TUBB2A

Protein-coding gene in the species Homo sapiens
TUBB2A
Identifiers
AliasesTUBB2A, CDCBM5, TUBB, TUBB2, dJ40E16.7, tubulin beta 2A class IIa
External IDsOMIM: 615101; MGI: 107861; HomoloGene: 134314; GeneCards: TUBB2A; OMA:TUBB2A - orthologs
Gene location (Human)
Chromosome 6 (human)
Chr.Chromosome 6 (human)[1]
Chromosome 6 (human)
Genomic location for TUBB2A
Genomic location for TUBB2A
Band6p25.2Start3,153,497 bp[1]
End3,157,544 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for TUBB2A
Genomic location for TUBB2A
Band13 A3.3|13 14.03 cMStart34,258,257 bp[2]
End34,261,990 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • endothelial cell

  • pons

  • frontal pole

  • spinal ganglia

  • Pars compacta

  • superior vestibular nucleus

  • Brodmann area 10

  • Brodmann area 23

  • orbitofrontal cortex

  • pars reticulata
Top expressed in
  • barrel cortex

  • trigeminal ganglion

  • piriform cortex

  • medial dorsal nucleus

  • anterior amygdaloid area

  • ventral tegmental area

  • supraoptic nucleus

  • ventromedial nucleus

  • lateral hypothalamus

  • subiculum
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GTP binding
  • structural constituent of cytoskeleton
  • protein binding
  • GTPase activity
Cellular component
  • cytoplasm
  • extracellular vesicle
  • microtubule
  • extracellular exosome
  • cytoskeleton
  • nucleus
  • microtubule cytoskeleton
Biological process
  • microtubule-based process
  • cytoskeleton organization
  • microtubule cytoskeleton organization
  • mitotic cell cycle
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7280

22151

Ensembl

ENSG00000137267

ENSMUSG00000058672

UniProt

Q13885

Q7TMM9

RefSeq (mRNA)

NM_001310315
NM_001069

NM_009450

RefSeq (protein)

NP_001060
NP_001297244

NP_033476

Location (UCSC)Chr 6: 3.15 – 3.16 MbChr 13: 34.26 – 34.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tubulin beta-2A chain is a protein that in humans is encoded by the TUBB2A gene.[5][6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000137267 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000058672 – 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. ^ Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S (Oct 2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
  6. ^ "Entrez Gene: TUBB2A tubulin, beta 2A".

Further reading

  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
  • Horisberger MA (1992). "Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins". J. Virol. 66 (8): 4705–9. doi:10.1128/JVI.66.8.4705-4709.1992. PMC 241296. PMID 1629950.
  • Wang D, Villasante A, Lewis SA, Cowan NJ (1987). "The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype". J. Cell Biol. 103 (5): 1903–10. doi:10.1083/jcb.103.5.1903. PMC 2114403. PMID 3782288.
  • Lee MG, Lewis SA, Wilde CD, Cowan NJ (1983). "Evolutionary history of a multigene family: an expressed human beta-tubulin gene and three processed pseudogenes". Cell. 33 (2): 477–87. doi:10.1016/0092-8674(83)90429-4. PMID 6688039.
  • Takahashi M, Tomizawa K, Sato K, et al. (1995). "A novel tau-tubulin kinase from bovine brain". FEBS Lett. 372 (1): 59–64. doi:10.1016/0014-5793(95)00955-9. PMID 7556643. S2CID 42295269.
  • Yamaguchi N, Fukuda MN (1995). "Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins". J. Biol. Chem. 270 (20): 12170–6. doi:10.1074/jbc.270.33.19551. PMID 7744867.
  • Waterman-Storer CM, Karki S, Holzbaur EL (1995). "The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)". Proc. Natl. Acad. Sci. U.S.A. 92 (5): 1634–8. Bibcode:1995PNAS...92.1634W. doi:10.1073/pnas.92.5.1634. PMC 42574. PMID 7878030.
  • Carr D, Knull H (1993). "Aldolase-tubulin interactions: removal of tubulin C-terminals impairs interactions". Biochem. Biophys. Res. Commun. 195 (1): 289–93. doi:10.1006/bbrc.1993.2043. PMID 8103323.
  • Volz A, Weiss E, Trowsdale J, Ziegler A (1994). "Presence of an expressed beta-tubulin gene (TUBB) in the HLA class I region may provide the genetic basis for HLA-linked microtubule dysfunction". Hum. Genet. 93 (1): 42–6. doi:10.1007/BF00218911. PMID 8270253. S2CID 7853030.
  • Paschal BM, Holzbaur EL, Pfister KK, et al. (1993). "Characterization of a 50-kDa polypeptide in cytoplasmic dynein preparations reveals a complex with p150GLUED and a novel actin". J. Biol. Chem. 268 (20): 15318–23. doi:10.1016/S0021-9258(18)82472-3. PMID 8325901.
  • Linhartová I, Dráberová E, Viklický V, Dráber P (1993). "Distribution of non-class-III beta-tubulin isoforms in neuronal and non-neuronal cells". FEBS Lett. 320 (1): 79–82. doi:10.1016/0014-5793(93)81662-J. PMID 8462682. S2CID 38579660.
  • Huby RD, Carlile GW, Ley SC (1996). "Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein Vav, and tubulin in Jurkat T cells". J. Biol. Chem. 270 (51): 30241–4. doi:10.1074/jbc.270.51.30241. PMID 8530437.
  • Bosc C, Cronk JD, Pirollet F, et al. (1996). "Cloning, expression, and properties of the microtubule-stabilizing protein STOP". Proc. Natl. Acad. Sci. U.S.A. 93 (5): 2125–30. Bibcode:1996PNAS...93.2125B. doi:10.1073/pnas.93.5.2125. PMC 39921. PMID 8700896.
  • Tian G, Huang Y, Rommelaere H, et al. (1996). "Pathway leading to correctly folded beta-tubulin". Cell. 86 (2): 287–96. doi:10.1016/S0092-8674(00)80100-2. PMID 8706133. S2CID 18359371.
  • Tokito MK, Howland DS, Lee VM, Holzbaur EL (1997). "Functionally distinct isoforms of dynactin are expressed in human neurons". Mol. Biol. Cell. 7 (8): 1167–80. doi:10.1091/mbc.7.8.1167. PMC 275970. PMID 8856662.
  • 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.
  • Niethammer M, Valtschanoff JG, Kapoor TM, et al. (1998). "CRIPT, a novel postsynaptic protein that binds to the third PDZ domain of PSD-95/SAP90". Neuron. 20 (4): 693–707. doi:10.1016/S0896-6273(00)81009-0. PMID 9581762. S2CID 16068361.
  • Rasmussen RK, Ji H, Eddes JS, et al. (1998). "Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins". Electrophoresis. 19 (5): 809–17. doi:10.1002/elps.1150190535. PMID 9629920. S2CID 21204230.
  • Ciruela F, Robbins MJ, Willis AC, McIlhinney RA (1999). "Interactions of the C terminus of metabotropic glutamate receptor type 1alpha with rat brain proteins: evidence for a direct interaction with tubulin". J. Neurochem. 72 (1): 346–54. doi:10.1046/j.1471-4159.1999.0720346.x. PMID 9886087. S2CID 3923065.
  • Chau MF, Radeke MJ, de Inés C, et al. (1999). "The microtubule-associated protein tau cross-links to two distinct sites on each alpha and beta tubulin monomer via separate domains". Biochemistry. 37 (51): 17692–703. doi:10.1021/bi9812118. PMID 9922135.
  • 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
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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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