| TRIM23 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | TRIM23, ARD1, ARFD1, RNF46, tripartite motif containing 23 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 601747 MGI: 1933161 HomoloGene: 1251 GeneCards: TRIM23 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000113595 - Ensembl, May 2017
- 1 2 3 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. doi:10.1016/S0021-9258(18)52945-8. PMID 8473324.
- 1 2 "Entrez Gene: TRIM23 tripartite motif-containing 23".
- 1 2 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.
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.
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