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Parp1 |
Protein FULL name:
poly [ADP-ribose] polymerase 1 [Mus musculus].
Parp1 (Mus musculus) is product of expression of Parp1 gene.
FUNCTION: Positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150 (By similarity). 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. Mediates the poly(ADP- ribosyl)ation of APLF and CHFR.
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, PARP2, POLB and LIG3. Homo- and heterodimer with PARP2. Interacts with PARP3, APTX and SRY Interacts (when poly-ADP-ribosylated) with CHD1L. Interacts with the DNA polymerase alpha catalytic subunit POLA1; this interaction functions as part of the control of replication fork progression (By similarity). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts with TIAM2 and ZNF423.
INTERACTION: Q61501:E2f1; NbExp=1; IntAct=EBI-642213, EBI-1025536;
SUBCELLULAR LOCATION: Nucleus.
TISSUE SPECIFICITY: Widely expressed. Expression is correlated with proliferation, with higher levels occurring during early fetal development and organogenesis and in the highly proliferative cell compartments of adult. Expressed in B-cells that have been induced to switch to various Ig isotypes.
DEVELOPMENTAL STAGE: At stage E12.5, expressed at high level in the developing liver and kidneys. Expressed at higher level in the genital ridge and the spinal ganglia. 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. Expressed at high level in the seminiferous tubules of the developing testis.
PTM: Phosphorylated by PRKDC. Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity).
PTM: Poly-ADP-ribosylated by PARP2. Poly-ADP-ribosylation mediates the recruitment of CHD1L to DNA damage sites (By similarity).
DISRUPTION PHENOTYPE: Mice show a complete lack of nuclear poly(ADP-ribosyl)ation. Mice are however viable and fertile. Moreover, repair of UV and MNNG induced DNA damage are not affected. However, about 30% of the mutant mice developed pathological skin aberrations on a mixed 129/Sv x C57B1/6 genetic background.
MISCELLANEOUS: The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
SIMILARITY: Contains 1 BRCT domain.
SIMILARITY: Contains 1 PARP alpha-helical domain.
SIMILARITY: Contains 1 PARP catalytic domain.
SIMILARITY: Contains 2 PARP-type zinc fingers.
SEQUENCE CAUTION: Sequence=AAF61293.1; Type=Erroneous initiation;
| NCBI GenPept GI number(s): |
20806109 |
| Species: | Mus musculus |
Links to other databases:
| Database | ID | Link |
| Uniprot | P11103 |
P11103 |
| PFAM: | - |
P11103 (Link - using uniprot id) |
| InterPro: | - |
P11103 (Link - using uniprot id) |
| CATH: | - | - |
| SCOP: | - | - |
| PDB: | - | - |
Protein sequence:
|
MAEASERLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPH WYHFSCFWKVGHSIRQPDVEVDGFSELRWDDQQKVKKTAEAGGVAGKGQD GSGGKAEKTLGDFLAEYAKSNRSMCKGCLEKIEKGQMRLSKKMVDPEKPQ LGMIDRWYHPTCFVKKRDELGFRPEYSASQLKGFSLLSAEDKEALKKQLP AIKNEGKRKGDEVDGTDEVAKKKSKKGKDKDSSKLEKALKAQNELIWNIK DELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECS GQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRKEWVTPKEFREISYLKKLK VKKQDRIFPPESSAPAPLALPLSVTSAPTAVNSSAPADKPLSNMKILTLG KLSQNKDEAKAVIEKLGGKLTGSANKASLCISTKKEVEKMSKKMEEVKAA NVRVVCEDFLQDVSASTKSLQELLSAHSLSSWGAEVKAEPGEVVAPKGKS AAPSKKSKGAVKEEGVNKSEKRMKLTLKGGAAVDPDSGLEHSAHVLEKGG KVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGSNK LEQMPSKEDAVEHFMKLYEEKTGNAWHSKNFTKYPKKFYPLEIDYGQDEE AVKKLTVKPGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGK LSRRQIQAAYSILSEVQQAVSQGSSESQILDLSNRFYTLIPHDFGMKKPP LLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTD IKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRYKP FRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKG LGKTTPDPSASITLEGVEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLK YLLKLKFNFKTSLW |
Parp1 (Mus musculus) is able to recognize following damages:
Parp1 (Mus musculus) belongs to following protein families:
References:
| Title | Authors | Journal |
| Sequence and organization of the mouse poly (ADP-ribose) polymerase gene. | Huppi K, Bhatia K, Siwarski D, Klinman D, Cherney B, Smulson M | Nucleic Acids Res May 11, 1989 |
| On the biological role of the nuclear polymerizing NAD+: protein(ADP-ribosyl) transferase (ADPRT): ADPRT from Dictyostelium discoideum and inactivation of the ADPRT gene in the mouse. | Auer B, Flick K, Wang ZQ, Haidacher D, Jager S, Berghammer H, Kofler B, Schweiger M, Wagner EF | Biochimie Jan. 1, 1995 |
| A B-cell-specific DNA recombination complex. | Borggrefe T, Wabl M, Akhmedov AT, Jessberger R | J Biol Chem July 3, 1998 |
| Characterization of sPARP-1. An alternative product of PARP-1 gene with poly(ADP-ribose) polymerase activity independent of DNA strand breaks. | Sallmann FR, Vodenicharov MD, Wang ZQ, Poirier GG | J Biol Chem May 19, 2000 |
| 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 |
| Poly(ADP-ribose) polymerase 1 interacts with OAZ and regulates BMP-target genes. | Ku MC, Stewart S, Hata A | Biochem Biophys Res Commun Nov. 21, 2003 |
| Rho-kinase modulates the function of STEF, a Rac GEF, through its phosphorylation. | Takefuji M, Mori K, Morita Y, Arimura N, Nishimura T, Nakayama M, Hoshino M, Iwamatsu A, Murohara T, Kaibuchi K, Amano M | Biochem Biophys Res Commun April 13, 2007 |
| PARP-1 transcriptional activity is regulated by sumoylation upon heat shock. | Martin N, Schwamborn K, Schreiber V, Werner A, Guillier C, Zhang XD, Bischof O, Seeler JS, Dejean A | EMBO J Nov. 18, 2009 |
Last modification of this entry: Oct. 6, 2010.
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