TUBA1C

TUBA1C

Identifiers

TUBA1C, TUBA6, bcm948, tubulin alpha 1c

External IDs

MGI: 1095409 HomoloGene: 69045 GeneCards: TUBA1C

Gene ontology
Molecular function	• nucleotide binding • GTP binding • structural constituent of cytoskeleton • protein binding • structural molecule activity • GTPase activity
Cellular component	• cytoplasm • vesicle • microtubule • cytoskeleton • nucleus
Biological process	• cytoskeleton-dependent intracellular transport • microtubule-based process • cell division • cytoskeleton organization
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse


84790


22146


ENSG00000167553


ENSMUSG00000043091


Q9BQE3


P68373

RefSeq (mRNA)


NM_032704 NM_001303114 NM_001303115 NM_001303116 NM_001303117


NM_009448

RefSeq (protein)


NP_116093.1


NP_033474.1

Location (UCSC)

Chr 12: 49.19 – 49.27 Mb

Chr 15: 99.03 – 99.04 Mb

PubMed search

^[1]

^[2]

View/Edit Human

View/Edit Mouse

Tubulin alpha-1C chain is a protein that in humans is encoded by the TUBA1C gene.^[3]^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (Feb 1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–250. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
↑ "Entrez Gene: TUBA1C tubulin, alpha 1c".

Further reading

Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–320. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Watts NR, Sackett DL, Ward RD, et al. (2000). "HIV-1 rev depolymerizes microtubules to form stable bilayered rings". J. Cell Biol. 150 (2): 349–360. doi:10.1083/jcb.150.2.349. PMC 2180222. PMID 10908577.
Irobi J, Nelis E, Verhoeven K, et al. (2002). "Mutation analysis of 12 candidate genes for distal hereditary motor neuropathy type II (distal HMN II) linked to 12q24.3". J. Peripher. Nerv. Syst. 7 (2): 87–95. doi:10.1046/j.1529-8027.2002.02014.x. PMID 12090300.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Chen D, Wang M, Zhou S, Zhou Q (2004). "HIV-1 Tat targets microtubules to induce apoptosis, a process promoted by the pro-apoptotic Bcl-2 relative Bim". EMBO J. 21 (24): 6801–6810. doi:10.1093/emboj/cdf683. PMC 139103. PMID 12486001.
Xu Y, Kulkosky J, Acheampong E, et al. (2004). "HIV-1-mediated apoptosis of neuronal cells: Proximal molecular mechanisms of HIV-1-induced encephalopathy". Proc. Natl. Acad. Sci. U.S.A. 101 (18): 7070–7075. doi:10.1073/pnas.0304859101. PMC 406467. PMID 15103018.
Campbell GR, Pasquier E, Watkins J, et al. (2005). "The glutamine-rich region of the HIV-1 Tat protein is involved in T-cell apoptosis". J. Biol. Chem. 279 (46): 48197–48204. doi:10.1074/jbc.M406195200. PMID 15331610.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
de Mareuil J, Carre M, Barbier P, et al. (2006). "HIV-1 Tat protein enhances microtubule polymerization". Retrovirology. 2: 5. doi:10.1186/1742-4690-2-5. PMC 549075. PMID 15691386.
Giacca M (2006). "HIV-1 Tat, apoptosis and the mitochondria: a tubulin link?". Retrovirology. 2: 7. doi:10.1186/1742-4690-2-7. PMC 549042. PMID 15698476.
Valenzuela-Fernández A, Alvarez S, Gordon-Alonso M, et al. (2006). "Histone deacetylase 6 regulates human immunodeficiency virus type 1 infection". Mol. Biol. Cell. 16 (11): 5445–5454. doi:10.1091/mbc.E05-04-0354. PMC 1266439. PMID 16148047.
Guo D, Han J, Adam BL, et al. (2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochem. Biophys. Res. Commun. 337 (4): 1308–1318. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.
Canani RB, De Marco G, Passariello A, et al. (2006). "Inhibitory effect of HIV-1 Tat protein on the sodium-D-glucose symporter of human intestinal epithelial cells". AIDS. 20 (1): 5–10. doi:10.1097/01.aids.0000198088.85572.68. PMID 16327313.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Frum R, Busby SA, Ramamoorthy M, et al. (2007). "HDM2-binding partners: interaction with translation elongation factor EF1alpha". J. Proteome Res. 6 (4): 1410–1417. doi:10.1021/pr060584p. PMID 17373842.

PDB gallery

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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