※ dbPPT Protein Information
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UniProt Accession | |||||||||||||||||||||||||||||||||||
Theoretical PI | 8.8 | ||||||||||||||||||||||||||||||||||
Molecular Weight | 111233 | ||||||||||||||||||||||||||||||||||
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; At2g31320; F16D14.16 | ||||||||||||||||||||||||||||||||||
Created Date | 2005-08-30 | ||||||||||||||||||||||||||||||||||
Organism | Arabidopsis thaliana(Mouse-ear cress) | ||||||||||||||||||||||||||||||||||
NCBI Taxa ID | 3702 | ||||||||||||||||||||||||||||||||||
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 1 983 Poly [ADP-ribose] polymerase 1 domain 394 484 BRCT domain 633 751 PARP alpha-helical domain 758 983 PARP catalytic zinc finger region 8 91 PARP-type 1 zinc finger region 114 194 PARP-type 2 strand 7 12 strand 21 23 strand 29 36 strand 41 44 strand 49 52 helix 53 57 strand 59 61 helix 66 68 turn 71 74 helix 77 87 strand 91 93 Keyword 3D-structure,ADP-ribosylation,Complete proteome,DNA-binding,Glycosyltransferase,Metal-binding,NAD,Nucleus,Reference proteome,Repeat,Transferase,Zinc,Zinc-finger Sequence Source UniProt 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; IEP: TAIR GO:0006979; P: response to oxidative stress; IEP: TAIR Interpro Pfam SMART PROSITE PRINTS |