| Identification |
|---|
| 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
|
|
|
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 |
