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Protein

Poly [ADP-ribose] polymerase 9

Gene

Parp9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

In concert with DTX3L plays a role in PARP1-dependent DNA damage repair. PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. Involved in inducing the expression of IFN-gamma-responsive genes (By similarity).By similarity

Catalytic activityi

NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Poly [ADP-ribose] polymerase 9 (EC:2.4.2.30)
Short name:
PARP-9
Alternative name(s):
ADP-ribosyltransferase diphtheria toxin-like 9
Short name:
ARTD9
B aggressive lymphoma protein homolog
Gene namesi
Name:Parp9
Synonyms:Bal
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1933117. Parp9.

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Nucleus By similarity

  • Note: Shuttles between the nucleus and the cytosol. Export to the cytosol depends on the interaction with DTX3L (By similarity). Localizes at sites of DNA damage in a PARP1-dependent manner (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 866866Poly [ADP-ribose] polymerase 9PRO_0000211340Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8CAS9.
MaxQBiQ8CAS9.
PaxDbiQ8CAS9.
PeptideAtlasiQ8CAS9.
PRIDEiQ8CAS9.

PTM databases

iPTMnetiQ8CAS9.
PhosphoSiteiQ8CAS9.

Expressioni

Tissue specificityi

Highly expressed in the thymus and intestine.1 Publication

Developmental stagei

Developmentally regulated. Expressed prominently in the developing thymus and the gut, and also weakly expressed in specific regions of the developing brain.1 Publication

Gene expression databases

BgeeiQ8CAS9.
CleanExiMM_PARP9.
ExpressionAtlasiQ8CAS9. baseline and differential.
GenevisibleiQ8CAS9. MM.

Interactioni

Subunit structurei

Interacts with DTX3L. Interacts with PARP1 (when poly-ADP-ribosylated).By similarity

Protein-protein interaction databases

IntActiQ8CAS9. 2 interactions.
MINTiMINT-4089071.
STRINGi10090.ENSMUSP00000110528.

Structurei

3D structure databases

ProteinModelPortaliQ8CAS9.
SMRiQ8CAS9. Positions 110-498, 675-827.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 298190Macro 1PROSITE-ProRule annotationAdd
BLAST
Domaini313 – 492180Macro 2PROSITE-ProRule annotationAdd
BLAST
Domaini635 – 853219PARP catalyticPROSITE-ProRule annotationAdd
BLAST

Domaini

The domain macro 2 is required for recruitment to DNA damage sites.By similarity

Sequence similaritiesi

Contains 2 Macro domains.PROSITE-ProRule annotation
Contains 1 PARP catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2633. Eukaryota.
COG2110. LUCA.
GeneTreeiENSGT00760000119084.
HOGENOMiHOG000115452.
HOVERGENiHBG045406.
InParanoidiQ8CAS9.
KOiK15260.
OMAiSGIFQFP.
OrthoDBiEOG786H2D.
PhylomeDBiQ8CAS9.
TreeFamiTF328965.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR002589. Macro_dom.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
[Graphical view]
PfamiPF01661. Macro. 2 hits.
[Graphical view]
SMARTiSM00506. A1pp. 2 hits.
[Graphical view]
PROSITEiPS51154. MACRO. 2 hits.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CAS9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAYYMDTWAA APAERPGMIA SLSLSFKKAF AELFPQRRRG HSEGDYPPLR
60 70 80 90 100
GSANNSLEEH YRWQIPIKHN VFEILKSNES QLCEVLQNKF GCISTLSCPT
110 120 130 140 150
LAGSSSPAQR VFRRTLIPGI ELSVWKDDLT RHVVDAVVNA ANENLLHGSG
160 170 180 190 200
LAGSLVKTGG FEIQEESKRI IANVGKISVG GIAITGAGRL PCHLIIHAVG
210 220 230 240 250
PRWTVTNSQT AIELLKFAIR NILDYVTKYD LRIKTVAIPA LSSGIFQFPL
260 270 280 290 300
DLCTSIILET IRLYFQDKQM FGNLREIHLV SNEDPTVASF KSASESILGR
310 320 330 340 350
DLSSWGGPET DPASTMTLRI GRGLTLQIVQ GCIEMQTTDV IVNSGYMQDF
360 370 380 390 400
KSGRVAQSIL RQAGVEMEKE LDKVNLSTDY QEVWVTKGFK LSCQYVFHVA
410 420 430 440 450
WHSQINKYQI LKDAMKSCLE KCLKPDINSI SFPALGTGLM DLKKSTAAQI
460 470 480 490 500
MFEEVFAFAK EHKEKTLTVK IVIFPVDVET YKIFYAEMTK RSNELNLSGN
510 520 530 540 550
SGALALQWSS GEQRRGGLEA GSPAINLMGV KVGEMCEAQE WIERLLVSLD
560 570 580 590 600
HHIIENNHIL YLGKKEHDVL SELQTSTRVS ISETVSPRTA TLEIKGPQAD
610 620 630 640 650
LIDAVMRIEC MLCDVQEEVA GKREKNLWSL SGQGTNQQEK LDKMEESYTF
660 670 680 690 700
QRYPASLTQE LQDRKKQFEK CGLWVVQVEQ IDNKVLLAAF QEKKKMMEER
710 720 730 740 750
TPKGSGSQRL FQQVPHQFCN TVCRVGFHRM YSTSYNPVYG AGIYFTKSLK
760 770 780 790 800
NLADKVKKTS STDKLIYVFE AEVLTGSFCQ GNSSNIIPPP LSPGALDVND
810 820 830 840 850
SVVDNVSSPE TIVVFNGMQA MPLYLWTCTQ DRTFSQHPMW SQGYSSGPGM
860
VSSLQSWEWV LNGSSV
Note: No experimental confirmation available.
Length:866
Mass (Da):96,659
Last modified:October 10, 2003 - v2
Checksum:i790AF1968F6C035D
GO
Isoform 2 (identifier: Q8CAS9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     17-52: Missing.

Show »
Length:830
Mass (Da):92,669
Checksum:i779197039E99D012
GO
Isoform 3 (identifier: Q8CAS9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     679-866: Missing.

Note: No experimental confirmation available.
Show »
Length:678
Mass (Da):75,739
Checksum:i19EBC4E623A9C48B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei17 – 5236Missing in isoform 2. 2 PublicationsVSP_008506Add
BLAST
Alternative sequencei679 – 866188Missing in isoform 3. 1 PublicationVSP_008507Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037903 mRNA. Translation: BAC29897.1.
AK050032 mRNA. Translation: BAC34040.1.
BC003281 mRNA. Translation: AAH03281.1.
BC070466 mRNA. Translation: AAH70466.1.
CCDSiCCDS37326.1. [Q8CAS9-2]
RefSeqiNP_084529.1. NM_030253.3. [Q8CAS9-2]
XP_006522818.1. XM_006522755.2. [Q8CAS9-1]
XP_006522819.1. XM_006522756.2. [Q8CAS9-1]
XP_006522820.1. XM_006522757.2. [Q8CAS9-2]
UniGeneiMm.49074.

Genome annotation databases

EnsembliENSMUST00000114877; ENSMUSP00000110527; ENSMUSG00000022906. [Q8CAS9-3]
ENSMUST00000114878; ENSMUSP00000110528; ENSMUSG00000022906. [Q8CAS9-2]
GeneIDi80285.
KEGGimmu:80285.
UCSCiuc007zbx.1. mouse. [Q8CAS9-1]
uc007zby.2. mouse. [Q8CAS9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037903 mRNA. Translation: BAC29897.1.
AK050032 mRNA. Translation: BAC34040.1.
BC003281 mRNA. Translation: AAH03281.1.
BC070466 mRNA. Translation: AAH70466.1.
CCDSiCCDS37326.1. [Q8CAS9-2]
RefSeqiNP_084529.1. NM_030253.3. [Q8CAS9-2]
XP_006522818.1. XM_006522755.2. [Q8CAS9-1]
XP_006522819.1. XM_006522756.2. [Q8CAS9-1]
XP_006522820.1. XM_006522757.2. [Q8CAS9-2]
UniGeneiMm.49074.

3D structure databases

ProteinModelPortaliQ8CAS9.
SMRiQ8CAS9. Positions 110-498, 675-827.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CAS9. 2 interactions.
MINTiMINT-4089071.
STRINGi10090.ENSMUSP00000110528.

PTM databases

iPTMnetiQ8CAS9.
PhosphoSiteiQ8CAS9.

Proteomic databases

EPDiQ8CAS9.
MaxQBiQ8CAS9.
PaxDbiQ8CAS9.
PeptideAtlasiQ8CAS9.
PRIDEiQ8CAS9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114877; ENSMUSP00000110527; ENSMUSG00000022906. [Q8CAS9-3]
ENSMUST00000114878; ENSMUSP00000110528; ENSMUSG00000022906. [Q8CAS9-2]
GeneIDi80285.
KEGGimmu:80285.
UCSCiuc007zbx.1. mouse. [Q8CAS9-1]
uc007zby.2. mouse. [Q8CAS9-2]

Organism-specific databases

CTDi83666.
MGIiMGI:1933117. Parp9.

Phylogenomic databases

eggNOGiKOG2633. Eukaryota.
COG2110. LUCA.
GeneTreeiENSGT00760000119084.
HOGENOMiHOG000115452.
HOVERGENiHBG045406.
InParanoidiQ8CAS9.
KOiK15260.
OMAiSGIFQFP.
OrthoDBiEOG786H2D.
PhylomeDBiQ8CAS9.
TreeFamiTF328965.

Miscellaneous databases

PROiQ8CAS9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CAS9.
CleanExiMM_PARP9.
ExpressionAtlasiQ8CAS9. baseline and differential.
GenevisibleiQ8CAS9. MM.

Family and domain databases

Gene3Di3.90.228.10. 1 hit.
InterProiIPR002589. Macro_dom.
IPR012317. Poly(ADP-ribose)pol_cat_dom.
[Graphical view]
PfamiPF01661. Macro. 2 hits.
[Graphical view]
SMARTiSM00506. A1pp. 2 hits.
[Graphical view]
PROSITEiPS51154. MACRO. 2 hits.
PS51059. PARP_CATALYTIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Liver and Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Eye and Mammary tumor.
  3. "The macroPARP genes Parp-9 and Parp-14 are developmentally and differentially regulated in mouse tissues."
    Hakme A., Huber A., Dolle P., Schreiber V.
    Dev. Dyn. 237:209-215(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver, Lung and Spleen.

Entry informationi

Entry nameiPARP9_MOUSE
AccessioniPrimary (citable) accession number: Q8CAS9
Secondary accession number(s): Q6IRT6, Q99LF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 10, 2003
Last modified: July 6, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.