CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003876
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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; msPARP 
Gene Name
 Parp1 
Gene Synonyms/Alias
 Adprp; Adprt; Adprt1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
97EAGGVAGKGQDGSGGacetylation[1]
148KKMVDPEKPQLGMIDacetylation[1]
414EAKAVIEKLGGKLTGacetylation[1]
418VIEKLGGKLTGSANKacetylation[1]
547HSAHVLEKGGKVFSAubiquitination[2]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 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). 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. 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 385 476 BRCT.
 DOMAIN 661 778 PARP alpha-helical.
 DOMAIN 787 1013 PARP catalytic.
 DNA_BIND 2 372
 ZN_FING 9 93 PARP-type 1.
 ZN_FING 113 203 PARP-type 2.
 REGION 373 523 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 407 407 PolyADP-ribosyl glutamic acid
 MOD_RES 413 413 PolyADP-ribosyl glutamic acid
 MOD_RES 435 435 PolyADP-ribosyl glutamic acid
 MOD_RES 437 437 PolyADP-ribosyl glutamic acid
 MOD_RES 444 444 PolyADP-ribosyl glutamic acid
 MOD_RES 445 445 PolyADP-ribosyl glutamic acid
 MOD_RES 448 448 PolyADP-ribosyl glutamic acid
 MOD_RES 456 456 PolyADP-ribosyl glutamic acid
 MOD_RES 484 484 PolyADP-ribosyl glutamic acid
 MOD_RES 488 488 PolyADP-ribosyl glutamic acid
 MOD_RES 491 491 PolyADP-ribosyl glutamic acid
 MOD_RES 512 512 PolyADP-ribosyl glutamic acid
 MOD_RES 513 513 PolyADP-ribosyl glutamic acid
 MOD_RES 519 519 PolyADP-ribosyl glutamic acid
 MOD_RES 599 599 N6-acetyllysine (By similarity).
 MOD_RES 620 620 N6-acetyllysine (By similarity).
 MOD_RES 781 781 Phosphoserine (By similarity).  
Keyword
 Acetylation; ADP-ribosylation; Alternative initiation; Complete proteome; Direct protein sequencing; 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
 1013 AA 
Protein Sequence
MAEASERLYR VQYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV 60
GQSIRHPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD GSGGKAEKTL GDFAAEYAKS 120
NRSMCKGCLE KIEKGQMRLS KKMVDPEKPQ LGMIDRWYHP TCFVKKRDEL GFRPEYSASQ 180
LKGFSLLSAE DKEALKKQLP AIKNEGKRKG DEVDGTDEVA KKKSRKETDK YSKLEKALKA 240
QNELIWNIKD ELKKACSTND LKELLIFNQQ QVPSGESAIL DRVADGMAFG ALLPCKECSG 300
QLVFKSDAYY CTGDVTAWTK CMVKTQNPSR KEWVTPKEFR EISYLKKLKV KKQDRIFPPE 360
SSAPITVHWP LSVTSAPTAV NSSAPADKPL SNMKILTLGK LSQNKDEAKA VIEKLGGKLT 420
GSANKASLCI SIKKEVEKMN KKMEEVKEAN IRVVSEDFLQ DVSASTKSLQ DLLSAHSLSP 480
WGAEVKAEPG EVVAPRGKSA APSKKSKGCF KEEGVNKSEK RMKLTLKGGA AVDPDSGLEH 540
SAHVLEKGGK VFSATLGLVD IVKGTNSYYK LQLLEDDKES RYWIFRSWGR LGTVIGSNKL 600
EQMPSKEEAV EQFMKLYEEK TGNAWHSKNF TKYPKKFYPL EIDYGQDEEA VKKLTVKPGT 660
KSKLPKPVQE LVGMIFDVDS MKKALVEYEI DLQKMPLGKL SRRQIQAAYS ILSEVQQPVS 720
QGSSESQILD LSNRFYTLIP HDFGMKKPPL LNNADSVQAK VEMLDNLLDI EVAYSLLRGG 780
SDDSSKDPID VNYEKLKTDI KVVDRDSEEA EVIRKYVKNT HATTHNAYDL EVIDIFKIER 840
EGESQRYKPF RQLHNRRLLW HGSRTTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV 900
SKSANYCHTS QGDPIGLIML GEVALGNMYE LKHASHISKL PKGKHSVKGL GKTTPDPSAS 960
ITLEGVEVPL GTGIPSGVND TALLYNEYIV YDIAQVNLKY LLKLKFNFKT SLW 1013 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:BHF-UCL.
 GO:0005730; C:nucleolus; IDA:MGI.
 GO:0005654; C:nucleoplasm; IDA:MGI.
 GO:0043234; C:protein complex; IDA:MGI.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:EC.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006284; P:base-excision repair; IMP:MGI.
 GO:0006302; P:double-strand break repair; ISS:UniProtKB.
 GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
 GO:0040009; P:regulation of growth rate; IMP:MGI.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0000723; P:telomere maintenance; IMP:MGI.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
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