TRIM23

TRIM23
Identifiers
Aliases	TRIM23, ARD1, ARFD1, RNF46, tripartite motif containing 23
External IDs	OMIM: 601747 MGI: 1933161 HomoloGene: 1251 GeneCards: TRIM23
Gene location (Human)
Chr.	Chromosome 5 (human)[1]
End	65,625,975 bp[1]
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)[2]
End	104,203,372 bp[2]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• GO:0010577 enzyme activator activity; • identical protein binding; • GTPase activity; • ubiquitin-protein transferase activity; • GO:0001948 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; • cell nucleus; • lysosomal membrane; • intracellular; • membrane; • lysosome; • cytoplasm; • Golgi apparatus; • cell membrane;
Biological process	• protein ubiquitination; • GO:0022415 viral process; • GO:0048554 positive regulation of catalytic activity; • immune system process; • innate immune system; • intracellular protein transport; • Golgi to plasma membrane transport; • vesicle-mediated transport;
	Sources:Amigo / QuickGO
Orthologs
	373
	81003
	ENSG00000113595
	ENSMUSG00000021712
	P36406
	Q8BGX0
	NM_001656; NM_033227; NM_033228
	NM_030731; NM_001361538; NM_001361539
	NP_001647; NP_150230; NP_150231
	NP_001348467; NP_001348468
	Wikidata
View/Edit Human	View/Edit Mouse

GTP-binding protein ARD-1 is a protein that in humans is encoded by the TRIM23 gene.[5][6]

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.[6]

Interactions

TRIM23 has been shown to interact with TRIM31,[7] TRIM29[7] and PSCD1.[8]

References

GRCh38: Ensembl release 89: ENSG00000113595 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000021712 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Mishima K, Tsuchiya M, Nightingale MS, Moss J, Vaughan M (Apr 1993). "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain". The Journal of Biological Chemistry. 268 (12): 8801–7. PMID 8473324.
"Entrez Gene: TRIM23 tripartite motif-containing 23".
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.
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, 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.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000113595 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000021712 - 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.

[pmid8473324-5] Mishima K, Tsuchiya M, Nightingale MS, Moss J, Vaughan M (Apr 1993). "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain". The Journal of Biological Chemistry. 268 (12): 8801–7. PMID 8473324.

[entrez-6] "Entrez Gene: TRIM23 tripartite motif-containing 23".

[pmid11331580-7] 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.

[pmid10748148-8] 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.

TRIM23

Function

Interactions

References

Further reading