ID:PARP9_HUMAN DESCRIPTION: RecName: Full=Poly [ADP-ribose] polymerase 9; Short=PARP-9; EC=2.4.2.30; AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 9; Short=ARTD9; AltName: Full=B aggressive lymphoma protein; FUNCTION: Involved in inducing the expression of IFN-gamma- responsive genes. CATALYTIC ACTIVITY: NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. SUBUNIT: Interacts with DTX3L. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=Shuttles between the nucleus and the cytosol. Export to the cytosol depends on the interaction with DTX3L. TISSUE SPECIFICITY: Expressed in lymphocyte-rich tissues, spleen, lymph nodes, peripheral blood lymphocytes and colonic mucosa. Also expressed in nonhematopoietic tissues such as heart and skeletal muscle. Isoform 2 is the predominant form. Most abundantly expressed in lymphomas with a brisk host inflammatory response. In diffuse large B-cell lymphomas tumors, expressed specifically by malignant B-cells. INDUCTION: Up-regulated by IFN-gamma in B-cell lymphoma cell lines. 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. SIMILARITY: Contains 2 Macro domains. SIMILARITY: Contains 1 PARP catalytic domain.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q8IXQ6
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0001191 transcriptional repressor activity, RNA polymerase II transcription factor binding GO:0003950 NAD+ ADP-ribosyltransferase activity GO:0004857 enzyme inhibitor activity GO:0005515 protein binding GO:0016740 transferase activity GO:0019899 enzyme binding GO:0042393 histone binding GO:0044389 ubiquitin-like protein ligase binding GO:0072570 ADP-D-ribose binding GO:0097677 STAT family protein binding GO:0070403 NAD+ binding
Biological Process: GO:0000122 negative regulation of transcription from RNA polymerase II promoter GO:0002230 positive regulation of defense response to virus by host GO:0002376 immune system process GO:0006281 DNA repair GO:0006302 double-strand break repair GO:0006471 protein ADP-ribosylation GO:0006974 cellular response to DNA damage stimulus GO:0010608 posttranscriptional regulation of gene expression GO:0010629 negative regulation of gene expression GO:0016477 cell migration GO:0034356 NAD biosynthesis via nicotinamide riboside salvage pathway GO:0035563 positive regulation of chromatin binding GO:0042531 positive regulation of tyrosine phosphorylation of STAT protein GO:0043086 negative regulation of catalytic activity GO:0045087 innate immune response GO:0045893 positive regulation of transcription, DNA-templated GO:0051607 defense response to virus GO:0060330 regulation of response to interferon-gamma GO:0060335 positive regulation of interferon-gamma-mediated signaling pathway GO:1900182 positive regulation of protein localization to nucleus GO:2001034 positive regulation of double-strand break repair via nonhomologous end joining GO:0070212 protein poly-ADP-ribosylation