PARP3

Protein-coding gene in the species Homo sapiens
PARP3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2EOC, 3C49, 3C4H, 3CE0, 3FHB, 4GV0, 4GV2, 4GV4, 4L6Z, 4L70, 4L7L, 4L7N, 4L7O, 4L7P, 4L7R, 4L7U

Identifiers
AliasesPARP3, ADPRT3, ADPRTL2, ADPRTL3, ARTD3, IRT1, PADPRT-3, poly(ADP-ribose) polymerase family member 3
External IDsOMIM: 607726; MGI: 1891258; HomoloGene: 4005; GeneCards: PARP3; OMA:PARP3 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for PARP3
Genomic location for PARP3
Band3p21.2Start51,942,345 bp[1]
End51,948,867 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for PARP3
Genomic location for PARP3
Band9|9 F1Start106,347,521 bp[2]
End106,354,148 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right adrenal cortex

  • left adrenal gland

  • left adrenal cortex

  • right lobe of liver

  • apex of heart

  • right lobe of thyroid gland

  • left lobe of thyroid gland

  • muscle layer of sigmoid colon

  • transverse colon

  • stromal cell of endometrium
Top expressed in
  • extraocular muscle

  • ankle

  • temporal muscle

  • triceps brachii muscle

  • digastric muscle

  • sternocleidomastoid muscle

  • vastus lateralis muscle

  • gastrocnemius muscle

  • mesenteric lymph nodes

  • medial head of gastrocnemius muscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • glycosyltransferase activity
  • catalytic activity
  • NAD+ ADP-ribosyltransferase activity
  • DNA ligase (ATP) activity
  • protein ADP-ribosylase activity
  • protein binding
  • NAD DNA ADP-ribosyltransferase activity
Cellular component
  • cytoplasm
  • site of double-strand break
  • centriole
  • cytoskeleton
  • nucleus
  • microtubule organizing center
  • nucleolus
  • chromosome
Biological process
  • protein localization to site of double-strand break
  • DNA ligation involved in DNA repair
  • lagging strand elongation
  • regulation of mitotic spindle organization
  • positive regulation of DNA ligation
  • telomere maintenance
  • double-strand break repair
  • protein ADP-ribosylation
  • DNA repair
  • negative regulation of telomerase RNA reverse transcriptase activity
  • protein poly-ADP-ribosylation
  • DNA ADP-ribosylation
  • negative regulation of isotype switching
  • protein auto-ADP-ribosylation
  • protein mono-ADP-ribosylation
  • positive regulation of double-strand break repair via nonhomologous end joining
  • cellular response to DNA damage stimulus
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10039

235587

Ensembl

ENSG00000041880

ENSMUSG00000023249

UniProt

Q9Y6F1

Q3ULW8

RefSeq (mRNA)

NM_001003931
NM_001003935
NM_005485
NM_001370239
NM_001370240

NM_145619
NM_001311150

RefSeq (protein)

NP_001003931
NP_005476
NP_001357168
NP_001357169

NP_001298079
NP_663594

Location (UCSC)Chr 3: 51.94 – 51.95 MbChr 9: 106.35 – 106.35 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Poly [ADP-ribose] polymerase 3 is an enzyme that in humans is encoded by the PARP3 gene.[5][6]

The protein encoded by this gene belongs to the PARP family. These enzymes modify nuclear proteins by poly-ADP-ribosylation, which is required for DNA repair, regulation of apoptosis, and maintenance of genomic stability. This gene encodes the poly(ADP-ribosyl)transferase 3, which is preferentially localized to the daughter centriole throughout the cell cycle. Alternatively spliced transcript variants encoding different isoforms have been identified.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000041880 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023249 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Johansson M (Aug 1999). "A human poly(ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues". Genomics. 57 (3): 442–5. doi:10.1006/geno.1999.5799. PMID 10329013.
  6. ^ a b "Entrez Gene: PARP3 poly (ADP-ribose) polymerase family, member 3".

Further reading

  • Bashford CL, Chance B, Lloyd D, Poole RK (1981). "Oscillations of redox states in synchronously dividing cultures of Acanthamoeba castellanii and Schizosaccharomyces pombe". Biophys. J. 29 (1): 1–11. Bibcode:1980BpJ....29....1B. doi:10.1016/S0006-3495(80)85114-9. PMC 1328658. PMID 7260241.
  • Borggrefe T, Wabl M, Akhmedov AT, Jessberger R (1998). "A B-cell-specific DNA recombination complex". J. Biol. Chem. 273 (27): 17025–35. doi:10.1074/jbc.273.27.17025. PMID 9642267.
  • Berghammer H, Ebner M, Marksteiner R, Auer B (1999). "pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene related to truncated pADPRT homologues in plants and Caenorhabditis elegans". FEBS Lett. 449 (2–3): 259–63. doi:10.1016/S0014-5793(99)00448-2. PMID 10338144. S2CID 3251763.
  • Still IH, Vince P, Cowell JK (2000). "Identification of a novel gene (ADPRTL1) encoding a potential Poly(ADP-ribosyl)transferase protein". Genomics. 62 (3): 533–6. doi:10.1006/geno.1999.6024. PMID 10644454.
  • Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. Bibcode:2000PNAS...97.3491D. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
  • Glowacki G, Braren R, Cetkovic-Cvrlje M, et al. (2001). "Structure, chromosomal localization, and expression of the gene for mouse ecto-mono(ADP-ribosyl)transferase ART5". Gene. 275 (2): 267–77. doi:10.1016/S0378-1119(01)00608-4. PMID 11587854.
  • Wistow G, Bernstein SL, Wyatt MK, et al. (2002). "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants". Mol. Vis. 8: 205–20. PMID 12107410.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Augustin A, Spenlehauer C, Dumond H, et al. (2004). "PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression". J. Cell Sci. 116 (Pt 8): 1551–62. doi:10.1242/jcs.00341. PMID 12640039.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Rouleau M, McDonald D, Gagné P, et al. (2007). "PARP-3 associates with polycomb group bodies and with components of the DNA damage repair machinery". J. Cell. Biochem. 100 (2): 385–401. doi:10.1002/jcb.21051. PMID 16924674. S2CID 25618577.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • Lehtiö L, Jemth AS, Collins R, et al. (2009). "Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3". J. Med. Chem. 52 (9): 3108–3111. doi:10.1021/jm900052j. PMID 19354255.
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