poly [ADP-ribose] polymerase 1 selections

poly [ADP-ribose] polymerase 1; PARP-1; NAD(+) ADP-ribosyltransferase 1; ADPRT 1; poly[ADP-ribose] synthase 1 (PARP1, ADPRT, PPOL)

also see poly[ADP-ribose]polymerase Function: - role in the base excision repair pathway, by catalyzing poly-ADP-ribosylation of a limited number of acceptor proteins involved in chromatin architecture & in DNA metabolism - poly-ADP-ribosylation follows DNA damage & appears as an obligatory step in a detection/signaling pathway leading to repair of DNA double-strand breaks - mediates poly-ADP-ribosylation of APLF & CHFR - positively regulates transcription of MTUS1 & negatively regulates transcription of MTUS2/TIP150 - with EEF1A1 & TXK, forms a complex that acts as a Th1 cell-specific transcription factor & binds the promoter of IFN-gamma to directly regulate its transcription, & thus seves a role in Th1 cytokine production - phosphorylated by PRKDC & TXK - phosphorylated upon DNA damage, probably by ATM or ATR - poly-ADP-ribosylated by PARP2 - poly-ADP-ribosylation mediates recruitment of CHD1L to DNA damage sites - S-nitrosylated, inhibiting of transcription (putative) - component of a base excision repair complex - homodimer & heterodimer with PARP2 - interacts with PARP3, APTX & SRY - component of SWAP complex - interacts with TIAM2 & ZNF423 (putative) - interacts (when poly-ADP-ribosylated) with CHD1L - interacts with DNA polymerase alpha catalytic subunit POLA1; - interaction functions in replication fork progression - interacts with EEF1A1, RNF4 & TXK Structure: - contains 1 BRCT domain - contains 1 PARP alpha-helical domain - contains 1 PARP catalytic domain - contains 2 PARP-type Zn⁺² fingers Compartment: nucleus Notes: - the ADP-D-ribosyl group of NAD⁺ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, & 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

General

NAD+ ADP-ribosyltransferase or poly ADP-ribose polymerase

Properties

SIZE: entity length = 1014 aa MW = 113 kD COMPARTMENT: cell nucleus MOTIF: DNA-binding motif SITE: 2-372 acetylation site SITE: N-TERMINUS EFFECTOR-BOUND: acetyl Zn finger PARP-type NAME: Zn finger PARP-type SITE: 9-93 EFFECTOR-BOUND: Zn+2 MOTIF: Ser phosphorylation site {S41} Zn finger PARP-type NAME: Zn finger PARP-type SITE: 113-203 EFFECTOR-BOUND: Zn+2 MOTIF: Ser phosphorylation site {S179} nuclear translocation signal {207-209} nuclear translocation signal {221-226} Thr phosphorylation site {T368} Automodification {373-524} MOTIF: BRCA1 C-terminal (BRCT) motif SITE: 385-476 PARP alpha-helical {662-779} Ser phosphorylation site {S782} catalytic domain SITE: 788-1014

References

UniProt :accession P09874
NIEHS-SNPs http://egp.gs.washington.edu/data/adprt/

Component-of

base excision repair (BER) complex

Databases & Figures

OMIM 173870 UniProt P09874 PFAM correlations Entrez Gene 142 Kegg hsa:142 ENZYME 2.4.2.30 Mechanism of base excision repair (v.2)

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