Alpha-tubulin 3C
Protein-coding gene in the species Homo sapiens
| TUBA3C | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | TUBA3C, TUBA2, bA408E5.3, Alpha-tubulin 3C, tubulin alpha 3c | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 602528; HomoloGene: 134742; GeneCards: TUBA3C; OMA:TUBA3C - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Tubulin alpha-3C/D chain is a protein that in humans is encoded by the TUBA3C gene.[3][4]
Function
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes and they are highly conserved among and between species. This gene is an alpha tubulin gene that encodes a protein 99% to the mouse testis-specific Tuba3 and Tuba7 gene products. This gene is located in the 13q11 region, which is associated with the genetic diseases Clouston hidrotic ectodermal dysplasia and Kabuki syndrome. Alternative splicing has been observed for this gene and two variants have been identified.[4]
Interactions
Alpha-tubulin 3C has been shown to interact with FYN[5] and NMI.[6]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000198033 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Dodé C, Weil D, Levilliers J, Crozet F, Chaïb H, Levi-Acobas F, Guilford P, Petit C (Jan 1998). "Sequence characterization of a newly identified human alpha-tubulin gene (TUBA2)". Genomics. 47 (1): 125–30. doi:10.1006/geno.1997.5081. PMID 9465305.
- ^ a b "Entrez Gene: TUBA3C tubulin, alpha 3c".
- ^ Klein C, Kramer EM, Cardine AM, Schraven B, Brandt R, Trotter J (Feb 2002). "Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau". The Journal of Neuroscience. 22 (3): 698–707. doi:10.1523/JNEUROSCI.22-03-00698.2002. PMC 6758498. PMID 11826099.
- ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
External links
- Human TUBA3C genome location and TUBA3C gene details page in the UCSC Genome Browser.
Further reading
- Desai A, Mitchison TJ (Jul 1998). "Tubulin and FtsZ structures: functional and therapeutic implications". BioEssays. 20 (7): 523–7. doi:10.1002/(SICI)1521-1878(199807)20:7<523::AID-BIES1>3.0.CO;2-L. PMID 9722999.
- Oakley BR (Dec 2000). "An abundance of tubulins". Trends in Cell Biology. 10 (12): 537–42. doi:10.1016/S0962-8924(00)01857-2. PMID 11121746.
- Dutcher SK (Feb 2001). "The tubulin fraternity: alpha to eta". Current Opinion in Cell Biology. 13 (1): 49–54. doi:10.1016/S0955-0674(00)00173-3. PMID 11163133.
- Alexandrova N, Niklinski J, Bliskovsky V, Otterson GA, Blake M, Kaye FJ, Zajac-Kaye M (Sep 1995). "The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro". Molecular and Cellular Biology. 15 (9): 5188–95. doi:10.1128/MCB.15.9.5188. PMC 230766. PMID 7651436.
- Guilford P, Dodé C, Crozet F, Blanchard S, Chaïb H, Levilliers J, Levi-Acobas F, Weil D, Weissenbach J, Cohen D (Sep 1995). "A YAC contig and an EST map in the pericentromeric region of chromosome 13 surrounding the loci for neurosensory nonsyndromic deafness (DFNB1 and DFNA3) and limb-girdle muscular dystrophy type 2C (LGMD2C)". Genomics. 29 (1): 163–9. doi:10.1006/geno.1995.1227. PMID 8530067.
- Marie-Cardine A, Kirchgessner H, Eckerskorn C, Meuer SC, Schraven B (Dec 1995). "Human T lymphocyte activation induces tyrosine phosphorylation of alpha-tubulin and its association with the SH2 domain of the p59fyn protein tyrosine kinase". European Journal of Immunology. 25 (12): 3290–7. doi:10.1002/eji.1830251214. PMID 8566014. S2CID 37614803.
- Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J (Dec 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Molecular and Cellular Biology. 17 (12): 7375–85. doi:10.1128/MCB.17.12.7375. PMC 232593. PMID 9372968.
- Kibar Z, Lafrenière RG, Chakravarti A, Wang JC, Chevrette M, Der Kaloustian VM, Rouleau GA (Feb 1999). "A radiation hybrid map of 48 loci including the clouston hidrotic ectodermal dysplasia locus in the pericentromeric region of chromosome 13q". Genomics. 56 (1): 127–30. doi:10.1006/geno.1998.5698. PMID 10036193.
- Herreros L, Rodríguez-Fernandez JL, Brown MC, Alonso-Lebrero JL, Cabañas C, Sánchez-Madrid F, Longo N, Turner CE, Sánchez-Mateos P (Aug 2000). "Paxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeleton". The Journal of Biological Chemistry. 275 (34): 26436–40. doi:10.1074/jbc.M003970200. hdl:10261/135387. PMID 10840040.
- Watts NR, Sackett DL, Ward RD, Miller MW, Wingfield PT, Stahl SS, Steven AC (Jul 2000). "HIV-1 rev depolymerizes microtubules to form stable bilayered rings". The Journal of Cell Biology. 150 (2): 349–60. doi:10.1083/jcb.150.2.349. PMC 2180222. PMID 10908577.
- Takeoka A, Shimizu M, Horio T (Dec 2000). "Identification of an alpha-tubulin mutant of fission yeast from gamma-tubulin-interacting protein screening: genetic evidence for alpha-/gamma-tubulin interaction". Journal of Cell Science. 113 (24): 4557–62. doi:10.1242/jcs.113.24.4557. PMID 11082048.
- Germani A, Bruzzoni-Giovanelli H, Fellous A, Gisselbrecht S, Varin-Blank N, Calvo F (Dec 2000). "SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis". Oncogene. 19 (52): 5997–6006. doi:10.1038/sj.onc.1204002. PMID 11146551. S2CID 41279377.
- Kourmouli N, Dialynas G, Petraki C, Pyrpasopoulou A, Singh PB, Georgatos SD, Theodoropoulos PA (Apr 2001). "Binding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulin". The Journal of Biological Chemistry. 276 (16): 13007–14. doi:10.1074/jbc.M007135200. PMID 11278332.
- Rommelaere H, De Neve M, Neirynck K, Peelaers D, Waterschoot D, Goethals M, Fraeyman N, Vandekerckhove J, Ampe C (Nov 2001). "Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families". The Journal of Biological Chemistry. 276 (44): 41023–8. doi:10.1074/jbc.M106591200. PMID 11535601.
- Klein C, Kramer EM, Cardine AM, Schraven B, Brandt R, Trotter J (Feb 2002). "Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau". The Journal of Neuroscience. 22 (3): 698–707. doi:10.1523/JNEUROSCI.22-03-00698.2002. PMC 6758498. PMID 11826099.
- Saugstad JA, Yang S, Pohl J, Hall RA, Conn PJ (Mar 2002). "Interaction between metabotropic glutamate receptor 7 and alpha tubulin". Journal of Neurochemistry. 80 (6): 980–8. doi:10.1046/j.0022-3042.2002.00778.x. PMC 2925652. PMID 11953448.
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PDB gallery
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1ffx: TUBULIN:STATHMIN-LIKE DOMAIN COMPLEX -
1ia0: KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM -
1jff: Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol -
1sa0: TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX -
1sa1: Tubulin-podophyllotoxin: stathmin-like domain complex -
1tub: TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION -
1tvk: The binding mode of epothilone A on a,b-tubulin by electron crystallography -
1z2b: Tubulin-colchicine-vinblastine: stathmin-like domain complex -
2hxf: KIF1A head-microtubule complex structure in amppnp-form -
2hxh: KIF1A head-microtubule complex structure in adp-form
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