TRIM23

From Wikipedia, the free encyclopedia

Tripartite motif-containing 23

Identifiers

TRIM23; ARD1; ARFD1; RNF46

External IDs

OMIM: 601747 MGI: 1933161 HomoloGene: 1251

Gene ontology
Molecular Function:	• nucleotide binding • GTPase activity • ubiquitin-protein ligase activity • protein binding • GTP binding • enzyme activator activity • zinc ion binding • GDP binding • metal ion binding
Cellular Component:	• Golgi membrane • intracellular • nucleus • cytoplasm • lysosomal membrane
Biological Process:	• small GTPase mediated signal transduction • protein ubiquitination

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001656 (mRNA)
NP_001647 (protein)

NM_030731 (mRNA)
NP_109656 (protein)

Location

Chr 5: 64.92 - 64.96 Mb

Chr 13: 105.3 - 105.32 Mb

Pubmed search

[1]

[2]

Tripartite motif-containing 23, also known as TRIM23, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: TRIM23 tripartite motif-containing 23.

[edit] 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.