Carboxypeptidase Direct protein sequencing Disulfide bond Hydrolase Metal-binding Metalloprotease Protease Reference proteome Secreted Signal Zinc Zymogen MQGLLILSVL MQGLLILSVLLGAALGKEDFVGHQVLRITAADEAEVQTVKELEDLEHLQLDFWRGPGQPGSPIDVRVPFPSLQAVKVFLEAHGIRYRIMIEDVQSLLDEEQEQMFASQSRARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKYGSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTLNNLY |
cell wall organization proteolysis | extracellular region | metal ion binding zinc D-Ala-D-Ala carboxypeptidase activity | Streptomyces albus G | 3D-structure Carboxypeptidase Cell wall biogenesis/degradation Direct protein sequencing Disulfide bond Hydrolase Metal-binding Metalloprotease Protease Secreted Signal Zinc | MRPRPIRLLL | MRPRPIRLLLTALVGAGLAFAPVSAVAAPTATASASADVGALDGCYTWSGTLSEGSSGEAVRQLQIRVAGYPGTGAQLAIDGQFGPATKAAVQRFQSAYGLAADGIAGPATFNKIYQLQDDDCTPVNFTYAELNRCNSDWSGGKVSAATARANALVTMWKLQAMRHAMGDKPITVNGGFRSVTCNSNVGGASNSRHMYGHAADLGAGSQGFCALAQAARNHGFTEILGPGYPGHNDHTHVAGGDGRFWSAPSCGI | cell wall organization proteolysis extracellular region metal ion binding zinc D-Ala-D-Ala carboxypeptidase activity Streptomyces albus G3D-structure Carboxypeptidase Cell wall biogenesis/degradation Direct protein sequencing Disulfide bond Hydrolase Metal-binding Metalloprotease Protease Secreted Signal Zinc MRPRPIRLLL MRPRPIRLLLTALVGAGLAFAPVSAVAAPTATASASADVGALDGCYTWSGTLSEGSSGEAVRQLQIRVAGYPGTGAQLAIDGQFGPATKAAVQRFQSAYGLAADGIAGPATFNKIYQLQDDDCTPVNFTYAELNRCNSDWSGGKVSAATARANALVTMWKLQAMRHAMGDKPITVNGGFRSVTCNSNVGGASNSRHMYGHAADLGAGSQGFCALAQAARNHGFTEILGPGYPGHNDHTHVAGGDGRFWSAPSCGI |
acute-phase response platelet activation positive regulation of blood coagulation protein polymerization proteolysis | collagen-containing extracellular matrix; extracellular space | calcium ion binding fibrinogen binding serine-type endopeptidase activity | Bos taurus | 3D-structure Acute phase Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hemostasis Hydrolase Kringle Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen | MARVRGPRLP | MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS | acute-phase response platelet activation positive regulation of blood coagulation protein polymerization proteolysis collagen-containing extracellular matrix; extracellular space calcium ion binding fibrinogen binding serine-type endopeptidase activity Bos taurus 3D-structure Acute phase Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hemostasis Hydrolase Kringle Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen MARVRGPRLP MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS |
complement activation, classical pathway immune response innate immune response zymogen activation | blood microparticle; extracellular exosome; extracellular region; extracellular space | calcium ion binding identical protein binding molecular sequestering activity serine-type endopeptidase activity serine-type peptidase activity | Homo sapiens | 3D-structure Complement pathway Direct protein sequencing Disease variant Disulfide bond EGF-like domain Ehlers-Danlos syndrome Glycoprotein Hydrolase Hydroxylation Immunity Innate immunity Phosphoprotein Protease Reference proteome Repeat Secreted Serine protease Signal Sushi | MWLLYLLVPA | MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED | complement activation, classical pathway immune response innate immune response zymogen activation blood microparticle; extracellular exosome; extracellular region; extracellular space calcium ion binding identical protein binding molecular sequestering activity serine-type endopeptidase activity serine-type peptidase activity Homo sapiens 3D-structure Complement pathway Direct protein sequencing Disease variant Disulfide bond EGF-like domain Ehlers-Danlos syndrome Glycoprotein Hydrolase Hydroxylation Immunity Innate immunity Phosphoprotein Protease Reference proteome Repeat Secreted Serine protease Signal Sushi MWLLYLLVPA MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED |
acute-phase response defense response defense response to bacterium immune system process negative regulation of hydrogen peroxide catabolic process negative regulation of oxidoreductase activity response to hydrogen peroxide | blood microparticle; endocytic vesicle lumen; extracellular exosome; extracellular region; extracellular space; haptoglobin-hemoglobin complex; specific granule lumen; tertiary granule lumen | antioxidant activity hemoglobin binding serine-type endopeptidase activity | Homo sapiens | 3D-structure Acute phase Alternative splicing Antibiotic Antimicrobial Antioxidant Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemoglobin-binding Immunity Reference proteome Repeat Secreted Serine protease homolog Signal Sushi | MSALGAVIAL | MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPEKKTPKSPVGVQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEEDTWYATGILSFDKSCAVAEYGVYVKVTSIQDWVQKTIAEN | acute-phase response defense response defense response to bacterium immune system process negative regulation of hydrogen peroxide catabolic process negative regulation of oxidoreductase activity response to hydrogen peroxide blood microparticle; endocytic vesicle lumen; extracellular exosome; extracellular region; extracellular space; haptoglobin-hemoglobin complex; specific granule lumen; tertiary granule lumen antioxidant activity hemoglobin binding serine-type endopeptidase activity Homo sapiens 3D-structure Acute phase Alternative splicing Antibiotic Antimicrobial Antioxidant Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hemoglobin-binding Immunity Reference proteome Repeat Secreted Serine protease homolog Signal Sushi MSALGAVIAL MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPEKKTPKSPVGVQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEEDTWYATGILSFDKSCAVAEYGVYVKVTSIQDWVQKTIAEN |
blood coagulation proteolysis zymogen activation | collagen-containing extracellular matrix; endoplasmic reticulum lumen; extracellular exosome; extracellular region; extracellular space; Golgi lumen; plasma membrane | calcium ion binding endopeptidase activity metal ion binding serine-type endopeptidase activity | Homo sapiens | 3D-structure Alternative splicing Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond EGF-like domain Gamma-carboxyglutamic acid Glycoprotein Hemophilia Hemostasis Hydrolase Hydroxylation Magnesium Metal-binding Pharmaceutical Phosphoprotein Protease Reference proteome Repeat Secreted Serine protease Signal Sulfation Thrombophilia Zymogen | MQRVNMIMAE | MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT | blood coagulation proteolysis zymogen activation collagen-containing extracellular matrix; endoplasmic reticulum lumen; extracellular exosome; extracellular region; extracellular space; Golgi lumen; plasma membrane calcium ion binding endopeptidase activity metal ion binding serine-type endopeptidase activity Homo sapiens 3D-structure Alternative splicing Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond EGF-like domain Gamma-carboxyglutamic acid Glycoprotein Hemophilia Hemostasis Hydrolase Hydroxylation Magnesium Metal-binding Pharmaceutical Phosphoprotein Protease Reference proteome Repeat Secreted Serine protease Signal Sulfation Thrombophilia Zymogen MQRVNMIMAE MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT |
blood coagulation proteolysis zymogen activation | endoplasmic reticulum lumen; extracellular space | calcium ion binding endopeptidase activity magnesium ion binding serine-type endopeptidase activity | Bos taurus | 3D-structure Blood coagulation Calcium Direct protein sequencing Disulfide bond EGF-like domain Gamma-carboxyglutamic acid Glycoprotein Hemophilia Hemostasis Hydrolase Hydroxylation Magnesium Metal-binding Phosphoprotein Protease Reference proteome Secreted Serine protease Signal Sulfation Zymogen | MWCLNMIMAE | MWCLNMIMAESPGLVTICLLGYLLSAECTVFLDRENATKILHRPKRYNSGKLEEFVRGNLERECKEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGMCKDDINSYECWCQAGFEGTNCELDATCSIKNGRCKQFCKRDTDNKVVCSCTDGYRLAEDQKSCEPAVPFPCGRVSVSHISKKLTRAETIFSNTNYENSSEAEIIWDNVTQSNQSFDEFSRVVGGEDAERGQFPWQVLLHGEIAAFCGGSIVNEKWVVTAAHCIKPGVKITVVAGEHNTEKPEPTEQKRNVIRAIPYHSYNASINKYSHDIALLELDEPLELNSYVTPICIADRDYTNIFLKFGYGYVSGWGKVFNRGRSASILQYLKVPLVDRATCLRSTKFSIYSHMFCAGYHEGGKDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT | blood coagulation proteolysis zymogen activation endoplasmic reticulum lumen; extracellular space calcium ion binding endopeptidase activity magnesium ion binding serine-type endopeptidase activity Bos taurus 3D-structure Blood coagulation Calcium Direct protein sequencing Disulfide bond EGF-like domain Gamma-carboxyglutamic acid Glycoprotein Hemophilia Hemostasis Hydrolase Hydroxylation Magnesium Metal-binding Phosphoprotein Protease Reference proteome Secreted Serine protease Signal Sulfation Zymogen MWCLNMIMAE MWCLNMIMAESPGLVTICLLGYLLSAECTVFLDRENATKILHRPKRYNSGKLEEFVRGNLERECKEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGMCKDDINSYECWCQAGFEGTNCELDATCSIKNGRCKQFCKRDTDNKVVCSCTDGYRLAEDQKSCEPAVPFPCGRVSVSHISKKLTRAETIFSNTNYENSSEAEIIWDNVTQSNQSFDEFSRVVGGEDAERGQFPWQVLLHGEIAAFCGGSIVNEKWVVTAAHCIKPGVKITVVAGEHNTEKPEPTEQKRNVIRAIPYHSYNASINKYSHDIALLELDEPLELNSYVTPICIADRDYTNIFLKFGYGYVSGWGKVFNRGRSASILQYLKVPLVDRATCLRSTKFSIYSHMFCAGYHEGGKDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT |
blood coagulation positive regulation of cell migration positive regulation of TOR signaling proteolysis | endoplasmic reticulum lumen; external side of plasma membrane; extracellular region; extracellular space; Golgi lumen; plasma membrane | calcium ion binding phospholipid binding serine-type endopeptidase activity | Homo sapiens | 3D-structure Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond EGF-like domain Gamma-carboxyglutamic acid Glycoprotein Hemostasis Hydrolase Hydroxylation Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen | MGRPLHLVLL | MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK | blood coagulation positive regulation of cell migration positive regulation of TOR signaling proteolysis endoplasmic reticulum lumen; external side of plasma membrane; extracellular region; extracellular space; Golgi lumen; plasma membrane calcium ion binding phospholipid binding serine-type endopeptidase activity Homo sapiens 3D-structure Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond EGF-like domain Gamma-carboxyglutamic acid Glycoprotein Hemostasis Hydrolase Hydroxylation Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen MGRPLHLVLL MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK |
blood coagulation proteolysis | extracellular space | calcium ion binding serine-type endopeptidase activity | Bos taurus | 3D-structure Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disulfide bond EGF-like domain Gamma-carboxyglutamic acid Glycoprotein Hemostasis Hydrolase Hydroxylation Protease Reference proteome Repeat Secreted Serine protease Signal Sulfation Zymogen | MAGLLHLVLL | MAGLLHLVLLSTALGGLLRPAGSVFLPRDQAHRVLQRARRANSFLEEVKQGNLERECLEEACSLEEAREVFEDAEQTDEFWSKYKDGDQCEGHPCLNQGHCKDGIGDYTCTCAEGFEGKNCEFSTREICSLDNGGCDQFCREERSEVRCSCAHGYVLGDDSKSCVSTERFPCGKFTQGRSRRWAIHTSEDALDASELEHYDPADLSPTESSLDLLGLNRTEPSAGEDGSQVVRIVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDWAEATLMTQKTGIVSGFGRTHEKGRLSSTLKMLEVPYVDRSTCKLSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKIMKARAGAAGSRGHSEAPATWTVPPPLPL | blood coagulation proteolysis extracellular space calcium ion binding serine-type endopeptidase activity Bos taurus 3D-structure Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disulfide bond EGF-like domain Gamma-carboxyglutamic acid Glycoprotein Hemostasis Hydrolase Hydroxylation Protease Reference proteome Repeat Secreted Serine protease Signal Sulfation Zymogen MAGLLHLVLL MAGLLHLVLLSTALGGLLRPAGSVFLPRDQAHRVLQRARRANSFLEEVKQGNLERECLEEACSLEEAREVFEDAEQTDEFWSKYKDGDQCEGHPCLNQGHCKDGIGDYTCTCAEGFEGKNCEFSTREICSLDNGGCDQFCREERSEVRCSCAHGYVLGDDSKSCVSTERFPCGKFTQGRSRRWAIHTSEDALDASELEHYDPADLSPTESSLDLLGLNRTEPSAGEDGSQVVRIVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDWAEATLMTQKTGIVSGFGRTHEKGRLSSTLKMLEVPYVDRSTCKLSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKIMKARAGAAGSRGHSEAPATWTVPPPLPL |
blood coagulation negative regulation of apoptotic process negative regulation of blood coagulation negative regulation of coagulation negative regulation of inflammatory response positive regulation of establishment of endothelial barrier proteolysis | endoplasmic reticulum; extracellular space; Golgi apparatus | calcium ion binding serine-type endopeptidase activity | Bos taurus | Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disulfide bond EGF-like domain Endoplasmic reticulum Gamma-carboxyglutamic acid Glycoprotein Golgi apparatus Hemostasis Hydrolase Hydroxylation Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen | XTSLLLFVTI | XTSLLLFVTIWGISSTPAPPDSVFSSSQRAHQVLRIRKRANSFLEELRPGNVERECSEEVCEFEEAREIFQNTEDTMAFWSFYSDGDQCEDRPSGSPCDLPCCGRGKCIDGLGGFRCDCAEGWEGRFCLHEVRFSNCSAENGGCAHYCMEEEGRRHCSCAPGYRLEDDHQLCVSKVTFPCGRLGKRMEKKRKTLKRDTNQVDQKDQLDPRIVDGQEAGWGESPWQAVLLDSKKKLVCGAVLIHVSWVLTVAHCLDSRKKLIVRLGEYDMRRWESWEVDLDIKEVIIHPNYTKSTSDNDIALLRLAKPATLSQTIVPICLPDSGLSERKLTQVGQETVVTGWGYRDETKRNRTFVLSFIKVPVVPYNACVHAMENKISENMLCAGILGDPRDACEGDSGGPMVTFFRGTWFLVGLVSWGEGCGRLYNYGVYTKVSRYLDWIYGHIKAQEAPLESQVP | blood coagulation negative regulation of apoptotic process negative regulation of blood coagulation negative regulation of coagulation negative regulation of inflammatory response positive regulation of establishment of endothelial barrier proteolysis endoplasmic reticulum; extracellular space; Golgi apparatus calcium ion binding serine-type endopeptidase activity Bos taurus Blood coagulation Calcium Cleavage on pair of basic residues Direct protein sequencing Disulfide bond EGF-like domain Endoplasmic reticulum Gamma-carboxyglutamic acid Glycoprotein Golgi apparatus Hemostasis Hydrolase Hydroxylation Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen XTSLLLFVTI XTSLLLFVTIWGISSTPAPPDSVFSSSQRAHQVLRIRKRANSFLEELRPGNVERECSEEVCEFEEAREIFQNTEDTMAFWSFYSDGDQCEDRPSGSPCDLPCCGRGKCIDGLGGFRCDCAEGWEGRFCLHEVRFSNCSAENGGCAHYCMEEEGRRHCSCAPGYRLEDDHQLCVSKVTFPCGRLGKRMEKKRKTLKRDTNQVDQKDQLDPRIVDGQEAGWGESPWQAVLLDSKKKLVCGAVLIHVSWVLTVAHCLDSRKKLIVRLGEYDMRRWESWEVDLDIKEVIIHPNYTKSTSDNDIALLRLAKPATLSQTIVPICLPDSGLSERKLTQVGQETVVTGWGYRDETKRNRTFVLSFIKVPVVPYNACVHAMENKISENMLCAGILGDPRDACEGDSGGPMVTFFRGTWFLVGLVSWGEGCGRLYNYGVYTKVSRYLDWIYGHIKAQEAPLESQVP |
complement activation complement activation, alternative pathway proteolysis response to bacterium | extracellular exosome; extracellular region; ficolin-1-rich granule lumen; platelet alpha granule lumen; secretory granule lumen | serine-type endopeptidase activity serine-type peptidase activity | Homo sapiens | 3D-structure Complement alternate pathway Direct protein sequencing Disease variant Disulfide bond Hydrolase Immunity Innate immunity Protease Reference proteome Secreted Serine protease Signal Zymogen | MHSWERLAVL | MHSWERLAVLVLLGAAACAAPPRGRILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYTRVASYAAWIDSVLA | complement activation complement activation, alternative pathway proteolysis response to bacterium extracellular exosome; extracellular region; ficolin-1-rich granule lumen; platelet alpha granule lumen; secretory granule lumen serine-type endopeptidase activity serine-type peptidase activity Homo sapiens 3D-structure Complement alternate pathway Direct protein sequencing Disease variant Disulfide bond Hydrolase Immunity Innate immunity Protease Reference proteome Secreted Serine protease Signal Zymogen MHSWERLAVL MHSWERLAVLVLLGAAACAAPPRGRILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYTRVASYAAWIDSVLA |
biological process involved in interaction with symbiont blood coagulation extracellular matrix disassembly fibrinolysis labyrinthine layer blood vessel development mononuclear cell migration muscle cell cellular homeostasis myoblast differentiation negative regulation of cell population proliferation negative regulation of cell-cell adhesion mediated by cadherin negative regulation of cell-substrate adhesion negative regulation of fibrinolysis positive regulation of blood vessel endothelial cell migration positive regulation of fibrinolysis proteolysis tissue regeneration tissue remodeling trans-synaptic signaling by BDNF, modulating synaptic transmission trophoblast giant cell differentiation | blood microparticle; cell surface; collagen-containing extracellular matrix; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; glutamatergic synapse; plasma membrane; platelet alpha granule lumen; Schaffer collateral - CA1 synapse | apolipoprotein binding endopeptidase activity enzyme binding kinase binding protease binding protein antigen binding protein domain specific binding protein-folding chaperone binding serine-type endopeptidase activity serine-type peptidase activity signaling receptor binding | Homo sapiens | 3D-structure Blood coagulation Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond Fibrinolysis Glycoprotein Hemostasis Hydrolase Kringle Phosphoprotein Protease Reference proteome Repeat Secreted Serine protease Signal Thrombophilia Tissue remodeling Zymogen | MEHKEVVLLL | MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN | biological process involved in interaction with symbiont blood coagulation extracellular matrix disassembly fibrinolysis labyrinthine layer blood vessel development mononuclear cell migration muscle cell cellular homeostasis myoblast differentiation negative regulation of cell population proliferation negative regulation of cell-cell adhesion mediated by cadherin negative regulation of cell-substrate adhesion negative regulation of fibrinolysis positive regulation of blood vessel endothelial cell migration positive regulation of fibrinolysis proteolysis tissue regeneration tissue remodeling trans-synaptic signaling by BDNF, modulating synaptic transmission trophoblast giant cell differentiation blood microparticle; cell surface; collagen-containing extracellular matrix; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; glutamatergic synapse; plasma membrane; platelet alpha granule lumen; Schaffer collateral - CA1 synapse apolipoprotein binding endopeptidase activity enzyme binding kinase binding protease binding protein antigen binding protein domain specific binding protein-folding chaperone binding serine-type endopeptidase activity serine-type peptidase activity signaling receptor binding Homo sapiens 3D-structure Blood coagulation Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond Fibrinolysis Glycoprotein Hemostasis Hydrolase Kringle Phosphoprotein Protease Reference proteome Repeat Secreted Serine protease Signal Thrombophilia Tissue remodeling Zymogen MEHKEVVLLL MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN |
blood coagulation blood coagulation, intrinsic pathway Factor XII activation fibrinolysis innate immune response plasma kallikrein-kinin cascade positive regulation of blood coagulation positive regulation of fibrinolysis positive regulation of plasminogen activation protein autoprocessing protein processing response to misfolded protein zymogen activation | collagen-containing extracellular matrix; extracellular exosome; extracellular region; extracellular space; plasma membrane; rough endoplasmic reticulum | calcium ion binding misfolded protein binding serine-type endopeptidase activity | Homo sapiens | 3D-structure Blood coagulation Direct protein sequencing Disease variant Disulfide bond EGF-like domain Fibrinolysis Glycoprotein Hemostasis Hydrolase Kringle Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen | MRALLLLGFL | MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS | blood coagulation blood coagulation, intrinsic pathway Factor XII activation fibrinolysis innate immune response plasma kallikrein-kinin cascade positive regulation of blood coagulation positive regulation of fibrinolysis positive regulation of plasminogen activation protein autoprocessing protein processing response to misfolded protein zymogen activation collagen-containing extracellular matrix; extracellular exosome; extracellular region; extracellular space; plasma membrane; rough endoplasmic reticulum calcium ion binding misfolded protein binding serine-type endopeptidase activity Homo sapiens 3D-structure Blood coagulation Direct protein sequencing Disease variant Disulfide bond EGF-like domain Fibrinolysis Glycoprotein Hemostasis Hydrolase Kringle Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen MRALLLLGFL MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS |
blood coagulation chemotaxis fibrinolysis negative regulation of fibrinolysis negative regulation of plasminogen activation plasminogen activation positive regulation of cell migration proteolysis regulation of cell adhesion regulation of cell adhesion mediated by integrin regulation of cell population proliferation regulation of fibrinolysis regulation of plasminogen activation regulation of signaling receptor activity regulation of smooth muscle cell migration regulation of smooth muscle cell-matrix adhesion regulation of wound healing response to hypoxia signal transduction smooth muscle cell migration urokinase plasminogen activator signaling pathway | cell surface; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; focal adhesion; plasma membrane; protein complex involved in cell-matrix adhesion; serine protease inhibitor complex; serine-type endopeptidase complex; specific granule membrane; tertiary granule membrane | serine-type endopeptidase activity | Homo sapiens | 3D-structure Alternative splicing Blood coagulation Direct protein sequencing Disulfide bond EGF-like domain Fibrinolysis Glycoprotein Hemostasis Hydrolase Kringle Pharmaceutical Phosphoprotein Plasminogen activation Protease Reference proteome Secreted Serine protease Signal Zymogen | MRALLARLLL | MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKLLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL | blood coagulation chemotaxis fibrinolysis negative regulation of fibrinolysis negative regulation of plasminogen activation plasminogen activation positive regulation of cell migration proteolysis regulation of cell adhesion regulation of cell adhesion mediated by integrin regulation of cell population proliferation regulation of fibrinolysis regulation of plasminogen activation regulation of signaling receptor activity regulation of smooth muscle cell migration regulation of smooth muscle cell-matrix adhesion regulation of wound healing response to hypoxia signal transduction smooth muscle cell migration urokinase plasminogen activator signaling pathway cell surface; external side of plasma membrane; extracellular exosome; extracellular region; extracellular space; focal adhesion; plasma membrane; protein complex involved in cell-matrix adhesion; serine protease inhibitor complex; serine-type endopeptidase complex; specific granule membrane; tertiary granule membrane serine-type endopeptidase activity Homo sapiens 3D-structure Alternative splicing Blood coagulation Direct protein sequencing Disulfide bond EGF-like domain Fibrinolysis Glycoprotein Hemostasis Hydrolase Kringle Pharmaceutical Phosphoprotein Plasminogen activation Protease Reference proteome Secreted Serine protease Signal Zymogen MRALLARLLL MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKLLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL |
blood coagulation fibrinolysis negative regulation of fibrinolysis negative regulation of plasminogen activation negative regulation of proteolysis plasminogen activation platelet-derived growth factor receptor signaling pathway prevention of polyspermy protein modification process proteolysis response to hypoxia smooth muscle cell migration trans-synaptic signaling by BDNF, modulating synaptic transmission | apical part of cell; cell surface; cytoplasm; extracellular exosome; extracellular region; extracellular space; glutamatergic synapse; Schaffer collateral - CA1 synapse; secretory granule; serine protease inhibitor complex | phosphoprotein binding serine-type endopeptidase activity signaling receptor binding | Homo sapiens | 3D-structure Alternative splicing Cleavage on pair of basic residues Direct protein sequencing Disulfide bond EGF-like domain Glycoprotein Hydrolase Kringle Pharmaceutical Plasminogen activation Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen | MDAMKRGLCC | MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARSYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP | blood coagulation fibrinolysis negative regulation of fibrinolysis negative regulation of plasminogen activation negative regulation of proteolysis plasminogen activation platelet-derived growth factor receptor signaling pathway prevention of polyspermy protein modification process proteolysis response to hypoxia smooth muscle cell migration trans-synaptic signaling by BDNF, modulating synaptic transmission apical part of cell; cell surface; cytoplasm; extracellular exosome; extracellular region; extracellular space; glutamatergic synapse; Schaffer collateral - CA1 synapse; secretory granule; serine protease inhibitor complex phosphoprotein binding serine-type endopeptidase activity signaling receptor binding Homo sapiens 3D-structure Alternative splicing Cleavage on pair of basic residues Direct protein sequencing Disulfide bond EGF-like domain Glycoprotein Hydrolase Kringle Pharmaceutical Plasminogen activation Protease Reference proteome Repeat Secreted Serine protease Signal Zymogen MDAMKRGLCC MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARSYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP |
complement activation complement activation, alternative pathway proteolysis response to bacterium | blood microparticle; classical-complement-pathway C3/C5 convertase complex; extracellular exosome; extracellular region; extracellular space; plasma membrane | complement binding serine-type endopeptidase activity | Homo sapiens | 3D-structure Age-related macular degeneration Alternative splicing Cleavage on pair of basic residues Complement alternate pathway Direct protein sequencing Disease variant Disulfide bond Glycation Glycoprotein Hemolytic uremic syndrome Hydrolase Immunity Innate immunity Protease Reference proteome Repeat Secreted Serine protease Signal Sushi Zymogen | MGSNLSPQLC | MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL | complement activation complement activation, alternative pathway proteolysis response to bacterium blood microparticle; classical-complement-pathway C3/C5 convertase complex; extracellular exosome; extracellular region; extracellular space; plasma membrane complement binding serine-type endopeptidase activity Homo sapiens 3D-structure Age-related macular degeneration Alternative splicing Cleavage on pair of basic residues Complement alternate pathway Direct protein sequencing Disease variant Disulfide bond Glycation Glycoprotein Hemolytic uremic syndrome Hydrolase Immunity Innate immunity Protease Reference proteome Repeat Secreted Serine protease Signal Sushi Zymogen MGSNLSPQLC MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL |
regulation of systemic arterial blood pressure zymogen activation | secretory granule | serine-type endopeptidase activity | Sus scrofa | 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Protease Reference proteome Serine protease Zymogen | APPIQSRIIG | APPIQSRIIGGRECEKNSHPWQVAIYHYSSFQCGGVLVNPKWVLTAAHCKNDNYEVWLGRHNLFENENTAQFFGVTADFPHPGFNLSLLKXHTKADGKDYSHDLMLLRLQSPAKITDAVKVLELPTQEPELGSTCEASGWGSIEPGPDBFEFPDEIQCVQLTLLQNTFCABAHPBKVTESMLCAGYLPGGKDTCMGDSGGPLICNGMWQGITSWGHTPCGSANKPSIYTKLIFYLDWINDTITENP | regulation of systemic arterial blood pressure zymogen activation secretory granule serine-type endopeptidase activity Sus scrofa 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Protease Reference proteome Serine protease Zymogen APPIQSRIIG APPIQSRIIGGRECEKNSHPWQVAIYHYSSFQCGGVLVNPKWVLTAAHCKNDNYEVWLGRHNLFENENTAQFFGVTADFPHPGFNLSLLKXHTKADGKDYSHDLMLLRLQSPAKITDAVKVLELPTQEPELGSTCEASGWGSIEPGPDBFEFPDEIQCVQLTLLQNTFCABAHPBKVTESMLCAGYLPGGKDTCMGDSGGPLICNGMWQGITSWGHTPCGSANKPSIYTKLIFYLDWINDTITENP |
bradykinin biosynthetic process cardiac muscle contraction left ventricular cardiac muscle tissue morphogenesis regulation of systemic arterial blood pressure tissue kallikrein-kinin cascade vasodilation zymogen activation | acrosomal vesicle; apical part of cell; extracellular space; nucleus; protein-containing complex; secretory granule | endopeptidase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides serine-type endopeptidase activity serine-type peptidase activity | Mus musculus | Disulfide bond Glycoprotein Hydrolase Protease Reference proteome Serine protease Signal Zymogen | MWFLILFLAL | MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYKEYICGGVLLDANWVLTAAHCYYEKNNVWLGKNNLYQDEPSAQHRLVSKSFLHPCYNMSLHRNRIQNPQDDYSYDLMLLRLSKPADITDVVKPIALPTEEPKLGSTCLASGWGSIIPVKFQYAKDLQCVNLKLLPNEDCDKAYVQKVTDVMLCAGVKGGGKDTCKGDSGGPLICDGVLQGLTSWGYNPCGEPKKPGVYTKLIKFTSWIKDTLAQNP | bradykinin biosynthetic process cardiac muscle contraction left ventricular cardiac muscle tissue morphogenesis regulation of systemic arterial blood pressure tissue kallikrein-kinin cascade vasodilation zymogen activation acrosomal vesicle; apical part of cell; extracellular space; nucleus; protein-containing complex; secretory granule endopeptidase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides serine-type endopeptidase activity serine-type peptidase activity Mus musculus Disulfide bond Glycoprotein Hydrolase Protease Reference proteome Serine protease Signal Zymogen MWFLILFLAL MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYKEYICGGVLLDANWVLTAAHCYYEKNNVWLGKNNLYQDEPSAQHRLVSKSFLHPCYNMSLHRNRIQNPQDDYSYDLMLLRLSKPADITDVVKPIALPTEEPKLGSTCLASGWGSIIPVKFQYAKDLQCVNLKLLPNEDCDKAYVQKVTDVMLCAGVKGGGKDTCKGDSGGPLICDGVLQGLTSWGYNPCGEPKKPGVYTKLIKFTSWIKDTLAQNP |
regulation of systemic arterial blood pressure zymogen activation | acrosomal vesicle; apical part of cell; extracellular space; nucleus; protein-containing complex; secretory granule | endopeptidase activity growth factor activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides metal ion binding serine-type endopeptidase activity serine-type peptidase activity | Mus musculus | 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Growth factor Hydrolase Metal-binding Protease Reference proteome Serine protease Signal Zinc Zymogen | MWFLILFLAL | MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYTQYLCGGVLLDPNWVLTAAHCYDDNYKVWLGKNNLFKDEPSAQHRFVSKAIPHPGFNMSLMRKHIRFLEYDYSNDLMLLRLSKPADITDTVKPITLPTEEPKLGSTCLASGWGSITPTKFQFTDDLYCVNLKLLPNEDCAKAHIEKVTDAMLCAGEMDGGKDTCKGDSGGPLICDGVLQGITSWGHTPCGEPDMPGVYTKLNKFTSWIKDTMAKNP | regulation of systemic arterial blood pressure zymogen activation acrosomal vesicle; apical part of cell; extracellular space; nucleus; protein-containing complex; secretory granule endopeptidase activity growth factor activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides metal ion binding serine-type endopeptidase activity serine-type peptidase activity Mus musculus 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Growth factor Hydrolase Metal-binding Protease Reference proteome Serine protease Signal Zinc Zymogen MWFLILFLAL MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYTQYLCGGVLLDPNWVLTAAHCYDDNYKVWLGKNNLFKDEPSAQHRFVSKAIPHPGFNMSLMRKHIRFLEYDYSNDLMLLRLSKPADITDTVKPITLPTEEPKLGSTCLASGWGSITPTKFQFTDDLYCVNLKLLPNEDCAKAHIEKVTDAMLCAGEMDGGKDTCKGDSGGPLICDGVLQGITSWGHTPCGEPDMPGVYTKLNKFTSWIKDTMAKNP |
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction regulation of systemic arterial blood pressure small GTPase mediated signal transduction zymogen activation | acrosomal vesicle; apical part of cell; extracellular space; nucleus; protein-containing complex; secretory granule | endopeptidase activity growth factor activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides metal ion binding serine-type endopeptidase activity serine-type peptidase activity | Mus musculus | 3D-structure Direct protein sequencing Disulfide bond Growth factor Metal-binding Reference proteome Serine protease homolog Signal Zinc | MWFLILFLAL | MWFLILFLALSLGGIDAAPPVQSQVDCENSQPWHVAVYRFNKYQCGGVLLDRNWVLTAAHCYNDKYQVWLGKNNFLEDEPSDQHRLVSKAIPHPDFNMSLLNEHTPQPEDDYSNDLMLLRLSKPADITDVVKPITLPTEEPKLGSTCLASGWGSTTPIKFKYPDDLQCVNLKLLPNEDCDKAHEMKVTDAMLCAGEMDGGSYTCEHDSGGPLICDGILQGITSWGPEPCGEPTEPSVYTKLIKFSSWIRETMANNP | positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction regulation of systemic arterial blood pressure small GTPase mediated signal transduction zymogen activation acrosomal vesicle; apical part of cell; extracellular space; nucleus; protein-containing complex; secretory granule endopeptidase activity growth factor activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides metal ion binding serine-type endopeptidase activity serine-type peptidase activity Mus musculus 3D-structure Direct protein sequencing Disulfide bond Growth factor Metal-binding Reference proteome Serine protease homolog Signal Zinc MWFLILFLAL MWFLILFLALSLGGIDAAPPVQSQVDCENSQPWHVAVYRFNKYQCGGVLLDRNWVLTAAHCYNDKYQVWLGKNNFLEDEPSDQHRLVSKAIPHPDFNMSLLNEHTPQPEDDYSNDLMLLRLSKPADITDVVKPITLPTEEPKLGSTCLASGWGSTTPIKFKYPDDLQCVNLKLLPNEDCDKAHEMKVTDAMLCAGEMDGGSYTCEHDSGGPLICDGILQGITSWGPEPCGEPTEPSVYTKLIKFSSWIRETMANNP |
regulation of systemic arterial blood pressure zymogen activation | secretory granule | metal ion binding serine-type endopeptidase activity serine-type peptidase activity | Rattus norvegicus | 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Metal-binding Protease Reference proteome Serine protease Signal Zinc Zymogen | MWLQILSLVL | MWLQILSLVLSVGRIDAAPPGQSRIVGGYKCEKNSQPWQVAVINEYLCGGVLIDPSWVITAAHCYSNNYQVLLGRNNLFKDEPFAQRRLVRQSFRHPDYIPLIVTNDTEQPVHDHSNDLMLLHLSEPADITGGVKVIDLPTKEPKVGSTCLASGWGSTNPSEMVVSHDLQCVNIHLLSNEKCIETYKDNVTDVMLCAGEMEGGKDTCAGDSGGPLICDGVLQGITSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP | regulation of systemic arterial blood pressure zymogen activation secretory granule metal ion binding serine-type endopeptidase activity serine-type peptidase activity Rattus norvegicus 3D-structure Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Metal-binding Protease Reference proteome Serine protease Signal Zinc Zymogen MWLQILSLVL MWLQILSLVLSVGRIDAAPPGQSRIVGGYKCEKNSQPWQVAVINEYLCGGVLIDPSWVITAAHCYSNNYQVLLGRNNLFKDEPFAQRRLVRQSFRHPDYIPLIVTNDTEQPVHDHSNDLMLLHLSEPADITGGVKVIDLPTKEPKVGSTCLASGWGSTNPSEMVVSHDLQCVNIHLLSNEKCIETYKDNVTDVMLCAGEMEGGKDTCAGDSGGPLICDGVLQGITSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP |
digestion proteolysis | extracellular space; serine protease inhibitor complex | endopeptidase activity metal ion binding serine-type endopeptidase activity serpin family protein binding | Bos taurus | 3D-structure Calcium Digestion Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen | MKTFIFLALL | MKTFIFLALLGAAVAFPVDDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN | digestion proteolysis extracellular space; serine protease inhibitor complex endopeptidase activity metal ion binding serine-type endopeptidase activity serpin family protein binding Bos taurus 3D-structure Calcium Digestion Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen MKTFIFLALL MKTFIFLALLGAAVAFPVDDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN |
digestion proteolysis | extracellular space | metal ion binding serine-type endopeptidase activity | Sus scrofa | 3D-structure Calcium Digestion Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Zymogen | FPTDDDDKIV | FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN | digestion proteolysis extracellular space metal ion binding serine-type endopeptidase activity Sus scrofa 3D-structure Calcium Digestion Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Zymogen FPTDDDDKIV FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN |
digestion proteolysis response to caffeine response to nicotine response to nutrient response to organic substance | extracellular space | metal ion binding serine-type endopeptidase activity | Rattus norvegicus | Calcium Digestion Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen | MSALLILALV | MSALLILALVGAAVAFPLEDDDKIVGGYTCPEHSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGDEQFINAAKIIKHPNYSSWTLNNDIMLIKLSSPVKLNARVAPVALPSACAPAGTQCLISGWGNTLSNGVNNPDLLQCVDAPVLSQADCEAAYPGEITSSMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCALPDNPGVYTKVCNFVGWIQDTIAAN | digestion proteolysis response to caffeine response to nicotine response to nutrient response to organic substance extracellular space metal ion binding serine-type endopeptidase activity Rattus norvegicus Calcium Digestion Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen MSALLILALV MSALLILALVGAAVAFPLEDDDKIVGGYTCPEHSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGDEQFINAAKIIKHPNYSSWTLNNDIMLIKLSSPVKLNARVAPVALPSACAPAGTQCLISGWGNTLSNGVNNPDLLQCVDAPVLSQADCEAAYPGEITSSMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCALPDNPGVYTKVCNFVGWIQDTIAAN |
collagen catabolic process digestion proteolysis response to nutrient | extracellular region; extracellular space | calcium ion binding serine-type endopeptidase activity | Rattus norvegicus | 3D-structure Calcium Digestion Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen | MRALLFLALV | MRALLFLALVGAAVAFPVDDDDKIVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN | collagen catabolic process digestion proteolysis response to nutrient extracellular region; extracellular space calcium ion binding serine-type endopeptidase activity Rattus norvegicus 3D-structure Calcium Digestion Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen MRALLFLALV MRALLFLALVGAAVAFPVDDDDKIVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN |
proteolysis | extracellular space | metal ion binding serine-type endopeptidase activity | Sus scrofa | 3D-structure Calcium Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen | MLRLLVVASL | MLRLLVVASLVLYGHSTQDFPETNARVVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN | proteolysis extracellular space metal ion binding serine-type endopeptidase activity Sus scrofa 3D-structure Calcium Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen MLRLLVVASL MLRLLVVASLVLYGHSTQDFPETNARVVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN |
digestive system development elastin catabolic process exocrine pancreas development inflammatory response multicellular organism growth negative regulation of transcription by RNA polymerase II pancreas morphogenesis positive regulation of angiogenesis positive regulation of transcription by RNA polymerase II post-embryonic development proteolysis regulation of cell differentiation regulation of cell population proliferation tissue remodeling transcription by RNA polymerase II Wnt signaling pathway | extracellular space | metal ion binding serine-type endopeptidase activity | Rattus norvegicus | Calcium Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen | MLRFLVFASL | MLRFLVFASLVLYGHSTQDFPETNARVVGGAEARRNSWPSQISLQYLSGGSWYHTCGGTLIRRNWVMTAAHCVSSQMTFRVVVGDHNLSQNDGTEQYVSVQKIMVHPTWNSNNVAAGYDIALLRLAQSVTLNNYVQLAVLPQEGTILANNNPCYITGWGRTRTNGQLSQTLQQAYLPSVDYSICSSSSYWGSTVKTTMVCAGGDGVRSGCQGDSGGPLHCLVNGQYSVHGVTSFVSSMGCNVSKKPTVFTRVSAYISWMNNVIAYT | digestive system development elastin catabolic process exocrine pancreas development inflammatory response multicellular organism growth negative regulation of transcription by RNA polymerase II pancreas morphogenesis positive regulation of angiogenesis positive regulation of transcription by RNA polymerase II post-embryonic development proteolysis regulation of cell differentiation regulation of cell population proliferation tissue remodeling transcription by RNA polymerase II Wnt signaling pathway extracellular space metal ion binding serine-type endopeptidase activity Rattus norvegicus Calcium Direct protein sequencing Disulfide bond Hydrolase Metal-binding Protease Reference proteome Secreted Serine protease Signal Zymogen MLRFLVFASL MLRFLVFASLVLYGHSTQDFPETNARVVGGAEARRNSWPSQISLQYLSGGSWYHTCGGTLIRRNWVMTAAHCVSSQMTFRVVVGDHNLSQNDGTEQYVSVQKIMVHPTWNSNNVAAGYDIALLRLAQSVTLNNYVQLAVLPQEGTILANNNPCYITGWGRTRTNGQLSQTLQQAYLPSVDYSICSSSSYWGSTVKTTMVCAGGDGVRSGCQGDSGGPLHCLVNGQYSVHGVTSFVSSMGCNVSKKPTVFTRVSAYISWMNNVIAYT |
proteolysis | extracellular region | serine-type endopeptidase activity | Streptomyces griseus | 3D-structure Direct protein sequencing Disulfide bond Hydrolase Protease Serine protease Signal Zymogen | MRIKRTSNRS | MRIKRTSNRSNAARRVRTTAVLAGLAAVAALAVPTANAETPRTFSANQLTAASDAVLGADIAGTAWNIDPQSKRLVVTVDSTVSKAEINQIKKSAGANADALRIERTPGKFTKLISGGDAIYSSTGRCSLGFNVRSGSTYYFLTAGHCTDGATTWWANSARTTVLGTTSGSSFPNNDYGIVRYTNTTIPKDGTVGGQDITSAANATVGMAVTRRGSTTGTHSGSVTALNATVNYGGGDVVYGMIRTNVCAEPGDSGGPLYSGTRAIGLTSGGSGNCSSGGTTFFQPVTEALSAYGVSVY | proteolysis extracellular region serine-type endopeptidase activity Streptomyces griseus3D-structure Direct protein sequencing Disulfide bond Hydrolase Protease Serine protease Signal Zymogen MRIKRTSNRS MRIKRTSNRSNAARRVRTTAVLAGLAAVAALAVPTANAETPRTFSANQLTAASDAVLGADIAGTAWNIDPQSKRLVVTVDSTVSKAEINQIKKSAGANADALRIERTPGKFTKLISGGDAIYSSTGRCSLGFNVRSGSTYYFLTAGHCTDGATTWWANSARTTVLGTTSGSSFPNNDYGIVRYTNTTIPKDGTVGGQDITSAANATVGMAVTRRGSTTGTHSGSVTALNATVNYGGGDVVYGMIRTNVCAEPGDSGGPLYSGTRAIGLTSGGSGNCSSGGTTFFQPVTEALSAYGVSVY |
proteolysis | extracellular region | metal ion binding serine-type endopeptidase activity | Bacillus licheniformis | 3D-structure Calcium Direct protein sequencing Hydrolase Metal-binding Protease Secreted Serine protease Signal Zymogen | MMRKKSFWLG | MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYAKGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ | proteolysis extracellular region metal ion binding serine-type endopeptidase activity Bacillus licheniformis3D-structure Calcium Direct protein sequencing Hydrolase Metal-binding Protease Secreted Serine protease Signal Zymogen MMRKKSFWLG MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYAKGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ |
fibrinolysis proteolysis sporulation resulting in formation of a cellular spore | extracellular region | metal ion binding serine-type endopeptidase activity | Bacillus amyloliquefaciens | 3D-structure Calcium Direct protein sequencing Hydrolase Metal-binding Protease Secreted Serine protease Signal Sporulation Zymogen | MRGKKVWISL | MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ | fibrinolysis proteolysis sporulation resulting in formation of a cellular spore extracellular region metal ion binding serine-type endopeptidase activity Bacillus amyloliquefaciens 3D-structure Calcium Direct protein sequencing Hydrolase Metal-binding Protease Secreted Serine protease Signal Sporulation Zymogen MRGKKVWISL MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ |
adaptive immune response apoptotic process bradykinin catabolic process cellular response to thyroid hormone stimulus dichotomous subdivision of terminal units involved in lung branching ERK1 and ERK2 cascade immune response immune response-regulating signaling pathway membrane protein proteolysis metanephros development negative regulation of apoptotic process neuropeptide catabolic process positive regulation of angiogenesis positive regulation of apoptotic signaling pathway positive regulation of cell migration positive regulation of cell population proliferation positive regulation of epithelial cell migration positive regulation of gene expression positive regulation of peptidase activity protein destabilization proteolysis proteolysis involved in protein catabolic process response to odorant response to retinoic acid spermatogenesis surfactant homeostasis T cell mediated cytotoxicity zymogen activation | acrosomal vesicle; alveolar lamellar body; axoneme; cytosol; extracellular space; lysosome; outer dense fiber | aminopeptidase activity cysteine-type endopeptidase activator activity involved in apoptotic process cysteine-type endopeptidase activity cysteine-type peptidase activity endopeptidase activity HLA-A specific activating MHC class I receptor activity kininogen binding peptidase activator activity involved in apoptotic process peptidase activity protein self-association protein-containing complex binding serine-type endopeptidase activity thyroid hormone binding | Rattus norvegicus | Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Lysosome Protease Reference proteome Signal Thiol protease Zymogen | MWTALPLLCA | MWTALPLLCAGAWLLSAGATAELTVNAIEKFHFTSWMKQHQKTYSSREYSHRLQVFANNWRKIQAHNQRNHTFKMGLNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPSSMDWRKKGNVVSPVKNQGACGSCWTFSTTGALESAVAIASGKMMTLAEQQLVDCAQNFNNHGCQGGLPSQAFEYILYNKGIMGEDSYPYIGKNGQCKFNPEKAVAFVKNVVNITLNDEAAMVEAVALYNPVSFAFEVTEDFMMYKSGVYSSNSCHKTPDKVNHAVLAVGYGEQNGLLYWIVKNSWGSNWGNNGYFLIERGKNMCGLAACASYPIPQV | adaptive immune response apoptotic process bradykinin catabolic process cellular response to thyroid hormone stimulus dichotomous subdivision of terminal units involved in lung branching ERK1 and ERK2 cascade immune response immune response-regulating signaling pathway membrane protein proteolysis metanephros development negative regulation of apoptotic process neuropeptide catabolic process positive regulation of angiogenesis positive regulation of apoptotic signaling pathway positive regulation of cell migration positive regulation of cell population proliferation positive regulation of epithelial cell migration positive regulation of gene expression positive regulation of peptidase activity protein destabilization proteolysis proteolysis involved in protein catabolic process response to odorant response to retinoic acid spermatogenesis surfactant homeostasis T cell mediated cytotoxicity zymogen activation acrosomal vesicle; alveolar lamellar body; axoneme; cytosol; extracellular space; lysosome; outer dense fiber aminopeptidase activity cysteine-type endopeptidase activator activity involved in apoptotic process cysteine-type endopeptidase activity cysteine-type peptidase activity endopeptidase activity HLA-A specific activating MHC class I receptor activity kininogen binding peptidase activator activity involved in apoptotic process peptidase activity protein self-association protein-containing complex binding serine-type endopeptidase activity thyroid hormone binding Rattus norvegicus Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Lysosome Protease Reference proteome Signal Thiol protease Zymogen MWTALPLLCA MWTALPLLCAGAWLLSAGATAELTVNAIEKFHFTSWMKQHQKTYSSREYSHRLQVFANNWRKIQAHNQRNHTFKMGLNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPSSMDWRKKGNVVSPVKNQGACGSCWTFSTTGALESAVAIASGKMMTLAEQQLVDCAQNFNNHGCQGGLPSQAFEYILYNKGIMGEDSYPYIGKNGQCKFNPEKAVAFVKNVVNITLNDEAAMVEAVALYNPVSFAFEVTEDFMMYKSGVYSSNSCHKTPDKVNHAVLAVGYGEQNGLLYWIVKNSWGSNWGNNGYFLIERGKNMCGLAACASYPIPQV |
autophagy cellular response to mechanical stimulus cellular response to thyroid hormone stimulus collagen catabolic process decidualization epithelial cell differentiation neuron apoptotic process protein catabolic process proteolysis proteolysis involved in protein catabolic process response to amine response to cytokine response to dexamethasone response to ethanol response to glucose response to interleukin-4 response to mechanical stimulus response to organic cyclic compound response to peptide hormone skeletal muscle tissue development spermatogenesis thyroid hormone generation viral entry into host cell | apical plasma membrane; cell surface; external side of plasma membrane; extracellular region; extracellular space; lysosome; melanosome; peptidase inhibitor complex; perinuclear region of cytoplasm; sarcolemma | collagen binding cysteine-type endopeptidase activity cysteine-type peptidase activity endopeptidase activity kininogen binding peptidase activity peptide binding protein self-association protein-containing complex binding proteoglycan binding | Rattus norvegicus | 3D-structure Acetylation Cell membrane Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Lysosome Membrane Protease Reference proteome Secreted Signal Thiol protease Zymogen | MWWSLIPLSC | MWWSLIPLSCLLALTSAHDKPSSHPLSDDMINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGGPNLPERVGFSEDINLPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAWNFWTRKGLVSGGVYNSHIGCLPYTIPPCEHHVNGSRPPCTGEGDTPKCNKMCEAGYSTSYKEDKHYGYTSYSVSDSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHCGIESEIVAGIPRTQQYWGRF | autophagy cellular response to mechanical stimulus cellular response to thyroid hormone stimulus collagen catabolic process decidualization epithelial cell differentiation neuron apoptotic process protein catabolic process proteolysis proteolysis involved in protein catabolic process response to amine response to cytokine response to dexamethasone response to ethanol response to glucose response to interleukin-4 response to mechanical stimulus response to organic cyclic compound response to peptide hormone skeletal muscle tissue development spermatogenesis thyroid hormone generation viral entry into host cell apical plasma membrane; cell surface; external side of plasma membrane; extracellular region; extracellular space; lysosome; melanosome; peptidase inhibitor complex; perinuclear region of cytoplasm; sarcolemma collagen binding cysteine-type endopeptidase activity cysteine-type peptidase activity endopeptidase activity kininogen binding peptidase activity peptide binding protein self-association protein-containing complex binding proteoglycan binding Rattus norvegicus 3D-structure Acetylation Cell membrane Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Lysosome Membrane Protease Reference proteome Secreted Signal Thiol protease Zymogen MWWSLIPLSC MWWSLIPLSCLLALTSAHDKPSSHPLSDDMINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGGPNLPERVGFSEDINLPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAWNFWTRKGLVSGGVYNSHIGCLPYTIPPCEHHVNGSRPPCTGEGDTPKCNKMCEAGYSTSYKEDKHYGYTSYSVSDSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHCGIESEIVAGIPRTQQYWGRF |
proteolysis | acrosomal vesicle; cytoplasm; plasma membrane | calcium ion binding calcium-dependent cysteine-type endopeptidase activity | Gallus gallus | Calcium Cell membrane Cytoplasm Hydrolase Membrane Metal-binding Protease Reference proteome Repeat Thiol protease | MMPFGGIAAR | MMPFGGIAARLQRDRLRAEGVGEHNNAVKYLNQDYEALKQECIESGTLFRDPQFPAGPTALGFKELGPYSSKTRGVEWKRPSELVDDPQFIVGGATRTDICQGALGDCWLLAAIGSLTLNEELLHRVVPHGQSFQEDYAGIFHFQIWQFGEWVDVVVDDLLPTKDGELLFVHSAECTEFWSALLEKAYAKLNGCYESLSGGSTTEGFEDFTGGVAEMYDLKRAPRNMGHIIRKALERGSLLGCSIDITSAFDMEAVTFKKLVKGHAYSVTAFKDVNYRGQQEQLIRIRNPWGQVEWTGAWSDGSSEWDNIDPSDREELQLKMEDGEFWMSFRDFMREFSRLEICNLTPDALTKDELSRWHTQVFEGTWRRGSTAGGCRNNPATFWINPQFKIKLLEEDDDPGDDEVACSFLVALMQKHRRRERRVGGDMHTIGFAVYEVPEEAQGSQNVHLKKDFFLRNQSRARSETFINLREVSNQIRLPPGEYIVVPSTFEPHKEADFILRVFTEKQSDTAELDEEISADLADEEEITEDDIEDGFKNMFQQLAGEDMEISVFELKTILNRVIARHKDLKTDGFSLDSCRNMVNLMDKDGSARLGLVEFQILWNKIRSWLTIFRQYDLDKSGTMSSYEMRMALESAGFKLNNKLHQVVVARYADAETGVDFDNFVCCLVKLETMFRFFHSMDRDGTGTAVMNLAEWLLLTMCG | proteolysis acrosomal vesicle; cytoplasm; plasma membrane calcium ion binding calcium-dependent cysteine-type endopeptidase activity Gallus gallus Calcium Cell membrane Cytoplasm Hydrolase Membrane Metal-binding Protease Reference proteome Repeat Thiol protease MMPFGGIAAR MMPFGGIAARLQRDRLRAEGVGEHNNAVKYLNQDYEALKQECIESGTLFRDPQFPAGPTALGFKELGPYSSKTRGVEWKRPSELVDDPQFIVGGATRTDICQGALGDCWLLAAIGSLTLNEELLHRVVPHGQSFQEDYAGIFHFQIWQFGEWVDVVVDDLLPTKDGELLFVHSAECTEFWSALLEKAYAKLNGCYESLSGGSTTEGFEDFTGGVAEMYDLKRAPRNMGHIIRKALERGSLLGCSIDITSAFDMEAVTFKKLVKGHAYSVTAFKDVNYRGQQEQLIRIRNPWGQVEWTGAWSDGSSEWDNIDPSDREELQLKMEDGEFWMSFRDFMREFSRLEICNLTPDALTKDELSRWHTQVFEGTWRRGSTAGGCRNNPATFWINPQFKIKLLEEDDDPGDDEVACSFLVALMQKHRRRERRVGGDMHTIGFAVYEVPEEAQGSQNVHLKKDFFLRNQSRARSETFINLREVSNQIRLPPGEYIVVPSTFEPHKEADFILRVFTEKQSDTAELDEEISADLADEEEITEDDIEDGFKNMFQQLAGEDMEISVFELKTILNRVIARHKDLKTDGFSLDSCRNMVNLMDKDGSARLGLVEFQILWNKIRSWLTIFRQYDLDKSGTMSSYEMRMALESAGFKLNNKLHQVVVARYADAETGVDFDNFVCCLVKLETMFRFFHSMDRDGTGTAVMNLAEWLLLTMCG |
digestion proteolysis | extracellular region | aspartic-type endopeptidase activity | Sus scrofa | 3D-structure Aspartyl protease Digestion Direct protein sequencing Disulfide bond Hydrolase Phosphoprotein Protease Reference proteome Secreted Signal Zymogen | MKWLLLLSLV | MKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA | digestion proteolysis extracellular region aspartic-type endopeptidase activity Sus scrofa 3D-structure Aspartyl protease Digestion Direct protein sequencing Disulfide bond Hydrolase Phosphoprotein Protease Reference proteome Secreted Signal Zymogen MKWLLLLSLV MKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA |
proteolysis | extracellular space; lysosome; melanosome | aspartic-type endopeptidase activity | Sus scrofa | Aspartyl protease Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Lysosome Protease Reference proteome Secreted Zymogen | GPIPEVLKNY | GPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSGKSSTYVKNGTTFAIHYGSGSLSGYLSSQDTVSVPCNSALSGVGGIKVERQTFGEATKQPGLTFIAAKFDGILGMAYPRISVNNVVPVFDNLMQQKLVDKDIFSFYLNRDPGAQPGGELMLGGIDSKYYKGSLDYHNVTRKAYWQIHMNQVAVGSSLTLCKGGCEAIVDTGTSLIVGQPEEVRELGKAIGAVPLIQGEYMIPCEKVPSLPDVTVTLGGKKYKLSSENYTLKVSQAGQTICLSGFMGMDIPPPGGPLWILGDVFIGRYYTVFDRDLNRVGLAEAA | proteolysis extracellular space; lysosome; melanosome aspartic-type endopeptidase activity Sus scrofa Aspartyl protease Direct protein sequencing Disulfide bond Glycoprotein Hydrolase Lysosome Protease Reference proteome Secreted Zymogen GPIPEVLKNY GPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSGKSSTYVKNGTTFAIHYGSGSLSGYLSSQDTVSVPCNSALSGVGGIKVERQTFGEATKQPGLTFIAAKFDGILGMAYPRISVNNVVPVFDNLMQQKLVDKDIFSFYLNRDPGAQPGGELMLGGIDSKYYKGSLDYHNVTRKAYWQIHMNQVAVGSSLTLCKGGCEAIVDTGTSLIVGQPEEVRELGKAIGAVPLIQGEYMIPCEKVPSLPDVTVTLGGKKYKLSSENYTLKVSQAGQTICLSGFMGMDIPPPGGPLWILGDVFIGRYYTVFDRDLNRVGLAEAA |
angiotensin maturation gene expression kidney development positive regulation of blood pressure proteolysis regulation of blood pressure regulation of MAPK cascade response to cAMP response to cGMP response to xenobiotic stimulus | apical part of cell; extracellular space | aspartic-type endopeptidase activity endopeptidase activity insulin-like growth factor receptor binding peptidase activity signaling receptor binding | Mus musculus | 3D-structure Aspartyl protease Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Hydrolase Protease Reference proteome Secreted Signal Zymogen | MDRRRMPLWA | MDRRRMPLWALLLLWSPCTFSLPTGTTFERIPLKKMPSVREILEERGVDMTRLSAEWDVFTKRSSLTDLISPVVLTNYLNSQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSRLYLACGIHSLYESSDSSSYMENGDDFTIHYGSGRVKGFLSQDSVTVGGITVTQTFGEVTELPLIPFMLAQFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEKVFSVYYNRGPHLLGGEVVLGGSDPEHYQGDFHYVSLSKTDSWQITMKGVSVGSSTLLCEEGCEVVVDTGSSFISAPTSSLKLIMQALGAKEKRLHEYVVSCSQVPTLPDISFNLGGRAYTLSSTDYVLQYPNRRDKLCTVALHAMDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR | angiotensin maturation gene expression kidney development positive regulation of blood pressure proteolysis regulation of blood pressure regulation of MAPK cascade response to cAMP response to cGMP response to xenobiotic stimulus apical part of cell; extracellular space aspartic-type endopeptidase activity endopeptidase activity insulin-like growth factor receptor binding peptidase activity signaling receptor binding Mus musculus 3D-structure Aspartyl protease Cleavage on pair of basic residues Direct protein sequencing Disulfide bond Hydrolase Protease Reference proteome Secreted Signal Zymogen MDRRRMPLWA MDRRRMPLWALLLLWSPCTFSLPTGTTFERIPLKKMPSVREILEERGVDMTRLSAEWDVFTKRSSLTDLISPVVLTNYLNSQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSRLYLACGIHSLYESSDSSSYMENGDDFTIHYGSGRVKGFLSQDSVTVGGITVTQTFGEVTELPLIPFMLAQFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEKVFSVYYNRGPHLLGGEVVLGGSDPEHYQGDFHYVSLSKTDSWQITMKGVSVGSSTLLCEEGCEVVVDTGSSFISAPTSSLKLIMQALGAKEKRLHEYVVSCSQVPTLPDISFNLGGRAYTLSSTDYVLQYPNRRDKLCTVALHAMDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR |
amyloid-beta metabolic process angiotensin maturation cell maturation cellular response to xenobiotic stimulus drinking behavior hormone-mediated signaling pathway juxtaglomerular apparatus development kidney development male gonad development mesonephros development proteolysis regulation of blood pressure regulation of MAPK cascade renin-angiotensin regulation of aldosterone production response to cAMP response to cGMP response to immobilization stress response to lipopolysaccharide | apical part of cell; extracellular region; extracellular space; plasma membrane | aspartic-type endopeptidase activity insulin-like growth factor receptor binding peptidase activity signaling receptor binding | Homo sapiens | 3D-structure Alternative splicing Aspartyl protease Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hydrolase Membrane Protease Reference proteome Secreted Signal Zymogen | MDGWRRMPRW | MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR | amyloid-beta metabolic process angiotensin maturation cell maturation cellular response to xenobiotic stimulus drinking behavior hormone-mediated signaling pathway juxtaglomerular apparatus development kidney development male gonad development mesonephros development proteolysis regulation of blood pressure regulation of MAPK cascade renin-angiotensin regulation of aldosterone production response to cAMP response to cGMP response to immobilization stress response to lipopolysaccharide apical part of cell; extracellular region; extracellular space; plasma membrane aspartic-type endopeptidase activity insulin-like growth factor receptor binding peptidase activity signaling receptor binding Homo sapiens 3D-structure Alternative splicing Aspartyl protease Cleavage on pair of basic residues Direct protein sequencing Disease variant Disulfide bond Glycoprotein Hydrolase Membrane Protease Reference proteome Secreted Signal Zymogen MDGWRRMPRW MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR |
proteolysis | extracellular region | metal ion binding metalloendopeptidase activity | Bacillus thermoproteolyticus | 3D-structure Calcium Direct protein sequencing Hydrolase Metal-binding Metalloprotease Protease Secreted Signal Zinc Zymogen | MKMKMKLASF | MKMKMKLASFGLAAGLAAQVFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSPEELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTSHVKDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEFVVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK | proteolysis extracellular region metal ion binding metalloendopeptidase activity Bacillus thermoproteolyticus3D-structure Calcium Direct protein sequencing Hydrolase Metal-binding Metalloprotease Protease Secreted Signal Zinc Zymogen MKMKMKLASF MKMKMKLASFGLAAGLAAQVFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSPEELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTSHVKDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEFVVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK |
protein processing proteolysis signal peptide processing | plasma membrane | endopeptidase activity peptidase activity serine-type endopeptidase activity | Escherichia coli | 3D-structure Cell inner membrane Cell membrane Disulfide bond Hydrolase Membrane Protease Reference proteome Transmembrane Transmembrane helix | MANMFALILV | MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGWLETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTLIETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENALPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILTVPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAIWMSFDKQEGEWPTGLRLSRIGGIH | protein processing proteolysis signal peptide processing plasma membrane endopeptidase activity peptidase activity serine-type endopeptidase activity Escherichia coli 3D-structure Cell inner membrane Cell membrane Disulfide bond Hydrolase Membrane Protease Reference proteome Transmembrane Transmembrane helix MANMFALILV MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGWLETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTLIETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENALPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILTVPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAIWMSFDKQEGEWPTGLRLSRIGGIH |
lipoprotein biosynthetic process via signal peptide cleavage proteolysis | plasma membrane | aspartic-type endopeptidase activity endopeptidase activity | Escherichia coli | Aspartyl protease Cell inner membrane Cell membrane Hydrolase Membrane Protease Reference proteome Transmembrane Transmembrane helix | MSQSICSTGL | MSQSICSTGLRWLWLVVVVLIIDLGSKYLILQNFALGDTVPLFPSLNLHYARNYGAAFSFLADSGGWQRWFFAGIAIGISVILAVMMYRSKATQKLNNIAYALIIGGALGNLFDRLWHGFVVDMIDFYVGDWHFATFNLADTAICVGAALIVLEGFLPSRAKKQ | lipoprotein biosynthetic process via signal peptide cleavage proteolysis plasma membrane aspartic-type endopeptidase activity endopeptidase activity Escherichia coli Aspartyl protease Cell inner membrane Cell membrane Hydrolase Membrane Protease Reference proteome Transmembrane Transmembrane helix MSQSICSTGL MSQSICSTGLRWLWLVVVVLIIDLGSKYLILQNFALGDTVPLFPSLNLHYARNYGAAFSFLADSGGWQRWFFAGIAIGISVILAVMMYRSKATQKLNNIAYALIIGGALGNLFDRLWHGFVVDMIDFYVGDWHFATFNLADTAICVGAALIVLEGFLPSRAKKQ |
asparagine catabolic process protein homotetramerization | outer membrane-bounded periplasmic space; periplasmic space; protein-containing complex | asparaginase activity identical protein binding | Escherichia coli | 3D-structure Direct protein sequencing Disulfide bond Hydrolase Periplasm Pharmaceutical Reference proteome Signal | MEFFKKTALA | MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY | asparagine catabolic process protein homotetramerization outer membrane-bounded periplasmic space; periplasmic space; protein-containing complex asparaginase activity identical protein binding Escherichia coli 3D-structure Direct protein sequencing Disulfide bond Hydrolase Periplasm Pharmaceutical Reference proteome Signal MEFFKKTALA MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY |
defense response to bacterium negative regulation of viral transcription peptidoglycan catabolic process viral release from host cell by cytolysis | host cell cytoplasm | N-acetylmuramoyl-L-alanine amidase activity zinc ion binding | Escherichia phage T7 | 3D-structure Antimicrobial Bacteriolytic enzyme Cytolysis Host cell lysis by virus Host cytoplasm Hydrolase Late protein Metal-binding Reference proteome Viral release from host cell Zinc | MARVQFKQRE | MARVQFKQRESTDAIFVHCSATKPSQNVGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDEMAVGSHAKGYNHNSIGVCLVGGIDDKGKFDANFTPAQMQSLRSLLVTLLAKYEGAVLRAHHEVAPKACPSFDLKRWWEKNELVTSDRG | defense response to bacterium negative regulation of viral transcription peptidoglycan catabolic process viral release from host cell by cytolysis host cell cytoplasm N-acetylmuramoyl-L-alanine amidase activity zinc ion binding Escherichia phage T7 3D-structure Antimicrobial Bacteriolytic enzyme Cytolysis Host cell lysis by virus Host cytoplasm Hydrolase Late protein Metal-binding Reference proteome Viral release from host cell Zinc MARVQFKQRE MARVQFKQRESTDAIFVHCSATKPSQNVGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDEMAVGSHAKGYNHNSIGVCLVGGIDDKGKFDANFTPAQMQSLRSLLVTLLAKYEGAVLRAHHEVAPKACPSFDLKRWWEKNELVTSDRG |
antibiotic catabolic process response to antibiotic | outer membrane-bounded periplasmic space | beta-lactamase activity | Escherichia coli | 3D-structure Antibiotic resistance Direct protein sequencing Hydrolase Periplasm Reference proteome Signal | MFKTTLCALL | MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNALQ | antibiotic catabolic process response to antibiotic outer membrane-bounded periplasmic space beta-lactamase activity Escherichia coli 3D-structure Antibiotic resistance Direct protein sequencing Hydrolase Periplasm Reference proteome Signal MFKTTLCALL MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNALQ |
arginine catabolic process to ornithine regulation of ornithine metabolic process urea cycle | cytoplasm; cytosol; mating projection tip; nucleus; ornithine carbamoyltransferase inhibitor complex | arginase activity manganese ion binding ornithine carbamoyltransferase inhibitor activity zinc ion binding | Saccharomyces cerevisiae | Acetylation Arginine metabolism Hydrolase Manganese Metal-binding Phosphoprotein Reference proteome | METGPHYNYY | METGPHYNYYKNRELSIVLAPFSGGQGKLGVEKGPKYMLKHGLQTSIEDLGWSTELEPSMDEAQFVGKLKMEKDSTTGGSSVMIDGVKAKRADLVGEATKLVYNSVSKVVQANRFPLTLGGDHSIAIGTVSAVLDKYPDAGLLWIDAHADINTIESTPSGNLHGCPVSFLMGLNKDVPHCPESLKWVPGNLSPKKIAYIGLRDVDAGEKKILKDLGIAAFSMYHVDKYGINAVIEMAMKAVHPETNGEGPIMCSYDVDGVDPLYIPATGTPVRGGLTLREGLFLVERLAESGNLIALDVVECNPDLAIHDIHVSNTISAGCAIARCALGETLL | arginine catabolic process to ornithine regulation of ornithine metabolic process urea cycle cytoplasm; cytosol; mating projection tip; nucleus; ornithine carbamoyltransferase inhibitor complex arginase activity manganese ion binding ornithine carbamoyltransferase inhibitor activity zinc ion binding Saccharomyces cerevisiae Acetylation Arginine metabolism Hydrolase Manganese Metal-binding Phosphoprotein Reference proteome METGPHYNYY METGPHYNYYKNRELSIVLAPFSGGQGKLGVEKGPKYMLKHGLQTSIEDLGWSTELEPSMDEAQFVGKLKMEKDSTTGGSSVMIDGVKAKRADLVGEATKLVYNSVSKVVQANRFPLTLGGDHSIAIGTVSAVLDKYPDAGLLWIDAHADINTIESTPSGNLHGCPVSFLMGLNKDVPHCPESLKWVPGNLSPKKIAYIGLRDVDAGEKKILKDLGIAAFSMYHVDKYGINAVIEMAMKAVHPETNGEGPIMCSYDVDGVDPLYIPATGTPVRGGLTLREGLFLVERLAESGNLIALDVVECNPDLAIHDIHVSNTISAGCAIARCALGETLL |
histidine biosynthetic process | cytoplasm | ATP binding histidinol dehydrogenase activity metal ion binding NAD binding phosphoribosyl-AMP cyclohydrolase activity phosphoribosyl-ATP diphosphatase activity | Saccharomyces cerevisiae | Amino-acid biosynthesis ATP-binding Histidine biosynthesis Hydrolase Metal-binding Multifunctional enzyme NAD Nucleotide-binding Oxidoreductase Reference proteome Zinc | MVLPILPLID | MVLPILPLIDDLASWNSKKEYVSLVGQVLLDGSSLSNEEILQFSKEEEVPLVALSLPSGKFSDDEIIAFLNNGVSSLFIASQDAKTAEHLVEQLNVPKERVVVEENGVFSNQFMVKQKFSQDKIVSIKKLSKDMLTKEVLGEVRTDRPDGLYTTLVVDQYERCLGLVYSSKKSIAKAIDLGRGVYYSRSRNEIWIKGETSGNGQKLLQISTDCDSDALKFIVEQENVGFCHLETMSCFGEFKHGLVGLESLLKQRLQDAPEESYTRRLFNDSALLDAKIKEEAEELTEAKGKKELSWEAADLFYFALAKLVANDVSLKDVENNLNMKHLKVTRRKGDAKPKFVGQPKAEEEKLTGPIHLDVVKASDKVGVQKALSRPIQKTSEIMHLVNPIIENVRDKGNSALLEYTEKFDGVKLSNPVLNAPFPEEYFEGLTEEMKEALDLSIENVRKFHAAQLPTETLEVETQPGVLCSRFPRPIEKVGLYIPGGTAILPSTALMLGVPAQVAQCKEIVFASPPRKSDGKVSPEVVYVAEKVGASKIVLAGGAQAVAAMAYGTETIPKVDKILGPGNQFVTAAKMYVQNDTQALCSIDMPAGPSEVLVIADEDADVDFVASDLLSQAEHGIDSQVILVGVNLSEKKIQEIQDAVHNQALQLPRVDIVRKCIAHSTIVLCDGYEEALEMSNQYAPEHLILQIANANDYVKLVDNAGSVFVGAYTPESCGDYSSGTNHTLPTYGYARQYSGANTATFQKFITAQNITPEGLENIGRAVMCVAKKEGLDGHRNAVKIRMSKLGLIPKDFQ | histidine biosynthetic process cytoplasm ATP binding histidinol dehydrogenase activity metal ion binding NAD binding phosphoribosyl-AMP cyclohydrolase activity phosphoribosyl-ATP diphosphatase activity Saccharomyces cerevisiae Amino-acid biosynthesis ATP-binding Histidine biosynthesis Hydrolase Metal-binding Multifunctional enzyme NAD Nucleotide-binding Oxidoreductase Reference proteome Zinc MVLPILPLID MVLPILPLIDDLASWNSKKEYVSLVGQVLLDGSSLSNEEILQFSKEEEVPLVALSLPSGKFSDDEIIAFLNNGVSSLFIASQDAKTAEHLVEQLNVPKERVVVEENGVFSNQFMVKQKFSQDKIVSIKKLSKDMLTKEVLGEVRTDRPDGLYTTLVVDQYERCLGLVYSSKKSIAKAIDLGRGVYYSRSRNEIWIKGETSGNGQKLLQISTDCDSDALKFIVEQENVGFCHLETMSCFGEFKHGLVGLESLLKQRLQDAPEESYTRRLFNDSALLDAKIKEEAEELTEAKGKKELSWEAADLFYFALAKLVANDVSLKDVENNLNMKHLKVTRRKGDAKPKFVGQPKAEEEKLTGPIHLDVVKASDKVGVQKALSRPIQKTSEIMHLVNPIIENVRDKGNSALLEYTEKFDGVKLSNPVLNAPFPEEYFEGLTEEMKEALDLSIENVRKFHAAQLPTETLEVETQPGVLCSRFPRPIEKVGLYIPGGTAILPSTALMLGVPAQVAQCKEIVFASPPRKSDGKVSPEVVYVAEKVGASKIVLAGGAQAVAAMAYGTETIPKVDKILGPGNQFVTAAKMYVQNDTQALCSIDMPAGPSEVLVIADEDADVDFVASDLLSQAEHGIDSQVILVGVNLSEKKIQEIQDAVHNQALQLPRVDIVRKCIAHSTIVLCDGYEEALEMSNQYAPEHLILQIANANDYVKLVDNAGSVFVGAYTPESCGDYSSGTNHTLPTYGYARQYSGANTATFQKFITAQNITPEGLENIGRAVMCVAKKEGLDGHRNAVKIRMSKLGLIPKDFQ |
phosphate-containing compound metabolic process | cytoplasm; nucleus | inorganic diphosphate phosphatase activity magnesium ion binding | Saccharomyces cerevisiae | 3D-structure Cytoplasm Direct protein sequencing Hydrolase Isopeptide bond Magnesium Metal-binding Phosphoprotein Reference proteome Ubl conjugation | MTYTTRQIGA | MTYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKENNIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFVRNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPIDVLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDINDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPENQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGIDLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWFFISGSV | phosphate-containing compound metabolic process cytoplasm; nucleus inorganic diphosphate phosphatase activity magnesium ion binding Saccharomyces cerevisiae 3D-structure Cytoplasm Direct protein sequencing Hydrolase Isopeptide bond Magnesium Metal-binding Phosphoprotein Reference proteome Ubl conjugation MTYTTRQIGA MTYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKENNIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFVRNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPIDVLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDINDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPENQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGIDLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWFFISGSV |
proton motive force-driven mitochondrial ATP synthesis | mitochondrial proton-transporting ATP synthase complex; proton-transporting ATP synthase complex, catalytic core F(1) | ATP binding ATP hydrolysis activity proton-transporting ATP synthase activity, rotational mechanism proton-transporting ATPase activity, rotational mechanism | Bos taurus | 3D-structure Acetylation ATP synthesis ATP-binding CF(1) Direct protein sequencing Glycoprotein Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Phosphoprotein Reference proteome Transit peptide Translocase Transport | MLGLVGRVVA | MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS | proton motive force-driven mitochondrial ATP synthesis mitochondrial proton-transporting ATP synthase complex; proton-transporting ATP synthase complex, catalytic core F(1) ATP binding ATP hydrolysis activity proton-transporting ATP synthase activity, rotational mechanism proton-transporting ATPase activity, rotational mechanism Bos taurus 3D-structure Acetylation ATP synthesis ATP-binding CF(1) Direct protein sequencing Glycoprotein Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Phosphoprotein Reference proteome Transit peptide Translocase Transport MLGLVGRVVA MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS |
proton motive force-driven ATP synthesis proton motive force-driven mitochondrial ATP synthesis | cytosol; mitochondrial inner membrane; mitochondrial intermembrane space; mitochondrial proton-transporting ATP synthase complex; mitochondrial proton-transporting ATP synthase, catalytic core; mitochondrion; proton-transporting ATP synthase complex, catalytic core F(1) | ATP binding ATP hydrolysis activity proton-transporting ATP synthase activity, rotational mechanism proton-transporting ATPase activity, rotational mechanism | Saccharomyces cerevisiae | 3D-structure ATP synthesis ATP-binding CF(1) Direct protein sequencing Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Phosphoprotein Reference proteome Transit peptide Translocase Transport | MVLPRLYTAT | MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN | proton motive force-driven ATP synthesis proton motive force-driven mitochondrial ATP synthesis cytosol; mitochondrial inner membrane; mitochondrial intermembrane space; mitochondrial proton-transporting ATP synthase complex; mitochondrial proton-transporting ATP synthase, catalytic core; mitochondrion; proton-transporting ATP synthase complex, catalytic core F(1) ATP binding ATP hydrolysis activity proton-transporting ATP synthase activity, rotational mechanism proton-transporting ATPase activity, rotational mechanism Saccharomyces cerevisiae 3D-structure ATP synthesis ATP-binding CF(1) Direct protein sequencing Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Nucleotide-binding Phosphoprotein Reference proteome Transit peptide Translocase Transport MVLPRLYTAT MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN |
proton motive force-driven ATP synthesis proton motive force-driven mitochondrial ATP synthesis response to hyperoxia | mitochondrial inner membrane; mitochondrial proton-transporting ATP synthase complex; proton-transporting ATP synthase complex, coupling factor F(o) | proton transmembrane transporter activity | Homo sapiens | 3D-structure ATP synthesis Cardiomyopathy CF(0) Disease variant Hydrogen ion transport Ion transport Leber hereditary optic neuropathy Leigh syndrome Membrane Mitochondrion Mitochondrion inner membrane Neuropathy Primary mitochondrial disease Reference proteome Retinitis pigmentosa Transmembrane Transmembrane helix Transport | MNENLFASFI | MNENLFASFIAPTILGLPAAVLIILFPPLLIPTSKYLINNRLITTQQWLIKLTSKQMMTMHNTKGRTWSLMLVSLIIFIATTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGTVIMGFRSKIKNALAHFLPQGTPTPLIPMLVIIETISLLIQPMALAVRLTANITAGHLLMHLIGSATLAMSTINLPSTLIIFTILILLTILEIAVALIQAYVFTLLVSLYLHDNT | proton motive force-driven ATP synthesis proton motive force-driven mitochondrial ATP synthesis response to hyperoxia mitochondrial inner membrane; mitochondrial proton-transporting ATP synthase complex; proton-transporting ATP synthase complex, coupling factor F(o) proton transmembrane transporter activity Homo sapiens 3D-structure ATP synthesis Cardiomyopathy CF(0) Disease variant Hydrogen ion transport Ion transport Leber hereditary optic neuropathy Leigh syndrome Membrane Mitochondrion Mitochondrion inner membrane Neuropathy Primary mitochondrial disease Reference proteome Retinitis pigmentosa Transmembrane Transmembrane helix Transport MNENLFASFI MNENLFASFIAPTILGLPAAVLIILFPPLLIPTSKYLINNRLITTQQWLIKLTSKQMMTMHNTKGRTWSLMLVSLIIFIATTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGTVIMGFRSKIKNALAHFLPQGTPTPLIPMLVIIETISLLIQPMALAVRLTANITAGHLLMHLIGSATLAMSTINLPSTLIIFTILILLTILEIAVALIQAYVFTLLVSLYLHDNT |
proton motive force-driven ATP synthesis | mitochondrial inner membrane; mitochondrial proton-transporting ATP synthase complex; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); mitochondrion | proton transmembrane transporter activity | Saccharomyces cerevisiae | 3D-structure ATP synthesis CF(0) Direct protein sequencing Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Transmembrane Transmembrane helix Transport | MFNLLNTYIT | MFNLLNTYITSPLDQFEIRTLFGLQSSFIDLSCLNLTTFSLYTIIVLLVITSLYTLTNNNNKIIGSRWLISQEAIYDTIMNMTKGQIGGKNWGLYFPMIFTLFMFIFIANLISMIPYSFALSAHLVFIISLSIVIWLGNTILGLYKHGWVFFSLFVPAGTPLPLVPLLVIIETLSYFARAISLGLRLGSNILAGHLLMVILAGLTFNFMLINLFTLVFGFVPLAMILAIMMLEFAIGIIQGYVWAILTASYLKDAVYLH | proton motive force-driven ATP synthesis mitochondrial inner membrane; mitochondrial proton-transporting ATP synthase complex; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); mitochondrion proton transmembrane transporter activity Saccharomyces cerevisiae 3D-structure ATP synthesis CF(0) Direct protein sequencing Hydrogen ion transport Ion transport Membrane Mitochondrion Mitochondrion inner membrane Reference proteome Transmembrane Transmembrane helix Transport MFNLLNTYIT MFNLLNTYITSPLDQFEIRTLFGLQSSFIDLSCLNLTTFSLYTIIVLLVITSLYTLTNNNNKIIGSRWLISQEAIYDTIMNMTKGQIGGKNWGLYFPMIFTLFMFIFIANLISMIPYSFALSAHLVFIISLSIVIWLGNTILGLYKHGWVFFSLFVPAGTPLPLVPLLVIIETLSYFARAISLGLRLGSNILAGHLLMVILAGLTFNFMLINLFTLVFGFVPLAMILAIMMLEFAIGIIQGYVWAILTASYLKDAVYLH |
cell population proliferation kidney development polyamine metabolic process positive regulation of cell population proliferation putrescine biosynthetic process putrescine biosynthetic process from ornithine regulation of protein catabolic process response to virus | cytoplasm; cytosol; perinuclear region of cytoplasm | ornithine decarboxylase activity protein homodimerization activity | Mus musculus | 3D-structure Decarboxylase Lyase Phosphoprotein Polyamine biosynthesis Pyridoxal phosphate Reference proteome S-nitrosylation | MSSFTKDEFD | MSSFTKDEFDCHILDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVSQIKYAASNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLKTSRLLLERAKELNIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEDTKLKFEEITSVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKTVWKEQPGSDDEDESNEQTFMYYVNDGVYGSFNCILYDHAHVKALLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYVMSRPMWQLMKQIQSHGFPPEVEEQDDGTLPMSCAQESGMDRHPAACASARINV | cell population proliferation kidney development polyamine metabolic process positive regulation of cell population proliferation putrescine biosynthetic process putrescine biosynthetic process from ornithine regulation of protein catabolic process response to virus cytoplasm; cytosol; perinuclear region of cytoplasm ornithine decarboxylase activity protein homodimerization activity Mus musculus 3D-structure Decarboxylase Lyase Phosphoprotein Polyamine biosynthesis Pyridoxal phosphate Reference proteome S-nitrosylation MSSFTKDEFD MSSFTKDEFDCHILDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVSQIKYAASNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLKTSRLLLERAKELNIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEDTKLKFEEITSVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKTVWKEQPGSDDEDESNEQTFMYYVNDGVYGSFNCILYDHAHVKALLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYVMSRPMWQLMKQIQSHGFPPEVEEQDDGTLPMSCAQESGMDRHPAACASARINV |
carbon fixation gluconeogenesis oxaloacetate metabolic process protein homotetramerization tricarboxylic acid cycle | cytosol | identical protein binding magnesium ion binding phosphoenolpyruvate carboxylase activity | Escherichia coli | 3D-structure Allosteric enzyme Carbon dioxide fixation Lyase Magnesium Reference proteome | MNEQYSALRS | MNEQYSALRSNVSMLGKVLGETIKDALGEHILERVETIRKLSKSSRAGNDANRQELLTTLQNLSNDELLPVARAFSQFLNLANTAEQYHSISPKGEAASNPEVIARTLRKLKNQPELSEDTIKKAVESLSLELVLTAHPTEITRRTLIHKMVEVNACLKQLDNKDIADYEHNQLMRRLRQLIAQSWHTDEIRKLRPSPVDEAKWGFAVVENSLWQGVPNYLRELNEQLEENLGYKLPVEFVPVRFTSWMGGDRDGNPNVTADITRHVLLLSRWKATDLFLKDIQVLVSELSMVEATPELLALVGEEGAAEPYRYLMKNLRSRLMATQAWLEARLKGEELPKPEGLLTQNEELWEPLYACYQSLQACGMGIIANGDLLDTLRRVKCFGVPLVRIDIRQESTRHTEALGELTRYLGIGDYESWSEADKQAFLIRELNSKRPLLPRNWQPSAETREVLDTCQVIAEAPQGSIAAYVISMAKTPSDVLAVHLLLKEAGIGFAMPVAPLFETLDDLNNANDVMTQLLNIDWYRGLIQGKQMVMIGYSDSAKDAGVMAASWAQYQAQDALIKTCEKAGIELTLFHGRGGSIGRGGAPAHAALLSQPPGSLKGGLRVTEQGEMIRFKYGLPEITVSSLSLYTGAILEANLLPPPEPKESWRRIMDELSVISCDVYRGYVRENKDFVPYFRSATPEQELGKLPLGSRPAKRRPTGGVESLRAIPWIFAWTQNRLMLPAWLGAGTALQKVVEDGKQSELEAMCRDWPFFSTRLGMLEMVFAKADLWLAEYYDQRLVDKALWPLGKELRNLQEEDIKVVLAIANDSHLMADLPWIAESIQLRNIYTDPLNVLQAELLHRSRQAEKEGQEPDPRVEQALMVTIAGIAAGMRNTG | carbon fixation gluconeogenesis oxaloacetate metabolic process protein homotetramerization tricarboxylic acid cycle cytosol identical protein binding magnesium ion binding phosphoenolpyruvate carboxylase activity Escherichia coli 3D-structure Allosteric enzyme Carbon dioxide fixation Lyase Magnesium Reference proteome MNEQYSALRS MNEQYSALRSNVSMLGKVLGETIKDALGEHILERVETIRKLSKSSRAGNDANRQELLTTLQNLSNDELLPVARAFSQFLNLANTAEQYHSISPKGEAASNPEVIARTLRKLKNQPELSEDTIKKAVESLSLELVLTAHPTEITRRTLIHKMVEVNACLKQLDNKDIADYEHNQLMRRLRQLIAQSWHTDEIRKLRPSPVDEAKWGFAVVENSLWQGVPNYLRELNEQLEENLGYKLPVEFVPVRFTSWMGGDRDGNPNVTADITRHVLLLSRWKATDLFLKDIQVLVSELSMVEATPELLALVGEEGAAEPYRYLMKNLRSRLMATQAWLEARLKGEELPKPEGLLTQNEELWEPLYACYQSLQACGMGIIANGDLLDTLRRVKCFGVPLVRIDIRQESTRHTEALGELTRYLGIGDYESWSEADKQAFLIRELNSKRPLLPRNWQPSAETREVLDTCQVIAEAPQGSIAAYVISMAKTPSDVLAVHLLLKEAGIGFAMPVAPLFETLDDLNNANDVMTQLLNIDWYRGLIQGKQMVMIGYSDSAKDAGVMAASWAQYQAQDALIKTCEKAGIELTLFHGRGGSIGRGGAPAHAALLSQPPGSLKGGLRVTEQGEMIRFKYGLPEITVSSLSLYTGAILEANLLPPPEPKESWRRIMDELSVISCDVYRGYVRENKDFVPYFRSATPEQELGKLPLGSRPAKRRPTGGVESLRAIPWIFAWTQNRLMLPAWLGAGTALQKVVEDGKQSELEAMCRDWPFFSTRLGMLEMVFAKADLWLAEYYDQRLVDKALWPLGKELRNLQEEDIKVVLAIANDSHLMADLPWIAESIQLRNIYTDPLNVLQAELLHRSRQAEKEGQEPDPRVEQALMVTIAGIAAGMRNTG |
photorespiration reductive pentose-phosphate cycle | chloroplast | magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity | Spinacia oleracea | 3D-structure Acetylation Calvin cycle Carbon dioxide fixation Chloroplast Direct protein sequencing Disulfide bond Lyase Magnesium Metal-binding Monooxygenase Oxidoreductase Photorespiration Photosynthesis Plastid Reference proteome | MSPQTETKAS | MSPQTETKASVEFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV | photorespiration reductive pentose-phosphate cycle chloroplast magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity Spinacia oleracea 3D-structure Acetylation Calvin cycle Carbon dioxide fixation Chloroplast Direct protein sequencing Disulfide bond Lyase Magnesium Metal-binding Monooxygenase Oxidoreductase Photorespiration Photosynthesis Plastid Reference proteome MSPQTETKAS MSPQTETKASVEFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV |
photorespiration reductive pentose-phosphate cycle | chloroplast | magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity | Nicotiana tabacum | 3D-structure Acetylation Calvin cycle Carbon dioxide fixation Chloroplast Direct protein sequencing Disulfide bond Lyase Magnesium Metal-binding Methylation Monooxygenase Oxidoreductase Photorespiration Photosynthesis Plastid | MSPQTETKAS | MSPQTETKASVGFKAGVKEYKLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIERVVGEKDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLAQEGNEIIREACKWSPELAAACEVWKEIVFNFAAVDVLDK | photorespiration reductive pentose-phosphate cycle chloroplast magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity Nicotiana tabacum 3D-structure Acetylation Calvin cycle Carbon dioxide fixation Chloroplast Direct protein sequencing Disulfide bond Lyase Magnesium Metal-binding Methylation Monooxygenase Oxidoreductase Photorespiration Photosynthesis Plastid MSPQTETKAS MSPQTETKASVGFKAGVKEYKLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIERVVGEKDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLAQEGNEIIREACKWSPELAAACEVWKEIVFNFAAVDVLDK |
photorespiration reductive pentose-phosphate cycle | chloroplast | magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity | Chlamydomonas reinhardtii | 3D-structure Acetylation Calvin cycle Carbon dioxide fixation Chloroplast Direct protein sequencing Disulfide bond Hydroxylation Lyase Magnesium Metal-binding Methylation Monooxygenase Oxidoreductase Photorespiration Photosynthesis Plastid Reference proteome | MVPQTETKAG | MVPQTETKAGAGFKAGVKDYRLTYYTPDYVVRDTDILAAFRMTPQLGVPPEECGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVPGEDNQYIAYVAYPIDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFVGPPHGIQVERDKLNKYGRGLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEAIYKAQAETGEVKGHYLNATAGTCEEMMKRAVCAKELGVPIIMHDYLTGGFTANTSLAIYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRMSGGDHLHSGTVVGKLEGEREVTLGFVDLMRDDYVEKDRSRGIYFTQDWCSMPGVMPVASGGIHVWHMPALVEIFGDDACLQFGGGTLGHPWGNAPGAAANRVALEACTQARNEGRDLAREGGDVIRSACKWSPELAAACEVWKEIKFEFDTIDKL | photorespiration reductive pentose-phosphate cycle chloroplast magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity Chlamydomonas reinhardtii 3D-structure Acetylation Calvin cycle Carbon dioxide fixation Chloroplast Direct protein sequencing Disulfide bond Hydroxylation Lyase Magnesium Metal-binding Methylation Monooxygenase Oxidoreductase Photorespiration Photosynthesis Plastid Reference proteome MVPQTETKAG MVPQTETKAGAGFKAGVKDYRLTYYTPDYVVRDTDILAAFRMTPQLGVPPEECGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVPGEDNQYIAYVAYPIDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFVGPPHGIQVERDKLNKYGRGLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEAIYKAQAETGEVKGHYLNATAGTCEEMMKRAVCAKELGVPIIMHDYLTGGFTANTSLAIYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRMSGGDHLHSGTVVGKLEGEREVTLGFVDLMRDDYVEKDRSRGIYFTQDWCSMPGVMPVASGGIHVWHMPALVEIFGDDACLQFGGGTLGHPWGNAPGAAANRVALEACTQARNEGRDLAREGGDVIRSACKWSPELAAACEVWKEIKFEFDTIDKL |
photorespiration reductive pentose-phosphate cycle | carboxysome | magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity | Nostoc sp. | 3D-structure Bacterial microcompartment Calvin cycle Carbon dioxide fixation Carboxysome Direct protein sequencing Disulfide bond Lyase Magnesium Metal-binding Monooxygenase Oxidoreductase Photorespiration Photosynthesis Reference proteome | MSYAQTKTQT | MSYAQTKTQTKSGYKAGVQDYRLTYYTPDYTPKDTDILAAFRVTPQPGVPFEEAAAAVAAESSTGTWTTVWTDLLTDLDRYKGRCYDIEPVPGEDNQFIAYIAYPLDLFEEGSITNVLTSIVGNVFGFKALRALRLEDIRFPVAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSAPFQRWRDRFLFVADAITKAQAETGEIKGHYLNVTAPTCEEMLKRAEYAKELKQPIIMHDYLTAGFTANTTLARWCRDNGVLLHIHRAMHAVIDRQKNHGIHFRVLAKALRLSGGDHIHTGTVVGKLEGERGITMGFVDLLRENYVEQDKSRGIYFTQDWASLPGVMAVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRNLAREGNDVIREAAKWSPELAVACELWKEIKFEFEAMDTV | photorespiration reductive pentose-phosphate cycle carboxysome magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity Nostoc sp. 3D-structure Bacterial microcompartment Calvin cycle Carbon dioxide fixation Carboxysome Direct protein sequencing Disulfide bond Lyase Magnesium Metal-binding Monooxygenase Oxidoreductase Photorespiration Photosynthesis Reference proteome MSYAQTKTQT MSYAQTKTQTKSGYKAGVQDYRLTYYTPDYTPKDTDILAAFRVTPQPGVPFEEAAAAVAAESSTGTWTTVWTDLLTDLDRYKGRCYDIEPVPGEDNQFIAYIAYPLDLFEEGSITNVLTSIVGNVFGFKALRALRLEDIRFPVAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSAPFQRWRDRFLFVADAITKAQAETGEIKGHYLNVTAPTCEEMLKRAEYAKELKQPIIMHDYLTAGFTANTTLARWCRDNGVLLHIHRAMHAVIDRQKNHGIHFRVLAKALRLSGGDHIHTGTVVGKLEGERGITMGFVDLLRENYVEQDKSRGIYFTQDWASLPGVMAVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRNLAREGNDVIREAAKWSPELAVACELWKEIKFEFEAMDTV |
photorespiration reductive pentose-phosphate cycle | carboxysome | magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity | Synechococcus sp. | 3D-structure Bacterial microcompartment Calvin cycle Carbon dioxide fixation Carboxysome Direct protein sequencing Disulfide bond Lyase Magnesium Metal-binding Monooxygenase Oxidoreductase Photorespiration Photosynthesis | MPKTQSAAGY | MPKTQSAAGYKAGVKDYKLTYYTPDYTPKDTDLLAAFRFSPQPGVPADEAGAAIAAESSTGTWTTVWTDLLTDMDRYKGKCYHIEPVQGEENSYFAFIAYPLDLFEEGSVTNILTSIVGNVFGFKAIRSLRLEDIRFPVALVKTFQGPPHGIQVERDLLNKYGRPMLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFQRWRDRFLFVADAIHKSQAETGEIKGHYLNVTAPTCEEMMKRAEFAKELGMPIIMHDFLTAGFTANTTLAKWCRDNGVLLHIHRAMHAVIDRQRNHGIHFRVLAKCLRLSGGDHLHSGTVVGKLEGDKASTLGFVDLMREDHIEADRSRGVFFTQDWASMPGVLPVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRDLYREGGDILREAGKWSPELAAALDLWKEIKFEFETMDKL | photorespiration reductive pentose-phosphate cycle carboxysome magnesium ion binding monooxygenase activity ribulose-bisphosphate carboxylase activity Synechococcus sp. 3D-structure Bacterial microcompartment Calvin cycle Carbon dioxide fixation Carboxysome Direct protein sequencing Disulfide bond Lyase Magnesium Metal-binding Monooxygenase Oxidoreductase Photorespiration Photosynthesis MPKTQSAAGY MPKTQSAAGYKAGVKDYKLTYYTPDYTPKDTDLLAAFRFSPQPGVPADEAGAAIAAESSTGTWTTVWTDLLTDMDRYKGKCYHIEPVQGEENSYFAFIAYPLDLFEEGSVTNILTSIVGNVFGFKAIRSLRLEDIRFPVALVKTFQGPPHGIQVERDLLNKYGRPMLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFQRWRDRFLFVADAIHKSQAETGEIKGHYLNVTAPTCEEMMKRAEFAKELGMPIIMHDFLTAGFTANTTLAKWCRDNGVLLHIHRAMHAVIDRQRNHGIHFRVLAKCLRLSGGDHLHSGTVVGKLEGDKASTLGFVDLMREDHIEADRSRGVFFTQDWASMPGVLPVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRDLYREGGDILREAGKWSPELAAALDLWKEIKFEFETMDKL |
glycolytic process negative regulation of Arp2/3 complex-mediated actin nucleation positive regulation of cell migration protein homotetramerization | I band; M band | fructose-bisphosphate aldolase activity | Oryctolagus cuniculus | 3D-structure Acetylation Cytoplasm Direct protein sequencing Glycolysis Hydroxylation Isopeptide bond Lyase Phosphoprotein Reference proteome Schiff base Ubl conjugation | MPHSHPALTP | MPHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISNHAY | glycolytic process negative regulation of Arp2/3 complex-mediated actin nucleation positive regulation of cell migration protein homotetramerization I band; M band fructose-bisphosphate aldolase activity Oryctolagus cuniculus 3D-structure Acetylation Cytoplasm Direct protein sequencing Glycolysis Hydroxylation Isopeptide bond Lyase Phosphoprotein Reference proteome Schiff base Ubl conjugation MPHSHPALTP MPHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISNHAY |
cellular response to extracellular stimulus cellular response to insulin stimulus fructose 1,6-bisphosphate metabolic process fructose catabolic process fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate fructose metabolic process gluconeogenesis glycolytic process liver development NADH oxidation negative regulation of pentose-phosphate shunt response to amino acid response to cAMP response to carbohydrate response to copper ion response to fructose response to glucocorticoid response to interleukin-6 response to organic cyclic compound response to peptide hormone response to starvation response to xenobiotic stimulus response to zinc ion vacuolar proton-transporting V-type ATPase complex assembly | centriolar satellite; cytosol; microtubule organizing center; perinuclear region of cytoplasm; rough endoplasmic reticulum membrane; smooth endoplasmic reticulum membrane | ATPase binding cytoskeletal protein binding fructose binding fructose-1-phosphate aldolase activity fructose-bisphosphate aldolase activity identical protein binding molecular adaptor activity phosphatidylcholine binding | Rattus norvegicus | Acetylation Cytoplasm Cytoskeleton Direct protein sequencing Glycolysis Lyase Phosphoprotein Reference proteome Schiff base | MAHRFPALTS | MAHRFPALTSEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMLTAGHACTKKYTPEQVAMATVTALHRTVPAAVPSICFLSGGMSEEDATLNLNAIYRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAVANCQAAQGQYVHTGSSGAASTQSLFTASYTY | cellular response to extracellular stimulus cellular response to insulin stimulus fructose 1,6-bisphosphate metabolic process fructose catabolic process fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate fructose metabolic process gluconeogenesis glycolytic process liver development NADH oxidation negative regulation of pentose-phosphate shunt response to amino acid response to cAMP response to carbohydrate response to copper ion response to fructose response to glucocorticoid response to interleukin-6 response to organic cyclic compound response to peptide hormone response to starvation response to xenobiotic stimulus response to zinc ion vacuolar proton-transporting V-type ATPase complex assembly centriolar satellite; cytosol; microtubule organizing center; perinuclear region of cytoplasm; rough endoplasmic reticulum membrane; smooth endoplasmic reticulum membrane ATPase binding cytoskeletal protein binding fructose binding fructose-1-phosphate aldolase activity fructose-bisphosphate aldolase activity identical protein binding molecular adaptor activity phosphatidylcholine binding Rattus norvegicus Acetylation Cytoplasm Cytoskeleton Direct protein sequencing Glycolysis Lyase Phosphoprotein Reference proteome Schiff base MAHRFPALTS MAHRFPALTSEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMLTAGHACTKKYTPEQVAMATVTALHRTVPAAVPSICFLSGGMSEEDATLNLNAIYRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAVANCQAAQGQYVHTGSSGAASTQSLFTASYTY |
carbohydrate metabolic process citrate metabolic process tricarboxylic acid cycle | mitochondrial matrix | citrate (Si)-synthase activity citrate synthase activity | Sus scrofa | 3D-structure Acetylation Direct protein sequencing Methylation Mitochondrion Phosphoprotein Reference proteome Transferase Transit peptide Tricarboxylic acid cycle | MALLTAAARL | MALLTAAARLFGAKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK | carbohydrate metabolic process citrate metabolic process tricarboxylic acid cycle mitochondrial matrix citrate (Si)-synthase activity citrate synthase activity Sus scrofa 3D-structure Acetylation Direct protein sequencing Methylation Mitochondrion Phosphoprotein Reference proteome Transferase Transit peptide Tricarboxylic acid cycle MALLTAAARL MALLTAAARLFGAKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK |
acetyl-CoA catabolic process carbohydrate metabolic process citrate metabolic process tricarboxylic acid cycle | cytosol; mitochondrial intermembrane space; mitochondrial matrix; mitochondrion | citrate (Si)-synthase activity citrate synthase activity | Saccharomyces cerevisiae | Direct protein sequencing Mitochondrion Phosphoprotein Reference proteome Transferase Transit peptide Tricarboxylic acid cycle | MSAILSTTSK | MSAILSTTSKSFLSRGSTRQCQNMQKALFALLNARHYSSASEQTLKERFAEIIPAKAEEIKKFKKEHGKTVIGEVLLEQAYGGMRGIKGLVWEGSVLDPEEGIRFRGRTIPEIQRELPKAEGSTEPLPEALFWLLLTGEIPTDAQVKALSADLAARSEIPEHVIQLLDSLPKDLHPMAQFSIAVTALESESKFAKAYAQGVSKKEYWSYTFEDSLDLLGKLPVIASKIYRNVFKDGKITSTDPNADYGKNLAQLLGYENKDFIDLMRLYLTIHSDHEGGNVSAHTTHLVGSALSSPYLSLAAGLNGLAGPLHGRANQEVLEWLFKLREEVKGDYSKETIEKYLWDTLNAGRVVPGYGHAVLRKTDPRYTAQREFALKHFPDYELFKLVSTIYEVAPGVLTKHGKTKNPWPNVDSHSGVLLQYYGLTEASFYTVLFGVARAIGVLPQLIIDRAVGAPIERPKSFSTEKYKELVKKIESKN | acetyl-CoA catabolic process carbohydrate metabolic process citrate metabolic process tricarboxylic acid cycle cytosol; mitochondrial intermembrane space; mitochondrial matrix; mitochondrion citrate (Si)-synthase activity citrate synthase activity Saccharomyces cerevisiae Direct protein sequencing Mitochondrion Phosphoprotein Reference proteome Transferase Transit peptide Tricarboxylic acid cycle MSAILSTTSK MSAILSTTSKSFLSRGSTRQCQNMQKALFALLNARHYSSASEQTLKERFAEIIPAKAEEIKKFKKEHGKTVIGEVLLEQAYGGMRGIKGLVWEGSVLDPEEGIRFRGRTIPEIQRELPKAEGSTEPLPEALFWLLLTGEIPTDAQVKALSADLAARSEIPEHVIQLLDSLPKDLHPMAQFSIAVTALESESKFAKAYAQGVSKKEYWSYTFEDSLDLLGKLPVIASKIYRNVFKDGKITSTDPNADYGKNLAQLLGYENKDFIDLMRLYLTIHSDHEGGNVSAHTTHLVGSALSSPYLSLAAGLNGLAGPLHGRANQEVLEWLFKLREEVKGDYSKETIEKYLWDTLNAGRVVPGYGHAVLRKTDPRYTAQREFALKHFPDYELFKLVSTIYEVAPGVLTKHGKTKNPWPNVDSHSGVLLQYYGLTEASFYTVLFGVARAIGVLPQLIIDRAVGAPIERPKSFSTEKYKELVKKIESKN |
branched-chain amino acid biosynthetic process isoleucine biosynthetic process valine biosynthetic process | acetolactate synthase complex; cytosol | acetolactate synthase activity flavin adenine dinucleotide binding magnesium ion binding thiamine pyrophosphate binding | Escherichia coli | Amino-acid biosynthesis Branched-chain amino acid biosynthesis Direct protein sequencing FAD Flavoprotein Magnesium Metal-binding Reference proteome Thiamine pyrophosphate Transferase | MEMLSGAEMV | MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRGGGMDEMWLSKTERT | branched-chain amino acid biosynthetic process isoleucine biosynthetic process valine biosynthetic process acetolactate synthase complex; cytosol acetolactate synthase activity flavin adenine dinucleotide binding magnesium ion binding thiamine pyrophosphate binding Escherichia coli Amino-acid biosynthesis Branched-chain amino acid biosynthesis Direct protein sequencing FAD Flavoprotein Magnesium Metal-binding Reference proteome Thiamine pyrophosphate Transferase MEMLSGAEMV MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRGGGMDEMWLSKTERT |
branched-chain amino acid biosynthetic process isoleucine biosynthetic process valine biosynthetic process | acetolactate synthase complex; cytosol | acetolactate synthase activity acetolactate synthase regulator activity | Escherichia coli | 3D-structure Amino-acid biosynthesis Branched-chain amino acid biosynthesis Reference proteome Transferase | MRRILSVLLE | MRRILSVLLENESGALSRVIGLFSQRGYNIESLTVAPTDDPTLSRMTIQTVGDEKVLEQIEKQLHKLVDVLRVSELGQGAHVEREIMLVKIQASGYGRDEVKRNTEIFRGQIIDVTPSLYTVQLAGTSGKLDAFLASIRDVAKIVEVARSGVVGLSRGDKIMR | branched-chain amino acid biosynthetic process isoleucine biosynthetic process valine biosynthetic process acetolactate synthase complex; cytosol acetolactate synthase activity acetolactate synthase regulator activity Escherichia coli 3D-structure Amino-acid biosynthesis Branched-chain amino acid biosynthesis Reference proteome Transferase MRRILSVLLE MRRILSVLLENESGALSRVIGLFSQRGYNIESLTVAPTDDPTLSRMTIQTVGDEKVLEQIEKQLHKLVDVLRVSELGQGAHVEREIMLVKIQASGYGRDEVKRNTEIFRGQIIDVTPSLYTVQLAGTSGKLDAFLASIRDVAKIVEVARSGVVGLSRGDKIMR |
folic acid biosynthetic process glutamine metabolic process para-aminobenzoic acid biosynthetic process tetrahydrofolate biosynthetic process tryptophan biosynthetic process | aminodeoxychorismate synthase complex | 4-amino-4-deoxychorismate synthase activity protein heterodimerization activity | Escherichia coli | Folate biosynthesis Glutamine amidotransferase Reference proteome Transferase | MILLIDNYDS | MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFDVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLHR | folic acid biosynthetic process glutamine metabolic process para-aminobenzoic acid biosynthetic process tetrahydrofolate biosynthetic process tryptophan biosynthetic process aminodeoxychorismate synthase complex 4-amino-4-deoxychorismate synthase activity protein heterodimerization activity Escherichia coli Folate biosynthesis Glutamine amidotransferase Reference proteome Transferase MILLIDNYDS MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFDVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLHR |
glutamine metabolic process phenazine biosynthetic process tryptophan biosynthetic process | anthranilate synthase complex | anthranilate phosphoribosyltransferase activity anthranilate synthase activity magnesium ion binding | Escherichia coli | Allosteric enzyme Amino-acid biosynthesis Aromatic amino acid biosynthesis Direct protein sequencing Glutamine amidotransferase Glycosyltransferase Lyase Multifunctional enzyme Reference proteome Transferase Tryptophan biosynthesis | MADILLLDNI | MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPANTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG | glutamine metabolic process phenazine biosynthetic process tryptophan biosynthetic process anthranilate synthase complex anthranilate phosphoribosyltransferase activity anthranilate synthase activity magnesium ion binding Escherichia coli Allosteric enzyme Amino-acid biosynthesis Aromatic amino acid biosynthesis Direct protein sequencing Glutamine amidotransferase Glycosyltransferase Lyase Multifunctional enzyme Reference proteome Transferase Tryptophan biosynthesis MADILLLDNI MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPANTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG |
one-carbon metabolic process | cytosol; extracellular exosome | arylesterase activity carbonate dehydratase activity cyanamide hydratase activity hydro-lyase activity zinc ion binding | Homo sapiens | 3D-structure Acetylation Cytoplasm Direct protein sequencing Lyase Metal-binding Reference proteome Zinc | MASPDWGYDD | MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF | one-carbon metabolic process cytosol; extracellular exosome arylesterase activity carbonate dehydratase activity cyanamide hydratase activity hydro-lyase activity zinc ion binding Homo sapiens 3D-structure Acetylation Cytoplasm Direct protein sequencing Lyase Metal-binding Reference proteome Zinc MASPDWGYDD MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF |
one-carbon metabolic process | cytoplasm | carbonate dehydratase activity cyanamide hydratase activity hydro-lyase activity zinc ion binding | Equus caballus | Acetylation Cytoplasm Direct protein sequencing Lyase Metal-binding Reference proteome Zinc | MAHSDWGYDS | MAHSDWGYDSPNGPZEWVKLYPIANGNNQSPIDIKTSETKHDTSLKPFSVSYDPATAKEIVNVGHSFQVKFEDSDNRSVLKDGPLPGSYRLVQFHFHWGSTDDYGSEHTVDGVKYSAELHLVHWNSSKYSSFDEASSQADGLAILGVLMKVGEANPKLQKVLDALNEVKTKGKKAPFKNFDPSSLLPSSPDYWTYSGSLTHPPLYESVTWIVCKENISISSQQLSQFRSLLSNVEGGKAVPIQHNNRPPQPLKGRTVRAFF | one-carbon metabolic process cytoplasm carbonate dehydratase activity cyanamide hydratase activity hydro-lyase activity zinc ion binding Equus caballus Acetylation Cytoplasm Direct protein sequencing Lyase Metal-binding Reference proteome Zinc MAHSDWGYDS MAHSDWGYDSPNGPZEWVKLYPIANGNNQSPIDIKTSETKHDTSLKPFSVSYDPATAKEIVNVGHSFQVKFEDSDNRSVLKDGPLPGSYRLVQFHFHWGSTDDYGSEHTVDGVKYSAELHLVHWNSSKYSSFDEASSQADGLAILGVLMKVGEANPKLQKVLDALNEVKTKGKKAPFKNFDPSSLLPSSPDYWTYSGSLTHPPLYESVTWIVCKENISISSQQLSQFRSLLSNVEGGKAVPIQHNNRPPQPLKGRTVRAFF |
angiotensin-activated signaling pathway carbon dioxide transport morphogenesis of an epithelium neuron cellular homeostasis one-carbon metabolic process positive regulation of cellular pH reduction positive regulation of dipeptide transmembrane transport positive regulation of synaptic transmission, GABAergic regulation of chloride transport regulation of intracellular pH regulation of monoatomic anion transport secretion | apical part of cell; cytoplasm; cytosol; extracellular exosome; myelin sheath; plasma membrane | arylesterase activity carbonate dehydratase activity cyanamide hydratase activity zinc ion binding | Homo sapiens | 3D-structure Acetylation Cell membrane Cytoplasm Direct protein sequencing Disease variant Lyase Membrane Metal-binding Osteopetrosis Phosphoprotein Reference proteome Zinc | MSHHWGYGKH | MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK | angiotensin-activated signaling pathway carbon dioxide transport morphogenesis of an epithelium neuron cellular homeostasis one-carbon metabolic process positive regulation of cellular pH reduction positive regulation of dipeptide transmembrane transport positive regulation of synaptic transmission, GABAergic regulation of chloride transport regulation of intracellular pH regulation of monoatomic anion transport secretion apical part of cell; cytoplasm; cytosol; extracellular exosome; myelin sheath; plasma membrane arylesterase activity carbonate dehydratase activity cyanamide hydratase activity zinc ion binding Homo sapiens 3D-structure Acetylation Cell membrane Cytoplasm Direct protein sequencing Disease variant Lyase Membrane Metal-binding Osteopetrosis Phosphoprotein Reference proteome Zinc MSHHWGYGKH MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK |
angiotensin-activated signaling pathway positive regulation of dipeptide transmembrane transport regulation of intracellular pH regulation of monoatomic anion transport | cytoplasm; plasma membrane | carbonate dehydratase activity cyanamide hydratase activity zinc ion binding | Oryctolagus cuniculus | Acetylation Cell membrane Cytoplasm Direct protein sequencing Lyase Membrane Metal-binding Phosphoprotein Reference proteome Zinc | MSHHWGYGKH | MSHHWGYGKHNGPEHWHKDFPIANGERQSPIDIDTNAAKHDPSLKPLRVCYEHPISRRIINNGHSFNVEFDDSHDKTVLKEGPLEGTYRLIQFHFHWGSSDGQGSEHTVNKKKYAAELHLVHWNTKYGDFGKAVKHPDGLAVLGIFLKIGSATPGLQKVVDTLSSIKTKGKSVDFTDFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPITVSSEQMLKFRNLNFNKEAEPEEPMVDNWRPTQPLKGRQVKASFV | angiotensin-activated signaling pathway positive regulation of dipeptide transmembrane transport regulation of intracellular pH regulation of monoatomic anion transport cytoplasm; plasma membrane carbonate dehydratase activity cyanamide hydratase activity zinc ion binding Oryctolagus cuniculus Acetylation Cell membrane Cytoplasm Direct protein sequencing Lyase Membrane Metal-binding Phosphoprotein Reference proteome Zinc MSHHWGYGKH MSHHWGYGKHNGPEHWHKDFPIANGERQSPIDIDTNAAKHDPSLKPLRVCYEHPISRRIINNGHSFNVEFDDSHDKTVLKEGPLEGTYRLIQFHFHWGSSDGQGSEHTVNKKKYAAELHLVHWNTKYGDFGKAVKHPDGLAVLGIFLKIGSATPGLQKVVDTLSSIKTKGKSVDFTDFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPITVSSEQMLKFRNLNFNKEAEPEEPMVDNWRPTQPLKGRQVKASFV |
angiotensin-activated signaling pathway carbon dioxide transport morphogenesis of an epithelium neuron cellular homeostasis one-carbon metabolic process positive regulation of bone resorption positive regulation of cellular pH reduction positive regulation of dipeptide transmembrane transport positive regulation of osteoclast differentiation positive regulation of synaptic transmission, GABAergic regulation of chloride transport regulation of intracellular pH regulation of monoatomic anion transport regulation of pH secretion | apical part of cell; axon; basolateral plasma membrane; cytoplasm; cytosol; extracellular space; microvillus; myelin sheath; plasma membrane | arylesterase activity carbonate dehydratase activity cyanamide hydratase activity zinc ion binding | Mus musculus | Acetylation Cell membrane Cytoplasm Direct protein sequencing Lyase Membrane Metal-binding Phosphoprotein Reference proteome Zinc | MSHHWGYSKH | MSHHWGYSKHNGPENWHKDFPIANGDRQSPVDIDTATAQHDPALQPLLISYDKAASKSIVNNGHSFNVEFDDSQDNAVLKGGPLSDSYRLIQFHFHWGSSDGQGSEHTVNKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKIGPASQGLQKVLEALHSIKTKGKRAAFANFDPCSLLPGNLDYWTYPGSLTTPPLLECVTWIVLREPITVSSEQMSHFRTLNFNEEGDAEEAMVDNWRPAQPLKNRKIKASFK | angiotensin-activated signaling pathway carbon dioxide transport morphogenesis of an epithelium neuron cellular homeostasis one-carbon metabolic process positive regulation of bone resorption positive regulation of cellular pH reduction positive regulation of dipeptide transmembrane transport positive regulation of osteoclast differentiation positive regulation of synaptic transmission, GABAergic regulation of chloride transport regulation of intracellular pH regulation of monoatomic anion transport regulation of pH secretion apical part of cell; axon; basolateral plasma membrane; cytoplasm; cytosol; extracellular space; microvillus; myelin sheath; plasma membrane arylesterase activity carbonate dehydratase activity cyanamide hydratase activity zinc ion binding Mus musculus Acetylation Cell membrane Cytoplasm Direct protein sequencing Lyase Membrane Metal-binding Phosphoprotein Reference proteome Zinc MSHHWGYSKH MSHHWGYSKHNGPENWHKDFPIANGDRQSPVDIDTATAQHDPALQPLLISYDKAASKSIVNNGHSFNVEFDDSQDNAVLKGGPLSDSYRLIQFHFHWGSSDGQGSEHTVNKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKIGPASQGLQKVLEALHSIKTKGKRAAFANFDPCSLLPGNLDYWTYPGSLTTPPLLECVTWIVLREPITVSSEQMSHFRTLNFNEEGDAEEAMVDNWRPAQPLKNRKIKASFK |
angiotensin-activated signaling pathway carbon dioxide transport one-carbon metabolic process positive regulation of dipeptide transmembrane transport regulation of intracellular pH regulation of monoatomic anion transport | apical part of cell; cytoplasm; plasma membrane | carbonate dehydratase activity cyanamide hydratase activity zinc ion binding | Bos taurus | 3D-structure Acetylation Cell membrane Cytoplasm Direct protein sequencing Lyase Membrane Metal-binding Phosphoprotein Reference proteome Zinc | MSHHWGYGKH | MSHHWGYGKHNGPEHWHKDFPIANGERQSPVDIDTKAVVQDPALKPLALVYGEATSRRMVNNGHSFNVEYDDSQDKAVLKDGPLTGTYRLVQFHFHWGSSDDQGSEHTVDRKKYAAELHLVHWNTKYGDFGTAAQQPDGLAVVGVFLKVGDANPALQKVLDALDSIKTKGKSTDFPNFDPGSLLPNVLDYWTYPGSLTTPPLLESVTWIVLKEPISVSSQQMLKFRTLNFNAEGEPELLMLANWRPAQPLKNRQVRGFPK | angiotensin-activated signaling pathway carbon dioxide transport one-carbon metabolic process positive regulation of dipeptide transmembrane transport regulation of intracellular pH regulation of monoatomic anion transport apical part of cell; cytoplasm; plasma membrane carbonate dehydratase activity cyanamide hydratase activity zinc ion binding Bos taurus 3D-structure Acetylation Cell membrane Cytoplasm Direct protein sequencing Lyase Membrane Metal-binding Phosphoprotein Reference proteome Zinc MSHHWGYGKH MSHHWGYGKHNGPEHWHKDFPIANGERQSPVDIDTKAVVQDPALKPLALVYGEATSRRMVNNGHSFNVEYDDSQDKAVLKDGPLTGTYRLVQFHFHWGSSDDQGSEHTVDRKKYAAELHLVHWNTKYGDFGTAAQQPDGLAVVGVFLKVGDANPALQKVLDALDSIKTKGKSTDFPNFDPGSLLPNVLDYWTYPGSLTTPPLLESVTWIVLKEPISVSSQQMLKFRTLNFNAEGEPELLMLANWRPAQPLKNRQVRGFPK |
angiotensin-activated signaling pathway positive regulation of dipeptide transmembrane transport regulation of intracellular pH regulation of monoatomic anion transport | cytoplasm; plasma membrane | carbonate dehydratase activity cyanamide hydratase activity zinc ion binding | Ovis aries | Acetylation Cell membrane Cytoplasm Direct protein sequencing Lyase Membrane Metal-binding Phosphoprotein Reference proteome Zinc | MSHHWGYGEH | MSHHWGYGEHNGPEHWHKDFPIADGERQSPVDIDTKAVVPDPALKPLALLYEQAASRRMVNNGHSFNVEFDDSQDKAVLKDGPLTGTYRLVQFHFHWGSSDDQGSEHTVDRKKYAAELHLVHWNTKYGDFGTAAQQPDGLAVVGVFLKVGDANPALQKVLDVLDSIKTKGKSADFPNFDPSSLLKRALNYWTYPGSLTNPPLLESVTWVVLKEPTSVSSQQMLKFRSLNFNAEGEPELLMLANWRPAQPLKNRQVRVFPK | angiotensin-activated signaling pathway positive regulation of dipeptide transmembrane transport regulation of intracellular pH regulation of monoatomic anion transport cytoplasm; plasma membrane carbonate dehydratase activity cyanamide hydratase activity zinc ion binding Ovis aries Acetylation Cell membrane Cytoplasm Direct protein sequencing Lyase Membrane Metal-binding Phosphoprotein Reference proteome Zinc MSHHWGYGEH MSHHWGYGEHNGPEHWHKDFPIADGERQSPVDIDTKAVVPDPALKPLALLYEQAASRRMVNNGHSFNVEFDDSQDKAVLKDGPLTGTYRLVQFHFHWGSSDDQGSEHTVDRKKYAAELHLVHWNTKYGDFGTAAQQPDGLAVVGVFLKVGDANPALQKVLDVLDSIKTKGKSADFPNFDPSSLLKRALNYWTYPGSLTNPPLLESVTWVVLKEPTSVSSQQMLKFRSLNFNAEGEPELLMLANWRPAQPLKNRQVRVFPK |
glycolytic process regulation of vacuole fusion, non-autophagic | cytoplasm; cytosol; fungal-type vacuole; mitochondrion; phosphopyruvate hydratase complex; plasma membrane | magnesium ion binding melatonin binding phosphopyruvate hydratase activity | Saccharomyces cerevisiae | 3D-structure Cytoplasm Direct protein sequencing Glycolysis Isopeptide bond Lyase Magnesium Metal-binding Phosphoprotein Reference proteome Ubl conjugation | MAVSKVYARS | MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKIKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL | glycolytic process regulation of vacuole fusion, non-autophagic cytoplasm; cytosol; fungal-type vacuole; mitochondrion; phosphopyruvate hydratase complex; plasma membrane magnesium ion binding melatonin binding phosphopyruvate hydratase activity Saccharomyces cerevisiae 3D-structure Cytoplasm Direct protein sequencing Glycolysis Isopeptide bond Lyase Magnesium Metal-binding Phosphoprotein Reference proteome Ubl conjugation MAVSKVYARS MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKIKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL |
glycolytic process regulation of vacuole fusion, non-autophagic | cytoplasmic side of plasma membrane; cytosol; fungal-type vacuole; mitochondrion; phosphopyruvate hydratase complex; plasma membrane | magnesium ion binding melatonin binding phosphopyruvate hydratase activity | Saccharomyces cerevisiae | Cytoplasm Direct protein sequencing Glycolysis Isopeptide bond Lyase Magnesium Metal-binding Phosphoprotein Reference proteome Ubl conjugation | MAVSKVYARS | MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDEDKSKWMGKGVMNAVNNVNNVIAAAFVKANLDVKDQKAVDDFLLSLDGTANKSKLGANAILGVSMAAARAAAAEKNVPLYQHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEAMRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASSEFFKDGKYDLDFKNPESDKSKWLTGVELADMYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPARIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAANWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDKAVYAGENFHHGDKL | glycolytic process regulation of vacuole fusion, non-autophagic cytoplasmic side of plasma membrane; cytosol; fungal-type vacuole; mitochondrion; phosphopyruvate hydratase complex; plasma membrane magnesium ion binding melatonin binding phosphopyruvate hydratase activity Saccharomyces cerevisiae Cytoplasm Direct protein sequencing Glycolysis Isopeptide bond Lyase Magnesium Metal-binding Phosphoprotein Reference proteome Ubl conjugation MAVSKVYARS MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDEDKSKWMGKGVMNAVNNVNNVIAAAFVKANLDVKDQKAVDDFLLSLDGTANKSKLGANAILGVSMAAARAAAAEKNVPLYQHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEAMRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASSEFFKDGKYDLDFKNPESDKSKWLTGVELADMYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPARIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAANWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDKAVYAGENFHHGDKL |
D-serine catabolic process D-serine metabolic process detoxification of nitrogen compound DNA damage response isoleucine biosynthetic process | cytoplasm; cytosol | D-serine ammonia-lyase activity hydro-lyase activity pyridoxal phosphate binding | Escherichia coli | 3D-structure Direct protein sequencing Lyase Pyridoxal phosphate Reference proteome | MENAKMNSLI | MENAKMNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSKLLSPEFKQFFSQYSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGYSVAGQRLKAQFAQQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQMHGFSAEQLRNTTHLVWATGGGMVPEEEMNQYLAKGR | D-serine catabolic process D-serine metabolic process detoxification of nitrogen compound DNA damage response isoleucine biosynthetic process cytoplasm; cytosol D-serine ammonia-lyase activity hydro-lyase activity pyridoxal phosphate binding Escherichia coli 3D-structure Direct protein sequencing Lyase Pyridoxal phosphate Reference proteome MENAKMNSLI MENAKMNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSKLLSPEFKQFFSQYSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGYSVAGQRLKAQFAQQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQMHGFSAEQLRNTTHLVWATGGGMVPEEEMNQYLAKGR |
isoleucine biosynthetic process L-serine catabolic process threonine catabolic process | mitochondrion | L-serine ammonia-lyase activity L-threonine ammonia-lyase activity pyridoxal phosphate binding | Saccharomyces cerevisiae | Allosteric enzyme Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis Lyase Mitochondrion Pyridoxal phosphate Reference proteome Repeat Transit peptide | MSATLLKQPL | MSATLLKQPLCTVVRQGKQSKVSGLNLLRLKAHLHRQHLSPSLIKLHSELKLDELQTDNTPDYVRLVLRSSVYDVINESPISQGVGLSSRLNTNVILKREDLLPVFSFKLRGAYNMIAKLDDSQRNQGVIACSAGNHAQGVAFAAKHLKIPATIVMPVCTPSIKYQNVSRLGSQVVLYGNDFDEAKAECAKLAEERGLTNIPPFDHPYVIAGQGTVAMEILRQVRTANKIGAVFVPVGGGGLIAGIGAYLKRVAPHIKIIGVETYDAATLHNSLQRNQRTPLPVVGTFADGTSVRMIGEETFRVAQQVVDEVVLVNTDEICAAVKDIFEDTRSIVEPSGALSVAGMKKYISTVHPEIDHTKNTYVPILSGANMNFDRLRFVSERAVLGEGKEVFMLVTLPDVPGAFKKMQKIIHPRSVTEFSYRYNEHRHESSSEVPKAYIYTSFSVVDREKEIKQVMQQLNALGFEAVDISDNELAKSHGRYLVGGASKVPNERIISFEFPERPGALTRFLGGLSDSWNLTLFHYRNHGADIGKVLAGISVPPRENLTFQKFLEDLGYTYHDETDNTVYQKFLKY | isoleucine biosynthetic process L-serine catabolic process threonine catabolic process mitochondrion L-serine ammonia-lyase activity L-threonine ammonia-lyase activity pyridoxal phosphate binding Saccharomyces cerevisiae Allosteric enzyme Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis Lyase Mitochondrion Pyridoxal phosphate Reference proteome Repeat Transit peptide MSATLLKQPL MSATLLKQPLCTVVRQGKQSKVSGLNLLRLKAHLHRQHLSPSLIKLHSELKLDELQTDNTPDYVRLVLRSSVYDVINESPISQGVGLSSRLNTNVILKREDLLPVFSFKLRGAYNMIAKLDDSQRNQGVIACSAGNHAQGVAFAAKHLKIPATIVMPVCTPSIKYQNVSRLGSQVVLYGNDFDEAKAECAKLAEERGLTNIPPFDHPYVIAGQGTVAMEILRQVRTANKIGAVFVPVGGGGLIAGIGAYLKRVAPHIKIIGVETYDAATLHNSLQRNQRTPLPVVGTFADGTSVRMIGEETFRVAQQVVDEVVLVNTDEICAAVKDIFEDTRSIVEPSGALSVAGMKKYISTVHPEIDHTKNTYVPILSGANMNFDRLRFVSERAVLGEGKEVFMLVTLPDVPGAFKKMQKIIHPRSVTEFSYRYNEHRHESSSEVPKAYIYTSFSVVDREKEIKQVMQQLNALGFEAVDISDNELAKSHGRYLVGGASKVPNERIISFEFPERPGALTRFLGGLSDSWNLTLFHYRNHGADIGKVLAGISVPPRENLTFQKFLEDLGYTYHDETDNTVYQKFLKY |
cysteine biosynthetic process via cystathionine methionine biosynthetic process transsulfuration | cytoplasm | cystathionine gamma-lyase activity cystathionine gamma-synthase activity cystathionine gamma-synthase activity (acts on O-phosphohomoserine) pyridoxal phosphate binding | Escherichia coli | 3D-structure Amino-acid biosynthesis Cytoplasm Direct protein sequencing Methionine biosynthesis Pyridoxal phosphate Reference proteome Transferase | MTRKQATIAV | MTRKQATIAVRSGLNDDEQYGCVVPPIHLSSTYNFTGFNEPRAHDYSRRGNPTRDVVQRALAELEGGAGAVLTNTGMSAIHLVTTVFLKPGDLLVAPHDCYGGSYRLFDSLAKRGCYRVLFVDQGDEQALRAALAEKPKLVLVESPSNPLLRVVDIAKICHLAREVGAVSVVDNTFLSPALQNPLALGADLVLHSCTKYLNGHSDVVAGVVIAKDPDVVTELAWWANNIGVTGGAFDSYLLLRGLRTLVPRMELAQRNAQAIVKYLQTQPLVKKLYHPSLPENQGHEIAARQQKGFGAMLSFELDGDEQTLRRFLGGLSLFTLAESLGGVESLISHAATMTHAGMAPEARAAAGISETLLRISTGIEDGEDLIADLENGFRAANKG | cysteine biosynthetic process via cystathionine methionine biosynthetic process transsulfuration cytoplasm cystathionine gamma-lyase activity cystathionine gamma-synthase activity cystathionine gamma-synthase activity (acts on O-phosphohomoserine) pyridoxal phosphate binding Escherichia coli 3D-structure Amino-acid biosynthesis Cytoplasm Direct protein sequencing Methionine biosynthesis Pyridoxal phosphate Reference proteome Transferase MTRKQATIAV MTRKQATIAVRSGLNDDEQYGCVVPPIHLSSTYNFTGFNEPRAHDYSRRGNPTRDVVQRALAELEGGAGAVLTNTGMSAIHLVTTVFLKPGDLLVAPHDCYGGSYRLFDSLAKRGCYRVLFVDQGDEQALRAALAEKPKLVLVESPSNPLLRVVDIAKICHLAREVGAVSVVDNTFLSPALQNPLALGADLVLHSCTKYLNGHSDVVAGVVIAKDPDVVTELAWWANNIGVTGGAFDSYLLLRGLRTLVPRMELAQRNAQAIVKYLQTQPLVKKLYHPSLPENQGHEIAARQQKGFGAMLSFELDGDEQTLRRFLGGLSLFTLAESLGGVESLISHAATMTHAGMAPEARAAAGISETLLRISTGIEDGEDLIADLENGFRAANKG |
cAMP biosynthetic process | cytoplasm | adenylate cyclase activity ATP binding | Escherichia coli | ATP-binding cAMP biosynthesis Cytoplasm Lyase Nucleotide-binding Phosphoprotein Reference proteome | MYLYIETLKQ | MYLYIETLKQRLDAINQLRVDRALAAMGPAFQQVYSLLPTLLHYHHPLMPGYLDGNVPKGICLYTPDETQRHYLNELELYRGMSVQDPPKGELPITGVYTMGSTSSVGQSCSSDLDIWVCHQSWLDSEERQLLQRKCSLLENWAASLGVEVSFFLIDENRFRHNESGSLGGEDCGSTQHILLLDEFYRTAVRLAGKRILWNMVPCDEEEHYDDYVMTLYAQGVLTPNEWLDLGGLSSLSAEEYFGASLWQLYKSIDSPYKAVLKTLLLEAYSWEYPNPRLLAKDIKQRLHDGEIVSFGLDPYCMMLERVTEYLTAIEDFTRLDLVRRCFYLKVCEKLSRERACVGWRRAVLSQLVSEWGWDEARLAMLDNRANWKIDQVREAHNELLDAMMQSYRNLIRFARRNNLSVSASPQDIGVLTRKLYAAFEALPGKVTLVNPQISPDLSEPNLTFIYVPPGRANRSGWYLYNRAPNIESIISHQPLEYNRYLNKLVAWAWFNGLLTSRTRLYIKGNGIVDLPKLQEMVADVSHHFPLRLPAPTPKALYSPCEIRHLAIIVNLEYDPTAAFRNQVVHFDFRKLDVFSFGENQNCLVGSVDLLYRNSWNEVRTLHFNGEQSMIEALKTILGKMHQDAAPPDSVEVFCYSQHLRGLIRTRVQQLVSECIELRLSSTRQETGRFKALRVSGQTWGLFFERLNVSVQKLENAIEFYGAISHNKLHGLSVQVETNHVKLPAVVDGFASEGIIQFFFEETQDENGFNIYILDESNRVEVYHHCEGSKEELVRDVSRFYSSSHDRFTYGSSFINFNLPQFYQIVKVDGREQVIPFRTKSIGNMPPANQDHDTPLLQQYFS | cAMP biosynthetic process cytoplasm adenylate cyclase activity ATP binding Escherichia coli ATP-binding cAMP biosynthesis Cytoplasm Lyase Nucleotide-binding Phosphoprotein Reference proteome MYLYIETLKQ MYLYIETLKQRLDAINQLRVDRALAAMGPAFQQVYSLLPTLLHYHHPLMPGYLDGNVPKGICLYTPDETQRHYLNELELYRGMSVQDPPKGELPITGVYTMGSTSSVGQSCSSDLDIWVCHQSWLDSEERQLLQRKCSLLENWAASLGVEVSFFLIDENRFRHNESGSLGGEDCGSTQHILLLDEFYRTAVRLAGKRILWNMVPCDEEEHYDDYVMTLYAQGVLTPNEWLDLGGLSSLSAEEYFGASLWQLYKSIDSPYKAVLKTLLLEAYSWEYPNPRLLAKDIKQRLHDGEIVSFGLDPYCMMLERVTEYLTAIEDFTRLDLVRRCFYLKVCEKLSRERACVGWRRAVLSQLVSEWGWDEARLAMLDNRANWKIDQVREAHNELLDAMMQSYRNLIRFARRNNLSVSASPQDIGVLTRKLYAAFEALPGKVTLVNPQISPDLSEPNLTFIYVPPGRANRSGWYLYNRAPNIESIISHQPLEYNRYLNKLVAWAWFNGLLTSRTRLYIKGNGIVDLPKLQEMVADVSHHFPLRLPAPTPKALYSPCEIRHLAIIVNLEYDPTAAFRNQVVHFDFRKLDVFSFGENQNCLVGSVDLLYRNSWNEVRTLHFNGEQSMIEALKTILGKMHQDAAPPDSVEVFCYSQHLRGLIRTRVQQLVSECIELRLSSTRQETGRFKALRVSGQTWGLFFERLNVSVQKLENAIEFYGAISHNKLHGLSVQVETNHVKLPAVVDGFASEGIIQFFFEETQDENGFNIYILDESNRVEVYHHCEGSKEELVRDVSRFYSSSHDRFTYGSSFINFNLPQFYQIVKVDGREQVIPFRTKSIGNMPPANQDHDTPLLQQYFS |
glutamine metabolic process tryptophan biosynthetic process | anthranilate synthase complex; cytoplasm | anthranilate synthase activity indole-3-glycerol-phosphate synthase activity | Saccharomyces cerevisiae | Amino-acid biosynthesis Aromatic amino acid biosynthesis Glutamine amidotransferase Lyase Multifunctional enzyme Phosphoprotein Reference proteome Tryptophan biosynthesis | MSVHAATNPI | MSVHAATNPINKHVVLIDNYDSFTWNVYEYLCQEGAKVSVYRNDAITVPEIAALNPDTLLISPGPGHPKTDSGISRDCIRYFTGKIPVFGICMGQQCMFDVFGGEVAYAGEIVHGKTSPISHDNCGIFKNVPQGIAVTRYHSLAGTESSLPSCLKVTASTENGIIMGVRHKKYTVEGVQFHPESILTEEGHLMIRNILNVSGGTWEENKSSPSNSILDRIYARRKIDVNEQSKIPGFTFQDLQSNYDLGLAPPLQDFYTVLSSSHKRAVVLAEVKRASPSKGPICLKAVAAEQALKYAEAGASAISVLTEPHWFHGSLQDLVNVRKILDLKFPPKERPCVLRKEFIFSKYQILEARLAGADTVLLIVKMLSQPLLKELYSYSKDLNMEPLVEVNSKEELQRALEIGAKVVGVNNRDLHSFNVDLNTTSNLVESIPKDVLLIALSGITTRDDAEKYKKEGVHGFLVGEALMKSTDVKKFIHELCE | glutamine metabolic process tryptophan biosynthetic process anthranilate synthase complex; cytoplasm anthranilate synthase activity indole-3-glycerol-phosphate synthase activity Saccharomyces cerevisiae Amino-acid biosynthesis Aromatic amino acid biosynthesis Glutamine amidotransferase Lyase Multifunctional enzyme Phosphoprotein Reference proteome Tryptophan biosynthesis MSVHAATNPI MSVHAATNPINKHVVLIDNYDSFTWNVYEYLCQEGAKVSVYRNDAITVPEIAALNPDTLLISPGPGHPKTDSGISRDCIRYFTGKIPVFGICMGQQCMFDVFGGEVAYAGEIVHGKTSPISHDNCGIFKNVPQGIAVTRYHSLAGTESSLPSCLKVTASTENGIIMGVRHKKYTVEGVQFHPESILTEEGHLMIRNILNVSGGTWEENKSSPSNSILDRIYARRKIDVNEQSKIPGFTFQDLQSNYDLGLAPPLQDFYTVLSSSHKRAVVLAEVKRASPSKGPICLKAVAAEQALKYAEAGASAISVLTEPHWFHGSLQDLVNVRKILDLKFPPKERPCVLRKEFIFSKYQILEARLAGADTVLLIVKMLSQPLLKELYSYSKDLNMEPLVEVNSKEELQRALEIGAKVVGVNNRDLHSFNVDLNTTSNLVESIPKDVLLIALSGITTRDDAEKYKKEGVHGFLVGEALMKSTDVKKFIHELCE |
canonical glycolysis gluconeogenesis glyceraldehyde-3-phosphate biosynthetic process methylglyoxal biosynthetic process | cytosol | methylglyoxal synthase activity protein homodimerization activity triose-phosphate isomerase activity ubiquitin protein ligase binding | Oryctolagus cuniculus | 3D-structure Acetylation Alternative initiation Cytoplasm Direct protein sequencing Gluconeogenesis Glycolysis Isomerase Isopeptide bond Lyase Methylation Nitration Phosphoprotein Reference proteome Ubl conjugation | MAPSRKFFVG | MAPSRKFFVGGNWKMNGRKKNLGELITTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ | canonical glycolysis gluconeogenesis glyceraldehyde-3-phosphate biosynthetic process methylglyoxal biosynthetic process cytosol methylglyoxal synthase activity protein homodimerization activity triose-phosphate isomerase activity ubiquitin protein ligase binding Oryctolagus cuniculus 3D-structure Acetylation Alternative initiation Cytoplasm Direct protein sequencing Gluconeogenesis Glycolysis Isomerase Isopeptide bond Lyase Methylation Nitration Phosphoprotein Reference proteome Ubl conjugation MAPSRKFFVG MAPSRKFFVGGNWKMNGRKKNLGELITTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ |
canonical glycolysis gluconeogenesis glyceraldehyde-3-phosphate biosynthetic process glycerol catabolic process glycolytic process methylglyoxal biosynthetic process | cytosol | methylglyoxal synthase activity protein homodimerization activity triose-phosphate isomerase activity ubiquitin protein ligase binding | Gallus gallus | 3D-structure Cytoplasm Direct protein sequencing Gluconeogenesis Glycolysis Isomerase Lyase Reference proteome | MAPRKFFVGG | MAPRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSHVSDAVAQSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH | canonical glycolysis gluconeogenesis glyceraldehyde-3-phosphate biosynthetic process glycerol catabolic process glycolytic process methylglyoxal biosynthetic process cytosol methylglyoxal synthase activity protein homodimerization activity triose-phosphate isomerase activity ubiquitin protein ligase binding Gallus gallus 3D-structure Cytoplasm Direct protein sequencing Gluconeogenesis Glycolysis Isomerase Lyase Reference proteome MAPRKFFVGG MAPRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSHVSDAVAQSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH |
gluconeogenesis glyceraldehyde-3-phosphate biosynthetic process glycerol catabolic process glycolytic process | cytoplasm; cytosol; mitochondrion; plasma membrane | triose-phosphate isomerase activity | Saccharomyces cerevisiae | 3D-structure Direct protein sequencing Gluconeogenesis Glycolysis Isomerase Isopeptide bond Phosphoprotein Reference proteome Ubl conjugation | MARTFFVGGN | MARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFVDIINSRN | gluconeogenesis glyceraldehyde-3-phosphate biosynthetic process glycerol catabolic process glycolytic process cytoplasm; cytosol; mitochondrion; plasma membrane triose-phosphate isomerase activity Saccharomyces cerevisiae 3D-structure Direct protein sequencing Gluconeogenesis Glycolysis Isomerase Isopeptide bond Phosphoprotein Reference proteome Ubl conjugation MARTFFVGGN MARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFVDIINSRN |
colanic acid biosynthetic process GDP-mannose biosynthetic process mannose catabolic process | cytosol | mannose-6-phosphate isomerase activity zinc ion binding | Escherichia coli | Acetylation Cytoplasm Isomerase Metal-binding Reference proteome Zinc | MQKLINSVQN | MQKLINSVQNYAWGSKTALTELYGMENPSSQPMAELWMGAHPKSSSRVQNAAGDIVSLRDVIESDKSTLLGEAVAKRFGELPFLFKVLCAAQPLSIQVHPNKHNSEIGFAKENAAGIPMDAAERNYKDPNHKPELVFALTPFLAMNAFREFSEIVSLLQPVAGAHPAIAHFLQQPDAERLSELFASLLNMQGEEKSRALAILKSALDSQQGEPWQTIRLISEFYPEDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANQLLTQPVKQGAELDFPIPVDDFAFSLHDLSDKETTISQQSAAILFCVEGDATLWKGSQQLQLKPGESAFIAANESPVTVKGHGRLARVYNKL | colanic acid biosynthetic process GDP-mannose biosynthetic process mannose catabolic process cytosol mannose-6-phosphate isomerase activity zinc ion binding Escherichia coli Acetylation Cytoplasm Isomerase Metal-binding Reference proteome Zinc MQKLINSVQN MQKLINSVQNYAWGSKTALTELYGMENPSSQPMAELWMGAHPKSSSRVQNAAGDIVSLRDVIESDKSTLLGEAVAKRFGELPFLFKVLCAAQPLSIQVHPNKHNSEIGFAKENAAGIPMDAAERNYKDPNHKPELVFALTPFLAMNAFREFSEIVSLLQPVAGAHPAIAHFLQQPDAERLSELFASLLNMQGEEKSRALAILKSALDSQQGEPWQTIRLISEFYPEDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANQLLTQPVKQGAELDFPIPVDDFAFSLHDLSDKETTISQQSAAILFCVEGDATLWKGSQQLQLKPGESAFIAANESPVTVKGHGRLARVYNKL |
glucose metabolic process | sarcoplasmic reticulum | magnesium ion binding phosphoglucomutase activity | Oryctolagus cuniculus | 3D-structure Acetylation Alternative splicing Carbohydrate metabolism Cytoplasm Direct protein sequencing Glucose metabolism Isomerase Magnesium Metal-binding Phosphoprotein Reference proteome Sarcoplasmic reticulum | MVKIVTVKTK | MVKIVTVKTKAYPDQKPGTSGLRKRVKVFQSSTNYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIVRIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAICPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRNIFDFNALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVANATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWHKFGRNFFTRYDYEEVEAEGATKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYHDPVDGSVSKNQGLRLIFADGSRIIFRLSGTGSAGATIRLYIDSYEKDNAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT | glucose metabolic process sarcoplasmic reticulum magnesium ion binding phosphoglucomutase activity Oryctolagus cuniculus 3D-structure Acetylation Alternative splicing Carbohydrate metabolism Cytoplasm Direct protein sequencing Glucose metabolism Isomerase Magnesium Metal-binding Phosphoprotein Reference proteome Sarcoplasmic reticulum MVKIVTVKTK MVKIVTVKTKAYPDQKPGTSGLRKRVKVFQSSTNYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIVRIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAICPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRNIFDFNALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVANATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWHKFGRNFFTRYDYEEVEAEGATKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYHDPVDGSVSKNQGLRLIFADGSRIIFRLSGTGSAGATIRLYIDSYEKDNAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT |
gluconeogenesis glycolytic process | cytosol; mitochondrial intermembrane space; mitochondrial outer membrane; mitochondrion | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity phosphoglycerate mutase activity | Saccharomyces cerevisiae | 3D-structure Cytoplasm Direct protein sequencing Glycolysis Isomerase Isopeptide bond Membrane Mitochondrion Mitochondrion outer membrane Phosphoprotein Reference proteome Ubl conjugation | MPKLVLVRHG | MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK | gluconeogenesis glycolytic process cytosol; mitochondrial intermembrane space; mitochondrial outer membrane; mitochondrion 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity phosphoglycerate mutase activity Saccharomyces cerevisiae 3D-structure Cytoplasm Direct protein sequencing Glycolysis Isomerase Isopeptide bond Membrane Mitochondrion Mitochondrion outer membrane Phosphoprotein Reference proteome Ubl conjugation MPKLVLVRHG MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK |
regulation of protein complex stability tyrosyl-tRNA aminoacylation | cytoplasm; protein-containing complex | ATP binding protein homodimerization activity tRNA binding tyrosine-tRNA ligase activity | Geobacillus stearothermophilus | 3D-structure Aminoacyl-tRNA synthetase ATP-binding Cytoplasm Direct protein sequencing Ligase Nucleotide-binding Protein biosynthesis RNA-binding tRNA-binding | MDLLAELQWR | MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGEARAFGLTIPLVTKADGTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRISEALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA | regulation of protein complex stability tyrosyl-tRNA aminoacylation cytoplasm; protein-containing complex ATP binding protein homodimerization activity tRNA binding tyrosine-tRNA ligase activity Geobacillus stearothermophilus 3D-structure Aminoacyl-tRNA synthetase ATP-binding Cytoplasm Direct protein sequencing Ligase Nucleotide-binding Protein biosynthesis RNA-binding tRNA-binding MDLLAELQWR MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGEARAFGLTIPLVTKADGTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRISEALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA |
isoleucyl-tRNA aminoacylation response to antibiotic | cytosol | aminoacyl-tRNA editing activity ATP binding isoleucine-tRNA ligase activity tRNA binding zinc ion binding | Escherichia coli | Acetylation Aminoacyl-tRNA synthetase Antibiotic resistance ATP-binding Cytoplasm Direct protein sequencing Ligase Metal-binding Nucleotide-binding Protein biosynthesis Reference proteome Zinc | MSDYKSTLNL | MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFQAVDQDALKAKFAVSNVNGPISLVIWTTTPWTLPANRAISIAPDFDYALVQIDGQAVILAKDLVESVMQRIGVTDYTILGTVKGAELELLRFTHPFMGFDVPAILGDHVTLDAGTGAVHTAPGHGPDDYVIGQKYGLETANPVGPDGTYLPGTYPTLDGVNVFKANDIVVALLQEKGALLHVEKMQHSYPCCWRHKTPIIFRATPQWFVSMDQKGLRAQSLKEIKGVQWIPDWGQARIESMVANRPDWCISRQRTWGVPMSLFVHKDTEELHPRTLELMEEVAKRVEVDGIQAWWDLDAKEILGDEADQYVKVPDTLDVWFDSGSTHSSVVDVRPEFAGHAADMYLEGSDQHRGWFMSSLMISTAMKGKAPYRQVLTHGFTVDGQGRKMSKSIGNTVSPQDVMNKLGADILRLWVASTDYTGEMAVSDEILKRAADSYRRIRNTARFLLANLNGFDPAKDMVKPEEMVVLDRWAVGCAKAAQEDILKAYEAYDFHEVVQRLMRFCSVEMGSFYLDIIKDRQYTAKADSVARRSCQTALYHIAEALVRWMAPILSFTADEVWGYLPGEREKYVFTGEWYEGLFGLADSEAMNDAFWDELLKVRGEVNKVIEQARADKKVGGSLEAAVTLYAEPELSAKLTALGDELRFVLLTSGATVADYNDAPADAQQSEVLKGLKVALSKAEGEKCPRCWHYTQDVGKVAEHAEICGRCVSNVAGDGEKRKFA | isoleucyl-tRNA aminoacylation response to antibiotic cytosol aminoacyl-tRNA editing activity ATP binding isoleucine-tRNA ligase activity tRNA binding zinc ion binding Escherichia coli Acetylation Aminoacyl-tRNA synthetase Antibiotic resistance ATP-binding Cytoplasm Direct protein sequencing Ligase Metal-binding Nucleotide-binding Protein biosynthesis Reference proteome Zinc MSDYKSTLNL MSDYKSTLNLPETGFPMRGDLAKREPGMLARWTDDDLYGIIRAAKKGKKTFILHDGPPYANGSIHIGHSVNKILKDIIVKSKGLSGYDSPYVPGWDCHGLPIELKVEQEYGKPGEKFTAAEFRAKCREYAATQVDGQRKDFIRLGVLGDWSHPYLTMDFKTEANIIRALGKIIGNGHLHKGAKPVHWCVDCRSALAEAEVEYYDKTSPSIDVAFQAVDQDALKAKFAVSNVNGPISLVIWTTTPWTLPANRAISIAPDFDYALVQIDGQAVILAKDLVESVMQRIGVTDYTILGTVKGAELELLRFTHPFMGFDVPAILGDHVTLDAGTGAVHTAPGHGPDDYVIGQKYGLETANPVGPDGTYLPGTYPTLDGVNVFKANDIVVALLQEKGALLHVEKMQHSYPCCWRHKTPIIFRATPQWFVSMDQKGLRAQSLKEIKGVQWIPDWGQARIESMVANRPDWCISRQRTWGVPMSLFVHKDTEELHPRTLELMEEVAKRVEVDGIQAWWDLDAKEILGDEADQYVKVPDTLDVWFDSGSTHSSVVDVRPEFAGHAADMYLEGSDQHRGWFMSSLMISTAMKGKAPYRQVLTHGFTVDGQGRKMSKSIGNTVSPQDVMNKLGADILRLWVASTDYTGEMAVSDEILKRAADSYRRIRNTARFLLANLNGFDPAKDMVKPEEMVVLDRWAVGCAKAAQEDILKAYEAYDFHEVVQRLMRFCSVEMGSFYLDIIKDRQYTAKADSVARRSCQTALYHIAEALVRWMAPILSFTADEVWGYLPGEREKYVFTGEWYEGLFGLADSEAMNDAFWDELLKVRGEVNKVIEQARADKKVGGSLEAAVTLYAEPELSAKLTALGDELRFVLLTSGATVADYNDAPADAQQSEVLKGLKVALSKAEGEKCPRCWHYTQDVGKVAEHAEICGRCVSNVAGDGEKRKFA |
alanyl-tRNA aminoacylation negative regulation of DNA-templated transcription | cytosol; membrane | alanine-tRNA ligase activity aminoacyl-tRNA editing activity ATP binding DNA-binding transcription repressor activity identical protein binding protein homodimerization activity Ser-tRNA(Ala) hydrolase activity tRNA binding zinc ion binding | Escherichia coli | 3D-structure Acetylation Aminoacyl-tRNA synthetase ATP-binding Cytoplasm Direct protein sequencing Ligase Metal-binding Nucleotide-binding Protein biosynthesis Reference proteome RNA-binding tRNA-binding Zinc | MSKSTAEIRQ | MSKSTAEIRQAFLDFFHSKGHQVVASSSLVPHNDPTLLFTNAGMNQFKDVFLGLDKRNYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIQFAWELLTSEKWFALPKERLWVTVYESDDEAYEIWEKEVGIPRERIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRQADGTMEPLPKPSVDTGMGLERIAAVLQHVNSNYDIDLFRTLIQAVAKVTGATDLSNKSLRVIADHIRSCAFLIADGVMPSNENRGYVLRRIIRRAVRHGNMLGAKETFFYKLVGPLIDVMGSAGEDLKRQQAQVEQVLKTEEEQFARTLERGLALLDEELAKLSGDTLDGETAFRLYDTYGFPVDLTADVCRERNIKVDEAGFEAAMEEQRRRAREASGFGADYNAMIRVDSASEFKGYDHLELNGKVTALFVDGKAVDAINAGQEAVVVLDQTPFYAESGGQVGDKGELKGANFSFAVEDTQKYGQAIGHIGKLAAGSLKVGDAVQADVDEARRARIRLNHSATHLMHAALRQVLGTHVSQKGSLVNDKVLRFDFSHNEAMKPEEIRAVEDLVNTQIRRNLPIETNIMDLEAAKAKGAMALFGEKYDERVRVLSMGDFSTELCGGTHASRTGDIGLFRIISESGTAAGVRRIEAVTGEGAIATVHADSDRLSEVAHLLKGDSNNLADKVRSVLERTRQLEKELQQLKEQAAAQESANLSSKAIDVNGVKLLVSELSGVEPKMLRTMVDDLKNQLGSTIIVLATVVEGKVSLIAGVSKDVTDRVKAGELIGMVAQQVGGKGGGRPDMAQAGGTDAAALPAALASVKGWVSAKLQ | alanyl-tRNA aminoacylation negative regulation of DNA-templated transcription cytosol; membrane alanine-tRNA ligase activity aminoacyl-tRNA editing activity ATP binding DNA-binding transcription repressor activity identical protein binding protein homodimerization activity Ser-tRNA(Ala) hydrolase activity tRNA binding zinc ion binding Escherichia coli 3D-structure Acetylation Aminoacyl-tRNA synthetase ATP-binding Cytoplasm Direct protein sequencing Ligase Metal-binding Nucleotide-binding Protein biosynthesis Reference proteome RNA-binding tRNA-binding Zinc MSKSTAEIRQ MSKSTAEIRQAFLDFFHSKGHQVVASSSLVPHNDPTLLFTNAGMNQFKDVFLGLDKRNYSRATTSQRCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKHDAIQFAWELLTSEKWFALPKERLWVTVYESDDEAYEIWEKEVGIPRERIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGPPGSPEEDGDRYIEIWNIVFMQFNRQADGTMEPLPKPSVDTGMGLERIAAVLQHVNSNYDIDLFRTLIQAVAKVTGATDLSNKSLRVIADHIRSCAFLIADGVMPSNENRGYVLRRIIRRAVRHGNMLGAKETFFYKLVGPLIDVMGSAGEDLKRQQAQVEQVLKTEEEQFARTLERGLALLDEELAKLSGDTLDGETAFRLYDTYGFPVDLTADVCRERNIKVDEAGFEAAMEEQRRRAREASGFGADYNAMIRVDSASEFKGYDHLELNGKVTALFVDGKAVDAINAGQEAVVVLDQTPFYAESGGQVGDKGELKGANFSFAVEDTQKYGQAIGHIGKLAAGSLKVGDAVQADVDEARRARIRLNHSATHLMHAALRQVLGTHVSQKGSLVNDKVLRFDFSHNEAMKPEEIRAVEDLVNTQIRRNLPIETNIMDLEAAKAKGAMALFGEKYDERVRVLSMGDFSTELCGGTHASRTGDIGLFRIISESGTAAGVRRIEAVTGEGAIATVHADSDRLSEVAHLLKGDSNNLADKVRSVLERTRQLEKELQQLKEQAAAQESANLSSKAIDVNGVKLLVSELSGVEPKMLRTMVDDLKNQLGSTIIVLATVVEGKVSLIAGVSKDVTDRVKAGELIGMVAQQVGGKGGGRPDMAQAGGTDAAALPAALASVKGWVSAKLQ |
glutamyl-tRNA aminoacylation methionyl-tRNA aminoacylation | aminoacyl-tRNA synthetase multienzyme complex; cytoplasm; cytosol; methionyl glutamyl tRNA synthetase complex | ATP binding methionine-tRNA ligase activity | Saccharomyces cerevisiae | 3D-structure Acetylation Aminoacyl-tRNA synthetase ATP-binding Cytoplasm Direct protein sequencing Ligase Nucleotide-binding Protein biosynthesis Reference proteome | MSFLISFDKS | MSFLISFDKSKKHPAHLQLANNLKIALALEYASKNLKPEVDNDNAAMELRNTKEPFLLFDANAILRYVMDDFEGQTSDKYQFALASLQNLLYHKELPQQHVEVLTNKAIENYLVELKEPLTTTDLILFANVYALNSSLVHSKFPELPSKVHNAVALAKKHVPRDSSSFKNIGAVKIQADLTVKPKDSEILPKPNERNILITSALPYVNNVPHLGNIIGSVLSADIFARYCKGRNYNALFICGTDEYGTATETKALEEGVTPRQLCDKYHKIHSDVYKWFQIGFDYFGRTTTDKQTEIAQHIFTKLNSNGYLEEQSMKQLYCPVHNSYLADRYVEGECPKCHYDDARGDQCDKCGALLDPFELINPRCKLDDASPEPKYSDHIFLSLDKLESQISEWVEKASEEGNWSKNSKTITQSWLKDGLKPRCITRDLVWGTPVPLEKYKDKVLYVWFDATIGYVSITSNYTKEWKQWWNNPEHVSLYQFMGKDNVPFHTVVFPGSQLGTEENWTMLHHLNTTEYLQYENGKFSKSRGVGVFGNNAQDSGISPSVWRYYLASVRPESSDSHFSWDDFVARNNSELLANLGNFVNRLIKFVNAKYNGVVPKFDPKKVSNYDGLVKDINEILSNYVKEMELGHERRGLEIAMSLSARGNQFLQENKLDNTLFSQSPEKSDAVVAVGLNIIYAVSSIITPYMPEIGEKINKMLNAPALKIDDRFHLAILEGHNINKAEYLFQRIDEKKIDEWRAKYGGQQV | glutamyl-tRNA aminoacylation methionyl-tRNA aminoacylation aminoacyl-tRNA synthetase multienzyme complex; cytoplasm; cytosol; methionyl glutamyl tRNA synthetase complex ATP binding methionine-tRNA ligase activity Saccharomyces cerevisiae 3D-structure Acetylation Aminoacyl-tRNA synthetase ATP-binding Cytoplasm Direct protein sequencing Ligase Nucleotide-binding Protein biosynthesis Reference proteome MSFLISFDKS MSFLISFDKSKKHPAHLQLANNLKIALALEYASKNLKPEVDNDNAAMELRNTKEPFLLFDANAILRYVMDDFEGQTSDKYQFALASLQNLLYHKELPQQHVEVLTNKAIENYLVELKEPLTTTDLILFANVYALNSSLVHSKFPELPSKVHNAVALAKKHVPRDSSSFKNIGAVKIQADLTVKPKDSEILPKPNERNILITSALPYVNNVPHLGNIIGSVLSADIFARYCKGRNYNALFICGTDEYGTATETKALEEGVTPRQLCDKYHKIHSDVYKWFQIGFDYFGRTTTDKQTEIAQHIFTKLNSNGYLEEQSMKQLYCPVHNSYLADRYVEGECPKCHYDDARGDQCDKCGALLDPFELINPRCKLDDASPEPKYSDHIFLSLDKLESQISEWVEKASEEGNWSKNSKTITQSWLKDGLKPRCITRDLVWGTPVPLEKYKDKVLYVWFDATIGYVSITSNYTKEWKQWWNNPEHVSLYQFMGKDNVPFHTVVFPGSQLGTEENWTMLHHLNTTEYLQYENGKFSKSRGVGVFGNNAQDSGISPSVWRYYLASVRPESSDSHFSWDDFVARNNSELLANLGNFVNRLIKFVNAKYNGVVPKFDPKKVSNYDGLVKDINEILSNYVKEMELGHERRGLEIAMSLSARGNQFLQENKLDNTLFSQSPEKSDAVVAVGLNIIYAVSSIITPYMPEIGEKINKMLNAPALKIDDRFHLAILEGHNINKAEYLFQRIDEKKIDEWRAKYGGQQV |
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