UniProt Accession

 PARP1_RAT; P27008; O35937 

Genbank Protein ID

 U94340; BC085765; X65496; X65497 

Genbank Nucleotide ID

 AAC53544.1; AAH85765.1; CAA46477.1; CAA46478.1 

Protein Name

 Poly [ADP-ribose] polymerase 1 

Protein Synonyms/Alias

 PARP-1; ADP-ribosyltransferase diphtheria toxin-like 1; ARTD1; NAD(+) ADP-ribosyltransferase 1; ADPRT 1; Poly[ADP-ribose] synthase 1 

Gene Name

 Parp1 

Gene Synonyms/Alias

 Adprt 

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
621	FMKLYEEKTGNAWHS	acetylation	[1]
940	KHASHISKLPKGKHS	acetylation	[1]
949	PKGKHSVKGLGKTAP	acetylation	[1]

Reference

 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

Functional Description

 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. Mediates the poly(ADP- ribosyl)ation of APLF and CHFR. 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 (By similarity). Required for PARP9 and DTX3L recruitement 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). 

Sequence Annotation

 DOMAIN 386 477 BRCT.
 DOMAIN 662 779 PARP alpha-helical.
 DOMAIN 788 1014 PARP catalytic.
 DNA_BIND 2 373
 ZN_FING 9 93 PARP-type 1.
 ZN_FING 113 203 PARP-type 2.
 REGION 374 524 Automodification domain.
 MOTIF 207 209 Nuclear localization signal.
 MOTIF 221 226 Nuclear localization signal.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 41 41 Phosphoserine (By similarity).
 MOD_RES 97 97 N6-acetyllysine (By similarity).
 MOD_RES 105 105 N6-acetyllysine (By similarity).
 MOD_RES 131 131 N6-acetyllysine (By similarity).
 MOD_RES 179 179 Phosphoserine (By similarity).
 MOD_RES 408 408 PolyADP-ribosyl glutamic acid
 MOD_RES 414 414 PolyADP-ribosyl glutamic acid
 MOD_RES 436 436 PolyADP-ribosyl glutamic acid
 MOD_RES 438 438 PolyADP-ribosyl glutamic acid
 MOD_RES 445 445 PolyADP-ribosyl glutamic acid
 MOD_RES 446 446 PolyADP-ribosyl glutamic acid
 MOD_RES 457 457 PolyADP-ribosyl glutamic acid
 MOD_RES 485 485 PolyADP-ribosyl glutamic acid
 MOD_RES 489 489 PolyADP-ribosyl glutamic acid
 MOD_RES 492 492 PolyADP-ribosyl glutamic acid
 MOD_RES 513 513 PolyADP-ribosyl glutamic acid
 MOD_RES 514 514 PolyADP-ribosyl glutamic acid
 MOD_RES 520 520 PolyADP-ribosyl glutamic acid
 MOD_RES 600 600 N6-acetyllysine (By similarity).
 MOD_RES 621 621 N6-acetyllysine (By similarity).
 MOD_RES 782 782 Phosphoserine (By similarity).  

Keyword

 3D-structure; Acetylation; ADP-ribosylation; Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosyltransferase; Metal-binding; NAD; Nucleus; Phosphoprotein; Reference proteome; Repeat; S-nitrosylation; Transcription; Transcription regulation; Transferase; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1014 AA 

Protein Sequence

Gene Ontology

 GO:0005635; C:nuclear envelope; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:BHF-UCL.
 GO:0005667; C:transcription factor complex; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0051287; F:NAD binding; IDA:RGD.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IMP:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006284; P:base-excision repair; IEA:Compara.
 GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
 GO:0042769; P:DNA damage response, detection of DNA damage; IDA:RGD.
 GO:0006302; P:double-strand break repair; ISS:UniProtKB.
 GO:0060391; P:positive regulation of SMAD protein import into nucleus; IMP:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:BHF-UCL.
 GO:0016540; P:protein autoprocessing; IDA:RGD.
 GO:0070212; P:protein poly-ADP-ribosylation; IMP:BHF-UCL.
 GO:0040009; P:regulation of growth rate; IEA:Compara.
 GO:0023019; P:signal transduction involved in regulation of gene expression; IMP:BHF-UCL.
 GO:0000723; P:telomere maintenance; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL. 

Interpro

 IPR001357; BRCT_dom.
 IPR008288; NAD_ADPRT.
 IPR012982; PADR1.
 IPR012317; Poly(ADP-ribose)pol_cat_dom.
 IPR004102; Poly(ADP-ribose)pol_reg_dom.
 IPR008893; WGR_domain.
 IPR001510; Znf_PARP. 

Pfam

 PF00533; BRCT
 PF08063; PADR1
 PF00644; PARP
 PF02877; PARP_reg
 PF05406; WGR
 PF00645; zf-PARP 

SMART

 SM00292; BRCT
 SM00773; WGR 

PROSITE

 PS50172; BRCT
 PS51060; PARP_ALPHA_HD
 PS51059; PARP_CATALYTIC
 PS00347; PARP_ZN_FINGER_1
 PS50064; PARP_ZN_FINGER_2 

PRINTS