TRIM23

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

GTP-binding protein ARD-1 is a protein that in humans is encoded by the TRIM23 gene.

Function

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phospholipase D activation. Three alternatively spliced transcript variants for this gene have been described.

Interactions

TRIM23 has been shown to interact with TRIM31, TRIM29 and PSCD1.

Further reading

• Vitale N, Moss J, Vaughan M (Mar 1996). "ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain". Proceedings of the National Academy of Sciences of the United States of America. 93 (5): 1941–4. doi:10.1073/pnas.93.5.1941. PMC 39887. PMID 8700863.
• Vitale N, Moss J, Vaughan M (Oct 1997). "Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1". The Journal of Biological Chemistry. 272 (40): 25077–82. doi:10.1074/jbc.272.40.25077. PMID 9312116.
• Vitale N, Moss J, Vaughan M (Jan 1998). "Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1)". The Journal of Biological Chemistry. 273 (5): 2553–60. doi:10.1074/jbc.273.5.2553. PMID 9446556.
• Vitale N, Horiba K, Ferrans VJ, Moss J, Vaughan M (Jul 1998). "Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus". Proceedings of the National Academy of Sciences of the United States of America. 95 (15): 8613–8. doi:10.1073/pnas.95.15.8613. PMC 21124. PMID 9671726.
• Vitale N, Pacheco-Rodriguez G, Ferrans VJ, Riemenschneider W, Moss J, Vaughan M (Jul 2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". The Journal of Biological Chemistry. 275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID 10748148.
• Vitale N, Ferrans VJ, Moss J, Vaughan M (Oct 2000). "Identification of lysosomal and Golgi localization signals in GAP and ARF domains of ARF domain protein 1". Molecular and Cellular Biology. 20 (19): 7342–52. doi:10.1128/MCB.20.19.7342-7352.2000. PMC 86288. PMID 10982851.
• Reymond A, Meroni G, Fantozzi A, Merla G, Cairo S, Luzi L, Riganelli D, Zanaria E, Messali S, Cainarca S, Guffanti A, Minucci S, Pelicci PG, Ballabio A (May 2001). "The tripartite motif family identifies cell compartments". The EMBO Journal. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMC 125245. PMID 11331580.
• Vichi A, Payne DM, Pacheco-Rodriguez G, Moss J, Vaughan M (Feb 2005). "E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)". Proceedings of the National Academy of Sciences of the United States of America. 102 (6): 1945–50. doi:10.1073/pnas.0409800102. PMC 548593. PMID 15684077.