ART3

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ART3
Identifiers
Aliases	ART3 , ARTC3, ADP-ribosyltransferase 3
External IDs	OMIM: 603086; MGI: 1202729; HomoloGene: 911; GeneCards: ART3; OMA:ART3 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) [1] Band 4q21.1|4p15.1-p14 Start 76,011,184 bp [1] End 76,112,802 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5 E2|5 46.54 cM Start 92,479,686 bp [2] End 92,562,487 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle muscle of thigh biceps brachii Skeletal muscle tissue of rectus abdominis vastus lateralis muscle Skeletal muscle tissue of biceps brachii right testis cardiac muscle tissue of right atrium left testis thoracic diaphragm Top expressed in spermatocyte spermatid interventricular septum cardiac muscle tissue of left ventricle sciatic nerve muscle of thigh extensor digitorum longus muscle extraocular muscle ankle masseter muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function NAD+ ADP-ribosyltransferase activity glycosyltransferase activity NAD+-protein-arginine ADP-ribosyltransferase activity transferase activity Cellular component anchored component of membrane membrane integral component of plasma membrane extracellular exosome extracellular region plasma membrane intrinsic component of plasma membrane Biological process protein ADP-ribosylation C-terminal protein lipidation peptidyl-arginine ADP-ribosylation Sources:Amigo / QuickGO
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 NM_001370591 RefSeq (protein) NP_001123488 NP_001123489 NP_001170 NP_001364102 NP_001364103 NP_001364104 NP_001364105 NP_001364106 NP_001364107 NP_001364108 NP_001364109 NP_001364110 NP_001364111 NP_001364112 NP_001364113 NP_001364114 NP_001297593 NP_001297594 NP_859417 NP_001357520 Location (UCSC) Chr 4: 76.01 – 76.11 Mb Chr 5: 92.48 – 92.56 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ecto-ADP-ribosyltransferase 3 is an enzyme that in humans is encoded by the ART3 gene. ^{[5] [6]}

References

1. GRCh38: Ensembl release 89: ENSG00000156219 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000034842 – 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. 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.
6. "Entrez Gene: ART3 ADP-ribosyltransferase 3".

External links

• Human ART3 genome location and ART3 gene details page in the UCSC Genome Browser .

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. S2CID   1083606.
• 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. CiteSeerX   10.1.1.325.7458 . 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.