CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024190
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Poly [ADP-ribose] polymerase 1 
Protein Synonyms/Alias
 PARP-1; NAD(+) ADP-ribosyltransferase 1; ADPRT-1; Poly[ADP-ribose] synthase 1 
Gene Name
 PARP1 
Gene Synonyms/Alias
 At2g31320; F16D14.16 
Created Date
 July 27, 2013 
Organism
 Arabidopsis thaliana (Mouse-ear cress) 
NCBI Taxa ID
 3702 
Lysine Modification
Position
Peptide
Type
References
565WGRVGNEKIGGNKVEacetylation[1]
570NEKIGGNKVEEMSKSacetylation[1]
Reference
 [1] Proteins of diverse function and subcellular location are lysine acetylated in Arabidopsis.
 Finkemeier I, Laxa M, Miguet L, Howden AJ, Sweetlove LJ.
 Plant Physiol. 2011 Apr;155(4):1779-90. [PMID: 21311031
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 (By similarity). 
Sequence Annotation
 DOMAIN 394 484 BRCT.
 DOMAIN 633 751 PARP alpha-helical.
 DOMAIN 758 983 PARP catalytic.
 ZN_FING 8 91 PARP-type 1.
 ZN_FING 114 194 PARP-type 2.  
Keyword
 3D-structure; ADP-ribosylation; Complete proteome; DNA-binding; Glycosyltransferase; Metal-binding; NAD; Nucleus; Reference proteome; Repeat; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 983 AA 
Protein Sequence
MASPHKPWRA EYAKSSRSSC KTCKSVINKE NFRLGKLVQS THFDGIMPMW NHASCILKKT 60
KQIKSVDDVE GIESLRWEDQ QKIRKYVESG AGSNTSTSTG TSTSSTANNA KLEYGIEVSQ 120
TSRAGCRKCS EKILKGEVRI FSKPEGPGNK GLMWHHAKCF LEMSSSTELE SLSGWRSIPD 180
SDQEALLPLV KKALPAAKTE TAEARQTNSR AGTKRKNDSV DNEKSKLAKS SFDMSTSGAL 240
QPCSKEKEME AQTKELWDLK DDLKKYVTSA ELREMLEVNE QSTRGSELDL RDKCADGMMF 300
GPLALCPMCS GHLSFSGGLY RCHGYISEWS KCSHSTLDPD RIKGKWKIPD ETENQFLLKW 360
NKSQKSVKPK RILRPVLSGE TSQGQGSKDA TDSSRSERLA DLKVSIAGNT KERQPWKKRI 420
EEAGAEFHAN VKKGTSCLVV CGLTDIRDAE MRKARRMKVA IVREDYLVDC FKKQRKLPFD 480
KYKIEDTSES LVTVKVKGRS AVHEASGLQE HCHILEDGNS IYNTTLSMSD LSTGINSYYI 540
LQIIQEDKGS DCYVFRKWGR VGNEKIGGNK VEEMSKSDAV HEFKRLFLEK TGNTWESWEQ 600
KTNFQKQPGK FLPLDIDYGV NKQVAKKEPF QTSSNLAPSL IELMKMLFDV ETYRSAMMEF 660
EINMSEMPLG KLSKHNIQKG FEALTEIQRL LTESDPQPTM KESLLVDASN RFFTMIPSIH 720
PHIIRDEDDF KSKVKMLEAL QDIEIASRIV GFDVDSTESL DDKYKKLHCD ISPLPHDSED 780
YRLIEKYLNT THAPTHTEWS LELEEVFALE REGEFDKYAP HREKLGNKML LWHGSRLTNF 840
VGILNQGLRI APPEAPATGY MFGKGIYFAD LVSKSAQYCY TCKKNPVGLM LLSEVALGEI 900
HELTKAKYMD KPPRGKHSTK GLGKKVPQDS EFAKWRGDVT VPCGKPVSSK VKASELMYNE 960
YIVYDTAQVK LQFLLKVRFK HKR 983 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0051287; F:NAD binding; IEA:InterPro.
 GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:TAIR.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006281; P:DNA repair; IEP:TAIR.
 GO:0006471; P:protein ADP-ribosylation; IDA:TAIR.
 GO:0009737; P:response to abscisic acid stimulus; IEP:TAIR.
 GO:0006979; P:response to oxidative stress; IEP:TAIR. 
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
 PS50064; PARP_ZN_FINGER_2 
PRINTS