TRIM23

Tripartite motif-containing 23
Identifiers
Symbols	TRIM23 ; ARD1; ARFD1; RNF46
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1251
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE TRIM23 204732 s at tn.png
File:PBB GE TRIM23 210994 x at tn.png
File:PBB GE TRIM23 210995 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
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

Tripartite motif-containing 23, also known as TRIM23, is a human gene.

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 phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described.

Further reading

• Mishima K, Tsuchiya M, Nightingale MS; et al. (1993). "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain". J. Biol. Chem. 268 (12): 8801–7. PMID 8473324.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Vitale N, Moss J, Vaughan M (1996). "ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 1941–4. PMID 8700863.CS1 maint: Multiple names: authors list (link)
• Vitale N, Moss J, Vaughan M (1997). "Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1". J. Biol. Chem. 272 (40): 25077–82. PMID 9312116.CS1 maint: Multiple names: authors list (link)
• Vitale N, Moss J, Vaughan M (1998). "Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1)". J. Biol. Chem. 273 (5): 2553–60. PMID 9446556.CS1 maint: Multiple names: authors list (link)
• Vitale N, Horiba K, Ferrans VJ; et al. (1998). "Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8613–8. PMID 9671726.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Vitale N, Pacheco-Rodriguez G, Ferrans VJ; et al. (2000). "Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1)". J. Biol. Chem. 275 (28): 21331–9. doi:10.1074/jbc.M909642199. PMID 10748148.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Vitale N, Ferrans VJ, Moss J, Vaughan M (2000). "Identification of lysosomal and Golgi localization signals in GAP and ARF domains of ARF domain protein 1". Mol. Cell. Biol. 20 (19): 7342–52. PMID 10982851.CS1 maint: Multiple names: authors list (link)
• Reymond A, Meroni G, Fantozzi A; et al. (2001). "The tripartite motif family identifies cell compartments". EMBO J. 20 (9): 2140–51. doi:10.1093/emboj/20.9.2140. PMID 11331580.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Vichi A, Payne DM, Pacheco-Rodriguez G; et al. (2005). "E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)". Proc. Natl. Acad. Sci. U.S.A. 102 (6): 1945–50. doi:10.1073/pnas.0409800102. PMID 15684077.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1038/nature04209. PMID 16189514.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)