TUBA1C

Tubulin, alpha 1c

PDB rendering based on 1ffx.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1ffx, 1ia0, 1jff, 1sa0, 1sa1, 1tub, 1tvk, 1z2b, 2hxf, 2hxh

Identifiers

TUBA1C ; TUBA6; bcm948

External IDs

MGI: 1095409 HomoloGene: 69045 GeneCards: TUBA1C Gene

Gene ontology
Molecular function	• GTPase activity • structural molecule activity • structural constituent of cytoskeleton • protein binding • GTP binding
Cellular component	• nucleus • microtubule • cytoplasmic microtubule
Biological process	• GTP catabolic process • protein folding • 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

ENSG00000167553

ENSMUSG00000043091

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
49.58 – 49.67 Mb

Chr 15:
99.03 – 99.04 Mb

PubMed search

Tubulin alpha-1C chain is a protein that in humans is encoded by the TUBA1C gene.^[1]^[2]

References

↑ 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