PARP9
entrez
83666
canonical
uniprot
Q8IXQ6
canonical
ensembl
ENSG00000138496
resolver
ensp
ENSP00000353512
resolver
ensp
ENSP00000418894
resolver
ensp
ENSP00000419001
resolver
ensp
ENSP00000419506
resolver
ensp
ENSP00000507390
resolver
ensp
ENSP00000563817
resolver
ensp
ENSP00000563818
resolver
ensp
ENSP00000563822
resolver
ensp
ENSP00000563823
resolver
ensp
ENSP00000563828
resolver
ensp
ENSP00000615530
resolver
ensp
ENSP00000615544
resolver
ensp
ENSP00000667314
resolver
ensp
ENSP00000667317
resolver
ensp
ENSP00000667318
resolver
ensp
ENSP00000667321
resolver
ensp
ENSP00000717402
resolver
ensp
ENSP00000717407
resolver
genesymbol
PARP9
resolver
genesymbol_syn
BAL
resolver
genesymbol_syn
BAL1
resolver
hgnc
HGNC:24118
resolver
uniprot
A8KA94
resolver
uniprot
B2R8S9
resolver
uniprot
E9PFM7
resolver
uniprot
Q59ER9
resolver
uniprot
Q8TCP3
resolver
uniprot
Q9BZL8
resolver
uniprot
Q9BZL9
resolver
uniprot_entry
PARP9_HUMAN
resolver
uniprot_entry
Q59ER9_HUMAN
resolver
uniprot_sec
A8KA94
resolver
uniprot_sec
B2R8S9
resolver
uniprot_sec
E9PFM7
resolver
uniprot_sec
Q8TCP3
resolver
uniprot_sec
Q9BZL8
resolver
uniprot_sec
Q9BZL9
resolver
activity_regulation
ACTIVITY REGULATION: Binding to poly(ADP-ribose) does not affect its activity. {ECO:0000269|PubMed:28525742}.
uniprot
proteins
amino_acid_sequence
MDFSMVAGAAAYNEKSGRITSLSLLFQKVFAQIFPQWRKGNTEECLPYKCSETGALGENYSWQIPINHNDFKILKNNERQLCEVLQNKFGCISTLVSPVQEGNSKSLQVFRKMLTPRIELSVWKDDLTTHAVDAVVNAANEDLLHGGGLALALVKAGGFEIQEESKQFVARYGKVSAGEIAVTGAGRLPCKQIIHAVGPRWMEWDKQGCTGKLQRAIVSILNYVIYKNTHIKTVAIPALSSGIFQFPLNLCTKTIVETIRVSLQGKPMMSNLKEIHLVSNEDPTVAAFKAASEFILGKSELGQETTPSFNAMVVNNLTLQIVQGHIEWQTADVIVNSVNPHDITVGPVAKSILQQAGVEMKSEFLATKAKQFQRSQLVLVTKGFNLFCKYIYHVLWHSEFPKPQILKHAMKECLEKCIEQNITSISFPALGTGNMEIKKETAAEILFDEVLTFAKDHVKHQLTVKFVIFPTDLEIYKAFSSEMAKRSKMLSLNNYSVPQSTREEKRENGLEARSPAINLMGFNVEEMYEAHAWIQRILSLQNHHIIENNHILYLGRKEHDILSQLQKTSSVSITEIISPGRTELEIEGARADLIEVVMNIEDMLCKVQEEMARKKERGLWRSLGQWTIQQQKTQDEMKENIIFLKCPVPPTQELLDQKKQFEKCGLQVLKVEKIDNEVLMAAFQRKKKMMEEKLHRQPVSHRLFQQVPYQFCNVVCRVGFQRMYSTPCDPKYGAGIYFTKNLKNLAEKAKKISAADKLIYVFEAEVLTGFFCQGHPLNIVPPPLSPGAIDGHDSVVDNVSSPETFVIFSGMQAIPQYLWTCTQEYVQSQDYSSGPMRPFAQHPWRGFASGSPVD
uniprot
proteins
disease_involvement
DISEASE: Note=Overexpressed at significantly higher levels in fatal high-risk diffuse large B-cell lymphomas (DLB-CL) compared to cured low-risk tumors. Overexpression in B-cell lymphoma transfectants may promote malignant B-cell migration. May therefore be involved in promoting B-cell migration and dissemination of high-risk DLB-CL tumors (PubMed:11110709). {ECO:0000269|PubMed:11110709}.
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:16809771, PubMed:23230272, PubMed:26479788, PubMed:27796300). Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP-ribose) (PubMed:28525742). 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 (PubMed:28525742). During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1 (PubMed:23230272). 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 (PubMed:23230272, PubMed:28525742). In response to DNA damage, PARP9-DTX3L complex is required for efficient non-homologous end joining (NHEJ); the complex function is negatively modulated by PARP9 activity (PubMed:28525742). Dispensable for B-cell receptor (BCR) assembly through V(D)J recombination and class switch recombination (CSR) (By similarity). 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 (PubMed:27796300). {ECO:0000250|UniProtKB:Q8CAS9, ECO:0000269|PubMed:16809771, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:27796300, ECO:0000269|PubMed:28525742}.
uniprot
proteins
mass_dalton
96343
uniprot
proteins
mutagenesis
MUTAGEN 147; /note="G->E: Reduces the binding to poly(ADP-ribose) by 50 percent and prevents increase in DTX3L-mediated histone ubiquitination without affecting ubiquitin ADP ribosylation, interaction with DTX3L and STAT1 and DTX3L catalytic activity; when associated with E-346."; /evidence="ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28525742"; MUTAGEN 346; /note="G->E: Reduces the binding to poly(ADP-ribose) by 50 percent and prevents increase in DTX3L-mediated histone ubiquitination without affecting ubiquitin ADP ribosylation, interaction with DTX3L and STAT1 and DTX3L catalytic activity; when associated with E-147."; /evidence="ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28525742"; MUTAGEN 719..722; /note="Missing: Loss of ADP ribosylation activity and interaction with DTX3L."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 737; /note="Y->A: No defect in ubiquitin ADP ribosylation and the interaction with DTX3L."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 738; /note="F->K: Severe reduction in ubiquitin ADP ribosylation. No effect on the interaction with DTX3L and on DTX3LE3 ligase activity. Increases DNA repair."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 766..769; /note="Missing: Loss of ADP ribosylation activity and interaction with DTX3L."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 780..784; /note="Missing: Reduces ADP ribosylation activity and interaction with DTX3L."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 802..803; /note="PE->AA: No defect in ADP ribosylation and interaction with DTX3L."; /evidence="ECO:0000269|PubMed:28525742"; MUTAGEN 831..854; /note="Missing: No defect in ADP ribosylation and interaction with DTX3L."; /evidence="ECO:0000269|PubMed:28525742
uniprot
proteins
post_translational_modification
PTM: ADP-ribosylated by PARP14. {ECO:0000269|PubMed:27796300}.
uniprot
proteins
protein_family
ARTD/PARP family
uniprot
proteins
pubmed
11110709
uniprot
proteins
pubmed
12670957
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16809771
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
20106667
uniprot
proteins
pubmed
23230272
uniprot
proteins
pubmed
26479788
uniprot
proteins
pubmed
27796300
uniprot
proteins
pubmed
28525742
uniprot
proteins
sequence_length
854
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16809771, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:27796300}. Nucleus {ECO:0000269|PubMed:11110709, ECO:0000269|PubMed:16809771, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28525742}. Note=Shuttles between the nucleus and the cytosol (PubMed:16809771). Translocates to the nucleus in response to IFNG or IFNB1 stimulation (PubMed:26479788). Export to the cytosol depends on the interaction with DTX3L (PubMed:16809771). Localizes at sites of DNA damage in a PARP1-dependent manner (PubMed:23230272, PubMed:28525742). {ECO:0000269|PubMed:16809771, ECO:0000269|PubMed:23230272, ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28525742}.
uniprot
proteins