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[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Embryo;
DOI=10.1074/jbc.274.25.17860; PubMed=10364231 [NCBI, ExPASy, EBI, Israel, Japan]
Ame J.-C.,
Rolli V.,
Schreiber V.,
Niedergang C.,
Apiou F.,
Decker P.,
Muller S.,
Hoeger T.,
Menissier-de Murcia J.,
de Murcia G.M.;
"PARP-2, a novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase.";
J. Biol. Chem. 274:17860-17868(1999).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
DOI=10.1074/jbc.M007870200; PubMed=11133988 [NCBI, ExPASy, EBI, Israel, Japan]
Ame J.-C.,
Schreiber V.,
Fraulob V.,
Dolle P.,
de Murcia G.M.,
Niedergang C.P.;
"A bidirectional promoter connects the poly(ADP-ribose) polymerase 2 (PARP-2) gene to the gene for RNase P RNA. Structure and expression of the mouse PARP-2 gene.";
J. Biol. Chem. 276:11092-11099(2001).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] OF 9-559.
STRAIN=C57BL/6 X 129/Sv;
DOI=10.1016/S0014-5793(99)00448-2; PubMed=10338144 [NCBI, ExPASy, EBI, Israel, Japan]
Berghammer H.,
Ebner M.,
Marksteiner R.,
Auer B.;
"pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans.";
FEBS Lett. 449:259-263(1999).
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[5]
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INTERACTION WITH PARP1; XRCC1; POLB AND LIG3, AND POLY-ADP-RIBOSYLATION.
DOI=10.1074/jbc.M202390200; PubMed=11948190 [NCBI, ExPASy, EBI, Israel, Japan]
Schreiber V.,
Ame J.-C.,
Dolle P.,
Schultz I.,
Rinaldi B.,
Fraulob V.,
Menissier-de Murcia J.,
de Murcia G.M.;
"Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1.";
J. Biol. Chem. 277:23028-23036(2002).
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- FUNCTION: 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.
- CATALYTIC ACTIVITY: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.
- SUBUNIT: Component of a base excision repair (BER) complex, containing at least XRCC1, PARP1, POLB and LIG3. Homo- and heterodimer with PARP1.
- SUBCELLULAR LOCATION: Nucleus.
- TISSUE SPECIFICITY: Widely expressed; the highest levels were in testis followed by ovary. Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult.
- DEVELOPMENTAL STAGE: At stage E12.5, expressed at high level in the developing liver and kidneys. At E18.5, preferentially expressed in the thymus and in regions of the nervous system. Within the developing trunk, preferential expression persisted in the liver and became restricted to the cortical region of the kidney, spleen, adrenal gland, and to stomach and intestinal epithelia. From E14.5 to E18.5, as well as in the adult, expressed at the highest level in thymus. Expression is particularly high in the subcapsular zone of the thymus where immature lymphocytes proliferate.
- INDUCTION: By high levels of DNA-damaging agents.
- PTM: Poly-ADP-ribosylated by PARP1.
- SIMILARITY: Contains 1 PARP alpha-helical domain.
- SIMILARITY: Contains 1 PARP catalytic domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 559 AA [This is the length of the unprocessed precursor] |
Molecular weight: 63397 Da [This is the MW of the unprocessed precursor] |
CRC64: E0AEDAEE412C1445 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAPRRQRSGS GRRVLNEAKK VDNGNKATED DSPPGKKMRT CQRKGPMAGG KDADRTKDNR
70 80 90 100 110 120
DSVKTLLLKG KAPVDPECAA KLGKAHVYCE GDDVYDVMLN QTNLQFNNNK YYLIQLLEDD
130 140 150 160 170 180
AQRNFSVWMR WGRVGKTGQH SLVTCSGDLN KAKEIFQKKF LDKTKNNWED RENFEKVPGK
190 200 210 220 230 240
YDMLQMDYAA STQDESKTKE EETLKPESQL DLRVQELLKL ICNVQTMEEM MIEMKYDTKR
250 260 270 280 290 300
APLGKLTVAQ IKAGYQSLKK IEDCIRAGQH GRALVEACNE FYTRIPHDFG LSIPPVIRTE
310 320 330 340 350 360
KELSDKVKLL EALGDIEIAL KLVKSERQGL EHPLDQHYRN LHCALRPLDH ESNEFKVISQ
370 380 390 400 410 420
YLQSTHAPTH KDYTMTLLDV FEVEKEGEKE AFREDLPNRM LLWHGSRLSN WVGILSHGLR
430 440 450 460 470 480
VAPPEAPITG YMFGKGIYFA DMSSKSANYC FASRLKNTGL LLLSEVALGQ CNELLEANPK
490 500 510 520 530 540
AQGLLRGKHS TKGMGKMAPS PAHFITLNGS TVPLGPASDT GILNPEGYTL NYNEFIVYSP
550
NQVRMRYLLK IQFNFLQLW
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O88554 in FASTA format |
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