ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P23371 | MNRNPDQNTLPNITLKIIETYLGRVPSVNEYHMLKLQARNIQKITVFNKDIFVSLVKKNKKRFFSDVNTSASEIKDRILSYFSKQTQTYNIGKLFTIIELQSVLVTTYTDILGVLTIKAPNVISSKISYNVTSMEELARDMLNSMNVAVIDKAKVMGRHNVSSLVKNVNKLMEEYLRRHNKSCICYGSYSLYLINPNIRYGDIDILQTNSRTFLIDLAFLIKFITGNNIILSKIPYLRNYMVIKDENDNHIIDSFNIRQDTMNVVPKIFIDNIYIVDPTFQLLNMIKMFSQIDRLEDLSKDPEKFNARMATMLEYVRYTH... | Function: Polymerase that creates the 3'-poly(A) tail of mRNA's.
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 55531
Sequence Length: 479
EC: 2.7.7.19
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P23067 | GFFALIPKIISSPIFKTLLSAVGSALSSSGGQE | Function: Exhibits unusual shark repellent and surfactant properties. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis.
Sequence Mass (Da): 3324
Sequence Length: 33
Domain: Consists of a C-terminal hydrophilic region and a predominantly hydrophobic remainder... |
P13720 | MKKWFPAFLFLSLSGGNDALAGWHNVMFYAFNDYLTTNAGNVKVIDQPQLYIPWNTGSATATYYSCSGPEFASGVYFQEYLAWMVVPKHVYTNEGFNIFLDVQSKYGWSMENENDKDFYFFVNGYEWDTWTNNGARICFYPGNMKQLNNKFNDLVFRVLLPVDLPKGHYNFPVRYIRGIQHHYYDLWQDHYKMPYDQIKQLPATNTLMLSFDNVGGCQPSTQVLNIDHGSIVIDRANGNIASQTLSIYCDVPVSVKISLLRNTPPIYNNNKFSVGLGNGWDSIISLDGVEQSEEILRWYTAGSKTVKIESRLYGEEGKRK... | Function: Tip adhesin component of type P pili that binds preferentially to host cell glycosphingolipids such as globotriaosylceramide.
PTM: Contains disulfide bonds .
Sequence Mass (Da): 38281
Sequence Length: 335
Subcellular Location: Secreted
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P72542 | MTAAAPTLAQALDEATGQLTGAGITADAARADTRLLAAHACQVAPGDLDTCLAGPVPPRFWHYVRRRLTREPAERIVGHAYFMGHRFDLAPGVFVPKPETEEITRDAIARLEALVRRGTTAPLVVDLCAGPGTMAVTLARHVPAARVLGIELSQAAARAARRNARGTGARIVQGDARDAFPELSGTVDLVVTNPPYIPIGLRTSAPEVLEHDPPLALWAGEEGLGMIRAMERTAARLLAPGGVLLLEHGSYQLASVPALFRATGRWSHASSRPTCNDGCLTAVRNHTCAPPA | Function: Involved in pristinamycin I biosynthesis . Catalyzes the SAM-dependent methylation of 4-amino-L-phenylalanine (PAPA) to 4-methylamino-L-phenylalanine (MMPAPA), and of MMPAPA to 4-dimethylamino-L-phenylalanine (DMPAPA) .
Catalytic Activity: 4-amino-L-phenylalanine + S-adenosyl-L-methionine = 4-methylamino-L-ph... |
P51005 | MLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRAVMVEEFKQGLAITDEILLVKAEWSKLFDAPNFFQKYKHYILLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPSPSENSEKEEFRTMWVIGLVFKKMENSENLSVDLTYDIQSFTDTVYRQAINSKMFETEIKIAAMHVKRKQLHQLLPSHVLPKKKKHSVEGVKLVSLNDSSIDLSVDSDNSMSVPSPTNATRTSPLNSTGLSQGNSPATPVSLSVTNTQ... | Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (CPSF).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 53830
Sequence Length: 484
Subcellular Location: Nucleus
E... |
P51006 | MPFPLASQGSQQSQKTYGITSPISLATPKDTDCTLTQKLIETLKPYGVFEEEDELQHRILSLGKLNNLVKEWIREISELKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDLFSSFYEKLKQQEEVKDLRSVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDSFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQ... | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. May acquire specificity through interaction with a cleavage and polyadenylation factor (CPSF).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (D... |
P25500 | MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCLLTQKLVETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAY... | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CP... |
P51003 | MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCVLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAY... | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CP... |
Q61183 | MPFPVTTQGSQQTQPPQRHYGITSPISLAAPKETDCLLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAY... | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CP... |
Q9GN62 | MDAPSTSSGAQSKLLMPGDDEADEDHQNRGDPNLQQKQKIQLNVDPDYDDDEDDDCFIDGCEASAPITRELVDGAIERRSKDRNVKMSIGVYDEYDDDDDDEEETEEDQRRRFVEGIRNIRHKQQESFDLEEHPIPVESEAMRQFINQQVNNAMMFNQDNSEFQHIEFEPIVKQKGPKIIEGYMWGGQIGTGSYGKVKECIDMYTLTRRAVKIMKYDKLRKITNGWENIRSEMSILRRMNHRNVIKLIEIFNIPAKGKVYMVFEYCIGSVQQLLDMEPARRLTIGESHAIFIELCQGLNYLHSKRVSHKDIKPGNLLVSI... | Function: Required for cytoplasmic partitioning and asymmetric cell division in early embryogenesis . Controls the asymmetric cell division of the Q.p neuroblast lineage . Involved in mediating cell polarization via regulation of anillin family scaffold proteins . Phosphorylates and restricts the asymmetry effectors me... |
Q96RI0 | MWGRLLLWPLVLGFSLSGGTQTPSVYDESGSTGGGDDSTPSILPAPRGYPGQVCANDSDTLELPDSSRALLLGWVPTRLVPALYGLVLVVGLPANGLALWVLATQAPRLPSTMLLMNLAAADLLLALALPPRIAYHLRGQRWPFGEAACRLATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGRRLALGLCMAAWLMAAALALPLTLQRQTFRLARSDRVLCHDALPLDAQASHWQPAFTCLALLGCFLPLLAMLLCYGATLHTLAASGRRYGHALRLTAVVLASAVAFFVPSNLLLLLHYSDPSPSAWGNLYG... | Function: Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis . May play a role in platelets activation .
PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da):... |
O88634 | MCWPLLYPLVLGLSISLAEGIQTPSIYDDVESTRGSHEGPLGPTVELKEPKSSDKPNPRGYPGKFCANDSDTLELPASSQALLLGWVPTRLVPALYGLVVAVGLPANGLALWVLATRVPRLPSTILLMNLAVADLLLALVLPPRLAYHLRGQRWPFGEAACRVATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGQRLTTGLCLVAWLSAATLALPLTLHRQTFRLAGSDRMLCHDALPLTEQTSHWRPAFICLAVLGCFVPLLAMGLCYGATLRALAANGQRYSHALRLTALVLFSAVASFTPSNVLLVLHYS... | Function: Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.
PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 4... |
Q9NPB6 | MARPQRTPARSPDSIVEVKSKFDAEFRRFALPRASVSGFQEFSRLLRAVHQIPGLDVLLGYTDAHGDLLPLTNDDSLHRALASGPPPLRLLVQKRAEADSSGLAFASNSLQRRKKGLLLRPVAPLRTRPPLLISLPQDFRQVSSVIDVDLLPETHRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSDEILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQRNNVVRGASGRLTGPPSAGPGPAEPDSDDDSSDLVIENRQPPSSNGLSQGPPCWDLHPGCRHPGTRSSL... | Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in the formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bo... |
Q9Z101 | MARPQRTPARSPDSIVEVKSKFDAEFRRFALPRTSVRGFQEFSRLLCVVHQIPGLDVLLGYTDAHGDLLPLTNDDSLHRALASGPPPLRLLVQKRAEGDSSGLAFASNSLQRRKKGLLLRPVAPLRTRPPLLISLPQDFRQVSSVIDVDLLPETHRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSDEILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQRNNVVRGASGRLTGPSSVGPGPTDPDSDDDSSDLVIENRHPPCSNGLSQGPLCWDLQPGCLLPGAGSSL... | Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in the formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bo... |
Q9BYG5 | MNRSHRHGAGSGCLGTMEVKSKFGAEFRRFSLERSKPGKFEEFYGLLQHVHKIPNVDVLVGYADIHGDLLPINNDDNYHKAVSTANPLLRIFIQKKEEADYSAFGTDTLIKKKNVLTNVLRPDNHRKKPHIVISMPQDFRPVSSIIDVDILPETHRRVRLYKYGTEKPLGFYIRDGSSVRVTPHGLEKVPGIFISRLVPGGLAQSTGLLAVNDEVLEVNGIEVSGKSLDQVTDMMIANSRNLIITVRPANQRNNVVRNSRTSGSSGQSTDNSLLGYPQQIEPSFEPEDEDSEEDDIIIEDNGVPQQIPKAVPNTESLESL... | Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound ... |
Q9JK83 | MNRGHRHGASSGCLGTMEVKSKFGAEFRRFSLERSKPGKFEEFYGLLQHVHKIPNVDVLVGYADIHGDLLPINNDDNYHKAVSTANPLLRIFIQKKEEADYSAFGTDTLIRKKNMLSNVLRPDNHRKKPHIVISMPQDFRPVSSIIDVDILPETHRRVRLYKYGTEKPLGFYIRDGSSVRVTPHGLEKVPGIFISRLVPGGLAQSTGLLAVNDEVLEVNGIEVSGKSLDQVTDMMIANSRNLIITVRPANQRNNVVRNSRTSGSSSQSTDNSLLGFPQQVEASFEPEDQDSDEDDIIIEDSGEPQQIPKATPAQSLESLT... | Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. Probably involved in formation of epithelial tight junctions. Association with PARD3 may prevent the interaction of PARD3 with F11R/JAM1, thereby preventing tight junction assembly. The PARD6-PARD3 complex links GTP-bound ... |
Q9BYG4 | MNRSFHKSQTLRFYDCSAVEVKSKFGAEFRRFSLDRHKPGKFEDFYKLVVHTHHISNSDVTIGYADVHGDLLPINNDDNFCKAVSSANPLLRVFIQKREEAERGSLGAGSLCRRRRALGALRDEGPRRRAHLDIGLPRDFRPVSSIIDVDLVPETHRRVRLHRHGCEKPLGFYIRDGASVRVTPHGLEKVPGIFISRMVPGGLAESTGLLAVNDEVLEVNGIEVAGKTLDQVTDMMIANSHNLIVTVKPANQRNNVVRGGRALGSSGPPSDGTAGFVGPPAPRVLQNFHPDEAESDEDNDVVIEGTLEPARPPQTPGAPA... | Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (By similarity).
Sequence Mass (Da): 40883
Sequence Length: 37... |
Q9JK84 | MNRSFHKSQTLRFYDCSAVEVKSKFGAEFRRFSLDRHKPGKFEDFYQLVVHTHHISNTEVTIGYADVHGDLLPINNDDNFCKAVSSANPLLRVFIQKREEADHYSFGAGTLSRKKKVLVTLRDDGLRRRPHLNISMPHDFRPVSSIIDVDILPETHRRVRLYRHGYEKPLGFYIRDGTSVRVTPHGLEKVPGIFISRMVPGGLAESTGLLAVNDEVLEVNGIEVAGKTLDQVTDMMIANSHNLIVTVKPANQRNNVVRSSRTSGSSVHSTDSTTSHHSLPGAHVLQNSEDVESDEEADIVIEGALEPQHIPKTQAVPPGS... | Function: Adapter protein involved in asymmetrical cell division and cell polarization processes. May play a role in the formation of epithelial tight junctions. The PARD6-PARD3 complex links GTP-bound Rho small GTPases to atypical protein kinase C proteins (By similarity).
Sequence Mass (Da): 42341
Sequence Length: 38... |
Q9NAN2 | MSYNGSYHQNHHSTLQVKSKFDSEWRRFSIPMHSASGVSYDGFRSLVEKLHHLESVQFTLCYNSTGGDLLPITNDDNLRKSFESARPLLRLLIQRRGESWEEKYGYGTDSDKRWKGISSLMAQKPPKRSYSISNPEDFRQVSAIIDVDIVPEAHRRVRLCKHGQERPLGFYIRDGTSVRVTERGVVKVSGIFISRLVDGGLAESTGLLGVNDEVLEVNGIEVLGKTLDQVTDMMVANAHNLIITVKPANQRNTLSRGPSQQGTPNASEMSAATAAATGGIQRPMKMNGSSDGSYHPKQHDANDSDSGED | Function: Necessary for apicobasal and anterior-posterior asymmetries associated with cell adhesion and gastrulation during the first few cell cycles of embryogenesis . Required for localizing/ maintaining par-3 at the cell periphery . Regulates mes-1 expression and/or localization pattern during early embryogenesis . ... |
Q8VDG3 | MEIIRSNFKINLHKVYQAIEEADFFAIDGEFSGISDGPSVTALTSGFDTPEERYQKLKKHSMDFLLFQFGLCAFKYDHTDSKHVTKSFNFYVFPKPFSRSSPDVKFVCQSSSIDFLASQGFDFNKVFCSGIPYLNQEEERQLREQFDEKRSQANGAGALAKCPVTIPEDQKKFIDQVIEKIEDFLQSEEKRSLELDPCTGFQRKLIYQTLSWKYPKGIHVETLETDKKERHIVISKVDEEERKRREQEKYTKEQEELNDAVGFSRVIHAIANSGKLVVGHNMLLDVMHTIHQFYCPLPADLNEFKEMAICVFPRLLDTKL... | Cofactor: Divalent metal cations. Mg(2+) is the most probable.
Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence c... |
Q90ZA1 | MEITRSNFKDTLPKVYKAIEEADFLAIDGEFSGISDGPSVSTLTNGFDTPEERYTKLKKHSMEFLLFQFGLCTFNYDNTEAKYLMKSFNFYIFPKPFNRNSPDKKFVCQSSSIDFLANQGFDFNKVFRNGIPYLNQEEERVLRDQYEDRRSQSNGASTMSYISPNSSKTPVSIPDEQKGFIDKVVERVEDFLKNEQKSMNVEPCTGYQRKLIYQTLNWKYPRGIHVETVESEKKERYIVISKVDEEERKRMEQQKQAKEREELDDAVGFSRIIQAISSSGKLVVGHNMLLDVMHTIHQFFCQLPDELNEFKEVTNCVFPR... | Function: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. Required during meiotic maturation to silence certain maternal mRNAs translationally. Does ... |
Q9ZP54 | MASPHKPWRAEYAKSSRSSCKTCKSVINKENFRLGKLVQSTHFDGIMPMWNHASCILKKTKQIKSVDDVEGIESLRWEDQQKIRKYVESGAGSNTSTSTGTSTSSTANNAKLEYGIEVSQTSRAGCRKCSEKILKGEVRIFSKPEGPGNKGLMWHHAKCFLEMSSSTELESLSGWRSIPDSDQEALLPLVKKALPAAKTETAEARQTNSRAGTKRKNDSVDNEKSKLAKSSFDMSTSGALQPCSKEKEMEAQTKELWDLKDDLKKYVTSAELREMLEVNEQSTRGSELDLRDKCADGMMFGPLALCPMCSGHLSFSGGLY... | Function: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to th... |
Q9N4H4 | MIHSNEPLPYAIEYAKSGRSNCKTCKKNIALDQLRMSMNRPSTFFDGNMDSWFHYNCFWIKMIRGRDDINISSIRGVDWLRWEDQEKLRQEIQHFKTASPPTLTPLCSTTTVILSTIKTEKSLSNRGKCGKCGQNFERGEIKAHNKGKANHFKCFLQEFDKISGTVEDIPGWADYEENFKIKAVGEYVEALAAKRRSTEPATPASASPTPPEAETPVLSAEGSPESSNKRPASSEIIEIDGEGNPDENDFAKKRRMKKEARLMEVQKKRMKKQSDLLWEYRQIFERMPYTDKISILRENEQDIPEGHDPTAQVIERLVDN... | Function: Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation, a post-translational modification synthesized after DNA damage that appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks and programmed cell death . Involved in pro... |
Q5RHR0 | MADSQDDKLYKAEYAKSGRASCKKCKDNIAKDSLRMAIMVQSPMFDGKVPHWHHFSCFWLRAAVQSPSDISGFTDLRWDDQEKVKTAIESGGATGGKGGQKGAAKGEKTLNDFAVEYAKSNRSTCKGCDQKIEKDQIRVSKKTVDPEKPQLGLIDRWYHTGCFVSRREELIFKPEYSAAQLKGFAVLRDEDKEELKKRLPAVKSEGKRKADEVDGGVSKKQKKEDEKLEQNLKDQSQLIWGIKDKLKKFCSINDMKELLIANSQEVPSGESNIVDRLSDCMAFGSLKPCETCKGQLVFKSDAYYCTGDISAWTKCVFKTQ... | Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair . Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and fur... |
P09874 | MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTK... | Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair . Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and fur... |
Q9ZSV1 | MAAPPKAWKAEYAKSGRASCKSCRSPIAKDQLRLGKMVQASQFDGFMPMWNHARCIFSKKNQIKSVDDVEGIDALRWDDQEKIRNYVGSASAGTSSTAAPPEKCTIEIAPSARTSCRRCSEKITKGSVRLSAKLESEGPKGIPWYHANCFFEVSPSATVEKFSGWDTLSDEDKRTMLDLVKKDVGNNEQNKGSKRKKSENDIDSYKSARLDESTSEGTVRNKGQLVDPRGSNTSSADIQLKLKEQSDTLWKLKDGLKTHVSAAELRDMLEANGQDTSGPERHLLDRCADGMLFGALGPCPVCANGMYYYNGQYQCSGNVS... | Function: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to th... |
P11103 | MAEASERLYRVQYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGQSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVAGKGQDGSGGKAEKTLGDFAAEYAKSNRSMCKGCLEKIEKGQMRLSKKMVDPEKPQLGMIDRWYHPTCFVKKRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAIKNEGKRKGDEVDGTDEVAKKKSRKETDKYSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTK... | Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair . Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and fur... |
Q08824 | QAKVEMLDNLLDIEVAYSLLKGGAEDNKKDPIDINYEKLKTKIEVVDKTTKEAEIILQYVKNTHAATHNTYTLVVEEIFKIVREGEYQKYRPFQDLPNRQLLWHGSRATNYAGILSQGLRIAPPEAPVTGYMFGK | Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (By similarity). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target r... |
P27008 | MAEATERLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRQPDTEVDGFSELRWDDQQKVKKTAEAGGVAGKGQHGGGGKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQMRLSKKMLDPEKPQLGMIDRWYHPTCFVKNRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAVKSEGKRKCDEVDGIDEVAKKKSKKGKDKESSKLEKALKAQNELVWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWT... | Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (By similarity). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target r... |
Q11207 | MANKLKVDELRLKLAERGLSTTGVKAVLVERLEEAIAEDTKKEESKSKRKRNSSNDTYESNKLIAIGEFRGMIVKELREEAIKRGLDTTGTKKDLLERLCNDANNVSNAPVKSSNGTDEAEDDNNGFEEEKKEEKIVTATKKGAAVLDQWIPDEIKSQYHVLQRGDDVYDAILNQTNVRDNNNKFFVLQVLESDSKKTYMVYTRWGRVGVKGQSKLDGPYDSWDRAIEIFTNKFNDKTKNYWSDRKEFIPHPKSYTWLEMDYGKEENDSPVNNDIPSSSSEVKPEQSKLDTRVAKFISLICNVSMMAQHMMEIGYNANKL... | Function: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to th... |
Q09525 | MSIINDENGRGYKVHLCKTNIAQNNNKFYDMELLDEGGDFIVKLINGRIGYRGVTQLKDFDDLDRAKKFFESKFYEKTHLHWEERDDEPVPNKYAVVELATNARQTEKEVKKEEPEPEPKVDEKNTRGRKKRGIVKEKKEIKKEEEPVEEVNEKLKELMKCICDEDVHLGLLKQLKFNEAFGRPIDCLSLAQLTTGYEILSKIEESIGGKSARRSTRGRPRVADRVLAVKSDGPSLHDINKYYSLIPHSFGFCVPPKIDSHAKIQAERELLDALKGSIEASLELKDLKKTASSKDIYQRLYERLPCHLEPVSEEIAGKIG... | Function: Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation, a post-translational modification synthesized after DNA damage that appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks and programmed cell death.
Catalytic Activi... |
Q9UGN5 | MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPL... | Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair . Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl grou... |
O50017 | MSARLRVADVRAELQRRGLDVSGTKPALVRRLDAAICEAEKAVVAAAPTSVANGYDVAVDGKRNCGNNKRKRSGDGGEEGNGDTCTDVTKLEGMSYRELQGLAKARGVAANGGKKDVIQRLLSATAGPAAVADGGPLGAKEVIKGGDEEVEVKKEKMVTATKKGAAVLDQHIPDHIKVNYHVLQVGDEIYDATLNQTNVGDNNNKFYIIQVLESDAGGSFMVYNRWGRVGVRGQDKLHGPSPTRDQAIYEFEGKFHNKTNNHWSDRKNFKCYAKKYTWLEMDYGETEKEIEKGSITDQIKETKLETRIAQFISLICNISM... | Function: Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to th... |
A7KE01 | MERHLMDSQIKGVSTGTTILAVTFNGGVIIGSDSRASIGGSYVSSKTINKLIQVHDRIFCCIAGSLADAQAVTKAAKFQISFHSIQMESPPLVKAAASVLKELCYNNKEELQAGFITAGWDRKKGPQVYTVALGGMLLSQPFTIGGSGSTYIYGYADAKYKPDMSKEECLQFAKNALALAMGRDNVSGGVAHLVVITEEGVEHVVIPGDKLPKFHDE | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... |
Q9LRY1 | MSCFSCFSSKVLDNEGSSMPAPYKQPNSPKRTTGEVVAKNANGPSNNMGARIFTFRELATATKNFRQECLIGEGGFGRVYKGKLENPAQVVAVKQLDRNGLQGQREFLVEVLMLSLLHHRNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLLDLEPGQKPLDWNTRIKIALGAAKGIEYLHDEADPPVIYRDLKSSNILLDPEYVAKLSDFGLAKLGPVGDTLHVSSRVMGTYGYCAPEYQRTGYLTNKSDVYSFGVVLLELISGRRVIDTMRPSHEQNLVTWALPIFRDPTRYWQLADPLLRGDYPEKSLNQAIAVAAM... | Function: May be involved in plant defense signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 42427
Sequence Length: 381
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9SFT7 | MNCFSCFYFHEKKKVPRDSDNSYRRNGEVTGRDNNKTHPENPKTVNEQNKNNDEDKEVTNNIAAQTFSFRELATATKNFRQECLIGEGGFGRVYKGKLEKTGMIVAVKQLDRNGLQGNKEFIVEVLMLSLLHHKHLVNLIGYCADGDQRLLVYEYMSRGSLEDHLLDLTPDQIPLDWDTRIRIALGAAMGLEYLHDKANPPVIYRDLKAANILLDGEFNAKLSDFGLAKLGPVGDKQHVSSRVMGTYGYCAPEYQRTGQLTTKSDVYSFGVVLLELITGRRVIDTTRPKDEQNLVTWAQPVFKEPSRFPELADPSLEGVF... | Function: May be involved in plant defense signaling.
PTM: Palmitoylation at Cys-3 and Cys-6 are required for plasma membrane location.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46067
Sequence Length: 414
Subcellular Locati... |
Q1PDV6 | MSGCLPCFGSSAKDAASKDSVKKELSAKDGSVTQSHHISLDKSKSRRGPEQKKELTAPKEGPTAHIAAQTFTFRELAAATKNFRPECLLGEGGFGRVYKGRLETTGQIVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLHDLPPDKEPLDWSTRMTIAAGAAKGLEYLHDKANPPVIYRDLKSSNILLGDGYHPKLSDFGLAKLGPVGDKTHVSTRVMGTYGYCAPEYAMTGQLTLKSDVYSFGVVFLELITGRKAIDNARAPGEHNLVAWARPLFKDRRKFPKMADPSL... | Function: Receptor-like cytoplasmic kinase involved in the transduction of signal between the host cell surface chitin receptor complex CERK1-LYK5 and the intracellular MAPKKK5-dependent mitogen-activated protein kinase (MAPK) cascade that leads to chitin-induced immunity . Phosphorylates and activates MAPKKK5 when pho... |
Q84M95 | MHFPLVSAWNKRRRSKSYDTDPCTFLFSIIFARWHKRVYRTAECWQIEDQASQPRKRRFGSSVYTLKEMEEATSSFSDENLLGKGGFGRVYQGTLKTGEVVAIKKMDLPTFKKADGEREFRVEVDILSRLDHPNLVSLIGYCADGKHRFLVYEYMQNGNLQDHLNGIKEAKISWPIRLRIALGAAKGLAYLHSSSSVGIPIVHRDFKSTNVLLDSNYNAKISDFGLAKLMPEGKDTCVTARVLGTFGYFDPEYTSTGKLTLQSDIYAFGVVLLELLTGRRAVDLTQGPNEQNLVLQVRNILNDRKKLRKVIDVELPRNSY... | Function: May be involved in plant defense signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42541
Sequence Length: 375
Subcellular Location: Cell membrane
EC: 2.7.11.1
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O49839 | MGNCLDSSAKVDNSNHSPHANSASSGSKVSSKTSRSTGPSGLSTTSYSTDSSFGPLPTLRTEGEILSSPNLKAFTFNELKNATKNFRQDNLLGEGGFGCVFKGWIDQTSLTASRPGSGIVVAVKQLKPEGFQGHKEWLTEVNYLGQLSHPNLVLLVGYCAEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAVGAAKGLTFLHEAKSQVIYRDFKAANILLDADFNAKLSDFGLAKAGPTGDNTHVSTKVIGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELISGRRAMDNSNGGNEYSLVDWATPYLGDKRK... | Function: Involved in disease resistance signaling . Contributes to pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) signaling and defense responses downstream of FLS2 . Acts as a BIK1 decoy and enables Xanthomonas campestris AvrAC/XopAC detection; X.campestris effector AvrAC/XopAC-mediated uridyly... |
Q9LFP7 | MGLDAVKAKGNWKSEKPKETENKNHKKKNGDDNKSRNEEEEEGEASGCWVKFRFMIGCIPSKSDLDASSSSIYGSNCTVTTMESKSANEKSNDQPVGQVSSTTTTSNAESSSSTPVISEELNISSHLRKFTFNDLKLSTRNFRPESLLGEGGFGCVFKGWIEENGTAPVKPGTGLTVAVKTLNPDGLQGHKEWLAEINFLGNLLHPNLVKLVGYCIEDDQRLLVYEFMPRGSLENHLFRRSLPLPWSIRMKIALGAAKGLSFLHEEALKPVIYRDFKTSNILLDADYNAKLSDFGLAKDAPDEGKTHVSTRVMGTYGYAA... | Function: Involved in chitin-triggered immune signaling and is required for reactive oxygen species (ROS) production . Acts downstream of SD129 in defense signaling triggered by the pathogen-associated molecular pattern (PAMP) 3-OH-C10:0, a medium-chain 3-hydroxy fatty acid .
PTM: Phosphorylated by SD129 at Thr-306 and... |
Q9SRH7 | MGFDSVKVMENWQSKTSNENEKKKKKRRRKKNNNVRNSEHYEEEANGCWVKFRYIVCCASSTSDVETSLTLSTSTVGSQSAIVQSNDQPVGPVSSTTTTSNAESSLSTPIISEELNIYSHLKKFSFIDLKLATRNFRPESLLGEGGFGCVFKGWVEENGTAPVKPGTGLTVAVKTLNPDGLQGHKEWLAEINYLGNLLHPNLVKLVGYCIEDDQRLLVYEFMPRGSLENHLFRRSLPLPWSIRMKIALGAAKGLSFLHEEALKPVIYRDFKTSNILLDGEYNAKLSDFGLAKDAPDEGKTHVSTRVMGTYGYAAPEYVMT... | Function: Involved in chitin-triggered immune signaling and is required for reactive oxygen species (ROS) production . Acts downstream of SD129 in defense signaling triggered by the pathogen-associated molecular pattern (PAMP) 3-OH-C10:0, a medium-chain 3-hydroxy fatty acid .
PTM: Phosphorylated by SD129 in response to... |
O49840 | MGNCLDSSAKVDSSSHSPHANSASLSSRVSSKTSRSTVPSSLSINSYSSVESLPTPRTEGEILSSPNLKAFTFNELKNATRNFRPDSLLGEGGFGYVFKGWIDGTTLTASKPGSGIVVAVKKLKTEGYQGHKEWLTEVNYLGQLSHPNLVKLVGYCVEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAIGAAKGLTFLHDAKSQVIYRDFKAANILLDAEFNSKLSDFGLAKAGPTGDKTHVSTQVMGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELLSGRRAVDKSKVGMEQSLVDWATPYLGDKRKLFR... | Function: May be involved in plant defense signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 46289
Sequence Length: 426
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q5PP29 | MGNCFGFSAKVGNRESPYRGSSRISAKRSQSSRLSSLTIQSSSYNDDTSVASLQTPRSEGELLASPTLKAFTFNELKTATRNFRPDSVIGEGGFGYVYKGWIDERTLSPSKPGSGMVVAVKKLKEEGFQGHRQWLAEVDCLGRLHHMNLVKLIGYCSKGDHIRLLVYEYMPKGSLENHLFRRGAEPIPWRTRIKVAIGAARGLAFLHEAQVIYRDFKASNILLDSEFNAKLSDFGLAKVGPTGDRTHVSTQVMGTQGYAAPEYVATGRITAKSDVYSFGVVLLELLSGRLTVDKTKVGVERNLVDWAIPYLGDKRKVFRI... | Function: May be involved in plant defense signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 45527
Sequence Length: 412
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9LQQ8 | MGCFGCSKKSSKRSETNKDTVINRKIVGGTTSVAKSDKRDDQTQPSSDSTKVSPYRDVNNEGGVGKEDQLSLDVKGLNLNDQVTGKKAQTFTFQELAEATGNFRSDCFLGEGGFGKVFKGTIEKLDQVVAIKQLDRNGVQGIREFVVEVLTLSLADHPNLVKLIGFCAEGDQRLLVYEYMPQGSLEDHLHVLPSGKKPLDWNTRMKIAAGAARGLEYLHDRMTPPVIYRDLKCSNILLGEDYQPKLSDFGLAKVGPSGDKTHVSTRVMGTYGYCAPDYAMTGQLTFKSDIYSFGVVLLELITGRKAIDNTKTRKDQNLVG... | Function: May be involved in plant defense signaling.
PTM: Palmitoylation at Cys-3 and Cys-6 are required for plasma membrane location.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46763
Sequence Length: 423
Subcellular Locati... |
Q9SIB6 | MGCFGRTPKSNKRSDTKTTKNNDFTPKKLTVNANRDKLTQPSSDCLKVSICGDVSKEIVTKKDQLALDAKDTNVEDEVIVKKAQTFTFEELSVSTGNFKSDCFLGEGGFGKVYKGFIEKINQVVAIKQLDRNGAQGIREFVVEVLTLSLADHPNLVKLIGFCAEGVQRLLVYEYMPLGSLDNHLHDLPSGKNPLAWNTRMKIAAGAARGLEYLHDTMKPPVIYRDLKCSNILIDEGYHAKLSDFGLAKVGPRGSETHVSTRVMGTYGYCAPDYALTGQLTFKSDVYSFGVVLLELITGRKAYDNTRTRNHQSLVEWANPL... | Function: May be involved in plant defense signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 47279
Sequence Length: 424
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q0WRY5 | MGWIPCSGKSSGRNKTRRNGDHKLDRKSSDCSVSTSEKSRAKSSLSESKSKGSDHIVAQTFTFSELATATRNFRKECLIGEGGFGRVYKGYLASTSQTAAIKQLDHNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLHDISPGKQPLDWNTRMKIAAGAAKGLEYLHDKTMPPVIYRDLKCSNILLDDDYFPKLSDFGLAKLGPVGDKSHVSTRVMGTYGYCAPEYAMTGQLTLKSDVYSFGVVLLEIITGRKAIDSSRSTGEQNLVAWARPLFKDRRKFSQMADPMLQGQYPPRGLY... | Function: Serine/threonine-protein kinase involved in the positive regulation of brassinosteroid (BR) signaling and plant growth. Phosphorylates both BSU1 and BSL1 in vitro.
PTM: Phosphorylated at Ser-43, Ser-46 and Ser-234.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-ph... |
Q8GXZ3 | MGNCGTRDEAAVFTPQAQAQQLQKKHSRSVSDLSDPSTPRFRDDSRTPISYAQVIPFTLFELETITKSFRPDYILGEGGFGTVYKGYIDDNLRVGLKSLPVAVKVLNKEGLQGHREWLTEVNFLGQLRHPNLVKLIGYCCEDDHRLLVYEFMLRGSLENHLFRKTTAPLSWSRRMMIALGAAKGLAFLHNAERPVIYRDFKTSNILLDSDYTAKLSDFGLAKAGPQGDETHVSTRVMGTYGYAAPEYVMTGHLTARSDVYSFGVVLLEMLTGRKSVDKTRPSKEQNLVDWARPKLNDKRKLLQIIDPRLENQYSVRAAQK... | Function: May be involved in plant defense signaling.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Lipid-anchor
Sequence Mass (Da): 45618
Sequence Length: 410
Subcellular Location: Cell membrane
EC: 2.7.11.1
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B9HRL7 | MASKILFIGGTGYIGKFIVEASAKAGHPTFVLVRESTLSNPAKSVVIYNFKNLGVNFLIGDLFDHESLVKAIKQVDVVISTVGHAQLVEQDRIIAAIKEAGNVKRFFPSEFGNDVDRVNAVEPAKSAFATKANVRRAIEAEGIPYTYVSSNFFSGYFLLSFNQPGATAPPRDKVVILGDGNPKAVFNKEDDIATYTIKAVDDPRTLNKILYIKPPANTISFNDLVSLWEKKIGKTLERIYVPEEQLLKNIQEASVPVNVVLSIGHSVFVKGDHTNFEIEPSFGVEASELYPDVKYTTVDEYLKQFV | Function: Oxidoreductase involved in lignan biosynthesis. Catalyzes the NADPH-dependent reduction of phenylcoumaran benzylic ethers. Converts dehydrodiconiferyl alcohol (DDC) to isodihydrodehydrodiconiferyl alcohol (IDDDC), and dihydrodehydrodiconiferyl alcohol (DDDC) to tetrahydrodehydrodiconiferyl alcohol (TDDC).
Cat... |
Q15365 | MDAGVTESGLNVTLTIRLLMHGKEVGSIIGKKGESVKRIREESGARINISEGNCPERIITLTGPTNAIFKAFAMIIDKLEEDINSSMTNSTAASRPPVTLRLVVPATQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGVPQSVTECVKQICLVMLETLSQSPQGRVMTIPYQPMPASSPVICAGGQDRCSDAAGYPHATHDLEGPPLDAYSIQGQHTISPLDLAKLNQVARQQSHFAMMHGGTGFAGIDSSSPEVKGYWASLDASTQTTHELTIPNNLIGCIIGRQGANINEIRQMSGAQIKIANPVE... | Function: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC . Together with PCBP2, required for erythropoiesis, possibly by regulating mRNA splicing (By similarity).
PTM: Phosphorylated; lowers poly(rC)-binding activity.
Sequence Mass (Da): 37498
Sequence Length: 356
Subcellular Locatio... |
Q15366 | MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLETLSQSPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQ... | Function: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC . Major cellular poly(rC)-binding protein . Binds also poly(rU) . Acts as a negative regulator of antiviral signaling . Negatively regulates cellular antiviral responses mediated by MAVS signaling . It acts as an adapter betwee... |
P21902 | MLVNNVFSLLCFPLLMSVVRCSTLSRQRRQFVFPDEEELCSNRFTEEGTCKNVLDCRILLQKNDYNLLKESICGFEGITPKVCCPKSSHVISSTQAPPETTTTERPPKQIPPNLPEVCGIHNTTTTRIIGGREAPIGAWPWMTAVYIKQGGIRSVQCGGALVTNRHVITASHCVVNSAGTDVMPADVFSVRLGEHNLYSTDDDSNPIDFAVTSVKHHEHFVLATYLNDIAILTLNDTVTFTDRIRPICLPYRKLRYDDLAMRKPFITGWGTTAFNGPSSAVLREVQLPIWEHEACRQAYEKDLNITNVYMCAGFADGGKD... | Function: This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system in limulus . Its active form catalyzes the conversion of coagulogen to insoluble coagulin gel .
PTM: Proteolytically cleaved into its mature active form by serine protease factor B . Cleavage produces a 25 kDa light cha... |
Q8REI2 | MYGLEKLGINNVTAAHYNLSPAQLVEKALANNEGILSDTGAFVISTGKYTGRAPDDKFFVDTPEVHKYIDWSRNQPIEKEKFDAIFGKLVAYLQNREIFIFDGRAGANPEYTRRFRVINELASQNLFIHQLLIRTDEEYNENNDIDFTIISAPNFHCVPEIDGVNSEAAIIINFEKKIAIICATKYSGEIKKSVFSIMNYIMPHENILPMHCSANMDPVTHETAIFFGLSGTGKTTLSADPNRKLIGDDEHGWCDKGIFNFEGGCYAKCINLKEESEPEIYRAIKFGSLVENVVVDPITRKIQYEDASITPNTRVGYPID... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequen... |
Q39QU2 | MRLNDITRGTGLEEHGITNANLIYWTPPTAVLYEQIVKRGEGLVTHLGAVAVKTGHYTGRAANEKFIVDEPSSNDHIAWGKVNQPFDSAKFDALFGRMLAYLHGKDIFVQECFAGCSPDHRLPVRVITERAWHSLFARNMFVRATPEELVGFKPGFTVIDLPAFHAIPSVDGTNTETFIIVNFEKRLIIIGGTSYAGEIKKSIFTILNYLLPQHKNVLSMHCSANVGEKDDVAVFFGLSGTGKTTLSADPRRRLIGDDEHGWDNSGVFNFEGGCYAKIINLSPEAEPEIYQTTRRFGTILENVAIDTVSRRIDLNDDSFT... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequen... |
C4LGT5 | MSAPTIPGLEGNAPTTNQDMLNWIAECAELCQPDKVVFCDGSDEEWEAIAKDLVEKGTLIKLNEEKRPNSYLASSDPADVARVESRTFICSKTEDGAGPTNNWRDPDEMRAEMSEHFKGSMKGRTMYVVPFCMGPITDPDPKLGIELTDSGYVVMSMRIMTRMGKEALDKIGDGPFVKGLHSVGAPLEPGQEDVKWPCNETKYITQFPEDRVIWSYGSGYGGNAILAKKCYALRIASVMAKDEGWMAEHMLILKLISPEGKAYHICAAFPSQCGKTNLAMIQPTIPGWKAEVIGDDIAWLHFGDDGRLYAVNPENGFFGV... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Catalytic Activity: GTP + oxaloacetate = CO2 + GDP ... |
P20007 | MPELIEQSKIISGNVCGLPQLHKLRQDNCGLYSHIRGIPISYGNVDLLTTGVRAFVEEGIALCQPDQVHICDGSEQENKVLIKSLLEAGTIVPLPKYDNCWLARTNPADVARVESRTFICTERREETIPTPVEGVKGTLGNWISPSDMDAAVQQRFPGCMKGRTMYVVPFSMGPVGSPLSKIGIELTDSAYVVASMRIMTRMGAAVLRQLAKKEEFVRALHSVGAPANGQVEQPSWPCDPERTIILHKPAENLIVSYGSGYGGNSLLGKKCFALRIGSTIAKQEGWLAEHMLILGITDPKGEKKYITAAFPSACGKTNLA... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Catalytic Activity: GTP + oxaloacetate = CO2 + GDP ... |
P29190 | MKRLGHVPIHKGDFHLLPPKVQRFVAEKAELMRPRGIYICDGSQHEADEIIDKLIERGMLSPLKAYENNYICRTDPKDVARVESKTWMVTPDKYQTVCHTPDGIEPIMGHWMSPDSLATELDSRFPGCMAGRIMYVIPFSMGPVGGPLSKIGVQLTDSNYVVLSMRIMTRVGHEVWDALGDNDFVRCIHSVGLPRPVKQRVINHWPCNPERVLIAHRPAEREIWSFGSGYGGNSLLGKKMLALRIASNIAKDEGWMAEHMLIMGVTRPDGKEHFIAAAFPSACGKTNLAMLEPALPGWKVRCVGDDIAWMKFGEDGRLYA... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: In parasitic nematodes PEPCK carboxylates phosphoenolpyruvate to oxaloacetate thus introducing the products of glycolysis to mitochondrial metabolism.
Catalytic Activity: GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate
Sequence Mass (Da): 69656
Sequence Length: 6... |
P65687 | MTSATIPGLDTAPTNHQGLLSWVEEVAELTQPDRVVFTDGSEEEFQRLCDQLVEAGTFIRLNPEKHKNSYLALSDPSDVARVESRTYICSAKEIDAGPTNNWMDPGEMRSIMKDLYRGCMRGRTMYVVPFCMGPLGAEDPKLGVEITDSEYVVVSMRTMTRMGKAALEKMGDDGFFVKALHSVGAPLEPGQKDVAWPCSETKYITHFPETREIWSYGSGYGGNALLGKKCYSLRIASAMAHDEGWLAEHMLILKLISPENKAYYFAAAFPSACGKTNLAMLQPTIPGWRAETLGDDIAWMRFGKDGRLYAVNPEFGFFGV... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Catalytic Activity: GTP + oxaloacetate = CO2 + GDP ... |
P17918 | MFEARLIQGSILKKVLEALKDLINEACWDVSSGGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVIKMPSGEFARICRDLSHIGDAVVISCAKNGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVHLTFALRYLNFFTKATPLSPTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEAS | Function: Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimi... |
Q53596 | MHILVTGFAPFDNQDINPSWEAVTQLENIIGTHTIDKLKLPTSFKKVDTIINKTLASNHYDVVLAIGQAGGRNAITPERVAINIDDARIPDNDDFQPIDQAIHLDGAPRYFSNLPVKAMTQSVINQGLPGALSNSAGTFVCNHVLYHLGYLQDKHYPHLRFGFIHVPYIPEQVVGKSDTPSMPLEQIVAGLTAAIEAISDHDDLRIALGTTE | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Sequence Mass (Da): 23227
Sequence Length: 212
Subcellular Location: Cytoplasm
EC: 3.4.19.3
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Q9RL48 | MTRVLITGFAPFGGERVNPSWQAASLVAAEPPAGLAVTAAELPCVFGESLDALRDAIRADNPDLVLCLGQAGGRPGVTVERVGINVDDARIPDNAGGQPIDEPVVPDGPAAYFSTLPVKACVAAMREAGVPAAVSNTAGTFVCNHVAYGLGHLIATEFPHLRGGFAHVPWAPEQVPDGTAPALPPATVAHGLRALLAAAARTPAEQDLKVTEGATH | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Sequence Mass (Da): 22041
Sequence Length: 216
Subcellular Location: Cytoplasm
EC: 3.4.19.3
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Q8Y6C8 | MKHLFKLDPAKNLPTNDVTKLIHSGTDGFIIGGTDNVQIEAVQNLYELLVETDLPIFLEISNESMILPEADHFLIPVVLNTENSKWTHGLHKELIKEMGEFIPWKRVTSEGYVILNKDAKVAHLTEAKTDLTDEDIVAYARLAENIFHLPIFYVEYSGMYGDPEVVRKASAALSNTKFWYGGGIRSKEQAAEMAKYADTIIVGNIIYEDLEKALETATIFRKKTV | Function: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archa... |
Q8ES84 | MKNINEWHHIFKLDPAKEISDEHLDQICESGTDAIIVGGTDNVTLDGVLDLLSRIRRSHMVPVVLEVSEEETLTPGFDYYFVPMVLNSKEKKYMMDIQHKAIKEFIDMMEFAEVYFEGYCILNEDAKAFQYTNCVMPDLDDVKAYAYMAEKVFHLPFFYIEYSGAYGDPTLVKEVKEELQNTQLLYGGGIETTAQAKEMKEYADTIIVGNSIYTNINEALKTVEAVKGN | Function: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archa... |
Q53726 | MYDIKKWRHIFKLDPAKHISDDDLDAICMSQTDAIMIGGTDDVTEDNVIHLMSRVRRYPLPLVLEISNIESVMPGFDFYFVPTVLNSTDVVFHNGTLLEALKTYGHSIDFEEVIFEGYVVCNADSKVAKHTKANTDLTTEDLEAYAQMVNHMYRLPVMYIEYSGIYGDVSKVQAVSEHLTETQLFYGGGISSEQQATEMAAIADTIIVGDIIYKDIKKALKTVKIKESSK | Function: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archa... |
Q8C7K6 | MARAAPLLAVLATVLTTAAAGGDAPPGKIAVIGAGIGGSAVAHFLQQHFGPRVQIVVYEKGTVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLRQRREVVGRSAIFGGEHFVLEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGVEELLYSLGEATFVNMTQRSVAESLLQVGVTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTLHSTEGKALYQVAYESDKGNSSDFYDIVVIATPLHLDNSSNNNITFEGFT... | Function: Probable oxidoreductase.
Sequence Mass (Da): 54875
Sequence Length: 495
Subcellular Location: Secreted
EC: 1.8.3.-
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Q6PHH3 | MTMEEMKNEADATSMVSMTLYAVMYPVFNELESVNLSAAQTLRAAFKKAEKENPGLTQDIIMKILEKKNVEINFTESLLRMAADDVEEYMIDRPEREFQDLNERARALKQILSKIPDEINDRVRFLQTIKDIASAIKELLDTVNNVFKKYQYQNRRALEHQKKEFVKHSKSFSDTLKTYFKDGKAINVFASANRLIHQTNLILQTFKTVA | Function: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Required for normal angiogenesis, vasculogenesis and hematopoiesis durin... |
Q6NWL1 | MTMEEMKNEAEPNSIVSMTLYAVMYPVFNELGRINPSAAQTLRAAFVKAEKENPGLTQDIIMKILEKKNVEINFTESLLRMAADDVEEYLIKRPEQEFQDLNEKARALKHILSKIPDEINDRVRFLQTIKDIASAIKELLDTVNNVFRKYQYQNRRALEHQKKEFVKYSKSFSDTLKTYFKDGKAINVFISANRLIHQTNLILQTFKTVA | Function: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Required for normal angiogenesis, vasculogenesis and hematopoiesis durin... |
Q9NZQ7 | MRIFAVFIFMTYWHLLNAFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYNKINQRILVVDPVTSEHELTCQAEGYPKAEVIWTSSDHQVLSGKTTTTNSKREEKLFNVTSTLRINTTTNEIFYCTFRRLDPEENHTAELVIPELPLAHPPNERTHLVILGAILLCLGVALTFIFRLRKGRMMDVKKCGIQDTNSKKQSDTHLEET | Function: Plays a critical role in induction and maintenance of immune tolerance to self . As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response . Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly ... |
Q9BQ51 | MIFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSNVTLECNFDTGSHVNLGAITASLQKVENDTSPHRERATLLEEQLPLGKASFHIPQVQVRDEGQYQCIIIYGVAWDYKYLTLKVKASYRKINTHILKVPETDEVELTCQATGYPLAEVSWPNVSVPANTSHSRTPEGLYQVTSVLRLKPPPGRNFSCVFWNTHVRELTLASIDLQSQMEPRTHPTWLLHIFIPFCIIAFIFIATVIALRKQLCQKLYSSKDTTKRPVTTTKREVNSAI | Function: Involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production (By similarity).
Location Topology: Single-pass type I membrane protein
Se... |
Q9WUL5 | MLLLLPILNLSLQLHPVAALFTVTAPKEVYTVDVGSSVSLECDFDRRECTELEGIRASLQKVENDTSLQSERATLLEEQLPLGKALFHIPSVQVRDSGQYRCLVICGAAWDYKYLTVKVKASYMRIDTRILEVPGTGEVQLTCQARGYPLAEVSWQNVSVPANTSHIRTPEGLYQVTSVLRLKPQPSRNFSCMFWNAHMKELTSAIIDPLSRMEPKVPRTWPLHVFIPACTIALIFLAIVIIQRKRI | Function: Involved in the costimulatory signal essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da):... |
Q9Y5Y4 | MSANATLKPLCPILEQMSRLQSHSNTSIRYIDHAAVLLHGLASLLGLVENGVILFVVGCRMRQTVVTTWVLHLALSDLLASASLPFFTYFLAVGHSWELGTTFCKLHSSIFFLNMFASGFLLSAISLDRCLQVVRPVWAQNHRTVAAAHKVCLVLWALAVLNTVPYFVFRDTISRLDGRIMCYYNVLLLNPGPDRDATCNSRQVALAVSKFLLAFLVPLAIIASSHAAVSLRLQHRGRRRPGRFVRLVAAVVAAFALCWGPYHVFSLLEARAHANPGLRPLVWRGLPFVTSLAFFNSVANPVLYVLTCPDMLRKLRRSLR... | Function: Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-protein. Receptor activation may result in pertussis toxin-sensitive decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is also implicated in mediating PTGDR2 effects. PGD2 induced receptor internalization. CRTH2 internalization can be re... |
Q13258 | MKSPFYRCQNTTSVEKGNSAVMGGVLFSTGLLGNLLALGLLARSGLGWCSRRPLRPLPSVFYMLVCGLTVTDLLGKCLLSPVVLAAYAQNRSLRVLAPALDNSLCQAFAFFMSFFGLSSTLQLLAMALECWLSLGHPFFYRRHITLRLGALVAPVVSAFSLAFCALPFMGFGKFVQYCPGTWCFIQMVHEEGSLSVLGYSVLYSSLMALLVLATVLCNLGAMRNLYAMHRRLQRHPRSCTRDCAEPRADGREASPQPLEELDHLLLLALMTVLFTMCSLPVIYRAYYGAFKDVKEKNRTSEEAEDLRALRFLSVISIVDP... | Function: Receptor for prostaglandin D2 (PGD2). The activity of this receptor is mainly mediated by G(s) proteins that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. A mobilization of calcium is also observed, but without formation of inositol 1,4,5-trisphosphate (By similarity). Involved... |
P70263 | MNESYRCQTSTWVERGSSATMGAVLFGAGLLGNLLALVLLARSGLGSCRPGPLHPPPSVFYVLVCGLTVTDLLGKCLISPMVLAAYAQNQSLKELLPASGNQLCETFAFLMSFFGLASTLQLLAMAVECWLSLGHPFFYQRHVTLRRGVLVAPVVAAFCLAFCALPFAGFGKFVQYCPGTWCFIQMIHKERSFSVIGFSVLYSSLMALLVLATVVCNLGAMYNLYDMHRRQRHYPHRCSRDRAQSGSDYRHGSLHPLEELDHFVLLALMTVLFTMCSLPLIYRAYYGAFKLENKAEGDSEDLQALRFLSVISIVDPWIFI... | Function: Receptor for prostaglandin D2 (PGD2). The activity of this receptor is mainly mediated by G(s) proteins that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP. A mobilization of calcium is also observed, but without formation of inositol 1,4,5-trisphosphate (By similarity). Involved... |
O76074 | MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLY... | Cofactor: Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc.
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. This phosphodiestera... |
P91119 | MDDASVLKYLQENPKLVEDFVVSNEISPETFKRWAVRRTMKYKNVKNGTSGGTGAWTEPDLSMKRRVILETSDNRTRILYEITQCCGQLIGTNSIELIVQNDEGAFSCRKTENGELKLKKVKTSKSADYIQTIVNAGNQTIAEIHFYTQLDSTEKSIVNAVCTWAAATNYYSELYTHKQEGSDGQDIHENIAKQRKLSNFLLDVARSIFHDIVSMDAVIIKVMNFAQKLVDADRASLFLVDSKNAQIYARIFDVGTGDEEHVRVNSEGQKEIRFDMSKGIAGYVASTGEGLNIENAYEDERFNADVDSKTGYTTKTILCM... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: Redundantly with pde-1, plays a role in the AFD thermosensory neurons to regulate microvilli receptive ending morphology, possibly by regulating cG... |
Q8MLZ3 | MMFSKRKSIRFNPEGDYTELPRGGYVVPSKLGGIQFGVPPETIKDSMALKIDVPTIYVFPEELWDRKTGINAAEAEFPAYFNYFILKRKVSFVCTKEQEQRIRIVFQETLLGPPEFNTGIIINSSSSTTDTSKTSPIKKQTSSSSPPLSPQQQQPPPPLVKQPSQQQLEELATMDTCHYHHHHHHQEVNDNDNNNNTTTNNNNIEILEQQQQQQQQQQQQQDEDSTDVDEEFQKEFSSTFPRSEIPNLEKECKYLRTFNSVDELFDFILFDDNGIAKLSDDVEIHFQEDQSLFKVLQFEETGKGNKVQTLVATIPSKILF... | Cofactor: Divalent metal cation. Can use Mn(2+) or, to a lower extent, Mg(2+) or Zn(2+). Half-maximal activation occurs between 10 and 100 uM of Mn(2+) whereas maximal activation occurs with 10 mM of Zn(2+) or Mg(2+).
Function: Phosphodiesterase specific for cGMP, which is activated by cGMP but not by cAMP (Probable).... |
P35913 | MSLSEEQARSFLDQNPDFARQYFGKKLSPENVAAACEDGCPPDCDSLRDLCQVEESTALLELVQDMQESINMERVVFKVLRRLCTLLQADRCSLFMYRQRNGVAELATRLFSVQPDSVLEDCLVPPDSEIVFPLDIGVVGHVAQTKKMVNVEDVAECPHFSSFADELTDYKTKNMLATPIMNGKDVVAVIMAVNKLNGPFFTSEDEDVFLKYLNFATLYLKIYHLSYLHNCETRRGQVLLWSANKVFEELTDIERQFHKAFYTVRAYLNCERYSVGLLDMTKEKEFFDVWSVLMGESQPYSGPRTPDGREIVFYKVIDYV... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP . Necessary for the formation of a functional phosphodiestera... |
P23440 | MSLSEEQVRSFLDGNPTFAHQYFGKKLSPENVAGACEDGWLADCGSLRELCQVEESAALFELVQDMQESVNMERVVFKILRRLCTILHADRCSLFMYRQRNGIAELATRLFSVQPDSLLEDCLVPPDSEIVFPLDIGIVGHVAQTKKMINVQDVAECPHFSSFADELTDYVTKNILSTPIMNGKDVVAVIMAVNKLDGPCFTSEDEDVFTKYLNFATLNLKIYHLSYLHNCETRRGQVLLWSANKVFEELTDIERQFHKAFYTVRAYLNCERYSVGLLDMTKEKEFFDVWPVLMGEAQPYSGPRTPDGREIVFYKVIDYI... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP (By similarity). Necessary for the formation of a functional ... |
P16586 | MGEISQETVEKYLEANPQFAKEYFNRKLQVEVPSGGAQAPASASFPGRTLAEEAALYLELLEVLLEEAGSVELAAHRALQRLAQLLQADRCSMFLCRARNGTPEVASKLLDVTPTSKFEDNLVVPDREAVFPLDVGIVGWVAHTKKTFNVPDVKKNSHFSDFMDKQTGYVTRNLLATPIVMGKEVLAVFMAVNKVDASEFSKQDEEVFSKYLSFVSIILKLHHTNYLYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVRTYLNCERYSIGLLDMTKEKEFYDEWPVKLGEVEPYKGPKTPDGREVIFYKIIDYIL... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellul... |
P51160 | MGEINQVAVEKYLEENPQFAKEYFDRKLRVEVLGEIFKNSQVPVQSSMSFSELTQVEESALCLELLWTVQEEGGTPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEVASRLLDVTPTSKFEDNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVKKNSHFSDFMDKQTGYVTKNLLATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSYMYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEFYDEWPIKLGEVEPYKGPKTPDGREVNFYKI... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellul... |
Q91ZQ1 | MGEISQEAVERYLEKNPCFAKEYFDKKLRVEALGVIFKNSHAGVQTGLSLPEMTQVEESAVCLELLQCMQDEAGSAEQMAHRALQRLAQLLQADCCSMFSCRARNGIPEVASRLLNVTPTSKFEDNLVAPDREVVFPLDIGIVGWVAHVKKALNVSDVKKNSHFSDFMDKQTGYVTRNLLAVPIVAGKEVLAVVMAVNKISAPEFSKQDEEVFSKYLSFVAVALRLQHTSYLYSVESRRSQILMWSANKVFEELTDVERQFHKALYTIRTYLNCDRYSIGLLDMTKEKEFYDEWPIKLGEVEPYKGPKTPDGREIIFYKI... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: As cone-specific cGMP phosphodiesterase, it plays an essential role in light detection and cone phototransduction by rapidly decreasing intracellul... |
Q95142 | MSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKAVSRELNFSSAEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMMPASVLTGNVIIETKFFDDDLLVSTSRVRLFYV | Function: Promotes the release of prenylated target proteins from cellular membranes . Modulates the activity of prenylated or palmitoylated Ras family members by regulating their subcellular location (By similarity). Required for normal ciliary targeting of farnesylated target proteins, such as INPP5E (By similarity).... |
Q9XI01 | MAMRGFTLFSILVLSLCASSIRSEETETKEFVLTLDHTNFTDTINKHDFIVVEFYAPWCGHCKQLAPEYEKAASALSSNVPPVVLAKIDASEETNREFATQYEVQGFPTIKIFRNGGKAVQEYNGPREAEGIVTYLKKQSGPASAEIKSADDASEVVSDKKVVVVGIFPKLSGSEFDSFMAIAEKLRSELDFAHTSDAKLLPRGESSVTGPVVRLFKPFDEQFVDSKDFDGEALEKFVKESSIPLITVFDKDPNNHPYVIKFFESTNTKAMLFINFTGEGAESLKSKYREVATSNKGQGLSFLLGDAENSQGAFQYFGLE... | Function: Protein disulfide isomerase that associates with RD21A protease for trafficking from the ER through the Golgi to lytic and protein storage vacuoles of endothelial cells in developing seeds. Regulates the timing of programmed cell death (PCD) of the endothelial cells by chaperoning and inhibiting cysteine prot... |
Q9SRG3 | MAFKGFACFSILLLLSLFVSSIRSEETKEFVLTLDHSNFTETISKHDFIVVEFYAPWCGHCQKLAPEYEKAASELSSHNPPLALAKIDASEEANKEFANEYKIQGFPTLKILRNGGKSVQDYNGPREAEGIVTYLKKQSGPASVEIKSADSATEVVGEKNVVAVGVFPKLSGDEFDSFMALAEKLRADYDFAHTLDAKFLPRGESVEGPAVRLFKPFDELFVDSKDFNGEALEKFVKESSIPLVTVFDSDPNNHPYVAKFFESPATKAMMFVNFTGATAEALKSKYREVATSNKDQSLAFLVGDAESSQGAFQYFGLEES... | Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 56365
Sequence Length: 508
Subcellular Location: ... |
Q9FF55 | MAFRVLLLFSLTALLIFSAVSPSFAASSSDDVDDEDLSFLEDLKEDDVPGADSLSSSTGFDEFEGGEEEDPDMYNDDDDEEGDFSDLGNPDSDPLPTPEIDEKDVVVIKERNFTDVIENNQYVLVEFYAPWCGHCQSLAPEYAAAATELKEDGVVLAKIDATEENELAQEYRVQGFPTLLFFVDGEHKPYTGGRTKETIVTWVKKKIGPGVYNLTTLDDAEKVLTSGNKVVLGYLNSLVGVEHDQLNAASKAEDDVNFYQTVNPDVAKMFHLDPESKRPALVLVKKEEEKISHFDGEFVKSALVSFVSANKLALVSVFTR... | Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 66357
Sequence Length: 597
Subcellular Location: ... |
Q67IX6 | MRSRSLLLVALATLLLHASASASDDDLDYLIDNADDIPANDPDGWLQEGSPDDDDDDDLFHHGQAQDHPIDETHVFLLSAANFSDFLASHRHVMVEFYAPWCAHCQALAPDYAAAAADLSPLAHQVALAKVDATEDTDLAQKYDVQGFPTILFFIDGVPKDYNGARTKEAIVSWVNKKLAPGVQNITTVDEAEKILTGEDKAILAVLDSLSGAHSDEIAAASRLEDAINFYQTSNPDVAKLFHLDPAAKRPSLVLLKKQEEEKLTFYDGPFKASAIADFVSANKLPLVNTLTQETAPSIFDNPIKKQILLFVVANESSKF... | Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. May play a role in storage protein biogenesis (By similarity).
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequen... |
A3KPF5 | MSLIPKPISKVSTFTFILLILLSFTIIIAYSSPDSNVESNEPGFDSDLDQLLAVDEQLQEDRPEQQSEAETVSKAQRIVLELNGDYTKRVIDGNEFVMVLGYAPWCARSAELMPRFAEAATALKEIGSSVLMAKIDGDRYSKIASELEIKGFPTLLLFVNGTSLTYNGGSSAEDIVIWVQKKTGAPIITLNTVDEAPRFLDKYHTFVLGLFEKFEGSEHNEFVKAAKSDDEIQFIETRDSDVAKLLFPDLKSNNVFIGLVKPEAERYTVYDGSYKMEKILEFLGSNKFPLFTKLTETNTVWVYSSPVKLQVMLFSKADDF... | Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 60158
Sequence Length: 537
Subcellular Location: ... |
Q5WA72 | MRARRVVAAAAVLLLFAVVAVARLDLDDDGDDSEVLDELLAVDEEEERGELGGGGEAAAAEAVRRAQSMVLVLDNDNARRAVEENAEVLLLGYAPWCERSAQLMPRFAEAAAALRAMGSAVAFAKLDGERYPKAASAVGVKGFPTVLLFVNGTEHQFTGLHTKDAIVTWVRKKTGAPASRIQSKDSAEEFLKKDQTFAVGLFKNFEGAEYEEFVKAATSENEVQFVETNDRNVAKILFPGIASEEQFLGLVKSEPEKFEKFNGAFEEKEIIQFVELNKFPLITVFTDLNSGKVYGSPIKLQVFTFAEAYDFEDLESMIQE... | Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds. May play a role in storage protein biogenesis (By similarity).
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequen... |
Q17967 | MSLSVSFIFLLVASIGAVVADSENVLVLTESNFEETINGNEFVLVKFYAPWCVHCKSLAPKYDEAADLLKEEGSDIKLAKVDATENQALASKFEVRGYPTILYFKSGKPTKYTGGRATAQIVDWVKKKSGPTVTTVESVEQLEELKGKTRVVVLGYFKDAKSDAATIYNEVADSVDDAFFAVAGSAEVAAAASLNEDGVALIRTDGDDSETSTIAEAEITNTIALKQWLHAYKLSAVTEFTHESAQEIVGGDLKKFHFLIIRKSDSSFDETIAKFTEVAKKFRAKIVFVLLDVDVEENARILEFLGVDAKNTPANRIVSL... | Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 53436
Sequence Length: 485
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.3.4.1
|
Q86IA3 | MKILLFVTLIALAFVALCSAEGNVVVLSPDNFDTVVDGSKTVFVKFYAPWCGHCKKLAPDFEILADTFAPVSNKVVIAKVDCDQADNKALCSKYDVSGYPTLKIFDKSTTAKDYNGARSVDELLTYINNHAKTNVKVKKAPSNVVDLSPSNFDSVVLDKSKNVLVEFYAPWCGHCKKLMPDYEILGNTYANEKDVVIAKIDCDAADNKAICSKYGVTGFPTLKWFGKQSKDGEKYEQGRDLDTFINYINKQAGVNRVKGGKLAVGAGRVEQLDTIATEFIAAAAEVRKELVKKAQTVVDSLPEELRTEGSYYVKVMKTIA... | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 39905
Sequence Length: 363
Subcellular Location: Endoplasmic ret... |
Q10057 | MKISNLLAAFLAFSGGFFCASAEVPKVNKEGLNELITADKVLMVKFYAPWCGHCKALAPEYESAADELEKDGISLVEVDCTEEGDLCSEYSIRGYPTLNVFKNGKQISQYSGPRKHDALVKYMRKQLLPTVKPISKDTLENFVEKADDLAVVAFFKDQKLNDTYTEVAEVMKDDFVFAASDDKELAKSLGSNFPGIVAFTKDAAQDSDKLVYTGDWDPASIADFIGVSSIPLLDELNQMTFGKYQQSGLPLGIIFYNSTESRDELYDVFQPLAKKYQDTLRFAFLDAVRYGAVAKQMNVESDWPAFVIANLKSMLKYPFP... | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 54880
Sequence Length: 492
Subcellular Location: Endoplasmic ret... |
O22263 | MAKSQIWFGFALLALLLVSAVADDVVVLTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGSLEPQKYEGPRNAEALAEYVNKEGGTNVKLAAVPQNVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFPKDNKAGHDYDGGRDLDDFVSFINEKSGTSRDSKGQLTSKAGIVESLDALVKELVAASEDEKKAVLSRIEEEASTLKGSTTRYGKLYLKLAKSYIEKG... | Function: Protein disulfide isomerase that may be required for proper pollen development, ovule fertilization and embryo development.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 39497
Sequence Length: 361
Subcellular Location: Endoplasmic reticulum
EC: 5.3.4.1
|
Q9MAU6 | MERKMYKSTVFPICCLLFALFDRGNALYGSSSPVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVPGKPPIDYQGARDAKSISQFAIKQIKALLKDRLDGKTSGTKNGGGSSEKKKSEPSASVELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSDKSSPVPYEGARSASAIESFALEQLESNAGPAEVTELTGPDVMEDKCGSAAICFVSFLPDILDSKAEGRNKY... | Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 48403
Sequence Length: 447
Subcellular Location: ... |
O48773 | MYKSPLTLLTLLTICFGFFDLSSALYGSSSPVVQLTASNFKSKVLNSNGVVLVEFFAPWCGHCKALTPTWEKVANILKGVATVAAIDADAHQSAAQDYGIKGFPTIKVFVPGKAPIDYQGARDAKSIANFAYKQIKGLLSDRLEGKSKPTGGGSKEKKSEPSASVELNASNFDDLVIESNELWIVEFFAPWCGHCKKLAPEWKRAAKNLQGKVKLGHVNCDVEQSIMSRFKVQGFPTILVFGPDKSSPYPYEGARSASAIESFASELVESSAGPVEVTELTGPDVMEKKCGSAAICFISFLPDILDSKAEGRNKYLEMLL... | Function: Acts as a protein-folding catalyst that interacts with nascent polypeptides to catalyze the formation, isomerization, and reduction or oxidation of disulfide bonds.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 47755
Sequence Length: 440
Subcellular Location: ... |
Q9XF67 | MLAMEKEFDSKLVLQGNSSNGANVSRSKSFSFKAPQENFTSHDFEFGKIYGVGSYSKVVRAKKKETGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYMALESCEGGELFDQITRKGRLSEDEARFYTAEVVDALEYIHSMGLIHRDIKPENLLLTSDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTEPSRRPGAGSEGYVALKRHPFFNGVDWKNLR... | Function: May couple lipid signals to the activation-loop phosphorylation of several protein kinases of the so-called AGC kinase family. Interacts via its pleckstrin homology domain with phosphatidic acid, PtdIns3P and PtdIns(3,4)P2 and to a lesser extent with PtdIns(4,5)P2 and PtdIns4P. May play a general role in sign... |
Q9Y1J3 | MEDLTPTNTSLDTTTTNNDTTSDREAAPTTLNLTPTASESENSLSPVTAEDLIAKSIKEGCPKRTSNDFMFLQSMGEGAYSQVFRCREVATDAMFAVKVLQKSYLNRHQKMDAIIREKNILTYLSQECGGHPFVTQLYTHFHDQARIYFVIGLVENGDLGESLCHFGSFDMLTSKFFASEILTGLQFLHDNKIVHRDMKPDNVLIQKDGHILITDFGSAQAFGGLQLSQEGFTDANQASSRSSDSGSPPPTRFYSDEEVPEENTARRTTFVGTALYVSPEMLADGDVGPQTDIWGLGCILFQCLAGQPPFRAVNQYHLLK... | Function: Involved in the daf-2/insulin receptor-like transduction pathway, which controls longevity and prevents developmental arrest at the dauer stage . Phosphorylates and activates sgk-1, akt-1 and akt-2 .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 719... |
Q9W0V1 | MKCKSWSNKINNYVVRKIKSIKINGTQQQLQLPGSGASGIAAAAVITVASDCGENCSSNGTEHQQHFNIATTTATSATEATMPAMAKEKASATVSLGESNFRDINLKDLAVVVEAASRLHHQQNVCGCGAVSSTENNNNSRYGSSKYLTNGHTSPLAAAVASNSSSVATTPHCRMLHNCSLQQYQNDIRQQTEILDMLRQQHQQGYQSQQQQQQPQQQQEQQQQQEQSQQQQQLQNPAPRRSPNDFIFGRYIGEGSYSIVYLAVDIHSRREYAIKVCEKRLILRERKQDYIKREREVMHQMTNVPGFVNLSCTFQDQRSL... | Function: Serine/threonine kinase required for embryonic development. Inhibits apoptosis. Acts in the insulin receptor transduction pathway which regulates cell growth and organ size, by phosphorylating and activating Akt1 and S6k. May be involved in axonal pathfinding and synaptogenesis, and in spermatogenesis.
Cataly... |
O15530 | MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLD... | Function: Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3)... |
Q9Z2A0 | MARTTSQLYDAVPIQSSVVLCSCPSPSMVRSQTEPGSSPGIPSGVSRQGSTMDGTTAEARPSTNPLQQHPAQLPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYHFPEKFFPKARDLVEKLL... | Function: Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3)... |
Q6A1A2 | MVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMYIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTW... | Function: Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling processes and in development (By similarity).
PTM: Phosphorylated on tyrosine and serine/threonine.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-... |
Q54TW2 | MENIVITNTSGGGGGGVPSSSTDPPNNTTTTTATASAIDLNMSLSPFLSSPSLSSPSIQSAKKKTIEDFIIGKVLGEGSYGAVVLGTEKETQQQYAIKILEKKQIIKENKIKYVQIEKEIFCKSNHPNIVKLFFTFRSEQCLYYVLELCSQGDLLHQIKKVGSFDYRSCQYYVAEIISGLEHLHSLGIVHRDLKPENILMSSDLHVKITDFGTGKILPPPQSSQQQQQQQQQQQQLPTNSSGNLSSLLNNVNNLSVSTDLTQQQQNRTSSVDSASTTDSMISPNLQPTTTTTNNNNNNNNNNNNNNNNTAAGSNTNTNTN... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 75562
Sequence Length: 686
Domain: The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that... |
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