TUBA1A

Tubulin, alpha 1a
PDB rendering based on 1ffx.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1ffx​, 1ia0​, 1jff​, 1sa0​, 1sa1​, 1tub​, 1tvk​, 1z2b​, 2hxf​, 2hxh​
Identifiers
Symbols	TUBA1A ; B-ALPHA-1; LIS3; TUBA3
External IDs	OMIM: 602529 MGI: 98869 HomoloGene: 68498 ChEMBL: 3661 GeneCards: TUBA1A Gene
Gene ontology Molecular function • GTPase activity • structural molecule activity • structural constituent of cytoskeleton • protein binding • GTP binding • protein domain specific binding Cellular component • nucleus • cytosol • microtubule • cytoplasmic microtubule • cytoplasmic ribonucleoprotein granule • myelin sheath • recycling endosome • extracellular exosome Biological process • G2/M transition of mitotic cell cycle • mitotic cell cycle • protein folding • organelle organization • microtubule-based process • cytoskeleton-dependent intracellular transport • cellular protein metabolic process • 'de novo' posttranslational protein folding • protein polymerization • cell division Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7846	22142
Ensembl	ENSG00000167552	ENSMUSG00000072235
UniProt	Q71U36	P68369
RefSeq (mRNA)	NM_001270399	NM_011653
RefSeq (protein)	NP_001257328	NP_035783
Location (UCSC)	Chr 12: 49.18 – 49.19 Mb	Chr 15: 98.95 – 98.95 Mb
PubMed search

Tubulin alpha-1A chain is a protein that in humans is encoded by the TUBA1A gene.^[1][2][3]

Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulins. The genes encoding these microtubule constituents belong to 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, which are highly conserved among species. This gene encodes alpha tubulin and is highly similar to mouse and rat Tuba1 gene. Northern blotting studies have shown that the gene expression is predominantly found in morphologically differentiated neurologic cells. This gene is one of three alpha-tubulin genes in a cluster on chromosome 12q.^[3]

Interactions

TUBA1A has been shown to interact with PAFAH1B1.^[4]

References

1. Crabtree DV, Ojima I, Geng X, Adler AJ (August 2001). "Tubulins in the primate retina: evidence that xanthophylls may be endogenous ligands for the paclitaxel-binding site". Bioorg Med Chem 9 (8): 1967–76. doi:10.1016/S0968-0896(01)00103-1. PMID 11504633.
2. Hall JL, Cowan NJ (July 1985). "Structural features and restricted expression of a human alpha-tubulin gene". Nucleic Acids Res 13 (1): 207–23. doi:10.1093/nar/13.1.207. PMC 340985. PMID 3839072.
3. "Entrez Gene: TUBA1A tubulin, alpha 1a".
4. Sapir, T; Elbaum M; Reiner O (December 1997). "Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit". EMBO J. (ENGLAND) 16 (23): 6977–84. doi:10.1093/emboj/16.23.6977. ISSN 0261-4189. PMC 1170301. PMID 9384577.

Further reading

• Desai A, Mitchison TJ (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 (2001). "An abundance of tubulins". Trends Cell Biol. 10 (12): 537–42. doi:10.1016/S0962-8924(00)01857-2. PMID 11121746.
• Dutcher SK (2001). "The tubulin fraternity: alpha to eta". Curr. Opin. Cell Biol. 13 (1): 49–54. doi:10.1016/S0955-0674(00)00173-3. PMID 11163133.
• Miller FD, Naus CC, Durand M, et al. (1988). "Isotypes of alpha-tubulin are differentially regulated during neuronal maturation". J. Cell Biol. 105 (6 Pt 2): 3065–73. doi:10.1083/jcb.105.6.3065. PMC 2114727. PMID 3693406.
• Cowan NJ, Dobner PR, Fuchs EV, Cleveland DW (1984). "Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions". Mol. Cell. Biol. 3 (10): 1738–45. PMC 370035. PMID 6646120.
• Alexandrova N, Niklinski J, Bliskovsky V, et al. (1995). "The N-terminal domain of c-Myc associates with alpha-tubulin and microtubules in vivo and in vitro". Mol. Cell. Biol. 15 (9): 5188–95. PMC 230766. PMID 7651436.
• Sapir T, Elbaum M, Reiner O (1998). "Reduction of microtubule catastrophe events by LIS1, platelet-activating factor acetylhydrolase subunit". EMBO J. 16 (23): 6977–84. doi:10.1093/emboj/16.23.6977. PMC 1170301. PMID 9384577.
• Kinnunen T, Kaksonen M, Saarinen J, et al. (1998). "Cortactin-Src kinase signaling pathway is involved in N-syndecan-dependent neurite outgrowth". J. Biol. Chem. 273 (17): 10702–8. doi:10.1074/jbc.273.17.10702. PMID 9553134.
• Faruki S, Geahlen RL, Asai DJ (2000). "Syk-dependent phosphorylation of microtubules in activated B-lymphocytes". J. Cell. Sci. 113 (14): 2557–65. PMID 10862713.
• Watts NR, Sackett DL, Ward RD, et al. (2000). "HIV-1 Rev Depolymerizes Microtubules to Form Stable Bilayered Rings". J. Cell Biol. 150 (2): 349–60. doi:10.1083/jcb.150.2.349. PMC 2180222. PMID 10908577.
• Germani A, Bruzzoni-Giovanelli H, Fellous A, et al. (2001). "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.
• Payton JE, Perrin RJ, Clayton DF, George JM (2002). "Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells". Brain Res. Mol. Brain Res. 95 (1–2): 138–45. doi:10.1016/S0169-328X(01)00257-1. PMID 11687285.
• Bifulco M, Laezza C, Stingo S, Wolff J (2002). "2′,3′-Cyclic nucleotide 3′-phosphodiesterase: A membrane-bound, microtubule-associated protein and membrane anchor for tubulin". Proc. Natl. Acad. Sci. U.S.A. 99 (4): 1807–12. doi:10.1073/pnas.042678799. PMC 122275. PMID 11842207.
• Saugstad JA, Yang S, Pohl J, et al. (2002). "Interaction between metabotropic glutamate receptor 7 and alpha tubulin". J. Neurochem. 80 (6): 980–8. doi:10.1046/j.0022-3042.2002.00778.x. PMC 2925652. PMID 11953448.
• Ivings L, Pennington SR, Jenkins R, et al. (2002). "Identification of Ca2+-dependent binding partners for the neuronal calcium sensor protein neurocalcin delta: interaction with actin, clathrin and tubulin". Biochem. J. 363 (Pt 3): 599–608. doi:10.1042/0264-6021:3630599. PMC 1222513. PMID 11964161.