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PARP3

Gene
PARP3
Protein
Protein ADP-ribosyltransferase PARP3
Organism
Oryza sativa subsp. japonica
Length
831 amino acids
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).
Mass
92.404 kDa
Sequence
MVHETRSRTLAASQEEGKAAPKKQKTESKEQEGGQQAPSKNKKTADNEEHDGEQEPSKNKKLKAEESDLNGKATAVKEFSEFCKAIREHLTIEDMRKILQGNEQDASGSEDAVVPRCEDVMFYGPLDKCPVCGGQLECKGLKYNCTGTHSEWACCSFSTNNPSRRGGPIKVPDDVKNDFVRKWLKQQEGNKYPKRNLDDEGIFSGMMIALSGRMSRSHGYFKEQIMKHGGKVNNSVIGVTCVVASPAERHQGGSGGFAEALERGTPVVSENWIIDSVQKKEKQPLAAYDIASDVVPEGRGLPLGNLDPTEEAIETLAAELKLAGKRAVHKDSKLEKDGGHIYEKDGIIYNCAFSVCDLGGDINQLCIMQLIMVPENHLHLYYKKGPIGHDQMAEERVEDFGSRFNDAIKEFVRLFEEVTGNEFEPWEREKKFKKKCMKMYPLDMDDGVDVRHGGVALRQLGAAAAHCKLDPSVTFIMKQLCSQEIYRYALTEMGHDVPDLPIGMLTDLHLKRGEETLLEWKQDVESAPESGPAADAFWMEISNKWFTLFPTTRPYTMKGYEQIADNVASGLETVRDINVASRLIGDVFGSTLDDPLSQCYKKLGCSINRVVEDSEDYKMILKYLEKTYEPVKVGDVVYSATVERIYAVESSALPSYDEIKKLPNKVLLWCGTRSSNLLRHLRDGFVPAVCHIPVPGYMFGKAIVCSDAAAEAALYGFTAVDRPEGYLVLAVASLGKEIQEITGTPGSEDVKRMEEKKMGVKGVGRKTTDPSEHFTWRDGVTVPCGKLVPSTNKDGPLEYNEYAVYDPKQVSIAFLVGVKYEEQNMEVVPDE

Gene
PARP3
Protein
Protein ADP-ribosyltransferase PARP3
Organism
Glycine max
Length
815 amino acids
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).
Mass
91.689 kDa
Sequence
MKVQETRSHVHALGEEEKVMTRKQKAESKAHEVEHSPKKAKVEKEDGHINGKSETGVAEEYDEFCKATTEHLPLEQMRDILEANGLDSSGSDLEITRRCQDLLFYGALDKCSVCNGSLEFDGRRYVCRGFYSEWASCTFSTRNPPRKQEPIKLPDSVQNSLASDLLKKYQDPSHRPHRDLGLAEKPFTGMMISLMGRLTRTHHYWKTTIEKHGGKVANSIIGSTCLVASPAERERGGTSKLAEAMERSIPVVREAWLIDSIEKQEPQPLEAYDLVSDLSVDGKGIPWDKQDPGEEAIESLSAELKLYGKRGVYKDTKLQEQGGKIFERDGILYNCAFSVCDQGRGLNDYCVMQLIVVPENRLHLYFKKGRVGDDPNAEERLEEWDNVDGALKEFVRLFEEITGNEFEPWEREKKFQKKPLKFYPIDMDDGIEVRHGALGLRQLGIAATHCKLEPLVANFMKVLCSQEIYKYALMEMGYDCPDLPIGMVTNLHLKKCEDVLLEFIDKVKSLKETGPKAEAVWTDFSQRWFTLMHSTRPFNFRDYQEIADHAAAALEGVRDITQASHLIGDMTGSTIDDPLSETYKKLGCSISALDKSSDDYEMIVKYLEKTYEPVKVGDIEYGVSVENIFAVQTGGCPSYEDIIKLPNKVLLWCGSRSSNLLRHLQKGFLPAICSLPIPGYMFGKAIVCSDAAAEAARYGFTAVDRPEGFLVLAIASLGNEITELKTPPEDASSLEEKKVGVKGPGKKKTDESEHFVWKDDIKVPCGKLVASDHQDSPLEYNEYAVYDKKRARISYLVGVKYEEKEEKGAVIDTAE

Gene
PARP3
Protein
Protein ADP-ribosyltransferase PARP3
Organism
Arabidopsis thaliana
Length
814 amino acids
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).
Mass
91.406 kDa
Sequence
MKVHETRSHAHMSGDEQKGNLRKHKAEGKLPESEQSQKKAKPENDDGRSVNGAGDAASEYNEFCKAVEENLSIDQIKEVLEINGQDCSAPEETLLAQCQDLLFYGALAKCPLCGGTLICDNEKRFVCGGEISEWCSCVFSTKDPPRKEEPVKIPDSVMNSAISDLIKKHQDPKSRPKRELGSADKPFVGMMISLMGRLTRTHQYWKKKIERNGGKVSNTVQGVTCLVVSPAERERGGTSKMVEAMEQGLPVVSEAWLIDSVEKHEAQPLEAYDVVSDLSVEGKGIPWDKQDPSEEAIESFSAELKMYGKRGVYMDTKLQERGGKIFEKDGLLYNCAFSICDLGKGRNEYCIMQLVTVPDSNLNMYFKRGKVGDDPNAEERLEEWEDEEAAIKEFARLFEEIAGNEFEPWEREKKIQKKPHKFFPIDMDDGIEVRSGALGLRQLGIASAHCKLDSFVANFIKVLCGQEIYNYALMELGLDPPDLPMGMLTDIHLKRCEEVLLEFVEKVKTTKETGQKAEAMWADFSSRWFSLMHSTRPMRLHDVNELADHAASAFETVRDINTASRLIGDMRGDTLDDPLSDRYKKLGCKISVVDKESEDYKMVVKYLETTYEPVKVSDVEYGVSVQNVFAVESDAIPSLDDIKKLPNKVLLWCGSRSSNLLRHIYKGFLPAVCSLPVPGYMFGRAIVCSDAAAEAARYGFTAVDRPEGFLVLAVASLGEEVTEFTSPPEDTKTLEDKKIGVKGLGRKKTEESEHFMWRDDIKVPCGRLVPSEHKDSPLEYNEYAVYDPKQTSIRFLVEVKYEEKGTEIVDVEPE

Gene
PARP3
Protein
Protein ADP-ribosyltransferase PARP3
Organism
Medicago truncatula
Length
799 amino acids
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).
Mass
89.991 kDa
Sequence
MKVESRSHNVHHAHGEEEKVMTRKQKAESKAHEVEHSPKKAKVEDEKNGHTNGKSASDVVQEYDEFCKATNEQLSLEQMKEILEANDLDSSGSDLEITRRCQDLLFFGALEKCMVCNGNMEFDGRRYGCRGFYSEWSSCTFSTREPPRKDEPIKLPDSVQNSPVSDLLKKYQDPSKRPQRDLGLAIKPFTGMMISLMGRLNRTHLNFSGASCLVASPAERDRGGTSKLADAMERGIPVVREAWLTDSIEKQEPQPLESYDLVSDLSVDGKGIPWDKQDPGEEAIESLSAELKLYGKRGVYKDTKLHEQDGKIFEKDGILYNCAFSLCDQGRKLNDYCVMQLIVVPENSLHLYFKKGRVGDDPSAEERLEECENVDNAIKEFVRLFEEITGNEFESWEREKKFQKKPLKFYPIDMDDGVEVRHGALGLRQLGIAATHCKLEPMVANFMKVLCSQEIYKYALMEMGYDSPDLPIGMVTNLHLKRCEEILLEFIEKVKTLKETGPKADAIWSDFSQKWFTLMHSTRPFIFRDYQEIADHAAAALEGVRDITLASHLIGDMSGSTIDDPLSDTYKKLGCSITPLEKNSNDYEMIVKYLEKTYEPVKVGDIEYGVSVENIFTVESSACPSYADIVKMPNKVLLWCGSRSSNLLRHLHKGFLPAICSLPVPGYMFGKAIVCSDAAAEAARYGFTAVDRPEGFLVLAIASLGNEITELKSPPEDTTSLEEKKVGVKGLGKKKTDESEHFVWKDDIKVPCGSIIASEHEDSPLEYNEYAVYDPKQVRISYLVGVKYEEKDAVIDTAE

Gene
PARP3
Protein
Protein mono-ADP-ribosyltransferase PARP3
Organism
Homo sapiens
Length
533 amino acids
Function
Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:16924674, PubMed:20064938, PubMed:21211721, PubMed:21270334, PubMed:25043379, PubMed:24598253). Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (PubMed:20064938, PubMed:25043379). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:25043379). Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334). Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (PubMed:21211721). Cooperates with the XRRC6-XRCC5 (Ku70-Ku80) heterodimer to limit end-resection thereby promoting accurate NHEJ (PubMed:24598253). Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as XRRC5 and XRCC6 (PubMed:16924674, PubMed:24598253). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (PubMed:16924674, PubMed:21211721, PubMed:21270334). May link the DNA damage surveillance network to the mitotic fidelity checkpoint (PubMed:16924674). In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks (PubMed:29361132, PubMed:29520010). Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin (By similarity).
Mass
60.089 kDa
Sequence
MAPKPKPWVQTEGPEKKKGRQAGREEDPFRSTAEALKAIPAEKRIIRVDPTCPLSSNPGTQVYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAEDEAQEAVVKVDRGPVRTVTKRVQPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLEELSSHFYTVIPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEQEKTVEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTGSNHRCPTLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVIGMKCGAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPTQDTELELDGQQVVVPQGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVHL

Gene
Parp3
Protein
Protein mono-ADP-ribosyltransferase PARP3
Organism
Mus musculus
Length
533 amino acids
Function
Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins and plays a key role in the response to DNA damage (PubMed:21270334, PubMed:24598253). Mediates mono-ADP-ribosylation of glutamate, aspartate or lysine residues on target proteins (By similarity). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (By similarity). Associates with a number of DNA repair factors and is involved in the response to exogenous and endogenous DNA strand breaks (PubMed:21270334). Together with APLF, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ) (By similarity). Cooperates with the XRRC6-XRCC5 (Ku70-Ku80) heterodimer to limit end-resection thereby promoting accurate NHEJ (PubMed:24598253). Involved in DNA repair by mediating mono-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism, such as XRRC5 and XRCC6 (By similarity). ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks (By similarity). May link the DNA damage surveillance network to the mitotic fidelity checkpoint (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: mediates DNA mono-ADP-ribosylation of DNA strand break termini via covalent addition of a single ADP-ribose moiety to a 5'- or 3'-terminal phosphate residues in DNA containing multiple strand breaks (By similarity). Acts as a negative regulator of immunoglobulin class switch recombination, probably by controlling the level of AICDA /AID on the chromatin (PubMed:26000965).
Mass
59.949 kDa
Sequence
MAPKRKASVQTEGSKKRRQGTEEEDSFRSTAEALRAAPADNRVIRVDPSCPFSRNPGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERDRFVAQPNKYTLIEVQGEAESQEAVVKALSPQVYSGPVRTVVKPCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVIPHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAAPGEEEEKVEEVPHPLDRDYQLLRCQLQLLDSGESEYKAIQTYLKQTGNSYRCPDLRHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHSGGRVGKGIYFASENSKSAGYVTTMHCGGHQVGYMFLGEVALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIELELDGQPVVVPQGPPVQCPSFKSSSFSQSEYLIYKESQCRLRYLLEIHL