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Parp2 |
Protein FULL name:
poly [ADP-ribose] polymerase 2 [Mus musculus].
Parp2 (Mus musculus) is product of expression of Parp2 gene.
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.
PTM: Acetylation reduces DNA binding and enzymatic activity.
SIMILARITY: Contains 1 PARP alpha-helical domain.
SIMILARITY: Contains 1 PARP catalytic domain.
SEQUENCE CAUTION: Sequence=AAC25415.1; Type=Erroneous initiation;
| NCBI GenPept GI number(s): |
6752992 |
| Species: | Mus musculus |
Links to other databases:
| Database | ID | Link |
| Uniprot | O88554 |
O88554 |
| PFAM: | - |
O88554 (Link - using uniprot id) |
| InterPro: | - |
O88554 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MAPRRQRSGSGRRVLNEAKKVDNGNKATEDDSPPGKKMRTCQRKGPMAGG KDADRTKDNRDSVKTLLLKGKAPVDPECAAKLGKAHVYCEGDDVYDVMLN QTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKTGQHSLVTCSGDLN KAKEIFQKKFLDKTKNNWEDRENFEKVPGKYDMLQMDYAASTQDESKTKE EETLKPESQLDLRVQELLKLICNVQTMEEMMIEMKYDTKRAPLGKLTVAQ IKAGYQSLKKIEDCIRAGQHGRALVEACNEFYTRIPHDFGLSIPPVIRTE KELSDKVKLLEALGDIEIALKLVKSERQGLEHPLDQHYRNLHCALRPLDH ESNEFKVISQYLQSTHAPTHKDYTMTLLDVFEVEKEGEKEAFREDLPNRM LLWHGSRLSNWVGILSHGLRVAPPEAPITGYMFGKGIYFADMSSKSANYC FASRLKNTGLLLLSEVALGQCNELLEANPKAQGLLRGKHSTKGMGKMAPS PAHFITLNGSTVPLGPASDTGILNPEGYTLNYNEFIVYSPNQVRMRYLLK IQFNFLQLW |
Parp2 (Mus musculus) is able to recognize following damages:
Parp2 (Mus musculus) belongs to following protein families:
References:
| Title | Authors | Journal |
| pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans. | Berghammer H, Ebner M, Marksteiner R, Auer B | FEBS Lett April 23, 1999 |
| PARP-2, A novel mammalian DNA damage-dependent poly(ADP-ribose) polymerase. | Ame JC, Rolli V, Schreiber V, Niedergang C, Apiou F, Decker P, Muller S, Hoger T, Menissier-de Murcia J, de Murcia G | J Biol Chem June 18, 1999 |
| 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. | Ame JC, Schreiber V, Fraulob V, Dolle P, de Murcia G, Niedergang CP | J Biol Chem April 6, 2001 |
| Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. | Schreiber V, Ame JC, Dolle P, Schultz I, Rinaldi B, Fraulob V, Menissier-de Murcia J, de Murcia G | J Biol Chem June 21, 2002 |
| The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). | Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J | Genome Res Oct. 1, 2004 |
| Identification of lysines 36 and 37 of PARP-2 as targets for acetylation and auto-ADP-ribosylation. | Haenni SS, Hassa PO, Altmeyer M, Fey M, Imhof R, Hottiger MO | Int J Biochem Cell Biol Jan. 1, 2008 |
Last modification of this entry: Oct. 6, 2010.
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