Parp2
entrez
11546
canonical
uniprot
O88554
canonical
ensembl
ENSMUSG00000036023
resolver
ensp
ENSMUSP00000048877
resolver
ensp
ENSMUSP00000328200
resolver
enst
ENSMUST00000036126
resolver
genesymbol
Parp2
resolver
genesymbol_syn
Adprt2
resolver
genesymbol_syn
Adprtl2
resolver
genesymbol_syn
Aspartl2
resolver
uniprot
Q99N29
resolver
uniprot_entry
PARP2_MOUSE
resolver
uniprot_sec
Q99N29
resolver
activity_regulation
ACTIVITY REGULATION: ADP-ribosyltransferase activity is regulated via an allosteric activation mechanism. In absence of activation signal, PARP2 is autoinhibited by the PARP alpha-helical domain (also named HD region), which prevents effective NAD(+)-binding. Activity is highly stimulated by signals, which unfold the PARP alpha-helical domain, relieving autoinhibition. Poly-ADP-ribosyltransferase activity is tightly regulated and PARP2 is removed from damaged chromatin following initial poly-ADP-ribosylation of chromatin to avoid prolonged residence (trapping) that has cytotoxic consequences. CHD1L promotes PARP2 removal from chromatin. {ECO:0000250|UniProtKB:Q9UGN5}.
uniprot
proteins
amino_acid_sequence
MAPRRQRSGSGRRVLNEAKKVDNGNKATEDDSPPGKKMRTCQRKGPMAGGKDADRTKDNRDSVKTLLLKGKAPVDPECAAKLGKAHVYCEGDDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKTGQHSLVTCSGDLNKAKEIFQKKFLDKTKNNWEDRENFEKVPGKYDMLQMDYAASTQDESKTKEEETLKPESQLDLRVQELLKLICNVQTMEEMMIEMKYDTKRAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRALVEACNEFYTRIPHDFGLSIPPVIRTEKELSDKVKLLEALGDIEIALKLVKSERQGLEHPLDQHYRNLHCALRPLDHESNEFKVISQYLQSTHAPTHKDYTMTLLDVFEVEKEGEKEAFREDLPNRMLLWHGSRLSNWVGILSHGLRVAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAQGLLRGKHSTKGMGKMAPSPAHFITLNGSTVPLGPASDTGILNPEGYTLNYNEFIVYSPNQVRMRYLLKIQFNFLQLW
uniprot
proteins
ec_number
2.4.2.-
uniprot
proteins
ec_number
2.4.2.30
uniprot
proteins
function
FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:10364231, PubMed:12065591). Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues 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 (PubMed:12065591). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (By similarity). Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1 (By similarity). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site (By similarity). PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (By similarity). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP2 in order to limit the length of poly-ADP-ribose chains (By similarity). Specifically mediates formation of branched poly-ADP-ribosylation (By similarity). Branched poly-ADP-ribose chains are specifically recognized by some factors, such as APLF (By similarity). In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex (By similarity). {ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:10364231, ECO:0000269|PubMed:12065591}.
uniprot
proteins
mass_dalton
63397
uniprot
proteins
mutagenesis
MUTAGEN 36; /note="K->R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity."; /evidence="ECO:0000269|PubMed:18436469"; MUTAGEN 37; /note="K->R: Decreases levels of mono-ADP-ribosylation without loss of enzyme activity."; /evidence="ECO:0000269|PubMed:18436469"; MUTAGEN 187; /note="D->E: Decreased cleavages by caspase-8 (CASP8)."; /evidence="ECO:0000269|PubMed:12065591
uniprot
proteins
post_translational_modification
PTM: Auto poly-ADP-ribosylated on serine residues, leading to dissociation of the PARP2-HPF1 complex from chromatin (By similarity). Poly-ADP-ribosylated by PARP1 (PubMed:11948190). {ECO:0000250|UniProtKB:Q9UGN5, ECO:0000269|PubMed:11948190}.; PTM: Acetylation reduces DNA binding and enzymatic activity. {ECO:0000269|PubMed:18436469}.; PTM: Proteolytically cleaved by caspase-8 (CASP8) in response to apoptosis, leading to its inactivation. {ECO:0000269|PubMed:12065591}.
uniprot
proteins
protein_family
ARTD/PARP family
uniprot
proteins
pubmed
10338144
uniprot
proteins
pubmed
10364231
uniprot
proteins
pubmed
11133988
uniprot
proteins
pubmed
11948190
uniprot
proteins
pubmed
12065591
uniprot
proteins
pubmed
12727891
uniprot
proteins
pubmed
14739238
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18436469
uniprot
proteins
pubmed
34580230
uniprot
proteins
sequence_length
559
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10364231}. Chromosome {ECO:0000250|UniProtKB:Q9UGN5}. Note=Recruited to DNA damage sites in a PARP1-dependent process: recognizes and binds poly-ADP-ribose chains produced by PARP1 at DNA damage sites via its N-terminus, leading to its recruitment. {ECO:0000250|UniProtKB:Q9UGN5}.
uniprot
proteins