※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||||||
Theoretical PI | 8.74 | ||||||||||||||||||||||||||||||||||
Molecular Weight | 110475.33 | ||||||||||||||||||||||||||||||||||
Genbank Protein ID | |||||||||||||||||||||||||||||||||||
Genbank Nucleotide ID | |||||||||||||||||||||||||||||||||||
Protein Name | Poly [ADP-ribose] polymerase 1; PARP-1; NAD(+) ADP-ribosyltransferase 1; ADPRT-1; Poly[ADP-ribose] synthase 1 | ||||||||||||||||||||||||||||||||||
Gene Name | PARP1 | ||||||||||||||||||||||||||||||||||
Created Date | 2006-11-28 | ||||||||||||||||||||||||||||||||||
Organism | Zea mays(Maize) | ||||||||||||||||||||||||||||||||||
NCBI Taxa ID | 4577 | ||||||||||||||||||||||||||||||||||
Phosphorylation Sites |
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 chain 1 980 Poly [ADP-ribose] polymerase 1 domain 257 291 SAP domain 385 476 BRCT domain 629 748 PARP alpha-helical domain 755 980 PARP catalytic zinc finger region 8 91 PARP-type 1 zinc finger region 104 184 PARP-type 2 Keyword ADP-ribosylation,Complete proteome,DNA-binding,Glycosyltransferase,Metal-binding,NAD,Nucleus,Reference proteome,Repeat,Transferase,Zinc,Zinc-finger Sequence Source UniProt Protein Sequence MAAPPKAWKA EYAKSGRASC KSCRSPIAKD QLRLGKMVQA SQFDGFMPMW NHARCIFSKK 60 NQIKSVDDVE GIDALRWDDQ EKIRNYVGSA SAGTSSTAAP PEKCTIEIAP SARTSCRRCS 120 EKITKGSVRL SAKLESEGPK GIPWYHANCF FEVSPSATVE KFSGWDTLSD EDKRTMLDLV 180 KKDVGNNEQN KGSKRKKSEN DIDSYKSARL DESTSEGTVR NKGQLVDPRG SNTSSADIQL 240 KLKEQSDTLW KLKDGLKTHV SAAELRDMLE ANGQDTSGPE RHLLDRCADG MLFGALGPCP 300 VCANGMYYYN GQYQCSGNVS EWSKCTYSAT EPVRVKKKWQ IPHGTKNDYL MKWFKSQKVK 360 KPERVLPPMS PEKSGSKATQ RTSLLSSKGL DKLRFSVVGQ SKEAANEWIE KLKLAGANFY 420 ARVVKDIDCL IACGELDNEN AEVRKARRLK IPIVREGYIG ECVKKNKMLP FDLYKLENAL 480 ESSKGSTVTV KVKGRSAVHE SSGLQDTAHI LEDGKSIYNA TLNMSDLALG VNSYYVLQII 540 EQDDGSECYV FRKWGRVGSE KIGGQKLEEM SKTEAIKEFK RLFLEKTGNS WEAWECKTNF 600 RKQPGRFYPL DVDYGVKKAP KRKDISEMKS SLAPQLLELM KMLFNVETYR AAMMEFEINM 660 SEMPLGKLSK ENIEKGFEAL TEIQNLLKDT ADQALAVRES LIVAASNRFF TLIPSIHPHI 720 IRDEDDLMIK AKMLEALQDI EIASKIVGFD SDSDESLDDK YMKLHCDITP LAHDSEDYKL 780 IEQYLLNTHA PTHKDWSLEL EEVFSLDRDG ELNKYSRYKN NLHNKMLLWH GSRLTNFVGI 840 LSQGLRIAPP EAPVTGYMFG KGLYFADLVS KSAQYCYVDR NNPVGLMLLS EVALGDMYEL 900 KKATSMDKPP RGKHSTKGLG KTVPLESEFV KWRDDVVVPC GKPVPSSIRS SELMYNEYIV 960 YNTSQVKMQF LLKVRFHHKR 980 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; IEA: UniProtKB-EC GO:0008270; F: zinc ion binding; IEA: InterPro GO:0006281; P: DNA repair; IEA: EnsemblPlants/Gramene GO:0006471; P: protein ADP-ribosylation; IEA: InterPro GO:0009737; P: response to abscisic acid; IEA: EnsemblPlants/Gramene GO:0006979; P: response to oxidative stress; IEA: EnsemblPlants/Gramene Interpro Pfam SMART PROSITE PRINTS |