TRIM23: Difference between revisions
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{{ | '''GTP-binding protein ARD-1''' is a [[protein]] that in humans is encoded by the ''TRIM23'' [[gene]].<ref name="pmid8473324">{{cite journal | vauthors = Mishima K, Tsuchiya M, Nightingale MS, Moss J, Vaughan M | title = ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain | journal = The Journal of Biological Chemistry | volume = 268 | issue = 12 | pages = 8801–7 | date = Apr 1993 | pmid = 8473324 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TRIM23 tripartite motif-containing 23| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=373| accessdate = }}</ref> | ||
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== 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.<ref name="entrez" /> | |||
== | == Interactions == | ||
{{protein- | TRIM23 has been shown to [[Protein-protein interaction|interact]] with [[TRIM31]],<ref name=pmid11331580>{{cite journal | vauthors = 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 | title = The tripartite motif family identifies cell compartments | journal = The EMBO Journal | volume = 20 | issue = 9 | pages = 2140–51 | date = May 2001 | pmid = 11331580 | pmc = 125245 | doi = 10.1093/emboj/20.9.2140 }}</ref> [[TRIM29]]<ref name=pmid11331580/> and [[PSCD1]].<ref name=pmid10748148>{{cite journal | vauthors = Vitale N, Pacheco-Rodriguez G, Ferrans VJ, Riemenschneider W, Moss J, Vaughan M | title = Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1) | journal = The Journal of Biological Chemistry | volume = 275 | issue = 28 | pages = 21331–9 | date = Jul 2000 | pmid = 10748148 | doi = 10.1074/jbc.M909642199 }}</ref> | ||
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== References == | |||
{{Reflist}} | |||
== Further reading == | |||
{{Refbegin | 2}} | |||
* {{cite journal | vauthors = Vitale N, Moss J, Vaughan M | title = ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 5 | pages = 1941–4 | date = Mar 1996 | pmid = 8700863 | pmc = 39887 | doi = 10.1073/pnas.93.5.1941 }} | |||
* {{cite journal | vauthors = Vitale N, Moss J, Vaughan M | title = Characterization of a GDP dissociation inhibitory region of ADP-ribosylation factor domain protein ARD1 | journal = The Journal of Biological Chemistry | volume = 272 | issue = 40 | pages = 25077–82 | date = Oct 1997 | pmid = 9312116 | doi = 10.1074/jbc.272.40.25077 }} | |||
* {{cite journal | vauthors = Vitale N, Moss J, Vaughan M | title = Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1) | journal = The Journal of Biological Chemistry | volume = 273 | issue = 5 | pages = 2553–60 | date = Jan 1998 | pmid = 9446556 | doi = 10.1074/jbc.273.5.2553 }} | |||
* {{cite journal | vauthors = Vitale N, Horiba K, Ferrans VJ, Moss J, Vaughan M | title = Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 15 | pages = 8613–8 | date = Jul 1998 | pmid = 9671726 | pmc = 21124 | doi = 10.1073/pnas.95.15.8613 }} | |||
* {{cite journal | vauthors = Vitale N, Pacheco-Rodriguez G, Ferrans VJ, Riemenschneider W, Moss J, Vaughan M | title = Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1) | journal = The Journal of Biological Chemistry | volume = 275 | issue = 28 | pages = 21331–9 | date = Jul 2000 | pmid = 10748148 | doi = 10.1074/jbc.M909642199 }} | |||
* {{cite journal | vauthors = Vitale N, Ferrans VJ, Moss J, Vaughan M | title = Identification of lysosomal and Golgi localization signals in GAP and ARF domains of ARF domain protein 1 | journal = Molecular and Cellular Biology | volume = 20 | issue = 19 | pages = 7342–52 | date = Oct 2000 | pmid = 10982851 | pmc = 86288 | doi = 10.1128/MCB.20.19.7342-7352.2000 }} | |||
* {{cite journal | vauthors = 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 | title = The tripartite motif family identifies cell compartments | journal = The EMBO Journal | volume = 20 | issue = 9 | pages = 2140–51 | date = May 2001 | pmid = 11331580 | pmc = 125245 | doi = 10.1093/emboj/20.9.2140 }} | |||
* {{cite journal | vauthors = Vichi A, Payne DM, Pacheco-Rodriguez G, Moss J, Vaughan M | title = E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1) | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 102 | issue = 6 | pages = 1945–50 | date = Feb 2005 | pmid = 15684077 | pmc = 548593 | doi = 10.1073/pnas.0409800102 }} | |||
{{Refend}} | |||
{{Gene-5-stub}} |
Latest revision as of 12:16, 15 September 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
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GTP-binding protein ARD-1 is a protein that in humans is encoded by the TRIM23 gene.[1][2]
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.[2]
Interactions
TRIM23 has been shown to interact with TRIM31,[3] TRIM29[3] and PSCD1.[4]
References
- ↑ 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.
- ↑ 2.0 2.1 "Entrez Gene: TRIM23 tripartite motif-containing 23".
- ↑ 3.0 3.1 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. 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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