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Poly [ADP-ribose] polymerase 9 (PARP-9) (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 9) (ARTD9) (B aggressive lymphoma protein)

 PARP9_HUMAN             Reviewed;         854 AA.
Q8IXQ6; A8KA94; B2R8S9; E9PFM7; Q8TCP3; Q9BZL8; Q9BZL9;
10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
10-OCT-2003, sequence version 2.
05-DEC-2018, entry version 136.
RecName: Full=Poly [ADP-ribose] polymerase 9;
Short=PARP-9;
EC=2.4.2.30 {ECO:0000255|PROSITE-ProRule:PRU00397, ECO:0000269|PubMed:28525742};
AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 9;
Short=ARTD9;
AltName: Full=B aggressive lymphoma protein;
Name=PARP9; Synonyms=BAL, BAL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, VARIANT CYS-528, AND INVOLVEMENT IN B-CELL
LYMPHOMAS.
TISSUE=B-cell;
PubMed=11110709;
Aguiar R.C.T., Yakushijin Y., Kharbanda S., Salgia R., Fletcher J.A.,
Shipp M.A.;
"BAL is a novel risk-related gene in diffuse large B-cell lymphomas
that enhances cellular migration.";
Blood 96:4328-4334(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
CYS-528.
TISSUE=Trachea, and Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
VARIANTS VAL-517 AND CYS-528.
TISSUE=Mammary gland, and Melanoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 525-854.
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
INTERACTION WITH DTX3L.
PubMed=12670957; DOI=10.1074/jbc.M301157200;
Takeyama K., Aguiar R.C.T., Gu L., He C., Freeman G.J., Kutok J.L.,
Aster J.C., Shipp M.A.;
"The BAL-binding protein BBAP and related Deltex family members
exhibit ubiquitin-protein isopeptide ligase activity.";
J. Biol. Chem. 278:21930-21937(2003).
[7]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16809771; DOI=10.1128/MCB.02351-05;
Juszczynski P., Kutok J.L., Li C., Mitra J., Aguiar R.C.T.,
Shipp M.A.;
"BAL1 and BBAP are regulated by a gamma interferon-responsive
bidirectional promoter and are overexpressed in diffuse large B-cell
lymphomas with a prominent inflammatory infiltrate.";
Mol. Cell. Biol. 26:5348-5359(2006).
[8]
NOMENCLATURE.
PubMed=20106667; DOI=10.1016/j.tibs.2009.12.003;
Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.;
"Toward a unified nomenclature for mammalian ADP-
ribosyltransferases.";
Trends Biochem. Sci. 35:208-219(2010).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARP1, AND DOMAIN
MACRO 2.
PubMed=23230272; DOI=10.1128/MCB.00990-12;
Yan Q., Xu R., Zhu L., Cheng X., Wang Z., Manis J., Shipp M.A.;
"BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose)
activation, ubiquitylation, and double-strand DNA repair independent
of ATM, MDC1, and RNF8.";
Mol. Cell. Biol. 33:845-857(2013).
[10]
FUNCTION, INTERACTION WITH DTX3L AND STAT1, IDENTIFICATION IN A
COMPLEX WITH DTX3L; STAT1 AND HIST1H2BH, SUBCELLULAR LOCATION,
INDUCTION, DOMAIN, AND MUTAGENESIS OF GLY-147 AND GLY-346.
PubMed=26479788; DOI=10.1038/ni.3279;
Zhang Y., Mao D., Roswit W.T., Jin X., Patel A.C., Patel D.A.,
Agapov E., Wang Z., Tidwell R.M., Atkinson J.J., Huang G.,
McCarthy R., Yu J., Yun N.E., Paessler S., Lawson T.G., Omattage N.S.,
Brett T.J., Holtzman M.J.;
"PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C
protease to enhance interferon signaling and control viral
infection.";
Nat. Immunol. 16:1215-1227(2015).
[11]
FUNCTION, INTERACTION WITH PARP14, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, INDUCTION, AND ADP-RIBOSYLATION.
PubMed=27796300; DOI=10.1038/ncomms12849;
Iwata H., Goettsch C., Sharma A., Ricchiuto P., Goh W.W., Halu A.,
Yamada I., Yoshida H., Hara T., Wei M., Inoue N., Fukuda D.,
Mojcher A., Mattson P.C., Barabasi A.L., Boothby M., Aikawa E.,
Singh S.A., Aikawa M.;
"PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-
ribosylation.";
Nat. Commun. 7:12849-12849(2016).
[12]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, IDENTIFICATION IN A COMPLEX WITH WITH DTX3L, SUBCELLULAR
LOCATION, DOMAIN, AND MUTAGENESIS OF GLY-147; GLY-346;
719-GLY--ARG-722; TYR-737; PHE-738; 766-VAL--GLY-769;
780-VAL--LEU-784; 802-PRO--GLU-803 AND 831-TYR--ASP-854.
PubMed=28525742; DOI=10.1016/j.molcel.2017.04.028;
Yang C.S., Jividen K., Spencer A., Dworak N., Ni L., Oostdyk L.T.,
Chatterjee M., Kusmider B., Reon B., Parlak M., Gorbunova V.,
Abbas T., Jeffery E., Sherman N.E., Paschal B.M.;
"Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase
Dtx3L/Parp9.";
Mol. Cell 66:503-516(2017).
[13]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 310-493.
Elkins J.M.;
"Structure of Parp9 2Nd Macrodomain.";
Submitted (FEB-2015) to the PDB data bank.
-!- 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}.
-!- CATALYTIC ACTIVITY:
Reaction=NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide +
(ADP-D-ribosyl)(n+1)-acceptor.; EC=2.4.2.30;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00397,
ECO:0000269|PubMed:28525742};
-!- ACTIVITY REGULATION: Binding to poly(ADP-ribose) does not affect
its activity. {ECO:0000269|PubMed:28525742}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=196 uM for NAD(+) {ECO:0000269|PubMed:28525742};
-!- SUBUNIT: Forms a stable complex with E3 ligase DTX3L; the
interaction is required for PARP9 mediated ADP-ribosylation of
ubiquitin (PubMed:12670957, PubMed:28525742). Interacts (via PARP
catalytic domain) with DTX3L (via N-terminus) (PubMed:26479788).
Forms a complex with STAT1 and DTX3L independently of IFNB1 or
IFNG-mediated STAT1 'Tyr-701' phosphorylation (PubMed:26479788).
Forms a complex with STAT1, DTX3L and histone H2B HIST1H2BH/H2BJ;
the interaction is likely to induce HIST1H2BH/H2BJ ubiquitination
(PubMed:26479788). Interacts (via N-terminus) with STAT1
(PubMed:26479788). Interacts with PARP14 in IFNG-stimulated
macrophages; the interaction prevents PARP14-mediated STAT1 and
STAT6 ADP-riboslylation (PubMed:27796300). Interacts with PARP1
(when poly-ADP-ribosylated) (PubMed:23230272).
{ECO:0000269|PubMed:12670957, ECO:0000269|PubMed:23230272,
ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:27796300,
ECO:0000269|PubMed:28525742}.
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Long, L;
IsoId=Q8IXQ6-1; Sequence=Displayed;
Name=2; Synonyms=Short, S;
IsoId=Q8IXQ6-2; Sequence=VSP_008505;
Name=3;
IsoId=Q8IXQ6-3; Sequence=VSP_008505, VSP_046086, VSP_046087;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in lymphocyte-rich tissues, spleen,
lymph nodes, peripheral blood lymphocytes and colonic mucosa
(PubMed:11110709, PubMed:16809771). Expressed in macrophages
(PubMed:27796300). Also expressed in nonhematopoietic tissues such
as heart and skeletal muscle (PubMed:11110709, PubMed:16809771).
Isoform 2 is the predominant form (PubMed:11110709). Most
abundantly expressed in lymphomas with a brisk host inflammatory
response (PubMed:11110709, PubMed:16809771). In diffuse large B-
cell lymphomas tumors, expressed specifically by malignant B-cells
(PubMed:11110709, PubMed:16809771). {ECO:0000269|PubMed:11110709,
ECO:0000269|PubMed:16809771, ECO:0000269|PubMed:27796300}.
-!- INDUCTION: Up-regulated by IFNG in macrophages and in B-cell
lymphoma cell lines (PubMed:16809771, PubMed:27796300,
PubMed:26479788). Up-regulated by IFNB1 or viral infection
(PubMed:26479788). Down-regulated by IL4 in macrophages
(PubMed:27796300). {ECO:0000269|PubMed:16809771,
ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:27796300}.
-!- DOMAIN: Macro domains 1 and 2 may be involved in the binding to
poly(ADP-ribose) (PubMed:28525742, PubMed:26479788). Macro domain
2 is required for recruitment to DNA damage sites
(PubMed:23230272). Macro domains 1 and 2 are probably dispensable
for the interaction with STAT1 and DTX3L and for STAT1
phosphorylation (PubMed:26479788). {ECO:0000269|PubMed:23230272,
ECO:0000269|PubMed:26479788, ECO:0000269|PubMed:28525742}.
-!- PTM: ADP-ribosylated by PARP14. {ECO:0000269|PubMed:27796300}.
-!- 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}.
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EMBL; AF307338; AAK07558.1; -; mRNA.
EMBL; AF307339; AAK07559.1; -; mRNA.
EMBL; AK292959; BAF85648.1; -; mRNA.
EMBL; AK313494; BAG36276.1; -; mRNA.
EMBL; AC092908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC096861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017463; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC039580; AAH39580.1; -; mRNA.
EMBL; AL713679; CAD28483.1; -; mRNA.
CCDS; CCDS3014.1; -. [Q8IXQ6-1]
CCDS; CCDS54633.1; -. [Q8IXQ6-3]
CCDS; CCDS54634.1; -. [Q8IXQ6-2]
RefSeq; NP_001139574.1; NM_001146102.1. [Q8IXQ6-1]
RefSeq; NP_001139575.1; NM_001146103.1. [Q8IXQ6-2]
RefSeq; NP_001139576.1; NM_001146104.1. [Q8IXQ6-2]
RefSeq; NP_001139577.1; NM_001146105.1. [Q8IXQ6-2]
RefSeq; NP_113646.2; NM_031458.2. [Q8IXQ6-1]
RefSeq; XP_005247877.1; XM_005247820.2. [Q8IXQ6-1]
RefSeq; XP_016862793.1; XM_017007304.1. [Q8IXQ6-1]
RefSeq; XP_016862794.1; XM_017007305.1. [Q8IXQ6-2]
RefSeq; XP_016862795.1; XM_017007306.1. [Q8IXQ6-2]
UniGene; Hs.518200; -.
PDB; 5AIL; X-ray; 1.55 A; A/B=310-493.
PDBsum; 5AIL; -.
ProteinModelPortal; Q8IXQ6; -.
SMR; Q8IXQ6; -.
BioGrid; 123723; 11.
CORUM; Q8IXQ6; -.
IntAct; Q8IXQ6; 1.
STRING; 9606.ENSP00000353512; -.
iPTMnet; Q8IXQ6; -.
PhosphoSitePlus; Q8IXQ6; -.
BioMuta; PARP9; -.
DMDM; 48474734; -.
EPD; Q8IXQ6; -.
MaxQB; Q8IXQ6; -.
PaxDb; Q8IXQ6; -.
PeptideAtlas; Q8IXQ6; -.
PRIDE; Q8IXQ6; -.
ProteomicsDB; 71045; -.
ProteomicsDB; 71046; -. [Q8IXQ6-2]
Ensembl; ENST00000360356; ENSP00000353512; ENSG00000138496. [Q8IXQ6-1]
Ensembl; ENST00000462315; ENSP00000418894; ENSG00000138496. [Q8IXQ6-3]
Ensembl; ENST00000471785; ENSP00000419001; ENSG00000138496. [Q8IXQ6-2]
Ensembl; ENST00000477522; ENSP00000419506; ENSG00000138496. [Q8IXQ6-2]
GeneID; 83666; -.
KEGG; hsa:83666; -.
UCSC; uc003efh.5; human. [Q8IXQ6-1]
CTD; 83666; -.
DisGeNET; 83666; -.
EuPathDB; HostDB:ENSG00000138496.16; -.
GeneCards; PARP9; -.
HGNC; HGNC:24118; PARP9.
HPA; HPA066708; -.
MIM; 612065; gene.
neXtProt; NX_Q8IXQ6; -.
OpenTargets; ENSG00000138496; -.
PharmGKB; PA134870403; -.
eggNOG; KOG2633; Eukaryota.
eggNOG; COG2110; LUCA.
GeneTree; ENSGT00940000158837; -.
HOGENOM; HOG000115452; -.
HOVERGEN; HBG045406; -.
InParanoid; Q8IXQ6; -.
KO; K15260; -.
OMA; GSFCQGH; -.
OrthoDB; EOG091G02AK; -.
PhylomeDB; Q8IXQ6; -.
TreeFam; TF328965; -.
Reactome; R-HSA-197264; Nicotinamide salvaging.
ChiTaRS; PARP9; human.
GenomeRNAi; 83666; -.
PRO; PR:Q8IXQ6; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000138496; Expressed in 184 organ(s), highest expression level in ectocervix.
CleanEx; HS_PARP9; -.
ExpressionAtlas; Q8IXQ6; baseline and differential.
Genevisible; Q8IXQ6; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
GO; GO:0072570; F:ADP-D-ribose binding; IMP:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:0097677; F:STAT family protein binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IPI:UniProtKB.
GO; GO:0016477; P:cell migration; TAS:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0035563; P:positive regulation of chromatin binding; IGI:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IGI:UniProtKB.
GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IMP:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IGI:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:0010608; P:posttranscriptional regulation of gene expression; IMP:UniProtKB.
GO; GO:0006471; P:protein ADP-ribosylation; IDA:UniProtKB.
GO; GO:0060330; P:regulation of response to interferon-gamma; IDA:UniProtKB.
InterPro; IPR002589; Macro_dom.
InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
Pfam; PF01661; Macro; 2.
SMART; SM00506; A1pp; 2.
PROSITE; PS51154; MACRO; 2.
PROSITE; PS51059; PARP_CATALYTIC; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Alternative splicing;
Antiviral defense; Complete proteome; Cytoplasm; DNA damage;
DNA repair; Immunity; Innate immunity; NAD; Nucleus; Polymorphism;
Reference proteome; Repeat; Transferase.
CHAIN 1 854 Poly [ADP-ribose] polymerase 9.
/FTId=PRO_0000211339.
DOMAIN 107 296 Macro 1. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 306 487 Macro 2. {ECO:0000255|PROSITE-
ProRule:PRU00490}.
DOMAIN 628 850 PARP catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00397}.
VAR_SEQ 17 51 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11110709,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_008505.
VAR_SEQ 729 745 DPKYGAGIYFTKNLKNL -> GRCQCLIIGATLWNLVS
(in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046086.
VAR_SEQ 746 854 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046087.
VARIANT 21 21 S -> L (in dbSNP:rs34006803).
/FTId=VAR_056654.
VARIANT 517 517 I -> V (in dbSNP:rs28365795).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_056655.
VARIANT 528 528 Y -> C (in dbSNP:rs9851180).
{ECO:0000269|PubMed:11110709,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_056656.
VARIANT 651 651 T -> A (in dbSNP:rs6780543).
/FTId=VAR_056657.
MUTAGEN 147 147 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.
{ECO:0000269|PubMed:26479788,
ECO:0000269|PubMed:28525742}.
MUTAGEN 346 346 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.
{ECO:0000269|PubMed:26479788,
ECO:0000269|PubMed:28525742}.
MUTAGEN 719 722 Missing: Loss of ADP ribosylation
activity and interaction with DTX3L.
{ECO:0000269|PubMed:28525742}.
MUTAGEN 737 737 Y->A: No defect in ubiquitin ADP
ribosylation and the interaction with
DTX3L. {ECO:0000269|PubMed:28525742}.
MUTAGEN 738 738 F->K: Severe reduction in ubiquitin ADP
ribosylation. No effect on the
interaction with DTX3L and on DTX3L E3
ligase activity. Increases DNA repair.
{ECO:0000269|PubMed:28525742}.
MUTAGEN 766 769 Missing: Loss of ADP ribosylation
activity and interaction with DTX3L.
{ECO:0000269|PubMed:28525742}.
MUTAGEN 780 784 Missing: Reduces ADP ribosylation
activity and interaction with DTX3L.
{ECO:0000269|PubMed:28525742}.
MUTAGEN 802 803 PE->AA: No defect in ADP ribosylation and
interaction with DTX3L.
{ECO:0000269|PubMed:28525742}.
MUTAGEN 831 854 Missing: No defect in ADP ribosylation
and interaction with DTX3L.
{ECO:0000269|PubMed:28525742}.
CONFLICT 487 487 S -> P (in Ref. 2; BAF85648).
{ECO:0000305}.
CONFLICT 839 839 F -> S (in Ref. 2; BAG36276).
{ECO:0000305}.
STRAND 311 314 {ECO:0000244|PDB:5AIL}.
STRAND 317 324 {ECO:0000244|PDB:5AIL}.
HELIX 326 328 {ECO:0000244|PDB:5AIL}.
STRAND 330 339 {ECO:0000244|PDB:5AIL}.
HELIX 347 356 {ECO:0000244|PDB:5AIL}.
HELIX 358 370 {ECO:0000244|PDB:5AIL}.
STRAND 378 382 {ECO:0000244|PDB:5AIL}.
STRAND 386 395 {ECO:0000244|PDB:5AIL}.
HELIX 402 419 {ECO:0000244|PDB:5AIL}.
STRAND 423 427 {ECO:0000244|PDB:5AIL}.
STRAND 433 437 {ECO:0000244|PDB:5AIL}.
HELIX 439 456 {ECO:0000244|PDB:5AIL}.
STRAND 462 468 {ECO:0000244|PDB:5AIL}.
HELIX 473 490 {ECO:0000244|PDB:5AIL}.
SEQUENCE 854 AA; 96343 MW; CBBB3B4B7CA1CDA4 CRC64;
MDFSMVAGAA AYNEKSGRIT SLSLLFQKVF AQIFPQWRKG NTEECLPYKC SETGALGENY
SWQIPINHND FKILKNNERQ LCEVLQNKFG CISTLVSPVQ EGNSKSLQVF RKMLTPRIEL
SVWKDDLTTH AVDAVVNAAN EDLLHGGGLA LALVKAGGFE IQEESKQFVA RYGKVSAGEI
AVTGAGRLPC KQIIHAVGPR WMEWDKQGCT GKLQRAIVSI LNYVIYKNTH IKTVAIPALS
SGIFQFPLNL CTKTIVETIR VSLQGKPMMS NLKEIHLVSN EDPTVAAFKA ASEFILGKSE
LGQETTPSFN AMVVNNLTLQ IVQGHIEWQT ADVIVNSVNP HDITVGPVAK SILQQAGVEM
KSEFLATKAK QFQRSQLVLV TKGFNLFCKY IYHVLWHSEF PKPQILKHAM KECLEKCIEQ
NITSISFPAL GTGNMEIKKE TAAEILFDEV LTFAKDHVKH QLTVKFVIFP TDLEIYKAFS
SEMAKRSKML SLNNYSVPQS TREEKRENGL EARSPAINLM GFNVEEMYEA HAWIQRILSL
QNHHIIENNH ILYLGRKEHD ILSQLQKTSS VSITEIISPG RTELEIEGAR ADLIEVVMNI
EDMLCKVQEE MARKKERGLW RSLGQWTIQQ QKTQDEMKEN IIFLKCPVPP TQELLDQKKQ
FEKCGLQVLK VEKIDNEVLM AAFQRKKKMM EEKLHRQPVS HRLFQQVPYQ FCNVVCRVGF
QRMYSTPCDP KYGAGIYFTK NLKNLAEKAK KISAADKLIY VFEAEVLTGF FCQGHPLNIV
PPPLSPGAID GHDSVVDNVS SPETFVIFSG MQAIPQYLWT CTQEYVQSQD YSSGPMRPFA
QHPWRGFASG SPVD


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