ART3

ART3
Identifiers
Aliases	ART3, ARTC3, ADP-ribosyltransferase 3
External IDs	MGI: 1202729 HomoloGene: 911 GeneCards: ART3
Gene ontology Molecular function • NAD+ ADP-ribosyltransferase activity • transferase activity, transferring glycosyl groups • NAD(P)+-protein-arginine ADP-ribosyltransferase activity • transferase activity Cellular component • anchored component of membrane • plasma membrane • membrane • integral component of plasma membrane • extracellular exosome Biological process • protein ADP-ribosylation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	419	109979
Ensembl	ENSG00000156219	ENSMUSG00000034842
UniProt	Q13508	Q8R2G4
RefSeq (mRNA)	NM_001130016 NM_001130017 NM_001179	NM_181728 NM_001310664 NM_001310665
RefSeq (protein)	NP_001123488.1 NP_001123489.1 NP_001170.2	NP_001297594.1 NP_859417.2
Location (UCSC)	Chr 4: 76.01 – 76.11 Mb	Chr 5: 92.33 – 92.41 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Ecto-ADP-ribosyltransferase 3 is an enzyme that in humans is encoded by the ART3 gene.^[3][4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Koch-Nolte F, Haag F, Braren R, Kühl M, Hoovers J, Balasubramanian S, Bazan F, Thiele HG (1997). "Two novel human members of an emerging mammalian gene family related to mono-ADP-ribosylating bacterial toxins". Genomics. 39 (3): 370–6. doi:10.1006/geno.1996.4520. PMID 9119374.
4. "Entrez Gene: ART3 ADP-ribosyltransferase 3".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Lévy I, Wu YQ, Roeckel N, Bulle F, Pawlak A, Siegrist S, Mattéi MG, Guellaën G (1996). "Human testis specifically expresses a homologue of the rodent T lymphocytes RT6 mRNA". FEBS Lett. 382 (3): 276–80. doi:10.1016/0014-5793(96)00183-4. PMID 8605984.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Balducci E, Horiba K, Usuki J, Park M, Ferrans VJ, Moss J (1999). "Selective expression of RT6 superfamily in human bronchial epithelial cells". Am. J. Respir. Cell Mol. Biol. 21 (3): 337–46. doi:10.1165/ajrcmb.21.3.3638. PMID 10460751.
• Grahnert A, Friedrich M, Pfister M, Haag F, Koch-Nolte F, Hauschildt S (2002). "Mono-ADP-ribosyltransferases in human monocytes: regulation by lipopolysaccharide". Biochem. J. 362 (Pt 3): 717–23. doi:10.1042/0264-6021:3620717. PMC 1222437. PMID 11879200.
• Glowacki G, Braren R, Firner K, Nissen M, Kühl M, Reche P, Bazan F, Cetkovic-Cvrlje M, Leiter E, Haag F, Koch-Nolte F (2002). "The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse". Protein Sci. 11 (7): 1657–70. doi:10.1110/ps.0200602. PMC 2373659. PMID 12070318.
• Friedrich M, Grahnert A, Paasch U, Tannapfel A, Koch-Nolte F, Hauschildt S (2006). "Expression of toxin-related human mono-ADP-ribosyltransferase 3 in human testes". Asian J. Androl. 8 (3): 281–7. doi:10.1111/j.1745-7262.2006.00125.x. PMID 16625277.
• Friedrich M, Grahnert A, Klein C, Tschöp K, Engeland K, Hauschildt S (2006). "Genomic organization and expression of the human mono-ADP-ribosyltransferase ART3 gene". Biochim. Biophys. Acta. 1759 (6): 270–80. doi:10.1016/j.bbaexp.2006.06.004. PMID 16934346.