| Tag | Content |
|---|
| CPLM ID | CPLM-016770 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Poly [ADP-ribose] polymerase 9 |
Protein Synonyms/Alias | PARP-9; ADP-ribosyltransferase diphtheria toxin-like 9; ARTD9; B aggressive lymphoma protein homolog |
Gene Name | Parp9 |
Gene Synonyms/Alias | Bal |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 68 | YRWQIPIKHNVFEIL | ubiquitination | [1] | | 228 | NILDYVTKYDLRIKT | ubiquitination | [1] | | 625 | EVAGKREKNLWSLSG | ubiquitination | [1] | | 640 | QGTNQQEKLDKMEES | ubiquitination | [1] | | 643 | NQQEKLDKMEESYTF | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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). |
Sequence Annotation | DOMAIN 109 298 Macro 1.
DOMAIN 313 492 Macro 2.
DOMAIN 635 853 PARP catalytic.
MOD_RES 42 42 Phosphoserine. |
Keyword | Alternative splicing; Complete proteome; Cytoplasm; DNA damage; DNA repair; NAD; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 866 AA |
Protein Sequence | MAYYMDTWAA APAERPGMIA SLSLSFKKAF AELFPQRRRG HSEGDYPPLR GSANNSLEEH 60
YRWQIPIKHN VFEILKSNES QLCEVLQNKF GCISTLSCPT LAGSSSPAQR VFRRTLIPGI 120
ELSVWKDDLT RHVVDAVVNA ANENLLHGSG LAGSLVKTGG FEIQEESKRI IANVGKISVG 180
GIAITGAGRL PCHLIIHAVG PRWTVTNSQT AIELLKFAIR NILDYVTKYD LRIKTVAIPA 240
LSSGIFQFPL DLCTSIILET IRLYFQDKQM FGNLREIHLV SNEDPTVASF KSASESILGR 300
DLSSWGGPET DPASTMTLRI GRGLTLQIVQ GCIEMQTTDV IVNSGYMQDF KSGRVAQSIL 360
RQAGVEMEKE LDKVNLSTDY QEVWVTKGFK LSCQYVFHVA WHSQINKYQI LKDAMKSCLE 420
KCLKPDINSI SFPALGTGLM DLKKSTAAQI MFEEVFAFAK EHKEKTLTVK IVIFPVDVET 480
YKIFYAEMTK RSNELNLSGN SGALALQWSS GEQRRGGLEA GSPAINLMGV KVGEMCEAQE 540
WIERLLVSLD HHIIENNHIL YLGKKEHDVL SELQTSTRVS ISETVSPRTA TLEIKGPQAD 600
LIDAVMRIEC MLCDVQEEVA GKREKNLWSL SGQGTNQQEK LDKMEESYTF QRYPASLTQE 660
LQDRKKQFEK CGLWVVQVEQ IDNKVLLAAF QEKKKMMEER TPKGSGSQRL FQQVPHQFCN 720
TVCRVGFHRM YSTSYNPVYG AGIYFTKSLK NLADKVKKTS STDKLIYVFE AEVLTGSFCQ 780
GNSSNIIPPP LSPGALDVND SVVDNVSSPE TIVVFNGMQA MPLYLWTCTQ DRTFSQHPMW 840
SQGYSSGPGM VSSLQSWEWV LNGSSV 866 |
Gene Ontology | GO:0005737; C:cytoplasm; ISS:UniProtKB. GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. GO:0005634; C:nucleus; ISS:UniProtKB. GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB. GO:0006302; P:double-strand break repair; ISS:UniProtKB. GO:0060330; P:regulation of response to interferon-gamma; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |