TRIM23

TRIM23
Identifiers
Aliases	TRIM23, ARD1, ARFD1, RNF46, tripartite motif containing 23
External IDs	OMIM: 601747; MGI: 1933161; HomoloGene: 1251; GeneCards: TRIM23; OMA:TRIM23 - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5q12.3 Start 65,589,690 bp End 65,625,975 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 D1 Start 104,315,305 bp End 104,339,880 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in cerebellar vermis frontal pole Achilles tendon corpus callosum prefrontal cortex Brodmann area 10 inferior ganglion of vagus nerve lateral nuclear group of thalamus pars compacta ventricular zone Top expressed in spermatocyte lobe of cerebellum amygdala dentate gyrus of hippocampal formation granule cell intercostal muscle lateral septal nucleus mammillary body triceps brachii muscle superior frontal gyrus hippocampus proper More reference expression data BioGPS More reference expression data
Gene ontology Molecular function enzyme activator activity identical protein binding GTPase activity ubiquitin-protein transferase activity protein binding GDP binding zinc ion binding metal ion binding nucleotide binding GTP binding transferase activity nucleic acid binding Cellular component endomembrane system Golgi membrane nucleus lysosomal membrane intracellular anatomical structure membrane lysosome cytoplasm Golgi apparatus plasma membrane Biological process protein ubiquitination viral process positive regulation of catalytic activity immune system process innate immune response intracellular protein transport Golgi to plasma membrane transport vesicle-mediated transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 373 81003 Ensembl ENSG00000113595 ENSMUSG00000021712 UniProt P36406 Q8BGX0 RefSeq (mRNA) NM_001656 NM_033227 NM_033228 NM_030731 NM_001361538 NM_001361539 RefSeq (protein) NP_001647 NP_150230 NP_150231 NP_001348467 NP_001348468 Location (UCSC) Chr 5: 65.59 – 65.63 Mb Chr 13: 104.32 – 104.34 Mb PubMed search
Wikidata
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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. Bibcode:1996PNAS...93.1941V. 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. Bibcode:1998PNAS...95.8613V. 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. Bibcode:2005PNAS..102.1945V. doi:10.1073/pnas.0409800102. PMC 548593. PMID 15684077.