Protein: Protein mono-ADP-ribosyltransferase PARP9 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 9) (ARTD9) (B aggressive lymphoma protein homolog) (Poly [ADP-ribose] polymerase 9) (PARP-9) (Q8CAS9)
Organism: Mus musculus (Mouse)
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. 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). 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. Also suppresses PARP14-mediated STAT6 ADP-ribosylation (By similarity).
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}.
Interaction partners:
- E3 ubiquitin-protein ligase DTX3L
- Protein mono-ADP-ribosyltransferase PARP14
- Interferon-induced protein 44
- Interferon-induced helicase C domain-containing protein 1
- Signal transducer and activator of transcription 1
- Interferon-induced 35 kDa protein homolog
- Receptor-transporting protein 4
- Interferon regulatory factor 9
- Protein mono-ADP-ribosyltransferase PARP12
- Antiviral innate immune response receptor RIG-I
Sequence:
MAYYMDTWAAAPAERPGMIASLSLSFKKAFAELFPQRRRGHSEGDYPPLRGSANNSLEEHYRWQIPIKHNVFEILKSNESQLCEVLQNKFGCISTLSCPTLAGSSSPAQRVFRRTLIPGIELSVWKDDLTRHVVDAVVNAANENLLHGSGLAGSLVKTGGFEIQEESKRIIANVGKISVGGIAITGAGRLPCHLIIHAVGPRWTVTNSQTAIELLKFAIRNILDYVTKYDLRIKTVAIPALSSGIFQFPLDLCTSIILETIRLYFQDKQMFGNLREIHLVSNEDPTVASFKSASESILGRDLSSWGGPETDPASTMTLRIGRGLTLQIVQGCIEMQTTDVIVNSGYMQDFKSGRVAQSILRQAGVEMEKELDKVNLSTDYQEVWVTKGFKLSCQYVFHVAWHSQINKYQILKDAMKSCLEKCLKPDINSISFPALGTGLMDLKKSTAAQIMFEEVFAFAKEHKEKTLTVKIVIFPVDVETYKIFYAEMTKRSNELNLSGNSGALALQWSSGEQRRGGLEAGSPAINLMGVKVGEMCEAQEWIERLLVSLDHHIIENNHILYLGKKEHDVLSELQTSTRVSISETVSPRTATLEIKGPQADLIDAVMRIECMLCDVQEEVAGKREKNLWSLSGQGTNQQEKLDKMEESYTFQRYPASLTQELQDRKKQFEKCGLWVVQVEQIDNKVLLAAFQEKKKMMEERTPKGSGSQRLFQQVPHQFCNTVCRVGFHRMYSTSYNPVYGAGIYFTKSLKNLADKVKKTSSTDKLIYVFEAEVLTGSFCQGNSSNIIPPPLSPGALDVNDSVVDNVSSPETIVVFNGMQAMPLYLWTCTQDRTFSQHPMWSQGYSSGPGMVSSLQSWEWVLNGSSV