PARP4

Poly [ADP-ribose] polymerase 4 is an enzyme that in humans is encoded by the PARP4 gene.^[5][6]

PARP4
Identifiers
Aliases	PARP4, ADPRTL1, ARTD4, PARP-4, PARPL, PH5P, VAULT3, VPARP, VWA5C, p193, poly(ADP-ribose) polymerase family member 4
External IDs	OMIM: 607519; MGI: 2685589; HomoloGene: 124423; GeneCards: PARP4; OMA:PARP4 - orthologs
Gene location (Human) Chr. Chromosome 13 (human)[1] Band 13q12.12 Start 24,420,931 bp[1] End 24,512,778 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14|14 C3 Start 56,813,076 bp[2] End 56,897,251 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in rectum duodenum monocyte gallbladder bone marrow cell blood islet of Langerhans transverse colon Achilles tendon endometrium Top expressed in lumbar spinal ganglion granulocyte gastrula transitional epithelium of urinary bladder duodenum muscle of thigh spleen zygote conjunctival fornix thymus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity DNA binding glycosyltransferase activity protein binding enzyme binding NAD+ ADP-ribosyltransferase activity protein ADP-ribosylase activity Cellular component cytoplasm membrane spindle spindle microtubule extracellular exosome cytoskeleton nucleus cytosol ribonucleoprotein complex Biological process protein ADP-ribosylation cell death cellular response to DNA damage stimulus inflammatory response DNA repair regulation of telomerase activity transport protein mono-ADP-ribosylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 143 328417 Ensembl ENSG00000102699 ENSMUSG00000054509 UniProt Q9UKK3 E9PYK3 RefSeq (mRNA) NM_006437 NM_001145978 RefSeq (protein) NP_006428 NP_001139450 Location (UCSC) Chr 13: 24.42 – 24.51 Mb Chr 14: 56.81 – 56.9 Mb PubMed search [3] [4]
Wikidata
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This gene encodes poly(ADP-ribosyl)transferase-like 1 protein, which is capable of catalyzing a poly(ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, but lacks an N-terminal DNA binding domain which activates the C-terminal catalytic domain of poly (ADP-ribosyl) transferase. Since this protein is not capable of binding DNA directly, its transferase activity may be activated by other factors such as protein-protein interaction mediated by the extensive carboxyl terminus.^[6]

Interactions

PARP4 has been shown to interact with Major vault protein.^[7][8]