ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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P23371 | MNRNPDQNTLPNITLKIIETYLGRVPSVNEYHMLKLQARNIQKITVFNKDIFVSLVKKNKKRFFSDVNTSASEIKDRILSYFSKQTQTYNIGKLFTIIELQSVLVTTYTDILGVLTIKAPNVISSKISYNVTSMEELARDMLNSMNVAVIDKAKVMGRHNVSSLVKNVNKLMEEYLRRHNKSCICYGSYSLYLINPNIRYGDIDILQTNSRTFLIDLAFLIKFITGNNIILSKIPYLRNYMVIKDENDNHIIDSFNIRQDTMNVVPKIFIDNIYIVDPTFQLLNMIKMFSQIDRLEDLSKDPEKFNARMATMLEYVRYTHGIVFDGKRNNMPMKCIIDENNRIVTVTTKDYFSFKKCLVYLDENVLSSDILDLNADTSCDFESVTNSVYLIHDNIMYTYFSNTILLSDKGKVHEISARGLCAHILLYQMLTSGEYKQCLSDLLNSMMNRDKIPIYSHTERDKKPGRHGFINIEKDIIVF | 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.
Subcellular Location: Secreted
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P13720 | MKKWFPAFLFLSLSGGNDALAGWHNVMFYAFNDYLTTNAGNVKVIDQPQLYIPWNTGSATATYYSCSGPEFASGVYFQEYLAWMVVPKHVYTNEGFNIFLDVQSKYGWSMENENDKDFYFFVNGYEWDTWTNNGARICFYPGNMKQLNNKFNDLVFRVLLPVDLPKGHYNFPVRYIRGIQHHYYDLWQDHYKMPYDQIKQLPATNTLMLSFDNVGGCQPSTQVLNIDHGSIVIDRANGNIASQTLSIYCDVPVSVKISLLRNTPPIYNNNKFSVGLGNGWDSIISLDGVEQSEEILRWYTAGSKTVKIESRLYGEEGKRKPGELSGSMTMVLSFP | 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-phenylalanine + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30850
Sequence Length: 292
Pathway: Antibiotic biosynthesis.
EC: 2.1.1.-
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P51005 | MLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRAVMVEEFKQGLAITDEILLVKAEWSKLFDAPNFFQKYKHYILLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPSPSENSEKEEFRTMWVIGLVFKKMENSENLSVDLTYDIQSFTDTVYRQAINSKMFETEIKIAAMHVKRKQLHQLLPSHVLPKKKKHSVEGVKLVSLNDSSIDLSVDSDNSMSVPSPTNATRTSPLNSTGLSQGNSPATPVSLSVTNTQATDVMVPQNNSTENSGGSLNESIPETATHPAFSSTPRPLVTRVVSSMPLVNQVQKPVTNTVTKMPSPVAGVKRTSSPTNEESPKKTKTEEDENDSSNSTEVDEQNKLEPEELKEVHSEEKSSSPVPGALPSSQRSSSTDLSDISVLPATPIPVIKNSIKLRLNR | 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
EC: 2.7.7.19
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P51006 | MPFPLASQGSQQSQKTYGITSPISLATPKDTDCTLTQKLIETLKPYGVFEEEDELQHRILSLGKLNNLVKEWIREISELKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDLFSSFYEKLKQQEEVKDLRSVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDSFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRAVMVEEFKQGLAITDEILLLKAEWSKLFDAPNFFQKYKYVFYNLLAMFAWGEIINKNKKRCYTLKKKKK | 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 (Da): 46020
Sequence Length: 400
Subcellular Location: Nucleus
EC: 2.7.7.19
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P25500 | MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCLLTQKLVETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKENPDKEEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFEVDMKIAAMHVKRKQLHQLLPSHVLQKKKKHSTEGVKLTPLNDSSLDLSMDSDNSMSVPSPTSAMKTSPLNSSGSSQGRNSPAPAVTAASVTNIQATEVSLPQINSSESSGGTSSESIPQTATQPAISSPPKPTVSRVVSSTRLVNPPPRPSGNAAAKIPNPIVGVKRTSSPHKEESPKKTKTEEDETSEDANCLALSGHDKTETKEQLDTETSTTQSETIQTATSLLASQKTSSTDLSDIPALPANPIPVIKNSIKLRLNR | 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 (CPSF) at its C-terminus.
PTM: Polysumoylated. Varying sumoylation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 82441
Sequence Length: 739
Subcellular Location: Nucleus
EC: 2.7.7.19
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P51003 | MPFPVTTQGSQQTQPPQKHYGITSPISLAAPKETDCVLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKENPDKEEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFEVDMKIAAMHVKRKQLHQLLPNHVLQKKKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTSATKTSPLNSSGSSQGRNSPAPAVTAASVTNIQATEVSVPQVNSSESSGGTSSESIPQTATQPAISPPPKPTVSRVVSSTRLVNPPPRSSGNAATSGNAATKIPTPIVGVKRTSSPHKEESPKKTKTEEDETSEDANCLALSGHDKTEAKEQLDTETSTTQSETIQTAASLLASQKTSSTDLSDIPALPANPIPVIKNSIKLRLNR | 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 (CPSF) at its C-terminus.
PTM: Polysumoylated. Varying sumoylation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 82843
Sequence Length: 745
Subcellular Location: Cytoplasm
EC: 2.7.7.19
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Q61183 | MPFPVTTQGSQQTQPPQRHYGITSPISLAAPKETDCLLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFEAPNFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKESPDREEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFELDMKIAAMHVKRKQLHQLLPSHVLQKRKKHSTEGVKLTALNDSSLDLSMDSDNSMSVPSPTSAMKTSPLNSSGSSQGRNSPAPAVTAASVTSIQASEVSVPQANSSESPGGPSSESIPQTATQPAISPPPKPTVSRVVSSTRLVNPSPRPSGNTATKVPNPIVGVKRTSSPNKEESPKKTKTEEDETSEDANCLALSGHDKTETKEQVDLETSAVQSETVPASASLLASQKTSSTDLSDIPALPANPIPVIKNSIKLRLNR | 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 (CPSF) at its C-terminus.
PTM: Polysumoylated. Varying sumoylation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity.
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 82309
Sequence Length: 739
Subcellular Location: Nucleus
EC: 2.7.7.19
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Q9GN62 | MDAPSTSSGAQSKLLMPGDDEADEDHQNRGDPNLQQKQKIQLNVDPDYDDDEDDDCFIDGCEASAPITRELVDGAIERRSKDRNVKMSIGVYDEYDDDDDDEEETEEDQRRRFVEGIRNIRHKQQESFDLEEHPIPVESEAMRQFINQQVNNAMMFNQDNSEFQHIEFEPIVKQKGPKIIEGYMWGGQIGTGSYGKVKECIDMYTLTRRAVKIMKYDKLRKITNGWENIRSEMSILRRMNHRNVIKLIEIFNIPAKGKVYMVFEYCIGSVQQLLDMEPARRLTIGESHAIFIELCQGLNYLHSKRVSHKDIKPGNLLVSIDFTVKICDFGVAEQINLFQRDGRCTKVNGTPKFQPPECIYGNHDFFDGYKADMWSAGVTLYNLVSGKYPFEKPVLLKLYECIGTEPLQMPTNVQLTKDLQDLLTKLLEKDFNERPTCLETMIHPWFLSTFPEDQGLGRIMERMRTGDRPLTMLSSMTALYDGITPEDELIIEDNLGIIQQILPINLTSEAVLERGSFPGFKFLEAKPGDGPDGVEGSEDSAAPLGPQRRPSSRSMPTCAPPGPAAGNAQNSTAENGAETDGVASASDPPPTAAPGAPPRRRKRNFFSCIFRSRTDSA | 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 mex-5 and mex-6 to the anterior cytoplasm of the zygote and maintains these phosphorylations until fertilization . May phosphorylate par-1. Required for strd-1 localization to the cell cortex of early embryos and may be required for strd-1 protein stabilization. May regulate the integrity of the early embryonic cortex in a strd-1-dependent manner . Phosphorylates and regulates aak-2 in response to oxidative stress and during dauer development . May also play a role in motility, behavioral response, regulation of lifespan and dauer formation through this pathway . Required to establish germline stem cell (GSC) quiescence during dauer development . Acts downstream of unc-40 in dendrite outgrowth . May play a role in cell shedding during embryogenesis, probably by phosphorylating pig-1 .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 69648
Sequence Length: 617
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q96RI0 | MWGRLLLWPLVLGFSLSGGTQTPSVYDESGSTGGGDDSTPSILPAPRGYPGQVCANDSDTLELPDSSRALLLGWVPTRLVPALYGLVLVVGLPANGLALWVLATQAPRLPSTMLLMNLAAADLLLALALPPRIAYHLRGQRWPFGEAACRLATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGRRLALGLCMAAWLMAAALALPLTLQRQTFRLARSDRVLCHDALPLDAQASHWQPAFTCLALLGCFLPLLAMLLCYGATLHTLAASGRRYGHALRLTAVVLASAVAFFVPSNLLLLLHYSDPSPSAWGNLYGAYVPSLALSTLNSCVDPFIYYYVSAEFRDKVRAGLFQRSPGDTVASKASAEGGSRGMGTHSSLLQ | 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): 41133
Sequence Length: 385
Subcellular Location: Cell membrane
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O88634 | MCWPLLYPLVLGLSISLAEGIQTPSIYDDVESTRGSHEGPLGPTVELKEPKSSDKPNPRGYPGKFCANDSDTLELPASSQALLLGWVPTRLVPALYGLVVAVGLPANGLALWVLATRVPRLPSTILLMNLAVADLLLALVLPPRLAYHLRGQRWPFGEAACRVATAALYGHMYGSVLLLAAVSLDRYLALVHPLRARALRGQRLTTGLCLVAWLSAATLALPLTLHRQTFRLAGSDRMLCHDALPLTEQTSHWRPAFICLAVLGCFVPLLAMGLCYGATLRALAANGQRYSHALRLTALVLFSAVASFTPSNVLLVLHYSNPSPEAWGNLYGAYVPSLALSTLNSCVDPFIYYYVSHEFREKVRAMLCRQPEASSSSQASREAGSRGTAICSSTLL | 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): 42786
Sequence Length: 396
Subcellular Location: Cell membrane
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Q9NPB6 | MARPQRTPARSPDSIVEVKSKFDAEFRRFALPRASVSGFQEFSRLLRAVHQIPGLDVLLGYTDAHGDLLPLTNDDSLHRALASGPPPLRLLVQKRAEADSSGLAFASNSLQRRKKGLLLRPVAPLRTRPPLLISLPQDFRQVSSVIDVDLLPETHRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSDEILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQRNNVVRGASGRLTGPPSAGPGPAEPDSDDDSSDLVIENRQPPSSNGLSQGPPCWDLHPGCRHPGTRSSLPSLDDQEQASSGWGSRIRGDGSGFSL | 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-bound Rho small GTPases to atypical protein kinase C proteins . Regulates centrosome organization and function. Essential for the centrosomal recruitment of key proteins that control centrosomal microtubule organization .
PTM: Phosphorylated by the TGF-beta receptor.
Sequence Mass (Da): 37388
Sequence Length: 346
Domain: The pseudo-CRIB domain together with the PDZ domain is required for the interaction with Rho small GTPases.
Subcellular Location: Cytoplasm
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Q9Z101 | MARPQRTPARSPDSIVEVKSKFDAEFRRFALPRTSVRGFQEFSRLLCVVHQIPGLDVLLGYTDAHGDLLPLTNDDSLHRALASGPPPLRLLVQKRAEGDSSGLAFASNSLQRRKKGLLLRPVAPLRTRPPLLISLPQDFRQVSSVIDVDLLPETHRRVRLHKHGSDRPLGFYIRDGMSVRVAPQGLERVPGIFISRLVRGGLAESTGLLAVSDEILEVNGIEVAGKTLDQVTDMMVANSHNLIVTVKPANQRNNVVRGASGRLTGPSSVGPGPTDPDSDDDSSDLVIENRHPPCSNGLSQGPLCWDLQPGCLLPGAGSSLPSLDSREQANSGWGNGMRGDVSGFSL | 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-bound Rho small GTPases to atypical protein kinase C proteins . Regulates centrosome organization and function. Essential for the centrosomal recruitment of key proteins that control centrosomal microtubule organization (By similarity).
PTM: Phosphorylated by the TGF-beta receptor.
Sequence Mass (Da): 37333
Sequence Length: 346
Domain: The PB1 domain mediates interactions with MAP2K5.
Subcellular Location: Cytoplasm
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Q9BYG5 | MNRSHRHGAGSGCLGTMEVKSKFGAEFRRFSLERSKPGKFEEFYGLLQHVHKIPNVDVLVGYADIHGDLLPINNDDNYHKAVSTANPLLRIFIQKKEEADYSAFGTDTLIKKKNVLTNVLRPDNHRKKPHIVISMPQDFRPVSSIIDVDILPETHRRVRLYKYGTEKPLGFYIRDGSSVRVTPHGLEKVPGIFISRLVPGGLAQSTGLLAVNDEVLEVNGIEVSGKSLDQVTDMMIANSRNLIITVRPANQRNNVVRNSRTSGSSGQSTDNSLLGYPQQIEPSFEPEDEDSEEDDIIIEDNGVPQQIPKAVPNTESLESLTQIELSFESGQNGFIPSNEVSLAAIASSSNTEFETHAPDQKLLEEDGTIITL | 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 Rho small GTPases to atypical protein kinase C proteins.
Sequence Mass (Da): 41182
Sequence Length: 372
Domain: The pseudo-CRIB domain together with the PDZ domain is required for the interaction with Rho small GTPases.
Subcellular Location: Cytoplasm
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Q9JK83 | MNRGHRHGASSGCLGTMEVKSKFGAEFRRFSLERSKPGKFEEFYGLLQHVHKIPNVDVLVGYADIHGDLLPINNDDNYHKAVSTANPLLRIFIQKKEEADYSAFGTDTLIRKKNMLSNVLRPDNHRKKPHIVISMPQDFRPVSSIIDVDILPETHRRVRLYKYGTEKPLGFYIRDGSSVRVTPHGLEKVPGIFISRLVPGGLAQSTGLLAVNDEVLEVNGIEVSGKSLDQVTDMMIANSRNLIITVRPANQRNNVVRNSRTSGSSSQSTDNSLLGFPQQVEASFEPEDQDSDEDDIIIEDSGEPQQIPKATPAQSLESLTQIELSFESGQNGFSPPQDTSLVPVPGSLDTELESRAPDQKLLEEDGTIITL | 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 Rho small GTPases to atypical protein kinase C proteins.
Sequence Mass (Da): 41067
Sequence Length: 371
Domain: The pseudo-CRIB domain together with the PDZ domain is required for the interaction with Rho small GTPases.
Subcellular Location: Cytoplasm
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Q9BYG4 | MNRSFHKSQTLRFYDCSAVEVKSKFGAEFRRFSLDRHKPGKFEDFYKLVVHTHHISNSDVTIGYADVHGDLLPINNDDNFCKAVSSANPLLRVFIQKREEAERGSLGAGSLCRRRRALGALRDEGPRRRAHLDIGLPRDFRPVSSIIDVDLVPETHRRVRLHRHGCEKPLGFYIRDGASVRVTPHGLEKVPGIFISRMVPGGLAESTGLLAVNDEVLEVNGIEVAGKTLDQVTDMMIANSHNLIVTVKPANQRNNVVRGGRALGSSGPPSDGTAGFVGPPAPRVLQNFHPDEAESDEDNDVVIEGTLEPARPPQTPGAPAGSLSRVNGAGLAQRLQRDLALDGGLQRLLSSLRADPRHSLALPPGGVEEHGPAVTL | 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: 376
Domain: The pseudo-CRIB domain together with the PDZ domain is required for the interaction with Rho small GTPases.
Subcellular Location: Cytoplasm
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Q9JK84 | MNRSFHKSQTLRFYDCSAVEVKSKFGAEFRRFSLDRHKPGKFEDFYQLVVHTHHISNTEVTIGYADVHGDLLPINNDDNFCKAVSSANPLLRVFIQKREEADHYSFGAGTLSRKKKVLVTLRDDGLRRRPHLNISMPHDFRPVSSIIDVDILPETHRRVRLYRHGYEKPLGFYIRDGTSVRVTPHGLEKVPGIFISRMVPGGLAESTGLLAVNDEVLEVNGIEVAGKTLDQVTDMMIANSHNLIVTVKPANQRNNVVRSSRTSGSSVHSTDSTTSHHSLPGAHVLQNSEDVESDEEADIVIEGALEPQHIPKTQAVPPGSLSRANGTSLAHGLHRRDMSLHSSGRESNGSIHRFLSSLKPDPRHSLVLPQGGVEEHGPAITL | 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: 382
Domain: The pseudo-CRIB domain together with the PDZ domain is required for the interaction with Rho small GTPases.
Subcellular Location: Cytoplasm
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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 . Acts together with par-3 and pkc-3 in maintaining epithelial cell polarity in the distal spermatheca . Plays a role in endosome and Golgi body positioning .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34219
Sequence Length: 309
Subcellular Location: Cytoplasm
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Q8VDG3 | MEIIRSNFKINLHKVYQAIEEADFFAIDGEFSGISDGPSVTALTSGFDTPEERYQKLKKHSMDFLLFQFGLCAFKYDHTDSKHVTKSFNFYVFPKPFSRSSPDVKFVCQSSSIDFLASQGFDFNKVFCSGIPYLNQEEERQLREQFDEKRSQANGAGALAKCPVTIPEDQKKFIDQVIEKIEDFLQSEEKRSLELDPCTGFQRKLIYQTLSWKYPKGIHVETLETDKKERHIVISKVDEEERKRREQEKYTKEQEELNDAVGFSRVIHAIANSGKLVVGHNMLLDVMHTIHQFYCPLPADLNEFKEMAICVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFDPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSLLSPPKMCVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVQIAVNTSKYAESYRIQTYAEYVGKKQEGKQVKRKWTEDSWKEVDRKRPHMQGPCYHSNSFTAAGVLGKRTLSPDPREAALEDRESEEVSDSELEQTDSCTDPLPEGRKKSKKLKRMKKELSLAGSVSDSPAVLFEVPDTW | 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 certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (By similarity). Also able to recognize poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to leading to microRNAs degradation or snoRNA increased stability (By similarity).
PTM: Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 71559
Sequence Length: 624
Subcellular Location: Nucleus
EC: 3.1.13.4
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Q90ZA1 | MEITRSNFKDTLPKVYKAIEEADFLAIDGEFSGISDGPSVSTLTNGFDTPEERYTKLKKHSMEFLLFQFGLCTFNYDNTEAKYLMKSFNFYIFPKPFNRNSPDKKFVCQSSSIDFLANQGFDFNKVFRNGIPYLNQEEERVLRDQYEDRRSQSNGASTMSYISPNSSKTPVSIPDEQKGFIDKVVERVEDFLKNEQKSMNVEPCTGYQRKLIYQTLNWKYPRGIHVETVESEKKERYIVISKVDEEERKRMEQQKQAKEREELDDAVGFSRIIQAISSSGKLVVGHNMLLDVMHTIHQFFCQLPDELNEFKEVTNCVFPRVLDTKLMASTNPFKEIIYNTSLAELEKRLKEAPFKPPKVDSAEGFQSYNTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKDYVSCRSKIVRPFFNKLFLMRIMDIPYLNLEGPDLQPKRDNVLHVTFPKEWKTSDLYQLFSAFGNIQVSWIDDTSAFVSLSQPEQVQIAVNTSKYAESYRIQTYAEYIEKKNDESQTKRKWAEDGWKDLERKRLKTQYNSYIPQNPVFYGNCFAPSFAVKRSMSPIQEEAASDDTEEVHTHENDPSNPGATEQGKKPKNHKRQKIDSAPPETSDGGSSVLFEVPDTW | 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 not require an adenosine residue at the 3' end, however, the addition of 25 non-adenylate residues at the 3' terminus, or a 3' terminal phosphate is inhibitory. Involved in dormant mRNAs regulation during oocyte maturation by counteracting polyadenylation mediated by papd4/gld2nt in immature eggs. During maturation it is excluded from the ribonucleoprotein complex, allowing poly(A) elongation by papd4/gld2nt and activation of mRNAs.
PTM: A 62 kDa form, which is produced by proteolytic cleavage, also exists.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 72846
Sequence Length: 631
Subcellular Location: Cytoplasm
EC: 3.1.13.4
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Q9ZP54 | MASPHKPWRAEYAKSSRSSCKTCKSVINKENFRLGKLVQSTHFDGIMPMWNHASCILKKTKQIKSVDDVEGIESLRWEDQQKIRKYVESGAGSNTSTSTGTSTSSTANNAKLEYGIEVSQTSRAGCRKCSEKILKGEVRIFSKPEGPGNKGLMWHHAKCFLEMSSSTELESLSGWRSIPDSDQEALLPLVKKALPAAKTETAEARQTNSRAGTKRKNDSVDNEKSKLAKSSFDMSTSGALQPCSKEKEMEAQTKELWDLKDDLKKYVTSAELREMLEVNEQSTRGSELDLRDKCADGMMFGPLALCPMCSGHLSFSGGLYRCHGYISEWSKCSHSTLDPDRIKGKWKIPDETENQFLLKWNKSQKSVKPKRILRPVLSGETSQGQGSKDATDSSRSERLADLKVSIAGNTKERQPWKKRIEEAGAEFHANVKKGTSCLVVCGLTDIRDAEMRKARRMKVAIVREDYLVDCFKKQRKLPFDKYKIEDTSESLVTVKVKGRSAVHEASGLQEHCHILEDGNSIYNTTLSMSDLSTGINSYYILQIIQEDKGSDCYVFRKWGRVGNEKIGGNKVEEMSKSDAVHEFKRLFLEKTGNTWESWEQKTNFQKQPGKFLPLDIDYGVNKQVAKKEPFQTSSNLAPSLIELMKMLFDVETYRSAMMEFEINMSEMPLGKLSKHNIQKGFEALTEIQRLLTESDPQPTMKESLLVDASNRFFTMIPSIHPHIIRDEDDFKSKVKMLEALQDIEIASRIVGFDVDSTESLDDKYKKLHCDISPLPHDSEDYRLIEKYLNTTHAPTHTEWSLELEEVFALEREGEFDKYAPHREKLGNKMLLWHGSRLTNFVGILNQGLRIAPPEAPATGYMFGKGIYFADLVSKSAQYCYTCKKNPVGLMLLSEVALGEIHELTKAKYMDKPPRGKHSTKGLGKKVPQDSEFAKWRGDVTVPCGKPVSSKVKASELMYNEYIVYDTAQVKLQFLLKVRFKHKR | 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 the reparation of DNA strand breaks (By similarity).
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 111233
Sequence Length: 983
Subcellular Location: Nucleus
EC: 2.4.2.30
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Q9N4H4 | MIHSNEPLPYAIEYAKSGRSNCKTCKKNIALDQLRMSMNRPSTFFDGNMDSWFHYNCFWIKMIRGRDDINISSIRGVDWLRWEDQEKLRQEIQHFKTASPPTLTPLCSTTTVILSTIKTEKSLSNRGKCGKCGQNFERGEIKAHNKGKANHFKCFLQEFDKISGTVEDIPGWADYEENFKIKAVGEYVEALAAKRRSTEPATPASASPTPPEAETPVLSAEGSPESSNKRPASSEIIEIDGEGNPDENDFAKKRRMKKEARLMEVQKKRMKKQSDLLWEYRQIFERMPYTDKISILRENEQDIPEGHDPTAQVIERLVDNALFGCPIICQTCSNGKIVYNSSCRTYVCTGYATEYSKCTYESKNPIRTPFEVSHRLTEKHKLQDIVFNQMSERLYIGEEDGESVVKIDKRKSKGGTRGEQFIYAAEAFDSTNNVPIKVGDLTSTNTHIIKKGTVVDAKFALADRCHVFKNEIDGSLYQATLSFTDLTQNKNSYYKIQLLKDDQRENYYVFRSWGRVGTEVGGNKHESYSNSNEAILKFQDVFHEKTKNDWIYRKHFRKMPGMFSYVETDYSEFAQITDTEITPGSKTLLPKSVKEVVMSIFDVENMKSALKSFEMDVNKMPLGRLSHNQINLAFEVLNDISDLLVKLPIDASRILDFSNKFYTIIPHNFGMRVPEPIDSFHKIKEKNNMLNALLDIKFAYDQISGGDVPASTSLGIDPVDINYQKLKCIMEPLQQGCDDWNMIHQYLKNTHGATHDLKVELIDILKLNRDNESSKFKRHIGNRRLLWHGSGKMNFAGILGQGLRIAPPEAPVSGYMFGKGVYFADMFSKSFFYCRANAKEEAYLLLCDVALGNVQQLMASKNVSRQTLPAGFQSVQGLGRQCPREIGSYNHPDGYTIPLGLTYMQLQGKQDVDYHLLYNEFIVYDVDQIQLKYLVRVKMHHARHL | 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 protection of the genome against mutations .
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 108007
Sequence Length: 945
Subcellular Location: Nucleus
EC: 2.4.2.30
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Q5RHR0 | MADSQDDKLYKAEYAKSGRASCKKCKDNIAKDSLRMAIMVQSPMFDGKVPHWHHFSCFWLRAAVQSPSDISGFTDLRWDDQEKVKTAIESGGATGGKGGQKGAAKGEKTLNDFAVEYAKSNRSTCKGCDQKIEKDQIRVSKKTVDPEKPQLGLIDRWYHTGCFVSRREELIFKPEYSAAQLKGFAVLRDEDKEELKKRLPAVKSEGKRKADEVDGGVSKKQKKEDEKLEQNLKDQSQLIWGIKDKLKKFCSINDMKELLIANSQEVPSGESNIVDRLSDCMAFGSLKPCETCKGQLVFKSDAYYCTGDISAWTKCVFKTQTPDRKDWVTPKEFSEIPFLKKFKFKRQDRVFPKDAPPAAATPSSGSTTSAATSVSSASKNLTEAPADKPLTGMKLLAVGKLSKNKDDLKKFVEDLGGKITGTASKAALCISSKKEIEKMSKKMEEVRDAGVRVVADDFLTDIKESGKALQELISLHAISPWGAEVKVEAPAAAAATKSTGAHSSKSTGKVKEEEGGSKSKKMKLTVKGGAAVDPDSGLENCAHVLEQNGKIYSATLGLVDIVRGTNSYYKLQLLEDDVQKRYWVFRSWGRVGTTIGGNKLDKFYDKNSAMDNFCGVYEEKTGNAWASSNFTKYPNKFYPLEIDYGQDEEAVKKLTQSAGAKSQLEKPVQDLIRMIFDVESMKKAMVEFEIDLQKMPLGKLSKRQIQSAYSLLSEVQQAVADSSSESLILDLSNRFYTLIPHDFGMKKPPLLSNVDYIQQKVQMLDNLLDIEVAYSLLRGGVENNEKDPIDINYEKLKTKIEVVDKSSHEAQLILQYVKNTHAATHNTYTLDVEEIFKIEREGEYQRYRPFKELPNRQLLWHGSRTTNYAGILSQGLRIAPPEAPVTGYMFGKGVYFADMVSKSANYCHTSQADPVGLILLGEVALGNMHELKKASHITKLPKGKHSVKGLGRSAPDPRATVSLNGVDIPLGKGMNTNIDDTSLLYNEYIVYDVSQVNLKYLLKIRFNYQTSLW | 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 further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Specificity for the different amino acids is conferred by interacting factors, such as hpf1 and nmnat1 (By similarity). Following interaction with hpf1, catalyzes serine ADP-ribosylation of target proteins; hpf1 confers serine specificity by completing the parp1 active site. Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with hpf1 (By similarity). Following interaction with nmnat1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; nmnat1 confers glutamate and aspartate specificity (By similarity). Parp1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits hpf1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair. Mediates the poly-ADP-ribosylation of a number of proteins. In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (By similarity). Parp1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair . In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (By similarity). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II. Acts both as a positive and negative regulator of transcription elongation, depending on the context (By similarity). Poly-ADP-ribose chains generated by parp1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos. Also acts as a negative regulator of the cGAS-STING pathway by mediating poly-ADP-ribosylation and inactivation of cgas. Acts as a negative regulator of adipogenesis by catalyzing poly ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) (By similarity).
PTM: Poly-ADP-ribosylated on serine, glutamate and aspartate residues by autocatalysis. Auto-ADP-ribosylation on serine takes place following interaction with HPF1. Auto poly-ADP-ribosylation on serine residues promotes its dissociation from chromatin.
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 112776
Sequence Length: 1013
Domain: The two PARP-type zinc-fingers (also named Zn1 and Zn2) specifically recognize DNA strand breaks: PARP-type zinc-finger 1 binds PARP-type zinc-finger 2 from a separate parp1 molecule to form a dimeric module that specifically recognizes DNA strand breaks.
Subcellular Location: Chromosome
EC: 2.4.2.30
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P09874 | MAESSDKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVTGKGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQLGMIDRWYHPGCFVKNREELGFRPEYSASQLKGFSLLATEDKEALKKQLPGVKSEGKRKGDEVDGVDEVAKKKSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYLKKLKVKKQDRIFPPETSASVAATPPPSTASAPAAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELFLAHILSPWGAEVKAEPVEVVAPRGKSGAALSKKSKGQVKEEGINKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSDSQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISLDGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW | 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 further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units . Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage . Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 . Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site . Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 . Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks . HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains . In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation . Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR and NFAT5 . In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively . Required for PARP9 and DTX3L recruitment to DNA damage sites . PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites . PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity . Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II . Acts both as a positive and negative regulator of transcription elongation, depending on the context . Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing . Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 . Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression . Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity). Also acts as a negative regulator of the cGAS-STING pathway . Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS . Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 . Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming .
PTM: Poly-ADP-ribosylated on serine, glutamate and aspartate residues by autocatalysis . Auto-ADP-ribosylation on serine takes place following interaction with HPF1 . Auto poly-ADP-ribosylation on serine residues promotes its dissociation from chromatin . Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites . Mono-ADP-ribosylated at Lys-521 by SIRT6 in response to oxidative stress, promoting recruitment to double-strand breaks (DSBs) sites .
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 113084
Sequence Length: 1014
Domain: The two PARP-type zinc-fingers (also named Zn1 and Zn2) specifically recognize DNA strand breaks: PARP-type zinc-finger 1 binds PARP-type zinc-finger 2 from a separate PARP1 molecule to form a dimeric module that specifically recognizes DNA strand breaks.
Subcellular Location: Chromosome
EC: 2.4.2.30
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Q9ZSV1 | MAAPPKAWKAEYAKSGRASCKSCRSPIAKDQLRLGKMVQASQFDGFMPMWNHARCIFSKKNQIKSVDDVEGIDALRWDDQEKIRNYVGSASAGTSSTAAPPEKCTIEIAPSARTSCRRCSEKITKGSVRLSAKLESEGPKGIPWYHANCFFEVSPSATVEKFSGWDTLSDEDKRTMLDLVKKDVGNNEQNKGSKRKKSENDIDSYKSARLDESTSEGTVRNKGQLVDPRGSNTSSADIQLKLKEQSDTLWKLKDGLKTHVSAAELRDMLEANGQDTSGPERHLLDRCADGMLFGALGPCPVCANGMYYYNGQYQCSGNVSEWSKCTYSATEPVRVKKKWQIPHGTKNDYLMKWFKSQKVKKPERVLPPMSPEKSGSKATQRTSLLSSKGLDKLRFSVVGQSKEAANEWIEKLKLAGANFYARVVKDIDCLIACGELDNENAEVRKARRLKIPIVREGYIGECVKKNKMLPFDLYKLENALESSKGSTVTVKVKGRSAVHESSGLQDTAHILEDGKSIYNATLNMSDLALGVNSYYVLQIIEQDDGSECYVFRKWGRVGSEKIGGQKLEEMSKTEAIKEFKRLFLEKTGNSWEAWECKTNFRKQPGRFYPLDVDYGVKKAPKRKDISEMKSSLAPQLLELMKMLFNVETYRAAMMEFEINMSEMPLGKLSKENIEKGFEALTEIQNLLKDTADQALAVRESLIVAASNRFFTLIPSIHPHIIRDEDDLMIKAKMLEALQDIEIASKIVGFDSDSDESLDDKYMKLHCDITPLAHDSEDYKLIEQYLLNTHAPTHKDWSLELEEVFSLDRDGELNKYSRYKNNLHNKMLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGLYFADLVSKSAQYCYVDRNNPVGLMLLSEVALGDMYELKKATSMDKPPRGKHSTKGLGKTVPLESEFVKWRDDVVVPCGKPVPSSIRSSELMYNEYIVYNTSQVKMQFLLKVRFHHKR | 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 the reparation of DNA strand breaks (By similarity).
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 110475
Sequence Length: 980
Subcellular Location: Nucleus
EC: 2.4.2.30
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P11103 | MAEASERLYRVQYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGQSIRHPDVEVDGFSELRWDDQQKVKKTAEAGGVAGKGQDGSGGKAEKTLGDFAAEYAKSNRSMCKGCLEKIEKGQMRLSKKMVDPEKPQLGMIDRWYHPTCFVKKRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAIKNEGKRKGDEVDGTDEVAKKKSRKETDKYSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRKEWVTPKEFREISYLKKLKVKKQDRIFPPESSAPITVHWPLSVTSAPTAVNSSAPADKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKASLCISIKKEVEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQDLLSAHSLSPWGAEVKAEPGEVVAPRGKSAAPSKKSKGCFKEEGVNKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRLGTVIGSNKLEQMPSKEEAVEQFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLTVKPGTKSKLPKPVQELVGMIFDVDSMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQPVSQGSSESQILDLSNRFYTLIPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLIMLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSASITLEGVEVPLGTGIPSGVNDTALLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW | 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 further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (By similarity). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 . Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site (By similarity). Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (By similarity). Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity . PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (By similarity). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains (By similarity). In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation (By similarity). Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR and NFAT5 (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (By similarity). Required for PARP9 and DTX3L recruitment to DNA damage sites (By similarity). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (By similarity). PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair . In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity . Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II . Acts both as a positive and negative regulator of transcription elongation, depending on the context (By similarity). Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing (By similarity). Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 (By similarity). Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression (By similarity). Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos . Also acts as a negative regulator of the cGAS-STING pathway . Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS . Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes . Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (By similarity). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity).
PTM: Poly-ADP-ribosylated on serine, glutamate and aspartate residues by autocatalysis. Auto-ADP-ribosylation on serine takes place following interaction with HPF1. Auto poly-ADP-ribosylation on serine residues promotes its dissociation from chromatin. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (By similarity). Mono-ADP-ribosylated at Lys-520 by SIRT6 in response to oxidative stress, promoting recruitment to double-strand breaks (DSBs) sites .
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 113100
Sequence Length: 1013
Domain: The two PARP-type zinc-fingers (also named Zn1 and Zn2) specifically recognize DNA strand breaks: PARP-type zinc-finger 1 binds PARP-type zinc-finger 2 from a separate PARP1 molecule to form a dimeric module that specifically recognizes DNA strand breaks.
Subcellular Location: Chromosome
EC: 2.4.2.30
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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 residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Specificity for the different amino acids is conferred by interacting factors, such as hpf1 and nmnat1 (By similarity). Following interaction with hpf1, catalyzes serine ADP-ribosylation of target proteins; hpf1 confers serine specificity by completing the parp1 active site. Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with hpf1 (By similarity). Following interaction with nmnat1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; nmnat1 confers glutamate and aspartate specificity (By similarity). Parp1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits hpf1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair. Mediates the poly-ADP-ribosylation of a number of proteins. In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (By similarity). Parp1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (By similarity). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II. Acts both as a positive and negative regulator of transcription elongation, depending on the context (By similarity). Poly-ADP-ribose chains generated by parp1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos. Also acts as a negative regulator of the cGAS-STING pathway by mediating poly-ADP-ribosylation and inactivation of cgas. Acts as a negative regulator of adipogenesis by catalyzing poly ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) (By similarity).
PTM: Poly-ADP-ribosylated on serine, glutamate and aspartate residues by autocatalysis. Auto-ADP-ribosylation on serine takes place following interaction with HPF1. Auto poly-ADP-ribosylation on serine residues promotes its dissociation from chromatin.
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 15411
Sequence Length: 135
Domain: The two PARP-type zinc-fingers (also named Zn1 and Zn2) specifically recognize DNA strand breaks: PARP-type zinc-finger 1 binds PARP-type zinc-finger 2 from a separate parp1 molecule to form a dimeric module that specifically recognizes DNA strand breaks.
Subcellular Location: Chromosome
EC: 2.4.2.30
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P27008 | MAEATERLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRQPDTEVDGFSELRWDDQQKVKKTAEAGGVAGKGQHGGGGKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQMRLSKKMLDPEKPQLGMIDRWYHPTCFVKNRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLPAVKSEGKRKCDEVDGIDEVAKKKSKKGKDKESSKLEKALKAQNELVWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRKEWVTPKEFREISYLKKLKIKKQDRLFPPESSAPAPPAPPVSITSAPTAVNSSAPADKPLSNMKILTLGKLSQNKDEAKAMIEKLGGKLTGSANKASLCISTKKEVEKMSKKMEEVKAANVRVVCEDFLQDVSASAKSLQELLSAHSLSSWGAEVKVEPGEVVVPKGKSAAPSKKSKGAVKEEGVNKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLESDKESRYWIFRSWGRVGTVIGSNKLEQMPSKEDAVEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEEAVKKLAVKPGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQAVSQGSSESQILDLSNRFYTLIPHDFGMKKPPLLNNTDSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTAPDPSASITLDGVEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLKFNFKTSLW | 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 residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 (By similarity). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site. Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (By similarity). Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains. In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation. Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR and NFAT5. In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively. Required for PARP9 and DTX3L recruitment to DNA damage sites. PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (By similarity). PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair. In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (By similarity). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II. Acts both as a positive and negative regulator of transcription elongation, depending on the context. Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing. Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9. Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression (By similarity). Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos. Also acts as a negative regulator of the cGAS-STING pathway. Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS. Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (By similarity).
PTM: Poly-ADP-ribosylated on serine, glutamate and aspartate residues by autocatalysis. Auto-ADP-ribosylation on serine takes place following interaction with HPF1. Auto poly-ADP-ribosylation on serine residues promotes its dissociation from chromatin. Poly-ADP-ribosylated by PARP2; poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (By similarity). Mono-ADP-ribosylated at Lys-521 by SIRT6 in response to oxidative stress, promoting recruitment to double-strand breaks (DSBs) sites (By similarity).
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 112660
Sequence Length: 1014
Domain: The two PARP-type zinc-fingers (also named Zn1 and Zn2) specifically recognize DNA strand breaks: PARP-type zinc-finger 1 binds PARP-type zinc-finger 2 from a separate PARP1 molecule to form a dimeric module that specifically recognizes DNA strand breaks.
Subcellular Location: Chromosome
EC: 2.4.2.30
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Q11207 | MANKLKVDELRLKLAERGLSTTGVKAVLVERLEEAIAEDTKKEESKSKRKRNSSNDTYESNKLIAIGEFRGMIVKELREEAIKRGLDTTGTKKDLLERLCNDANNVSNAPVKSSNGTDEAEDDNNGFEEEKKEEKIVTATKKGAAVLDQWIPDEIKSQYHVLQRGDDVYDAILNQTNVRDNNNKFFVLQVLESDSKKTYMVYTRWGRVGVKGQSKLDGPYDSWDRAIEIFTNKFNDKTKNYWSDRKEFIPHPKSYTWLEMDYGKEENDSPVNNDIPSSSSEVKPEQSKLDTRVAKFISLICNVSMMAQHMMEIGYNANKLPLGKISKSTISKGYEVLKRISEVIDRYDRTRLEELSGEFYTVIPHDFGFKKMSQFVIDTPQKLKQKIEMVEALGEIELATKLLSVDPGLQDDPLYYHYQQLNCGLTPVGNDSEEFSMVANYMENTHAKTHSGYTVEIAQLFRASRAVEADRFQQFSSSKNRMLLWHGSRLTNWAGILSQGLRIAPPEAPVTGYMFGKGVYFADMFSKSANYCYANTGANDGVLLLCEVALGDMNELLYSDYNADNLPPGKLSTKGVGKTAPNPSEAQTLEDGVVVPLGKPVERSCSKGMLLYNEYIVYNVEQIKMRYVIQVKFNYKH | 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 the reparation of DNA strand breaks (By similarity).
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 72176
Sequence Length: 637
Subcellular Location: Nucleus
EC: 2.4.2.30
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Q09525 | MSIINDENGRGYKVHLCKTNIAQNNNKFYDMELLDEGGDFIVKLINGRIGYRGVTQLKDFDDLDRAKKFFESKFYEKTHLHWEERDDEPVPNKYAVVELATNARQTEKEVKKEEPEPEPKVDEKNTRGRKKRGIVKEKKEIKKEEEPVEEVNEKLKELMKCICDEDVHLGLLKQLKFNEAFGRPIDCLSLAQLTTGYEILSKIEESIGGKSARRSTRGRPRVADRVLAVKSDGPSLHDINKYYSLIPHSFGFCVPPKIDSHAKIQAERELLDALKGSIEASLELKDLKKTASSKDIYQRLYERLPCHLEPVSEEIAGKIGDCLAMRGPTHCYKLSLIDAFELKDPNEIPTEAPVEVQEVPKKRGRKSTKTAAPTVPPPTTKRLLWHGTRVTNVFSILMNGLQFPVGDRCGLMFGNGVYFANVPTKSANYCCPEASKRVFMLLCEVETANPLVLYESEIDADEKMEKAKKTSVYAAGKHTPRDTVEINGIPAFKSNLETIEEETRLLYDEYVMFNKEHFKIKYVVEVKVDRLTAKEMMA | 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 Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 61268
Sequence Length: 538
Subcellular Location: Nucleus
EC: 2.4.2.30
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Q9UGN5 | MAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQDGMPGRSWASKRVSESVKALLLKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALMEACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNGSTVPLGPASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW | 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 groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units . Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage . Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 . Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site . PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks . HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains . Specifically mediates formation of branched poly-ADP-ribosylation . Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF . In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex .
PTM: Auto poly-ADP-ribosylated on serine residues, leading to dissociation of the PARP2-HPF1 complex from chromatin . Poly-ADP-ribosylated by PARP1 (By similarity).
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 66206
Sequence Length: 583
Domain: The N-terminal region (NTR) recognizes and binds poly-ADP-ribose chains produced by PARP1, leading to its recruitment to DNA damage sites.
Subcellular Location: Nucleus
EC: 2.4.2.30
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O50017 | MSARLRVADVRAELQRRGLDVSGTKPALVRRLDAAICEAEKAVVAAAPTSVANGYDVAVDGKRNCGNNKRKRSGDGGEEGNGDTCTDVTKLEGMSYRELQGLAKARGVAANGGKKDVIQRLLSATAGPAAVADGGPLGAKEVIKGGDEEVEVKKEKMVTATKKGAAVLDQHIPDHIKVNYHVLQVGDEIYDATLNQTNVGDNNNKFYIIQVLESDAGGSFMVYNRWGRVGVRGQDKLHGPSPTRDQAIYEFEGKFHNKTNNHWSDRKNFKCYAKKYTWLEMDYGETEKEIEKGSITDQIKETKLETRIAQFISLICNISMMKQRMVEIGYNAEKLPLGKLRKATILKGYHVLKRISDVISKADRRHLEQLTGEFYTVIPHDFGFRKMREFIIDTPQKLKAKLEMVEALGEIEIATKLLEDDSSDQDDPLYARYKQLHCDFTPLEADSDEYSMIKSYLRNTHGKTHSGYTVDIVQIFKVSRHGETERFQKFASTRNRMLLWHGSRLSNWAGILSQGLRIAPPEAPVTGYMFGKGVYFADMFSKSANYCYASEACRSGVLLLCEVALGDMNELLNADYDANNLPKGKLRSKGVGQTAPNMVESKVADDGVVVPLGEPKQEPSKRGGLLYNEYIVYNVDQIRMRYVLHVNFNFKRR | 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 the reparation of DNA strand breaks (By similarity).
Catalytic Activity: NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).
Sequence Mass (Da): 72995
Sequence Length: 653
Subcellular Location: Nucleus
EC: 2.4.2.30
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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 processing to generate class I binding peptides (By similarity).
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
Sequence Mass (Da): 23201
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 3.4.25.1
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Q9LRY1 | MSCFSCFSSKVLDNEGSSMPAPYKQPNSPKRTTGEVVAKNANGPSNNMGARIFTFRELATATKNFRQECLIGEGGFGRVYKGKLENPAQVVAVKQLDRNGLQGQREFLVEVLMLSLLHHRNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLLDLEPGQKPLDWNTRIKIALGAAKGIEYLHDEADPPVIYRDLKSSNILLDPEYVAKLSDFGLAKLGPVGDTLHVSSRVMGTYGYCAPEYQRTGYLTNKSDVYSFGVVLLELISGRRVIDTMRPSHEQNLVTWALPIFRDPTRYWQLADPLLRGDYPEKSLNQAIAVAAMCLHEEPTVRPLMSDVITALSFLGASSNSSNTGSNHLQQNRSNKYQDAVQWDSSPRYANSQM | 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 | MNCFSCFYFHEKKKVPRDSDNSYRRNGEVTGRDNNKTHPENPKTVNEQNKNNDEDKEVTNNIAAQTFSFRELATATKNFRQECLIGEGGFGRVYKGKLEKTGMIVAVKQLDRNGLQGNKEFIVEVLMLSLLHHKHLVNLIGYCADGDQRLLVYEYMSRGSLEDHLLDLTPDQIPLDWDTRIRIALGAAMGLEYLHDKANPPVIYRDLKAANILLDGEFNAKLSDFGLAKLGPVGDKQHVSSRVMGTYGYCAPEYQRTGQLTTKSDVYSFGVVLLELITGRRVIDTTRPKDEQNLVTWAQPVFKEPSRFPELADPSLEGVFPEKALNQAVAVAAMCLQEEATVRPLMSDVVTALGFLGTAPDGSISVPHYDDPPQPSDETSVEDSVAAEERERAVAEAMEWGVASRAHSRNPSAS | 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 Location: Cell membrane
EC: 2.7.11.1
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Q1PDV6 | MSGCLPCFGSSAKDAASKDSVKKELSAKDGSVTQSHHISLDKSKSRRGPEQKKELTAPKEGPTAHIAAQTFTFRELAAATKNFRPECLLGEGGFGRVYKGRLETTGQIVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLHDLPPDKEPLDWSTRMTIAAGAAKGLEYLHDKANPPVIYRDLKSSNILLGDGYHPKLSDFGLAKLGPVGDKTHVSTRVMGTYGYCAPEYAMTGQLTLKSDVYSFGVVFLELITGRKAIDNARAPGEHNLVAWARPLFKDRRKFPKMADPSLQGRYPMRGLYQALAVAAMCLQEQAATRPLIGDVVTALTYLASQTFDPNAPSGQNSRSGSGPPFIRTRDDRRSLGDGSSLDSPAETRSRLGSPATHKNSPDYRRRDMVREVNAGSEGGSETGGGSGRKWGLSDLEGQESQRGSPASVGRSSRGTPRNRDLDRERAVAEAKVWGENWRERKRATNGPGSFDSTND | 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 phosphorylated by CERK1 after elicitation by chitin .
PTM: Phosphorylated by CERK1 upon elicitation by chitin.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55931
Sequence Length: 513
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q84M95 | MHFPLVSAWNKRRRSKSYDTDPCTFLFSIIFARWHKRVYRTAECWQIEDQASQPRKRRFGSSVYTLKEMEEATSSFSDENLLGKGGFGRVYQGTLKTGEVVAIKKMDLPTFKKADGEREFRVEVDILSRLDHPNLVSLIGYCADGKHRFLVYEYMQNGNLQDHLNGIKEAKISWPIRLRIALGAAKGLAYLHSSSSVGIPIVHRDFKSTNVLLDSNYNAKISDFGLAKLMPEGKDTCVTARVLGTFGYFDPEYTSTGKLTLQSDIYAFGVVLLELLTGRRAVDLTQGPNEQNLVLQVRNILNDRKKLRKVIDVELPRNSYSMEAITMFADLASRCIRIESKERPSVMDCVKELQLIIYTNSKGGLGGTIPTFRRL | 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 | MGNCLDSSAKVDNSNHSPHANSASSGSKVSSKTSRSTGPSGLSTTSYSTDSSFGPLPTLRTEGEILSSPNLKAFTFNELKNATKNFRQDNLLGEGGFGCVFKGWIDQTSLTASRPGSGIVVAVKQLKPEGFQGHKEWLTEVNYLGQLSHPNLVLLVGYCAEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAVGAAKGLTFLHEAKSQVIYRDFKAANILLDADFNAKLSDFGLAKAGPTGDNTHVSTKVIGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELISGRRAMDNSNGGNEYSLVDWATPYLGDKRKLFRIMDTKLGGQYPQKGAFTAANLALQCLNPDAKLRPKMSEVLVTLEQLESVAKPGTKHTQMESPRFHHSSVMQKSPVRYSHDRPLLHMTPGASPLPSYTQSPRVR | 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 uridylylation promotes the formation of a complex with RKS1 and RPP13L4/ZAR1 which, in turn, activates effector-triggered immunity (ETI) against X.campestris . Promotes, when uridylylated by AvrAC/XopAC, the release of ADP from the inactive RKS1-ZAR1 complex, thus activating the resistosome .
PTM: Uridylylated at Ser-253 and Thr-254 by Xanthomonas campestris effector AvrAC/XopAC; this uridylylation is necessary for specific recruitment to RKS1 and to trigger immunity.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46296
Sequence Length: 426
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9LFP7 | MGLDAVKAKGNWKSEKPKETENKNHKKKNGDDNKSRNEEEEEGEASGCWVKFRFMIGCIPSKSDLDASSSSIYGSNCTVTTMESKSANEKSNDQPVGQVSSTTTTSNAESSSSTPVISEELNISSHLRKFTFNDLKLSTRNFRPESLLGEGGFGCVFKGWIEENGTAPVKPGTGLTVAVKTLNPDGLQGHKEWLAEINFLGNLLHPNLVKLVGYCIEDDQRLLVYEFMPRGSLENHLFRRSLPLPWSIRMKIALGAAKGLSFLHEEALKPVIYRDFKTSNILLDADYNAKLSDFGLAKDAPDEGKTHVSTRVMGTYGYAAPEYVMTGHLTSKSDVYSFGVVLLEMLTGRRSMDKNRPNGEHNLVEWARPHLLDKRRFYRLLDPRLEGHFSIKGAQKVTQLAAQCLSRDPKIRPKMSDVVEALKPLPHLKDMASSSYYFQTMQAERLKNGSGRSQGFGSRNGQHQPVFRTLSSPHGSSPYRHQIPSPKPKGATT | 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 Thr-310 in response to the pathogen-associated molecular pattern (PAMP) 3-OH-C10:0, a medium-chain 3-hydroxy fatty acid.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54799
Sequence Length: 493
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9SRH7 | MGFDSVKVMENWQSKTSNENEKKKKKRRRKKNNNVRNSEHYEEEANGCWVKFRYIVCCASSTSDVETSLTLSTSTVGSQSAIVQSNDQPVGPVSSTTTTSNAESSLSTPIISEELNIYSHLKKFSFIDLKLATRNFRPESLLGEGGFGCVFKGWVEENGTAPVKPGTGLTVAVKTLNPDGLQGHKEWLAEINYLGNLLHPNLVKLVGYCIEDDQRLLVYEFMPRGSLENHLFRRSLPLPWSIRMKIALGAAKGLSFLHEEALKPVIYRDFKTSNILLDGEYNAKLSDFGLAKDAPDEGKTHVSTRVMGTYGYAAPEYVMTGHLTSKSDVYSFGVVLLEMLTGRRSMDKNRPNGEHNLVEWARPHLLDKRRFYRLLDPRLEGHFSVKGAQKVTQLAAQCLSRDSKIRPKMSEVVEVLKPLPHLKDMASASYYFQTMQAERLKAGSGSGSGRGFGSRNGQPVFRTLSSPHGQAGSSPYRHQIPSPKPKGATT | 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 the pathogen-associated molecular pattern (PAMP) 3-OH-C10:0, a medium-chain 3-hydroxy fatty acid.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54510
Sequence Length: 490
Subcellular Location: Cell membrane
EC: 2.7.11.1
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O49840 | MGNCLDSSAKVDSSSHSPHANSASLSSRVSSKTSRSTVPSSLSINSYSSVESLPTPRTEGEILSSPNLKAFTFNELKNATRNFRPDSLLGEGGFGYVFKGWIDGTTLTASKPGSGIVVAVKKLKTEGYQGHKEWLTEVNYLGQLSHPNLVKLVGYCVEGENRLLVYEFMPKGSLENHLFRRGAQPLTWAIRMKVAIGAAKGLTFLHDAKSQVIYRDFKAANILLDAEFNSKLSDFGLAKAGPTGDKTHVSTQVMGTHGYAAPEYVATGRLTAKSDVYSFGVVLLELLSGRRAVDKSKVGMEQSLVDWATPYLGDKRKLFRIMDTRLGGQYPQKGAYTAASLALQCLNPDAKLRPKMSEVLAKLDQLESTKPGTGVGNRQAQIDSPRGSNGSIVQKSPRRYSYDRPLLHITPGASPLPTHNHSPRVR | 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 | MGNCFGFSAKVGNRESPYRGSSRISAKRSQSSRLSSLTIQSSSYNDDTSVASLQTPRSEGELLASPTLKAFTFNELKTATRNFRPDSVIGEGGFGYVYKGWIDERTLSPSKPGSGMVVAVKKLKEEGFQGHRQWLAEVDCLGRLHHMNLVKLIGYCSKGDHIRLLVYEYMPKGSLENHLFRRGAEPIPWRTRIKVAIGAARGLAFLHEAQVIYRDFKASNILLDSEFNAKLSDFGLAKVGPTGDRTHVSTQVMGTQGYAAPEYVATGRITAKSDVYSFGVVLLELLSGRLTVDKTKVGVERNLVDWAIPYLGDKRKVFRIMDTKLGGQYPHKGACLTANTALQCLNQEPKLRPKMSDVLSTLEELEMTLKSGSISNSVMKLTSSSSSFTAKQRVRTPVADPVLSSRRCRRVR | 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 | MGCFGCSKKSSKRSETNKDTVINRKIVGGTTSVAKSDKRDDQTQPSSDSTKVSPYRDVNNEGGVGKEDQLSLDVKGLNLNDQVTGKKAQTFTFQELAEATGNFRSDCFLGEGGFGKVFKGTIEKLDQVVAIKQLDRNGVQGIREFVVEVLTLSLADHPNLVKLIGFCAEGDQRLLVYEYMPQGSLEDHLHVLPSGKKPLDWNTRMKIAAGAARGLEYLHDRMTPPVIYRDLKCSNILLGEDYQPKLSDFGLAKVGPSGDKTHVSTRVMGTYGYCAPDYAMTGQLTFKSDIYSFGVVLLELITGRKAIDNTKTRKDQNLVGWARPLFKDRRNFPKMVDPLLQGQYPVRGLYQALAISAMCVQEQPTMRPVVSDVVLALNFLASSKYDPNSPSSSSGKNPSFHRDRDDEEKRPHLVKETECEGSS | 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 Location: Cell membrane
EC: 2.7.11.1
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Q9SIB6 | MGCFGRTPKSNKRSDTKTTKNNDFTPKKLTVNANRDKLTQPSSDCLKVSICGDVSKEIVTKKDQLALDAKDTNVEDEVIVKKAQTFTFEELSVSTGNFKSDCFLGEGGFGKVYKGFIEKINQVVAIKQLDRNGAQGIREFVVEVLTLSLADHPNLVKLIGFCAEGVQRLLVYEYMPLGSLDNHLHDLPSGKNPLAWNTRMKIAAGAARGLEYLHDTMKPPVIYRDLKCSNILIDEGYHAKLSDFGLAKVGPRGSETHVSTRVMGTYGYCAPDYALTGQLTFKSDVYSFGVVLLELITGRKAYDNTRTRNHQSLVEWANPLFKDRKNFKKMVDPLLEGDYPVRGLYQALAIAAMCVQEQPSMRPVIADVVMALDHLASSKYDRSHRQKQDNVTETKVDEEKTLTTESNVCVEEKQEIKICSDQAT | 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 | MGWIPCSGKSSGRNKTRRNGDHKLDRKSSDCSVSTSEKSRAKSSLSESKSKGSDHIVAQTFTFSELATATRNFRKECLIGEGGFGRVYKGYLASTSQTAAIKQLDHNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLHDISPGKQPLDWNTRMKIAAGAAKGLEYLHDKTMPPVIYRDLKCSNILLDDDYFPKLSDFGLAKLGPVGDKSHVSTRVMGTYGYCAPEYAMTGQLTLKSDVYSFGVVLLEIITGRKAIDSSRSTGEQNLVAWARPLFKDRRKFSQMADPMLQGQYPPRGLYQALAVAAMCVQEQPNLRPLIADVVTALSYLASQKFDPLAQPVQGSLFAPGTPPRSKRV | 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-phospho-L-seryl-[protein]
Sequence Mass (Da): 41672
Sequence Length: 378
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q8GXZ3 | MGNCGTRDEAAVFTPQAQAQQLQKKHSRSVSDLSDPSTPRFRDDSRTPISYAQVIPFTLFELETITKSFRPDYILGEGGFGTVYKGYIDDNLRVGLKSLPVAVKVLNKEGLQGHREWLTEVNFLGQLRHPNLVKLIGYCCEDDHRLLVYEFMLRGSLENHLFRKTTAPLSWSRRMMIALGAAKGLAFLHNAERPVIYRDFKTSNILLDSDYTAKLSDFGLAKAGPQGDETHVSTRVMGTYGYAAPEYVMTGHLTARSDVYSFGVVLLEMLTGRKSVDKTRPSKEQNLVDWARPKLNDKRKLLQIIDPRLENQYSVRAAQKACSLAYYCLSQNPKARPLMSDVVETLEPLQCTGDALIPCATTTAGAAFAMGGVPDYRMHRRFAKNVGPGAICRSPNPNYSPGGPAACRVR | 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).
Catalytic Activity: (-)-dehydrodiconiferyl alcohol + H(+) + NADPH = (S)-isodihydrodehydrodiconiferyl alcohol + NADP(+)
Sequence Mass (Da): 33752
Sequence Length: 306
EC: 1.23.1.-
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Q15365 | MDAGVTESGLNVTLTIRLLMHGKEVGSIIGKKGESVKRIREESGARINISEGNCPERIITLTGPTNAIFKAFAMIIDKLEEDINSSMTNSTAASRPPVTLRLVVPATQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGVPQSVTECVKQICLVMLETLSQSPQGRVMTIPYQPMPASSPVICAGGQDRCSDAAGYPHATHDLEGPPLDAYSIQGQHTISPLDLAKLNQVARQQSHFAMMHGGTGFAGIDSSSPEVKGYWASLDASTQTTHELTIPNNLIGCIIGRQGANINEIRQMSGAQIKIANPVEGSSGRQVTITGSAASISLAQYLINARLSSEKGMGCS | 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 Location: Nucleus
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Q15366 | MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLETLSQSPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS | 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 between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitination and degradation . Negativeley regulates the cGAS-STING pathway via interaction with CGAS, preventing the formation of liquid-like droplets in which CGAS is activated . Together with PCBP1, required for erythropoiesis, possibly by regulating mRNA splicing (By similarity).
PTM: Phosphorylated. The non-phosphorylated form(s) exhibited the strongest poly(rC)-binding activity.
Sequence Mass (Da): 38580
Sequence Length: 365
Domain: The KH domains mediates poly(C) binding.
Subcellular Location: Nucleus
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P21902 | MLVNNVFSLLCFPLLMSVVRCSTLSRQRRQFVFPDEEELCSNRFTEEGTCKNVLDCRILLQKNDYNLLKESICGFEGITPKVCCPKSSHVISSTQAPPETTTTERPPKQIPPNLPEVCGIHNTTTTRIIGGREAPIGAWPWMTAVYIKQGGIRSVQCGGALVTNRHVITASHCVVNSAGTDVMPADVFSVRLGEHNLYSTDDDSNPIDFAVTSVKHHEHFVLATYLNDIAILTLNDTVTFTDRIRPICLPYRKLRYDDLAMRKPFITGWGTTAFNGPSSAVLREVQLPIWEHEACRQAYEKDLNITNVYMCAGFADGGKDACQGDSGGPMMLPVKTGEFYLIGIVSFGKKCALPGFPGVYTKVTEFLDWIAEHMV | 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 chain containing the CLIP domain and a catalytic 31 kDa heavy chain which remain covalently associated through an interchain disulfide bond . Proteolytically cleaved by clotting factor G subunit beta .
Catalytic Activity: Selective cleavage of 18-Arg-|- and 47-Arg-|- bonds in coagulogen to form coagulin and fragments.
Sequence Mass (Da): 41592
Sequence Length: 375
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Subcellular Location: Cytoplasmic vesicle
EC: 3.4.21.86
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Q8REI2 | MYGLEKLGINNVTAAHYNLSPAQLVEKALANNEGILSDTGAFVISTGKYTGRAPDDKFFVDTPEVHKYIDWSRNQPIEKEKFDAIFGKLVAYLQNREIFIFDGRAGANPEYTRRFRVINELASQNLFIHQLLIRTDEEYNENNDIDFTIISAPNFHCVPEIDGVNSEAAIIINFEKKIAIICATKYSGEIKKSVFSIMNYIMPHENILPMHCSANMDPVTHETAIFFGLSGTGKTTLSADPNRKLIGDDEHGWCDKGIFNFEGGCYAKCINLKEESEPEIYRAIKFGSLVENVVVDPITRKIQYEDASITPNTRVGYPIDYIPNAELSGVGGIPKVVIFLTADSFGVLPPISRLSQEAAMYHFVTGFTAKLAGTELGVKEPVPTFSTCFGEPFMPMDPSVYAEMLGERLKKHNTKVYLINTGWSGGAYGTGKRINLKYTRAMVTAVLNGYFDNAEYKHDDIFNLDIPQSCPGVPSEIMNPIDTWQDRDKYIIAAKKLANLFYNNFKEKYPNMPENITNAGPKYND | 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
Sequence Mass (Da): 58796
Sequence Length: 525
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.49
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Q39QU2 | MRLNDITRGTGLEEHGITNANLIYWTPPTAVLYEQIVKRGEGLVTHLGAVAVKTGHYTGRAANEKFIVDEPSSNDHIAWGKVNQPFDSAKFDALFGRMLAYLHGKDIFVQECFAGCSPDHRLPVRVITERAWHSLFARNMFVRATPEELVGFKPGFTVIDLPAFHAIPSVDGTNTETFIIVNFEKRLIIIGGTSYAGEIKKSIFTILNYLLPQHKNVLSMHCSANVGEKDDVAVFFGLSGTGKTTLSADPRRRLIGDDEHGWDNSGVFNFEGGCYAKIINLSPEAEPEIYQTTRRFGTILENVAIDTVSRRIDLNDDSFTENTRASYPITHIPNIVKSGMGGHPTNIIMLTCDAFGVLPPIARLTPDQAMYHFLSGYTAKVAGTEAGITEPQAAFSACFGAPFMALHPSVYAKLLGEKIARHGVSCWLVNTGWSGGPYGVGSRMKIAYSRALVNAAIDGTLNAGSFVKDQFFGLDIPTGCSGVPAEVLNPKNTWVDKTKYDETATMLVERFRKNFEQYRSYVSAGVAEVM | 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
Sequence Mass (Da): 58150
Sequence Length: 530
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.49
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C4LGT5 | MSAPTIPGLEGNAPTTNQDMLNWIAECAELCQPDKVVFCDGSDEEWEAIAKDLVEKGTLIKLNEEKRPNSYLASSDPADVARVESRTFICSKTEDGAGPTNNWRDPDEMRAEMSEHFKGSMKGRTMYVVPFCMGPITDPDPKLGIELTDSGYVVMSMRIMTRMGKEALDKIGDGPFVKGLHSVGAPLEPGQEDVKWPCNETKYITQFPEDRVIWSYGSGYGGNAILAKKCYALRIASVMAKDEGWMAEHMLILKLISPEGKAYHICAAFPSQCGKTNLAMIQPTIPGWKAEVIGDDIAWLHFGDDGRLYAVNPENGFFGVAPGTNYKSNPNAMKTMEAGNNIFTNVALTDDGDVWWEGLENEPDHLIDWKGKDWTPDEDCLSSHPNSRYCVPIEQCPVAAPEFNDPKGVPVDAILFGGRRPDTVPLVTEAIDWQHATFIGATLASGQTAAAAEAKVGTLRYDPMAMLPFIGYNVGDYLQHWLDIGKKGGDKLPKVFLVNWFRRGDDGRFLWPGFGENSRVLKWIVDRIEGRVDAKKTVVGYTAYSKDIDIDGLDTDPKDVKAALTAPADKWQMDLSDTEDWLKSLGPKVPQEIWDEFDFLKTRIKTANKDGNKALDNMKTK | 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 + phosphoenolpyruvate
Sequence Mass (Da): 68814
Sequence Length: 621
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.32
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P20007 | MPELIEQSKIISGNVCGLPQLHKLRQDNCGLYSHIRGIPISYGNVDLLTTGVRAFVEEGIALCQPDQVHICDGSEQENKVLIKSLLEAGTIVPLPKYDNCWLARTNPADVARVESRTFICTERREETIPTPVEGVKGTLGNWISPSDMDAAVQQRFPGCMKGRTMYVVPFSMGPVGSPLSKIGIELTDSAYVVASMRIMTRMGAAVLRQLAKKEEFVRALHSVGAPANGQVEQPSWPCDPERTIILHKPAENLIVSYGSGYGGNSLLGKKCFALRIGSTIAKQEGWLAEHMLILGITDPKGEKKYITAAFPSACGKTNLAMLNPSLANYKVECVGDDIAWMKFDSQGVLRAINPENGFFGVAPGTSMETNPIAMNTVFKNTIFTNVASTSDGGVFWEGMESSLAPNVQITDWLGKPWTKDSGKPAAHPNSRFCTPAAQCPIIDEAWEDPAGVPISAMLFGGRRPAGVPLIYEARDWTHGVFIGAAMRSEATAAAEHKGKVIMHDPFAMRPFFGYNFGDYVAHWLSMEKRGQVPKIFHVNWFRKSAEGKFMWPGYGENSRVLEWILRRVNGESCYVDSAIGHIPAEGALNLDGMKDKVDVKEIFSLPKEFWSQEVKDIRTYFESQVGADLPASIYQQLDELSSRVDNL | 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 + phosphoenolpyruvate
Sequence Mass (Da): 71129
Sequence Length: 647
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.1.1.32
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P29190 | MKRLGHVPIHKGDFHLLPPKVQRFVAEKAELMRPRGIYICDGSQHEADEIIDKLIERGMLSPLKAYENNYICRTDPKDVARVESKTWMVTPDKYQTVCHTPDGIEPIMGHWMSPDSLATELDSRFPGCMAGRIMYVIPFSMGPVGGPLSKIGVQLTDSNYVVLSMRIMTRVGHEVWDALGDNDFVRCIHSVGLPRPVKQRVINHWPCNPERVLIAHRPAEREIWSFGSGYGGNSLLGKKMLALRIASNIAKDEGWMAEHMLIMGVTRPDGKEHFIAAAFPSACGKTNLAMLEPALPGWKVRCVGDDIAWMKFGEDGRLYAINPEYGFFGVAPGTSKKTNPMAVATFQKNSIFTNVGETANGEYFWEGLEDEIKDKNVDMINWLGEKWRIGDPGLCAHPNSRFAAPASQCPIIHPEWESPKGVPIDAIIFGGRRPAGVPLVFETRSWLHGIFTGACLKSEATAAAEHKGKTVMHDPMAMRPFMGYNFGHYLQHWIDLNKDGRKVPKIYHVNWFRRDANNKFLWPGYGQNIRVIDWIVRRLDGEPDIGVDTPIGIVPKKGAINASGLPDIQWDELMSVPKEYWTNDAKEIRKFLEEQVGPDLPKEIRAEMDAQEERINKQA | 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: 619
EC: 4.1.1.32
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P65687 | MTSATIPGLDTAPTNHQGLLSWVEEVAELTQPDRVVFTDGSEEEFQRLCDQLVEAGTFIRLNPEKHKNSYLALSDPSDVARVESRTYICSAKEIDAGPTNNWMDPGEMRSIMKDLYRGCMRGRTMYVVPFCMGPLGAEDPKLGVEITDSEYVVVSMRTMTRMGKAALEKMGDDGFFVKALHSVGAPLEPGQKDVAWPCSETKYITHFPETREIWSYGSGYGGNALLGKKCYSLRIASAMAHDEGWLAEHMLILKLISPENKAYYFAAAFPSACGKTNLAMLQPTIPGWRAETLGDDIAWMRFGKDGRLYAVNPEFGFFGVAPGTNWKSNPNAMRTIAAGNTVFTNVALTDDGDVWWEGLEGDPQHLIDWKGNDWYFRETETNAAHPNSRYCTPMSQCPILAPEWDDPQGVPISGILFGGRRKTTVPLVTEARDWQHGVFIGATLGSEQTAAAEGKVGNVRRDPMAMLPFLGYNVGDYFQHWINLGKHADESKLPKVFFVNWFRRGDDGRFLWPGFGENSRVLKWIVDRIEHKAGGATTPIGTVPAVEDLDLDGLDVDAADVAAALAVDADEWRQELPLIEEWLQFVGEKLPTGVKDEFDALKERLG | 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 + phosphoenolpyruvate
Sequence Mass (Da): 67253
Sequence Length: 606
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.32
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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-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion (By similarity).
PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA (By similarity).
Sequence Mass (Da): 28785
Sequence Length: 261
Subcellular Location: Nucleus
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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 archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranylgeranyl diphosphate (GGPP; C20) as the prenyl donor.
Catalytic Activity: all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate
Sequence Mass (Da): 25360
Sequence Length: 225
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
EC: 2.5.1.n9
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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 archaea-type G1P-based membrane lipids found in Bacillales.
Catalytic Activity: all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate
Sequence Mass (Da): 26147
Sequence Length: 229
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
EC: 2.5.1.n9
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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 archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranylgeranyl diphosphate (GGPP; C20) as the prenyl donor.
Catalytic Activity: all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate
Sequence Mass (Da): 25889
Sequence Length: 230
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
EC: 2.5.1.n9
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Q8C7K6 | MARAAPLLAVLATVLTTAAAGGDAPPGKIAVIGAGIGGSAVAHFLQQHFGPRVQIVVYEKGTVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLRQRREVVGRSAIFGGEHFVLEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGVEELLYSLGEATFVNMTQRSVAESLLQVGVTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTLHSTEGKALYQVAYESDKGNSSDFYDIVVIATPLHLDNSSNNNITFEGFTPPIEDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFANILTTDFPSFFCTLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPRFALHDQLFYLNALEWAASSVEVTAVAAKNVALLAYNRWYQDLDKIDQKDLIHKVKTEL | 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 during embryonic development (By similarity). Required for normal cardiovascular development .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24380
Sequence Length: 210
Subcellular Location: Cytoplasm
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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 during embryonic development (By similarity). Required for normal cardiovascular development .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24425
Sequence Length: 210
Subcellular Location: Cytoplasm
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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 produce interleukin-10 (IL10) .
PTM: Ubiquitinated; STUB1 likely mediates polyubiquitination of PD-L1/CD274 triggering its degradation . Ubiquitinated by MARCHF8; leading to degradation .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 33275
Sequence Length: 290
Subcellular Location: Cell membrane
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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
Sequence Mass (Da): 30957
Sequence Length: 273
Subcellular Location: Secreted
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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): 27820
Sequence Length: 247
Subcellular Location: Cell membrane
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Q9Y5Y4 | MSANATLKPLCPILEQMSRLQSHSNTSIRYIDHAAVLLHGLASLLGLVENGVILFVVGCRMRQTVVTTWVLHLALSDLLASASLPFFTYFLAVGHSWELGTTFCKLHSSIFFLNMFASGFLLSAISLDRCLQVVRPVWAQNHRTVAAAHKVCLVLWALAVLNTVPYFVFRDTISRLDGRIMCYYNVLLLNPGPDRDATCNSRQVALAVSKFLLAFLVPLAIIASSHAAVSLRLQHRGRRRPGRFVRLVAAVVAAFALCWGPYHVFSLLEARAHANPGLRPLVWRGLPFVTSLAFFNSVANPVLYVLTCPDMLRKLRRSLRTVLESVLVDDSELGGAGSSRRRRTSSTARSASPLALCSRPEEPRGPARLLGWLLGSCAASPQTGPLNRALSSTSS | 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 regulated by diverse kinases such as, PKC, PKA, GRK2, GPRK5/GRK5 and GRK6. Receptor activation is responsible, at least in part, in immune regulation and allergic/inflammation responses.
PTM: Phosphorylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43268
Sequence Length: 395
Domain: The 330-DSEL-333 motif is involved in the recycling of PTGDR2 to the cell surface after agonist-induced internalization. This motif seems to be required for GRK2 and GPRK5/GRK5 to promote agonist-induced internalization. Thr-347 is a major site for PKC-induced internalization of the receptor.
Subcellular Location: Cell membrane
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Q13258 | MKSPFYRCQNTTSVEKGNSAVMGGVLFSTGLLGNLLALGLLARSGLGWCSRRPLRPLPSVFYMLVCGLTVTDLLGKCLLSPVVLAAYAQNRSLRVLAPALDNSLCQAFAFFMSFFGLSSTLQLLAMALECWLSLGHPFFYRRHITLRLGALVAPVVSAFSLAFCALPFMGFGKFVQYCPGTWCFIQMVHEEGSLSVLGYSVLYSSLMALLVLATVLCNLGAMRNLYAMHRRLQRHPRSCTRDCAEPRADGREASPQPLEELDHLLLLALMTVLFTMCSLPVIYRAYYGAFKDVKEKNRTSEEAEDLRALRFLSVISIVDPWIFIIFRSPVFRIFFHKIFIRPLRYRSRCSNSTNMESSL | 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 in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40271
Sequence Length: 359
Subcellular Location: Cell membrane
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P70263 | MNESYRCQTSTWVERGSSATMGAVLFGAGLLGNLLALVLLARSGLGSCRPGPLHPPPSVFYVLVCGLTVTDLLGKCLISPMVLAAYAQNQSLKELLPASGNQLCETFAFLMSFFGLASTLQLLAMAVECWLSLGHPFFYQRHVTLRRGVLVAPVVAAFCLAFCALPFAGFGKFVQYCPGTWCFIQMIHKERSFSVIGFSVLYSSLMALLVLATVVCNLGAMYNLYDMHRRQRHYPHRCSRDRAQSGSDYRHGSLHPLEELDHFVLLALMTVLFTMCSLPLIYRAYYGAFKLENKAEGDSEDLQALRFLSVISIVDPWIFIIFRTSVFRMLFHKVFTRPLIYRNWSSHSQQSNVESTL | 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 in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40005
Sequence Length: 357
Subcellular Location: Cell membrane
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O76074 | MERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWDFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSAPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRN | 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 phosphodiesterase catalyzes the specific hydrolysis of cGMP to 5'-GMP . Specifically regulates nitric-oxide-generated cGMP .
PTM: Phosphorylation is regulated by binding of cGMP to the two allosteric sites (By similarity). Phosphorylation by PRKG1 leads to its activation.
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Sequence Mass (Da): 99985
Sequence Length: 875
Domain: Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain which contains two homologous allosteric cGMP-binding regions, A and B.
Pathway: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
EC: 3.1.4.35
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P91119 | MDDASVLKYLQENPKLVEDFVVSNEISPETFKRWAVRRTMKYKNVKNGTSGGTGAWTEPDLSMKRRVILETSDNRTRILYEITQCCGQLIGTNSIELIVQNDEGAFSCRKTENGELKLKKVKTSKSADYIQTIVNAGNQTIAEIHFYTQLDSTEKSIVNAVCTWAAATNYYSELYTHKQEGSDGQDIHENIAKQRKLSNFLLDVARSIFHDIVSMDAVIIKVMNFAQKLVDADRASLFLVDSKNAQIYARIFDVGTGDEEHVRVNSEGQKEIRFDMSKGIAGYVASTGEGLNIENAYEDERFNADVDSKTGYTTKTILCMPILIRGIVIGVVQMVNKHDGVFTRQDEDAFEIFAVYCGLALHHAKLYDKIRRSEQKYRVALEVLAYHSVCNADEVNKLKKIEINNRIVELETIDFNGMRLSELEKPLYAVYMFKTLFADTLRFDTEDLIRFVLTVRKNYRRVAYHNWAHGWSVAHAMFATLMNSPDAFTKLEALALYVSCLCHDLDHRGKNNAYMKTMSTPLASIYSTSVMERHHFNQTVTILQQDGHNILKSLSSEDYKKTLSLIKHCILATDLALFFSNKAKLNVILDNNTFDINRQEHRLLTQAVMMTGCDLVASAKPWNIQTETVKVIFEEFYDQGDAERLSGKEPIPMMDRQQAHMLPQMQVGFMRGICMPCYDLIARIFPKNDKMRERCEYNAKKWEELAEEQRKKQEALAQQNGEANETQE | 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 cGMP levels.
Catalytic Activity: a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+)
Sequence Mass (Da): 83227
Sequence Length: 728
EC: 3.1.4.17
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Q8MLZ3 | MMFSKRKSIRFNPEGDYTELPRGGYVVPSKLGGIQFGVPPETIKDSMALKIDVPTIYVFPEELWDRKTGINAAEAEFPAYFNYFILKRKVSFVCTKEQEQRIRIVFQETLLGPPEFNTGIIINSSSSTTDTSKTSPIKKQTSSSSPPLSPQQQQPPPPLVKQPSQQQLEELATMDTCHYHHHHHHQEVNDNDNNNNTTTNNNNIEILEQQQQQQQQQQQQQDEDSTDVDEEFQKEFSSTFPRSEIPNLEKECKYLRTFNSVDELFDFILFDDNGIAKLSDDVEIHFQEDQSLFKVLQFEETGKGNKVQTLVATIPSKILFPDMINSISTINDNKIFDPPTFGITIIGSSHGFDPKKSTTGFVLWINKRGIMVDPPLNSSSFLQSQGVPTRMVDHIILTHCHADHDSGTFQKLLEEYQITVVTTPTILGSFLRKYGALSNLSTDLLRRLFIFRPVMIGEPMIISGAEFRFFYTIHTIPTISFEVFYGGKSIFYSGDTCYDPNRIKDMNKRGIMKTSRMKFFLRPWNHTVVLHEAGVPPIHTPVSVLRALPDEVKNRLYLVHISEHTLPAGSGLKIAKEGVAHTLSLDVMKSSHSEAVDILKLVESVDIFRSIPLTQACEILQTATKRKYSQGSVIIARDTEPDAFYVVASGVVCVNIGELKKNLIVGDYFGEMSLVMGGLRSANVQAVTDVEVLSFNKEDFLSITRNSTESIQFITRLWEMRNEKSWETMSLNSVFSRCTNSQKTAIQSILVRELIKKDETLWCKGEEALFGCLVAEGSFVFKEDDSLESFSQGSFLGDINAMTTQPPSIHKTTVVAKEESVIYKVLSQDLIKFFSNNPGIQLAFLDTIFVDALRDQVQQLVNSKLTY | 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). Involved in the degradation of intracellular cGMP, contributes to the control of cGMP signals .
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Sequence Mass (Da): 97992
Sequence Length: 867
Domain: The beta lactamase-like domain catalyzes the hydrolysis of cGMP.
Subcellular Location: Cytoplasm
EC: 3.1.4.35
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P35913 | MSLSEEQARSFLDQNPDFARQYFGKKLSPENVAAACEDGCPPDCDSLRDLCQVEESTALLELVQDMQESINMERVVFKVLRRLCTLLQADRCSLFMYRQRNGVAELATRLFSVQPDSVLEDCLVPPDSEIVFPLDIGVVGHVAQTKKMVNVEDVAECPHFSSFADELTDYKTKNMLATPIMNGKDVVAVIMAVNKLNGPFFTSEDEDVFLKYLNFATLYLKIYHLSYLHNCETRRGQVLLWSANKVFEELTDIERQFHKAFYTVRAYLNCERYSVGLLDMTKEKEFFDVWSVLMGESQPYSGPRTPDGREIVFYKVIDYVLHGKEEIKVIPTPSADHWALASGLPSYVAESGFICNIMNASADEMFKFQEGALDDSGWLIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDEQDEVLMESLTQFLGWSVMNTDTYDKMNKLENRKDIAQDMVLYHVKCDRDEIQLILPTRARLGKEPADCDEDELGEILKEELPGPTTFDIYEFHFSDLECTELDLVKCGIQMYYELGVVRKFQIPQEVLVRFLFSISKGYRRITYHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDIDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKFLLSEETLNIYQNLNRRQHEHVIHLMDIAIIATDLALYFKKRAMFQKIVDESKNYQDKKSWVEYLSLETTRKEIVMAMMMTACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTVLDQQPIPMMDRNKAAELPKLQVGFIDFVCTFVYKEFSRFHEEILPMFDRLQNNRKEWKALADEYEAKVKALEEKEEEERVAAKKVGTEICNGGPAPKSSTCCIL | 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 phosphodiesterase holoenzyme (By similarity). Involved in retinal circadian rhythm photoentrainment via modulation of UVA and orange light-induced phase-shift of the retina clock (By similarity). May participate in processes of transmission and amplification of the visual signal .
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 98336
Sequence Length: 854
Subcellular Location: Membrane
EC: 3.1.4.35
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P23440 | MSLSEEQVRSFLDGNPTFAHQYFGKKLSPENVAGACEDGWLADCGSLRELCQVEESAALFELVQDMQESVNMERVVFKILRRLCTILHADRCSLFMYRQRNGIAELATRLFSVQPDSLLEDCLVPPDSEIVFPLDIGIVGHVAQTKKMINVQDVAECPHFSSFADELTDYVTKNILSTPIMNGKDVVAVIMAVNKLDGPCFTSEDEDVFTKYLNFATLNLKIYHLSYLHNCETRRGQVLLWSANKVFEELTDIERQFHKAFYTVRAYLNCERYSVGLLDMTKEKEFFDVWPVLMGEAQPYSGPRTPDGREIVFYKVIDYILHGKEDIKVIPTPPADHWALASGLPTYVAESGFICNIMNASADEMFNFQEGPLDDSGWVIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDDQDEVLMESLTQFLGWSVLNTDTYDKMNKLENRKDIAQDMVLYHVRCDKDEIQEILPTRDRLGKEPADCEEDELGKILKEELPGPTKFDIYEFHFSDLECTELELVKCGIQMYYELGVVRKFQIPQEVLVRFLFSVSKAYRRITYHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDIDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKFLLAEESLNIYQNLNRRQHEHVIHLMDIAIIATDLALYFKKRTMFQKIVDESKNYEDKKSWVEYLSLETTRKEIVMAMMMTACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTVLDQQPIPMMDRNKAAELPKLQVGFIDFVCTFVYKEFSRFHEEILPMFDRLQNNRKEWKALADEYEAKVKALEEEKKKEEDRVAAKKVGTEVCNGGPAPKSSTCCIL | 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 phosphodiesterase holoenzyme . Involved in retinal circadian rhythm photoentrainment via modulation of UVA and orange light-induced phase-shift of the retina clock . May participate in processes of transmission and amplification of the visual signal (By similarity).
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 98535
Sequence Length: 856
Subcellular Location: Membrane
EC: 3.1.4.35
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P16586 | MGEISQETVEKYLEANPQFAKEYFNRKLQVEVPSGGAQAPASASFPGRTLAEEAALYLELLEVLLEEAGSVELAAHRALQRLAQLLQADRCSMFLCRARNGTPEVASKLLDVTPTSKFEDNLVVPDREAVFPLDVGIVGWVAHTKKTFNVPDVKKNSHFSDFMDKQTGYVTRNLLATPIVMGKEVLAVFMAVNKVDASEFSKQDEEVFSKYLSFVSIILKLHHTNYLYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVRTYLNCERYSIGLLDMTKEKEFYDEWPVKLGEVEPYKGPKTPDGREVIFYKIIDYILHGKEEIKVIPTPPMDHWTLISGLPTYVAENGFICNMLNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEYDEHIAETLTQFLGWSLLNTDTYEKMNKLENRKDIAQEMLMNHTKATPDEIKSILKFKEKLNIDVIEDCEEKQLVTILKEDLPDPRTADLYEFRFRHLPITEHELIKCGLRLFFEINVVEKFKVPVEVLTRWMYTVRKGYRAVTYHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGSSILERHHLEYSKTLLQDESLNIFQNLNKRQYETVIHLFEVAIIATDLALYFKKRTMFQKIVDACEKMETEEEAIKYVTIDPTKKEIIMAMMMTACDLSAITKPWEVQSQVALLVANEFWEQGDLERTVLQQQPIPMMDRNKKDELPKLQVGFIDFVCTFVYKEFSRFHKEITPMLNGLQNNRVEWKSLADEYDEKMKVIEEMKKQEEGNTTEKAVEDSGGGGDDKKSKTCLML | 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 intracellular levels of cGMP.
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 98798
Sequence Length: 855
Subcellular Location: Cell membrane
EC: 3.1.4.35
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P51160 | MGEINQVAVEKYLEENPQFAKEYFDRKLRVEVLGEIFKNSQVPVQSSMSFSELTQVEESALCLELLWTVQEEGGTPEQGVHRALQRLAHLLQADRCSMFLCRSRNGIPEVASRLLDVTPTSKFEDNLVGPDKEVVFPLDIGIVGWAAHTKKTHNVPDVKKNSHFSDFMDKQTGYVTKNLLATPIVVGKEVLAVIMAVNKVNASEFSKQDEEVFSKYLNFVSIILRLHHTSYMYNIESRRSQILMWSANKVFEELTDVERQFHKALYTVRSYLNCERYSIGLLDMTKEKEFYDEWPIKLGEVEPYKGPKTPDGREVNFYKIIDYILHGKEEIKVIPTPPADHWTLISGLPTYVAENGFICNMMNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEHDEYITETLTQFLGWSLLNTDTYDKMNKLENRKDIAQEMLMNQTKATPEEIKSILKFQEKLNVDVIDDCEEKQLVAILKEDLPDPRSAELYEFRFSDFPLTEHGLIKCGIRLFFEINVVEKFKVPVEVLTRWMYTVRKGYRAVTYHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGSSILERHHLEYSKTLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDACEQMQTEEEAIKYVTVDPTKKEIIMAMMMTACDLSAITKPWEVQSQVALMVANEFWEQGDLERTVLQQQPIPMMDRNKRDELPKLQVGFIDFVCTFVYKEFSRFHKEITPMLSGLQNNRVEWKSLADEYDAKMKVIEEEAKKQEGGAEKAAEDSGGGDDKKSKTCLML | 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 intracellular levels of cGMP.
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 99147
Sequence Length: 858
Subcellular Location: Cell membrane
EC: 3.1.4.35
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Q91ZQ1 | MGEISQEAVERYLEKNPCFAKEYFDKKLRVEALGVIFKNSHAGVQTGLSLPEMTQVEESAVCLELLQCMQDEAGSAEQMAHRALQRLAQLLQADCCSMFSCRARNGIPEVASRLLNVTPTSKFEDNLVAPDREVVFPLDIGIVGWVAHVKKALNVSDVKKNSHFSDFMDKQTGYVTRNLLAVPIVAGKEVLAVVMAVNKISAPEFSKQDEEVFSKYLSFVAVALRLQHTSYLYSVESRRSQILMWSANKVFEELTDVERQFHKALYTIRTYLNCDRYSIGLLDMTKEKEFYDEWPIKLGEVEPYKGPKTPDGREIIFYKIIDYILHGKEEINVIPSPPADHWTLVSGLPTYVAENGFICNMLNAPADEYFTFQKGPVDETGWVIKNVLSLPIVNKKEDIVGVATFYNRKDGKPFDEHDEHITETLTQFLGWSLLNTDTYERVNKLESRKDIAQEMVMNLTKATPDEISSILKFKEKLNVEVIEECEERQLLAILKEDLPDPRTADLYEFCFSDFPITEHELVKCGLRLFLEINVVEKFKVPVEVLTRWMYTVRKGYRPVTYHNWRHGFNVGQTMFTLLMTGRLKKYYTDLEAFAMLAAAFCHDIDHRGTNNLYQMKSTSPLARLHGTSILERHHLEYSKTLLQDESLNIFQNLNKRQFETVIHLFEVAIIATDLALYFKKRTMFQKIVDTCEQMQSEEETIKYVTSDPTKKEVIMAMMMTACDLSAITKPWEVQSQVALLVANEFWEQGDLERTVLQQQPIPMMDRSKKDELPKLQVGFIDFVCTFVYKEFSRFHGEITPMLNGLQNNRVEWKSLAEEYEAKVKVTEEEAGKQEEEASDGKAATDLGGSAEDKKSKTCLML | 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 intracellular levels of cGMP.
Catalytic Activity: 3',5'-cyclic GMP + H2O = GMP + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 98785
Sequence Length: 861
Subcellular Location: Cell membrane
EC: 3.1.4.35
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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). Modulates the subcellular location of target proteins by acting as a GTP specific dissociation inhibitor (GDI) (By similarity). Increases the affinity of ARL3 for GTP by several orders of magnitude. Stabilizes ARL3-GTP by decreasing the nucleotide dissociation rate (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17390
Sequence Length: 150
Subcellular Location: Cytoplasm
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Q9XI01 | MAMRGFTLFSILVLSLCASSIRSEETETKEFVLTLDHTNFTDTINKHDFIVVEFYAPWCGHCKQLAPEYEKAASALSSNVPPVVLAKIDASEETNREFATQYEVQGFPTIKIFRNGGKAVQEYNGPREAEGIVTYLKKQSGPASAEIKSADDASEVVSDKKVVVVGIFPKLSGSEFDSFMAIAEKLRSELDFAHTSDAKLLPRGESSVTGPVVRLFKPFDEQFVDSKDFDGEALEKFVKESSIPLITVFDKDPNNHPYVIKFFESTNTKAMLFINFTGEGAESLKSKYREVATSNKGQGLSFLLGDAENSQGAFQYFGLEESQVPLIIIQTADDKKYLKTNVEVDQIESWVKDFKDGKIAPHKKSQPIPAENNEPVKVVVSDSLDDIVLNSGKNVLLEFYAPWCGHCQKLAPILDEVAVSYQSDSSVVIAKLDATANDFPKDTFDVKGFPTIYFKSASGNVVVYEGDRTKEDFISFVDKNKDTVGEPKKEEETTEEVKDEL | 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 proteases during their trafficking to vacuoles.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 55602
Sequence Length: 501
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.3.4.1
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Q9SRG3 | MAFKGFACFSILLLLSLFVSSIRSEETKEFVLTLDHSNFTETISKHDFIVVEFYAPWCGHCQKLAPEYEKAASELSSHNPPLALAKIDASEEANKEFANEYKIQGFPTLKILRNGGKSVQDYNGPREAEGIVTYLKKQSGPASVEIKSADSATEVVGEKNVVAVGVFPKLSGDEFDSFMALAEKLRADYDFAHTLDAKFLPRGESVEGPAVRLFKPFDELFVDSKDFNGEALEKFVKESSIPLVTVFDSDPNNHPYVAKFFESPATKAMMFVNFTGATAEALKSKYREVATSNKDQSLAFLVGDAESSQGAFQYFGLEESQVPLIIIQTPDNKKYLKVNVEVDQIESWFKDFQDGKVAVHKKSQPIPAENNEPVKVVVAESLDDIVFKSGKNVLIEFYAPWCGHCQKLAPILDEVALSFQNDPSVIIAKLDATANDIPSDTFDVKGFPTIYFRSASGNVVVYEGDRTKEDFINFVEKNSEKKPTSHGEESTKSEEPKKTEETAAKDEL | 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: Endoplasmic reticulum lumen
EC: 5.3.4.1
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Q9FF55 | MAFRVLLLFSLTALLIFSAVSPSFAASSSDDVDDEDLSFLEDLKEDDVPGADSLSSSTGFDEFEGGEEEDPDMYNDDDDEEGDFSDLGNPDSDPLPTPEIDEKDVVVIKERNFTDVIENNQYVLVEFYAPWCGHCQSLAPEYAAAATELKEDGVVLAKIDATEENELAQEYRVQGFPTLLFFVDGEHKPYTGGRTKETIVTWVKKKIGPGVYNLTTLDDAEKVLTSGNKVVLGYLNSLVGVEHDQLNAASKAEDDVNFYQTVNPDVAKMFHLDPESKRPALVLVKKEEEKISHFDGEFVKSALVSFVSANKLALVSVFTRETAPEIFESAIKKQLLLFVTKNESEKVLTEFQEAAKSFKGKLIFVSVDLDNEDYGKPVAEYFGVSGNGPKLIGYTGNEDPKKYFFDGEIQSDKIKIFGEDFLNDKLKPFYKSDPIPEKNDEDVKIVVGDNFDEIVLDDSKDVLLEVYAPWCGHCQALEPMYNKLAKHLRSIDSLVITKMDGTTNEHPKAKAEGFPTILFFPAGNKTSEPITVDTDRTVVAFYKFLRKHATIPFKLEKPASTESPKTAESTPKVETTETKESPDSTTKSSQSDSKDEL | 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: Endoplasmic reticulum lumen
EC: 5.3.4.1
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Q67IX6 | MRSRSLLLVALATLLLHASASASDDDLDYLIDNADDIPANDPDGWLQEGSPDDDDDDDLFHHGQAQDHPIDETHVFLLSAANFSDFLASHRHVMVEFYAPWCAHCQALAPDYAAAAADLSPLAHQVALAKVDATEDTDLAQKYDVQGFPTILFFIDGVPKDYNGARTKEAIVSWVNKKLAPGVQNITTVDEAEKILTGEDKAILAVLDSLSGAHSDEIAAASRLEDAINFYQTSNPDVAKLFHLDPAAKRPSLVLLKKQEEEKLTFYDGPFKASAIADFVSANKLPLVNTLTQETAPSIFDNPIKKQILLFVVANESSKFLPIFKEASKSFKGKLLFVFVERDNEEVGEPVANYFGITGQETTVLAYTGNEDARNFFLDGEISVENIKRFAEDFLEEKLTPFYKSEPVPESNEGDVKIVVGKNLDQIVLDESKDALLEIYAPWCGHCQELEPTYNKLGKHLRGIDSLVIAKMDGTANEHPRAKPDGFPTILFYPAGKKSFEPITFEGDRTVVEMYKFIKKHASIPFKLKRPDSSATKTEKDQSTASTNLRGERSSGTNFKDEL | 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.
Sequence Mass (Da): 62253
Sequence Length: 563
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.3.4.1
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A3KPF5 | MSLIPKPISKVSTFTFILLILLSFTIIIAYSSPDSNVESNEPGFDSDLDQLLAVDEQLQEDRPEQQSEAETVSKAQRIVLELNGDYTKRVIDGNEFVMVLGYAPWCARSAELMPRFAEAATALKEIGSSVLMAKIDGDRYSKIASELEIKGFPTLLLFVNGTSLTYNGGSSAEDIVIWVQKKTGAPIITLNTVDEAPRFLDKYHTFVLGLFEKFEGSEHNEFVKAAKSDDEIQFIETRDSDVAKLLFPDLKSNNVFIGLVKPEAERYTVYDGSYKMEKILEFLGSNKFPLFTKLTETNTVWVYSSPVKLQVMLFSKADDFQKLAQPLEDIARKFKSKLMFIYVDITNENLAMPFLILFGIEAGNKTVVAAFDNNLNSKYLLESDPSPNSIEEFCSGLAHGTVSRYYRSEPVPDNENASIVTVVGKTFDGLVLNSRENVLLEVHTPWCVNCEALSKQIEKLAKHFKGFENLVFARIDASANEHTKLQVDDKYPIILLYKSGEKEKPLKLSTKLSAKDIAVFINEELLKPKNGSAKDEL | 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: Endoplasmic reticulum lumen
EC: 5.3.4.1
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Q5WA72 | MRARRVVAAAAVLLLFAVVAVARLDLDDDGDDSEVLDELLAVDEEEERGELGGGGEAAAAEAVRRAQSMVLVLDNDNARRAVEENAEVLLLGYAPWCERSAQLMPRFAEAAAALRAMGSAVAFAKLDGERYPKAASAVGVKGFPTVLLFVNGTEHQFTGLHTKDAIVTWVRKKTGAPASRIQSKDSAEEFLKKDQTFAVGLFKNFEGAEYEEFVKAATSENEVQFVETNDRNVAKILFPGIASEEQFLGLVKSEPEKFEKFNGAFEEKEIIQFVELNKFPLITVFTDLNSGKVYGSPIKLQVFTFAEAYDFEDLESMIQEVARGFKTKIMLIYVDTAEEKLAKPFLTLYGLEPEKPTVTAFDTSKGTKYLMEAEINAKNLQDFCLSLLEGTLPPYFRSEPVPEEKGPIEKVVGRTFDSSVLESPQNVFLEVHAPWCVDCEAISKNVEKLAKHFNDLGQTNLKFARIDASVNEHPKLQINNYPTLLLYPAQDKSNPIKLSKKSNLKDMAKFVKEKLQIADVETVAAGDIVKDEL | 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.
Sequence Mass (Da): 59032
Sequence Length: 533
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.3.4.1
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Q17967 | MSLSVSFIFLLVASIGAVVADSENVLVLTESNFEETINGNEFVLVKFYAPWCVHCKSLAPKYDEAADLLKEEGSDIKLAKVDATENQALASKFEVRGYPTILYFKSGKPTKYTGGRATAQIVDWVKKKSGPTVTTVESVEQLEELKGKTRVVVLGYFKDAKSDAATIYNEVADSVDDAFFAVAGSAEVAAAASLNEDGVALIRTDGDDSETSTIAEAEITNTIALKQWLHAYKLSAVTEFTHESAQEIVGGDLKKFHFLIIRKSDSSFDETIAKFTEVAKKFRAKIVFVLLDVDVEENARILEFLGVDAKNTPANRIVSLADQVEKFKPQEGEDFEAFTNSYLEGKSAQDLKAQDLPEDWNALPVKVLVASNFNEIALDETKTVFVKFYAPWCGHCKQLVPVWDELAEKYESNPNVVIAKLDATLNELADVKVNSFPTLKLWPAGSSTPVDYDGDRNLEKFEEFVNKYAGSASESETASQDHEEL | 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
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Q86IA3 | MKILLFVTLIALAFVALCSAEGNVVVLSPDNFDTVVDGSKTVFVKFYAPWCGHCKKLAPDFEILADTFAPVSNKVVIAKVDCDQADNKALCSKYDVSGYPTLKIFDKSTTAKDYNGARSVDELLTYINNHAKTNVKVKKAPSNVVDLSPSNFDSVVLDKSKNVLVEFYAPWCGHCKKLMPDYEILGNTYANEKDVVIAKIDCDAADNKAICSKYGVTGFPTLKWFGKQSKDGEKYEQGRDLDTFINYINKQAGVNRVKGGKLAVGAGRVEQLDTIATEFIAAAAEVRKELVKKAQTVVDSLPEELRTEGSYYVKVMKTIAEKSIDFVTTEIARITKLVSGSMSGKKADEFAKKLNILESFKSK | 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 reticulum lumen
EC: 5.3.4.1
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Q10057 | MKISNLLAAFLAFSGGFFCASAEVPKVNKEGLNELITADKVLMVKFYAPWCGHCKALAPEYESAADELEKDGISLVEVDCTEEGDLCSEYSIRGYPTLNVFKNGKQISQYSGPRKHDALVKYMRKQLLPTVKPISKDTLENFVEKADDLAVVAFFKDQKLNDTYTEVAEVMKDDFVFAASDDKELAKSLGSNFPGIVAFTKDAAQDSDKLVYTGDWDPASIADFIGVSSIPLLDELNQMTFGKYQQSGLPLGIIFYNSTESRDELYDVFQPLAKKYQDTLRFAFLDAVRYGAVAKQMNVESDWPAFVIANLKSMLKYPFPTTELTAKAMTKFVGDFVDGKLQPKIKSQPIPESQEDLVVLVADNFDDIVMDETKDVLVEFYAPWCGHCKNLAPTYEKLAEEYSDDSNVVVAKIDATENDISVSISGFPTIMFFKANDKVNPVRYEGDRTLEDLSAFIDKHASFEPIKKEKESVPAPDLEDQVAVEDEMADEL | 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 reticulum lumen
EC: 5.3.4.1
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O22263 | MAKSQIWFGFALLALLLVSAVADDVVVLTDDSFEKEVGKDKGALVEFYAPWCGHCKKLAPEYEKLGASFKKAKSVLIAKVDCDEQKSVCTKYGVSGYPTIQWFPKGSLEPQKYEGPRNAEALAEYVNKEGGTNVKLAAVPQNVVVLTPDNFDEIVLDQNKDVLVEFYAPWCGHCKSLAPTYEKVATVFKQEEGVVIANLDADAHKALGEKYGVSGFPTLKFFPKDNKAGHDYDGGRDLDDFVSFINEKSGTSRDSKGQLTSKAGIVESLDALVKELVAASEDEKKAVLSRIEEEASTLKGSTTRYGKLYLKLAKSYIEKGSDYASKETERLGRVLGKSISPVKADELTLKRNILTTFVASS | 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
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Q9MAU6 | MERKMYKSTVFPICCLLFALFDRGNALYGSSSPVLQLTPSNFKSKVLNSNGVVLVEFFAPWCGHCQSLTPTWEKVASTLKGIATVAAIDADAHKSVSQDYGVRGFPTIKVFVPGKPPIDYQGARDAKSISQFAIKQIKALLKDRLDGKTSGTKNGGGSSEKKKSEPSASVELNSSNFDELVTESKELWIVEFFAPWCGHCKKLAPEWKKAANNLKGKVKLGHVNCDAEQSIKSRFKVQGFPTILVFGSDKSSPVPYEGARSASAIESFALEQLESNAGPAEVTELTGPDVMEDKCGSAAICFVSFLPDILDSKAEGRNKYLEMLLSVADKFKKDPYGFVWVAAGKQPDLEKRVGVGGYGYPAMVALNAKKGAYAPLKSGFEVKHLKDFVKEAAKGGKGNLPIDGTMEIVKTEAWDGKDGEVVDADEFSLEDLMGNDDEASTESKDDL | 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: Endoplasmic reticulum lumen
EC: 5.3.4.1
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O48773 | MYKSPLTLLTLLTICFGFFDLSSALYGSSSPVVQLTASNFKSKVLNSNGVVLVEFFAPWCGHCKALTPTWEKVANILKGVATVAAIDADAHQSAAQDYGIKGFPTIKVFVPGKAPIDYQGARDAKSIANFAYKQIKGLLSDRLEGKSKPTGGGSKEKKSEPSASVELNASNFDDLVIESNELWIVEFFAPWCGHCKKLAPEWKRAAKNLQGKVKLGHVNCDVEQSIMSRFKVQGFPTILVFGPDKSSPYPYEGARSASAIESFASELVESSAGPVEVTELTGPDVMEKKCGSAAICFISFLPDILDSKAEGRNKYLEMLLSVAEKFKKQPYSFMWVAAVTQMDLEKRVNVGGYGYPAMVAMNVKKGVYAPLKSAFELQHLLEFVKDAGTGGKGNVPMNGTPEIVKTKEWDGKDGELIEEDEFSLDELMGGDDAVGSKDEL | 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: Endoplasmic reticulum lumen
EC: 5.3.4.1
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Q9XF67 | MLAMEKEFDSKLVLQGNSSNGANVSRSKSFSFKAPQENFTSHDFEFGKIYGVGSYSKVVRAKKKETGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYMALESCEGGELFDQITRKGRLSEDEARFYTAEVVDALEYIHSMGLIHRDIKPENLLLTSDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTEPSRRPGAGSEGYVALKRHPFFNGVDWKNLRSQTPPKLAPDPASQTASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSITRLASIDSFDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPKLIYVDPSKLVVKGNIIWSDNSNDLNVVVTSPSHFKICTPKKVLSFEDAKQRASVWKKAIETLQNR | 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 signaling processes controlling the pathogen/stress response, polar auxin transport and development. Transphosphorylates the AGC protein kinases OXI1/AGC2-1, PK1/S6K1, PK19/S6K2 and PID resulting in their activation.
PTM: Phosphorylation on Thr-211 in the activation loop is required for full activity. PDK1 itself can autophosphorylate Thr-211, leading to its own activation.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54711
Sequence Length: 491
Domain: The PH domain is responsible for the interaction with the 3-phosphoinositides. The activation loop within the kinase domain is the target of phosphorylation. The PIF-binding region in the kinase domain of PDK1 acts as a docking site, enabling it to interact with and enhance the phosphorylation of substrates containing the PIF motif.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9Y1J3 | MEDLTPTNTSLDTTTTNNDTTSDREAAPTTLNLTPTASESENSLSPVTAEDLIAKSIKEGCPKRTSNDFMFLQSMGEGAYSQVFRCREVATDAMFAVKVLQKSYLNRHQKMDAIIREKNILTYLSQECGGHPFVTQLYTHFHDQARIYFVIGLVENGDLGESLCHFGSFDMLTSKFFASEILTGLQFLHDNKIVHRDMKPDNVLIQKDGHILITDFGSAQAFGGLQLSQEGFTDANQASSRSSDSGSPPPTRFYSDEEVPEENTARRTTFVGTALYVSPEMLADGDVGPQTDIWGLGCILFQCLAGQPPFRAVNQYHLLKRIQELDFSFPEGFPEEASEIIAKILVRDPSTRITSQELMAHKFFENVDWVNIANIKPPVLHAYIPATFGEPEYYSNIGPVEPGLDDRALFRLMNLGNDASASQPSTFRPSNVEHRGDPFVSEIAPRANSEAEKNRAARAQKLEEQRVKNPFHIFTNNSLILKQGYLEKKRGLFARRRMFLLTEGPHLLYIDVPNLVLKGEVPWTPCMQVELKNSGTFFIHTPNRVYYLFDLEKKADEWCKAINDVRKRYSVTIEKTFNSAMRDGTFGSIYGKKKSRKEMMREQKALRRKQEKEEKKALKAEQVSKKLSMQMDKKSP | 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): 71917
Sequence Length: 636
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 can accommodate small compounds acting as allosteric inhibitors.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9W0V1 | MKCKSWSNKINNYVVRKIKSIKINGTQQQLQLPGSGASGIAAAAVITVASDCGENCSSNGTEHQQHFNIATTTATSATEATMPAMAKEKASATVSLGESNFRDINLKDLAVVVEAASRLHHQQNVCGCGAVSSTENNNNSRYGSSKYLTNGHTSPLAAAVASNSSSVATTPHCRMLHNCSLQQYQNDIRQQTEILDMLRQQHQQGYQSQQQQQQPQQQQEQQQQQEQSQQQQQLQNPAPRRSPNDFIFGRYIGEGSYSIVYLAVDIHSRREYAIKVCEKRLILRERKQDYIKREREVMHQMTNVPGFVNLSCTFQDQRSLYFVMTYARKGDMLPYINRVGSFDVACTRHYAAELLLACEHMHRRNVVHRDLKPENILLDEDMHTLIADFGSAKVMTAHERALATEHCSEQRRSNSDEDDEDSDRLENEDEDFYDRDSEELDDGDDEQQQEEMDSPRHRQRRYNRHRKASFVGTAQYVSPEVLQNGPITPAADLWALGCIVYQMIAGLPPFRGSNDYVIFKEILDCAVDFPQGFDKDAEDLVRKLLRVDPRDRLGAQDEFGYYESIRAHPFFAGIDWQTLRQQTPPPIYPYLPGVSQDEDFRSSYTVPGDLEPGLDERQISRLLSAELGVGSSVAMPVKRSTAKNSFDLNDAEKLQRLEQQKTDKWHVFADGEVILKKGFVNKRKGLFARKRMLLLTTGPRLIYIDPVQMIKKGEIPWSPDLRAEYKNFKIFFVHTPNRTYYLDDPEGYAIHWSEAIENMRKLAYGDPSSTSAVSCSSGSSNSLAVISNSSAASSSNSPTVKRSSPVNAPQASTASDNRTLGSTRTGTSPSKKTASK | 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.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 94079
Sequence Length: 836
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 can accommodate small compounds acting as allosteric inhibitors.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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O15530 | MARTTSQLYDAVPIQSSVVLCSCPSPSMVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGCMQVSSSSSSHSLSASDTGLPQRSGSNIEQYIHDLDSNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQRYQSHPDAAVQ | 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), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive.
PTM: Phosphorylation on Ser-241 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-241, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 (By similarity). Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-241 and palmitate-induced phosphorylation at Ser-529 and Ser-501 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-354 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-394 and Ser-398 by MAP3K5.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 63152
Sequence Length: 556
Domain: The PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q9Z2A0 | MARTTSQLYDAVPIQSSVVLCSCPSPSMVRSQTEPGSSPGIPSGVSRQGSTMDGTTAEARPSTNPLQQHPAQLPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMHIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYHFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFETITWENLHQQTPPKLTAYLPAMSEDDEDCYGNYDNLLSQFGFMQVSSSSSSHSLSTVETSLPQRSGSNIEQYIHDLDTNSFELDLQFSEDEKRLLLEKQAGGNPWHQFVENNLILKMGPVDKRKGLFARRRQLLLTEGPHLYYVDPVNKVLKGEIPWSQELRPEAKNFKTFFVHTPNRTYYLMDPSGNAHKWCRKIQEVWRQQYQSNPDAAVQ | 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), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages.
PTM: Phosphorylation on Ser-244 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-244, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 (By similarity). Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-376 and Tyr-379 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-244 and palmitate-induced phosphorylation at Ser-532 and Ser-504 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-357 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-397 and Ser-401 by MAP3K5 (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 63759
Sequence Length: 559
Domain: The PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q6A1A2 | MVRTQTESSTPPGIPGGSRQGPAMDGTAAEPRPGAGSLQHAQPPPQPRKKRPEDFKFGKILGEGSFSTVVLARELATSREYAIKILEKRHIIKENKVPYVTRERDVMSRLDHPFFVKLYFTFQDDEKLYFGLSYAKNGELLKYIRKIGSFDETCTRFYTAEIVSALEYLHGKGIIHRDLKPENILLNEDMYIQITDFGTAKVLSPESKQARANSFVGTAQYVSPELLTEKSACKSSDLWALGCIIYQLVAGLPPFRAGNEYLIFQKIIKLEYDFPEKFFPKARDLVEKLLVLDATKRLGCEEMEGYGPLKAHPFFESVTWENLHQQTPPKLTAYLPAMSEDDEDCYGNVSWPGWRARQVALGPPCTGLHARAPDPRVICSRKGRVSVPLRQACWWL | 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-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 44765
Sequence Length: 396
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 can accommodate small compounds acting as allosteric inhibitors.
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q54TW2 | MENIVITNTSGGGGGGVPSSSTDPPNNTTTTTATASAIDLNMSLSPFLSSPSLSSPSIQSAKKKTIEDFIIGKVLGEGSYGAVVLGTEKETQQQYAIKILEKKQIIKENKIKYVQIEKEIFCKSNHPNIVKLFFTFRSEQCLYYVLELCSQGDLLHQIKKVGSFDYRSCQYYVAEIISGLEHLHSLGIVHRDLKPENILMSSDLHVKITDFGTGKILPPPQSSQQQQQQQQQQQQLPTNSSGNLSSLLNNVNNLSVSTDLTQQQQNRTSSVDSASTTDSMISPNLQPTTTTTNNNNNNNNNNNNNNNNTAAGSNTNTNTNTNINTNINANINNIKTTEIPKLTRNNSFVGTAEYVSPELISNKETSTDSDLWALGCIIYQMASGRVPFRGKTEFLTFQKVSNRELVYPINMNPVIKDLVEKLLVIKPTDRLGSSSTPGGFDNLKAHPFFQDFNWSSLSNMSHPPPPIQPPQEKIIFDGDELFSPSLDCTTPRNNNVDENHQQNSCNNNNNNNNNINNINNNNNSSSNNISNSNSNSNSSNNLNISNGNLSTPRSSSSSSSQQPTQRSGSSGGSRDGGSSSNNISKWLNNGENVIYQGLVWKRKGFSIKKRQLILTDTPRLIYIDPKKMELKGEIPWSDSIKPKLKSNNNFVIKTPKRKYLLEDVAHNPQKWVDSIKSVILSSGSSN | 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 can accommodate small compounds acting as allosteric inhibitors.
EC: 2.7.11.1
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