Parp9
entrez
80285
canonical
uniprot
Q8CAS9
canonical
ensembl
ENSMUSG00000022906
resolver
ensp
ENSMUSP00000023622
resolver
ensp
ENSMUSP00000110528
resolver
ensp
ENSMUSP00000313733
resolver
ensp
ENSMUSP00000313738
resolver
ensp
ENSMUSP00000313739
resolver
enst
ENSMUST00000023622
resolver
genesymbol
Parp9
resolver
genesymbol_syn
Bal
resolver
uniprot
H7BWY5
resolver
uniprot
Q6IRT6
resolver
uniprot
Q99LF9
resolver
uniprot_entry
H7BWY5_MOUSE
resolver
uniprot_entry
PARP9_MOUSE
resolver
uniprot_sec
Q6IRT6
resolver
uniprot_sec
Q99LF9
resolver
activity_regulation
ACTIVITY REGULATION: Binding to poly(ADP-ribose) does not affect its activity. {ECO:0000250|UniProtKB:Q8IXQ6}.
uniprot
proteins
amino_acid_sequence
MAYYMDTWAAAPAERPGMIASLSLSFKKAFAELFPQRRRGHSEGDYPPLRGSANNSLEEHYRWQIPIKHNVFEILKSNESQLCEVLQNKFGCISTLSCPTLAGSSSPAQRVFRRTLIPGIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANVGKISVGGIAITGAGRLPCHLIIHAVGPRWTVTNSQTAIELLKFAIRNILDYVTKYDLRIKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQDKQMFGNLREIHLVSNEDPTVASFKSASESILGRDLSSWGGPETDPASTMTLRIGRGLTLQIVQGCIEMQTTDVIVNSGYMQDFKSGRVAQSILRQAGVEMEKELDKVNLSTDYQEVWVTKGFKLSCQYVFHVAWHSQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTLTVKIVIFPVDVETYKIFYAEMTKRSNELNLSGNSGALALQWSSGEQRRGGLEAGSPAINLMGVKVGEMCEAQEWIERLLVSLDHHIIENNHILYLGKKEHDVLSELQTSTRVSISETVSPRTATLEIKGPQADLIDAVMRIECMLCDVQEEVAGKREKNLWSLSGQGTNQQEKLDKMEESYTFQRYPASLTQELQDRKKQFEKCGLWVVQVEQIDNKVLLAAFQEKKKMMEERTPKGSGSQRLFQQVPHQFCNTVCRVGFHRMYSTSYNPVYGAGIYFTKSLKNLADKVKKTSSTDKLIYVFEAEVLTGSFCQGNSSNIIPPPLSPGALDVNDSVVDNVSSPETIVVFNGMQAMPLYLWTCTQDRTFSQHPMWSQGYSSGPGMVSSLQSWEWVLNGSSV
uniprot
proteins
ec_number
2.4.2.-
uniprot
proteins
function
FUNCTION: ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses (PubMed:27796300). Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP-ribose) (By similarity). In addition, positively regulates DTXL3 protein levels (By similarity). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones (By similarity). During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1 (By similarity). Subsequent PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (By similarity). In response to DNA damage, PARP9-DTX3L complex is required for efficient non-homologous end joining (NHEJ) but the complex function is restrained by PARP9 activity (By similarity). Dispensable for B-cell receptor (BCR) assembly through V(D)J recombination and class switch recombination (CSR) (PubMed:28105679). In macrophages, positively regulates pro-inflammatory cytokines production in response to IFNG stimulation by suppressing PARP14-mediated STAT1 ADP-ribosylation and thus promoting STAT1 phosphorylation (PubMed:27796300). Also suppresses PARP14-mediated STAT6 ADP-ribosylation (By similarity). {ECO:0000250|UniProtKB:Q8IXQ6, ECO:0000269|PubMed:27796300, ECO:0000269|PubMed:28105679}.
uniprot
proteins
mass_dalton
96659
uniprot
proteins
post_translational_modification
PTM: ADP-ribosylated by PARP14. {ECO:0000250|UniProtKB:Q8IXQ6}.
uniprot
proteins
protein_family
ARTD/PARP family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18069692
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
27796300
uniprot
proteins
pubmed
28105679
uniprot
proteins
sequence_length
866
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8IXQ6}. Nucleus {ECO:0000250|UniProtKB:Q8IXQ6}. Note=Shuttles between the nucleus and the cytosol. Translocates to the nucleus in response to IFNG or IFNB1 stimulation. Export to the cytosol depends on the interaction with DTX3L. Localizes at sites of DNA damage in a PARP1-dependent manner. {ECO:0000250|UniProtKB:Q8IXQ6}.
uniprot
proteins