CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-027704
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly (ADP-ribose) polymerase family, member 1 
Protein Synonyms/Alias
 Poly [ADP-ribose] polymerase 1 
Gene Name
 Parp1 
Gene Synonyms/Alias
 Adprt1; mCG_19846 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
108GSGGKAEKTLGDFLAacetylation[1, 2]
119DFLAEYAKSNRSMCKubiquitination[3]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] 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]
 [3] 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
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1014 AA 
Protein Sequence
MAEASERLYR VEYAKSGRAS CKKCSESIPK DSLRMAIMVQ SPMFDGKVPH WYHFSCFWKV 60
GHSIRQPDVE VDGFSELRWD DQQKVKKTAE AGGVAGKGQD GSGGKAEKTL GDFLAEYAKS 120
NRSMCKGCLE KIEKGQMRLS KKMVDPEKPQ LGMIDRWYHP TCFVKKRDEL GFRPEYSASQ 180
LKGFSLLSAE DKEALKKQLP AIKNEGKRKG DEVDGTDEVA KKKSKKGKDK DSSKLEKALK 240
AQNELIWNIK DELKKACSTN DLKELLIFNQ QQVPSGESAI LDRVADGMAF GALLPCKECS 300
GQLVFKSDAY YCTGDVTAWT KCMVKTQNPS RKEWVTPKEF REISYLKKLK VKKQDRIFPP 360
ESSAPAPLAL PLSVTSAPTA VNSSAPADKP LSNMKILTLG KLSQNKDEAK AVIEKLGGKL 420
TGSANKASLC ISTKKEVEKM SKKMEEVKAA NVRVVCEDFL QDVSASTKSL QELLSAHSLS 480
SWGAEVKAEP GEVVAPKGKS AAPSKKSKGA VKEEGVNKSE KRMKLTLKGG AAVDPDSGLE 540
HSAHVLEKGG KVFSATLGLV DIVKGTNSYY KLQLLEDDKE SRYWIFRSWG RVGTVIGSNK 600
LEQMPSKEDA VEHFMKLYEE KTGNAWHSKN FTKYPKKFYP LEIDYGQDEE AVKKLTVKPG 660
TKSKLPKPVQ ELVGMIFDVE SMKKALVEYE IDLQKMPLGK LSRRQIQAAY SILSEVQQAV 720
SQGSSESQIL DLSNRFYTLI PHDFGMKKPP LLNNADSVQA KVEMLDNLLD IEVAYSLLRG 780
GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEVIRKYVKN THATTHNAYD LEVIDIFKIE 840
REGESQRYKP FRQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM 900
VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTTPDPSA 960
SITLEGVEVP LGTGIPSGVN DTCLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW 1014 
Gene Ontology
 GO:0005635; C:nuclear envelope; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:MGI.
 GO:0005654; C:nucleoplasm; IDA:MGI.
 GO:0043234; C:protein complex; IDA:MGI.
 GO:0005667; C:transcription factor complex; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0051287; F:NAD binding; IEA:Compara.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006284; P:base-excision repair; IMP:MGI.
 GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
 GO:0042769; P:DNA damage response, detection of DNA damage; IEA:Compara.
 GO:0016540; P:protein autoprocessing; IEA:Compara.
 GO:0070212; P:protein poly-ADP-ribosylation; IEA:Compara.
 GO:0040009; P:regulation of growth rate; IMP:MGI.
 GO:0000723; P:telomere maintenance; IMP:MGI. 
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