TUBA1C

Protein-coding gene in the species Homo sapiens
TUBA1C
Identifiers
AliasesTUBA1C, TUBA6, bcm948, tubulin alpha 1c
External IDsMGI: 1095409; HomoloGene: 69045; GeneCards: TUBA1C; OMA:TUBA1C - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for TUBA1C
Genomic location for TUBA1C
Band12q13.12Start49,188,736 bp[1]
End49,274,600 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for TUBA1C
Genomic location for TUBA1C
Band15|15 F1Start98,927,772 bp[2]
End98,935,991 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • Brodmann area 46

  • spinal ganglia

  • orbitofrontal cortex

  • inferior ganglion of vagus nerve

  • superior vestibular nucleus

  • inferior olivary nucleus

  • pons

  • trigeminal ganglion

  • subthalamic nucleus
Top expressed in
  • Paneth cell

  • fetal liver hematopoietic progenitor cell

  • blastocyst

  • fossa

  • gastrula

  • lip

  • condyle

  • endothelial cell of lymphatic vessel

  • granulocyte

  • yolk sac
More reference expression data
BioGPS


More reference expression data
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
  • microtubule cytoskeleton
Biological process
  • cytoskeleton-dependent intracellular transport
  • microtubule-based process
  • cell division
  • cytoskeleton organization
  • microtubule cytoskeleton organization
  • mitotic cell cycle
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

84790

22146

Ensembl

ENSG00000167553

ENSMUSG00000043091

UniProt

Q9BQE3

P68373

RefSeq (mRNA)

NM_032704
NM_001303114
NM_001303115
NM_001303116
NM_001303117

NM_009448

RefSeq (protein)

NP_001290043
NP_001290044
NP_001290045
NP_001290046
NP_116093

NP_033474

Location (UCSC)Chr 12: 49.19 – 49.27 MbChr 15: 98.93 – 98.94 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tubulin alpha-1C chain is a protein that in humans is encoded by the TUBA1C gene.[5][6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167553 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000043091 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ "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. S2CID 8453412.
  • 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004PNAS..101.7070X. 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. S2CID 7200157.
  • 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. S2CID 21499158.
  • 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. S2CID 7827573.
  • 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. PMC 4626875. PMID 17373842.
  • v
  • t
  • e
  • 1ffx: TUBULIN:STATHMIN-LIKE DOMAIN COMPLEX
    1ffx: TUBULIN:STATHMIN-LIKE DOMAIN COMPLEX
  • 1ia0: KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM
    1ia0: KIF1A HEAD-MICROTUBULE COMPLEX STRUCTURE IN ATP-FORM
  • 1jff: Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol
    1jff: Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol
  • 1sa0: TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX
    1sa0: TUBULIN-COLCHICINE: STATHMIN-LIKE DOMAIN COMPLEX
  • 1sa1: Tubulin-podophyllotoxin: stathmin-like domain complex
    1sa1: Tubulin-podophyllotoxin: stathmin-like domain complex
  • 1tub: TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION
    1tub: TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION
  • 1tvk: The binding mode of epothilone A on a,b-tubulin by electron crystallography
    1tvk: The binding mode of epothilone A on a,b-tubulin by electron crystallography
  • 1z2b: Tubulin-colchicine-vinblastine: stathmin-like domain complex
    1z2b: Tubulin-colchicine-vinblastine: stathmin-like domain complex
  • 2hxf: KIF1A head-microtubule complex structure in amppnp-form
    2hxf: KIF1A head-microtubule complex structure in amppnp-form
  • 2hxh: KIF1A head-microtubule complex structure in adp-form
    2hxh: KIF1A head-microtubule complex structure in adp-form
  • v
  • t
  • e
Human
Microfilaments
and ABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
and MAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman
See also: cytoskeletal defects
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