Showing Protein Poly [ADP-ribose] polymerase 1 (BMDBP00832)
Identification | |
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BMDB Protein ID | BMDBP00832 |
Secondary Accession Numbers | None |
Name | Poly [ADP-ribose] polymerase 1 |
Synonyms | Not Available |
Gene Name | PARP1 |
Protein Type | Enzyme |
Biological Properties | |
General Function | Involved in DNA binding |
Specific Function | Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of glutamate and aspartate 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. Mediates the poly(ADP-ribosyl)ation of a number of proteins, including itself, APLF and CHFR. Also mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity. Probably also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1. Catalyzes the poly-ADP-ribosylation of histones in a HPF1-dependent manner. Involved in the base excision repair (BER) pathway by catalyzing the poly-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. ADP-ribosylation follows DNA damage and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. 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. 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. Acts as a regulator of transcription: positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. With EEF1A1 and TXK, forms a complex that acts as a T-helper 1 (Th1) cell-specific transcription factor and binds the promoter of IFN-gamma to directly regulate its transcription, and is thus involved importantly in Th1 cytokine production. 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. |
Pathways | Not Available |
Reactions | Not Available |
GO Classification | Not Available |
Cellular Location | Not Available |
Gene Properties | |
Chromosome Location | 16 |
Locus | Not Available |
SNPs | PARP1 |
Gene Sequence |
>3051 bp ATGGCGGAGTCTTCAGACAAGCTCTACCGGGTCGAGTACGCCAAGAGCGGGCGCGCGTCT TGCAAGAAATGCAAAGAGAGCATCCCCAAGGACTCGATCCGGATGGCCTTCATGGTGGAG TCGCCCATGTTCGATGGGAAAATCCCGCACTGGTACCACCTCTCCTGCTTCTGGAAGGTC GGCTTCTCCATCTGGCACCCTGATGTCGAGGTGGAGGGGTTCTCTGAGCTCCGCTGGGAT GACCAGCAGACGATCAAGAAGATGGCCGAGACTGGCGGACGGACAGATGTTTCAGGCAAA GGCCAAGATGGAGTTGGCAGCAAGACCGAGAAGACGTTGATTGACTTCGGGGCAGGGTAC GCCAAGTCCAACAGAAGCACGTGCAAGAGCTGCATGGAGAAGATAGACAAGGGCCAGGTG CGCCTGTCTAAGAAGGTGGTGTACCCCGATAAGCCCCAGCTGGGCATGGTTGACTGCTGG TACCACCCAAAGTGTTTTGTTCAGAAACGGGAGGAGCTGGGCTTCCGTCCCGAGTTCAGC GCAACGCACCTCATGGGCTTCAGCGTCCTCACCGCAGAGGACCAAGAAACCCTCAAGAAG CAACTCCCGGCCATCAAGGGTGAAAGAAAGAGAAAAGGTGATGAGGTGGATGGAATAGAT GAAGTGACCAAGAAGAAGTCTAAAAAAGAAAAAGACAAGGAGATTAAACTTGAAAAGGCC CTTAAGGCCCAGAACGACCTGATCTGGAATGTCAAGGACGAGCTAAAGAAAGCGTGCTCT ACGAACGACCTGAAAGAGTTGCTCATCTTCAACAAGCAGGAAGTGCCTTCCGGGGAGTCG GCGATCTTGGACCGCGTGGCCGACGGTATGGTGTTTGGCGCCCTCCTTCCCTGCGAGGAA TGCTCGGGCCAGCTGGTCTTCAAGGGCGACGCCTATTACTGTACCGGGGATGTGACTGCC TGGACCAAGTGTATGGTCAAGACACAGACGCCCAACCGGAAGGAGTGGGTGACCCCAAAG GAATTCCGAGAAATCTCTTACTTCAAGAAACTGAAGATCAAAAAGCAGGACCGTATATTC CCCCCAGAGAGCAGCACCCCAGTGGGGGCAGCAGCCCCACCCTCCGCAGCTTCAGCGCCT GCCGCTGTGCACTCTGGCCCCCCAGACAAGCCATTATCCAACATGAAGATCCTGACTCTC GGGAAACTCTCCCAGAACAAGGATGAAGTGAAGGCCACGATTGAGAAACTCGGGGGGAAA TTGACAGGGACGGCCAACAAGGCCTCCCTGTGTATCAGCACCAAAAAGGAGGTGGACAAG TTGAATAAAAAGATGGAGGAAGTAAAAGAAGCCAACATCCGTGTCGTGTCTGAGGACTTC CTCCAAGACATCTCCGCCTCCACCAAGAGCCTTCAGGAGTTGCTCTCCACCCACCTCTTG TCCCCCTGGGGAGCCGAGGTGAAGGTGGAGCCTGTTGAAGCAGTGGGCCCAAAGGGGAAG TCGGGGGCCGCGCCCTCCAAGAAGAGCAAGGGTCCCGTCAAGGAGGAAGGTACCAACAAA TCTGAAAAGAGGATGAAATTAACTCTTAAAGGAGGAGCAGCTGTCGACCCTGATTCAGGT CTGGAACACAATGCACACGTCCTCGAGAAAGGCGGGAAGGTCTTCAGCGCCACCCTCGGG CTCGTGGACATCGTCAAAGGGACCAACTCCTATTACAAGCTGCAGCTCCTGGAGGATGAC AAAGAGAGCAGGTACTGGATATTCAGGTCCTGGGGCCGTGTGGGCACGGTGATTGGTAGT AACAAACTGGAGCAGATGCCATCCAAGGAGGATGCCATTGAGCATTTTATGAAATTATAT GAAGAGAAAACCGGAAACGCCTGGCACTCTAAAAACTTTACGAAGCATCCCAAAAAGTTC TACCCTCTGGAGATTGACTACGGCCAGGATGAAGAGGCGGTGAAGAAGTTGACAGTAAAC CCTGGCACCAAGTCCAAGCTCCCCAAGCCAGTGCAGAACCTCATTAAGATGATCTTTGAT GTAGAGAGTATGAAGAAAGCCATGGTGGAGTATGAGATTGACCTTCAGAAGATGCCCTTG GGGAAGCTGAGCAAAAGGCAGATCCAGGCTGCATACTCCATCCTCAGTGAGGTCCAGCAG GCACTGTCCCAGGGCAGCAGTGACTCTCACATCCTGGATCTCTCCAACCGCTTCTACACC CTGATCCCCCACGACTTCGGGATGAAGAAGCCCCCGCTGCTGAACAACGCAAACAGCGTG CAGGCCAAGGTGGAAATGCTAGACAACCTGCTGGATATTGAGGTGGCCTACAGTCTACTT AGGGGTGGTTCTGATGACAGCAGCAAGGACCCCATTGATGTCAACTATGAGAAGCTCAAA ACTGACATTAAGGTTGTGGACAAAGATTCCGAAGAAGCCGAGATCATTAGGAAGTATGTG AAGAACACTCACGCGACCACACACAACGCGTACGACTTAGAAGTCGTCGACATCTTCAAG ATAGAGCGCGAAGGGGAAAGCCAGCGTTACAAGCCGTTTAAGCAGCTGCATAACCGGAGG CTGCTGTGGCACGGGTCCAGGACCACCAACTTCGCGGGCATCCTGTCCCAGGGTCTCCGG ATAGCCCCACCTGAAGCACCTGTGACGGGCTACATGTTTGGTAAGGGAATCTATTTCGCG GACATGGTCTCCAAGAGTGCCAACTACTGCCACACGTCCCAGGGAGACCCAATAGGCTTG ATCCTGTTGGGAGAAGCTGCCCTTGGAAACATGTATGAATTGAAACATGCTCGACATATC AGCAAGTTACCCAAGGGCAAGCACAGTGTCAAAGGTTTAGGCAAAACTACCCCTGACCCA TCGGCTAGTATTACTGTGGATGGTGTGGAGGTGCCTCTCGGGACAGGGATTTCATCTGGT GTTAATGACACCTGTCTGTTGTATAACGAGTACATCGTCTACGACATTGCTCAGGTCCAC CTGAAGTACCTGCTGAAGCTGAAGTTCAACTTTAAGACATCCCTGTGGTGA |
Protein Properties | |
Number of Residues | 1016 |
Molecular Weight | 113486.0 |
Theoretical pI | 9.3 |
Pfam Domain Function | Not Available |
Signals |
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Transmembrane Regions | Not Available |
Protein Sequence |
>Poly [ADP-ribose] polymerase 1 MAESSDKLYRVEYAKSGRASCKKCKESIPKDSIRMAFMVESPMFDGKIPHWYHLSCFWKV GFSIWHPDVEVEGFSELRWDDQQTIKKMAETGGRTDVSGKGQDGVGSKTEKTLIDFGAGY AKSNRSTCKSCMEKIDKGQVRLSKKVVYPDKPQLGMVDCWYHPKCFVQKREELGFRPEFS ATHLMGFSVLTAEDQETLKKQLPAIKGERKRKGDEVDGIDEVTKKKSKKEKDKEIKLEKA LKAQNDLIWNVKDELKKACSTNDLKELLIFNKQEVPSGESAILDRVADGMVFGALLPCEE CSGQLVFKGDAYYCTGDVTAWTKCMVKTQTPNRKEWVTPKEFREISYFKKLKIKKQDRIF PPESSTPVGAAAPPSAASAPAAVHSGPPDKPLSNMKILTLGKLSQNKDEVKATIEKLGGK LTGTANKASLCISTKKEVDKLNKKMEEVKEANIRVVSEDFLQDISASTKSLQELLSTHLL SPWGAEVKVEPVEAVGPKGKSGAAPSKKSKGPVKEEGTNKSEKRMKLTLKGGAAVDPDSG LEHNAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGS NKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFTKHPKKFYPLEIDYGQDEEAVKKLTVN PGTKSKLPKPVQNLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQ ALSQGSSDSHILDLSNRFYTLIPHDFGMKKPPLLNNANSVQAKVEMLDNLLDIEVAYSLL RGGSDDSSKDPIDVNYEKLKTDIKVVDKDSEEAEIIRKYVKNTHATTHNAYDLEVVDIFK IEREGESQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFA DMVSKSANYCHTSQGDPIGLILLGEAALGNMYELKHARHISKLPKGKHSVKGLGKTTPDP SASITVDGVEVPLGTGISSGVNDTCLLYNEYIVYDIAQVHLKYLLKLKFNFKTSLW |
External Links | |
GenBank ID Protein | BAA14114.1 |
UniProtKB/Swiss-Prot ID | P18493 |
UniProtKB/Swiss-Prot Entry Name | PARP1_BOVIN |
PDB IDs | |
GenBank Gene ID | D90073 |
GeneCard ID | PARP1 |
GenAtlas ID | Not Available |
HGNC ID | Not Available |
References | |
General References | Not Available |