TUBA1B

Protein-coding gene in the species Homo sapiens
TUBA1B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2E4H, 4TV8, 3RYI, 3JAR, 4TUY, 4TV9, 4YJ2, 3RYH, 3JAK, 3JAS, 4F61, 3UT5, 4O4J, 4YJ3, 4EB6, 4WBN, 3JAW, 4O2A, 3RYF, 3JAL, 4O4H, 4LNU, 3J8Y, 4IIJ, 4O4I, 3RYC, 4O4L, 4O2B, 4I50, 3JAT, 4HNA, 4F6R, 3J8X, 5CA0, 5ITZ, 5JQG, 5IJ0, 5FNV, 5IJ9

Identifiers
AliasesTUBA1B, K-ALPHA-1, tubulin alpha 1b
External IDsOMIM: 602530; MGI: 107804; HomoloGene: 134527; GeneCards: TUBA1B; OMA:TUBA1B - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for TUBA1B
Genomic location for TUBA1B
Band12q13.12Start49,127,782 bp[1]
End49,131,397 bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for TUBA1B
Genomic location for TUBA1B
Band15|15 F1Start98,829,306 bp[2]
End98,832,446 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • frontal pole

  • superior frontal gyrus

  • prefrontal cortex

  • Brodmann area 10

  • dorsolateral prefrontal cortex

  • cingulate gyrus

  • Brodmann area 9

  • ganglionic eminence

  • spinal ganglia

  • hypothalamus
Top expressed in
  • hypothalamus

  • mesencephalon

  • neural tube

  • cerebellar cortex

  • white adipose tissue

  • bone marrow

  • hippocampus proper

  • thymus

  • superior frontal gyrus

  • ganglionic eminence
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • nucleotide binding
  • GTP binding
  • structural molecule activity
  • structural constituent of cytoskeleton
  • protein binding
  • GTPase activity
  • double-stranded RNA binding
  • ubiquitin protein ligase binding
Cellular component
  • cytoplasm
  • myelin sheath
  • cytoplasmic microtubule
  • microtubule
  • cytoskeleton
  • microtubule cytoskeleton
  • membrane raft
Biological process
  • cellular response to interleukin-4
  • cytoskeleton-dependent intracellular transport
  • cell division
  • microtubule-based process
  • microtubule cytoskeleton organization
  • mitotic cell cycle
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10376

22143

Ensembl

ENSG00000123416

ENSMUSG00000023004

UniProt

P68363

P05213

RefSeq (mRNA)

NM_006082

NM_011654

RefSeq (protein)

NP_006073

NP_035784

Location (UCSC)Chr 12: 49.13 – 49.13 MbChr 15: 98.83 – 98.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tubulin alpha-1B chain is a protein that in humans is encoded by the TUBA1B gene.[5][6][7]


Interactions

TUBA1B has been shown to interact with PIK3R1.[8] Antibodies against tubulin alpha 1b can be used as markers for microtubules and spindles.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000123416 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000023004 – 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. ^ Banerjee A (Jun 2002). "Increased levels of tyrosinated alpha-, beta(III)-, and beta(IV)-tubulin isotypes in paclitaxel-resistant MCF-7 breast cancer cells". Biochem Biophys Res Commun. 293 (1): 598–601. doi:10.1016/S0006-291X(02)00269-3. PMID 12054644.
  6. ^ Cowan NJ, Dobner PR, Fuchs EV, Cleveland DW (Jan 1984). "Expression of human alpha-tubulin genes: interspecies conservation of 3' untranslated regions". Mol Cell Biol. 3 (10): 1738–45. doi:10.1128/mcb.3.10.1738. PMC 370035. PMID 6646120.
  7. ^ "Entrez Gene: TUBA1B tubulin, alpha 1b".
  8. ^ Kapeller, R; Toker A; Cantley L C; Carpenter C L (Oct 1995). "Phosphoinositide 3-kinase binds constitutively to alpha/beta-tubulin and binds to gamma-tubulin in response to insulin". J. Biol. Chem. 270 (43). UNITED STATES: 25985–91. doi:10.1074/jbc.270.43.25985. ISSN 0021-9258. PMID 7592789.
  9. ^ "Anti-alpha Tubulin antibody [GT114] (GTX628802) | GeneTex".

Further reading

  • Venter JC (1993). "Identification of new human receptor and transporter genes by high throughput cDNA (EST) sequencing". J. Pharm. Pharmacol. 45. Suppl 1: 355–60. PMID 8098743.
  • Lopez-Fanarraga M, Avila J, Guasch A, et al. (2002). "Review: postchaperonin tubulin folding cofactors and their role in microtubule dynamics". J. Struct. Biol. 135 (2): 219–29. doi:10.1006/jsbi.2001.4386. PMID 11580271.
  • Kapeller R, Toker A, Cantley LC, Carpenter CL (1995). "Phosphoinositide 3-kinase binds constitutively to alpha/beta-tubulin and binds to gamma-tubulin in response to insulin". J. Biol. Chem. 270 (43): 25985–91. doi:10.1074/jbc.270.43.25985. PMID 7592789.
  • 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. doi:10.1128/mcb.15.9.5188. PMC 230766. PMID 7651436.
  • Szasz J, Yaffe MB, Sternlicht H (1993). "Site-directed mutagenesis of alpha-tubulin. Reductive methylation studies of the Lys 394 region". Biophys. J. 64 (3): 792–802. Bibcode:1993BpJ....64..792S. doi:10.1016/S0006-3495(93)81440-1. PMC 1262393. PMID 8097117.
  • Baumann MH, Wisniewski T, Levy E, et al. (1996). "C-terminal fragments of alpha- and beta-tubulin form amyloid fibrils in vitro and associate with amyloid deposits of familial cerebral amyloid angiopathy, British type". Biochem. Biophys. Res. Commun. 219 (1): 238–42. doi:10.1006/bbrc.1996.0211. PMID 8619814.
  • Gress TM, Müller-Pillasch F, Geng M, et al. (1996). "A pancreatic cancer-specific expression profile". Oncogene. 13 (8): 1819–30. PMID 8895530.
  • Crépieux P, Kwon H, Leclerc N, et al. (1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Mol. Cell. Biol. 17 (12): 7375–85. doi:10.1128/mcb.17.12.7375. PMC 232593. PMID 9372968.
  • Herreros L, Rodríguez-Fernandez JL, Brown MC, et al. (2000). "Paxillin localizes to the lymphocyte microtubule organizing center and associates with the microtubule cytoskeleton". J. Biol. Chem. 275 (34): 26436–40. doi:10.1074/jbc.M003970200. hdl:10261/135387. PMID 10840040.
  • 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.
  • Takeoka A, Shimizu M, Horio T (2001). "Identification of an alpha-tubulin mutant of fission yeast from gamma-tubulin-interacting protein screening: genetic evidence for alpha-/gamma-tubulin interaction". J. Cell Sci. 113. Pt 24 (24): 4557–62. doi:10.1242/jcs.113.24.4557. PMID 11082048.
  • 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.
  • Yokota S, Yanagi H, Yura T, Kubota H (2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle". Eur. J. Biochem. 268 (17): 4664–73. doi:10.1046/j.1432-1327.2001.02393.x. PMID 11532003.
  • Rommelaere H, De Neve M, Neirynck K, et al. (2001). "Prefoldin recognition motifs in the nonhomologous proteins of the actin and tubulin families". J. Biol. Chem. 276 (44): 41023–8. doi:10.1074/jbc.M106591200. PMID 11535601.
  • Klein C, Kramer EM, Cardine AM, et al. (2002). "Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau". J. Neurosci. 22 (3): 698–707. doi:10.1523/JNEUROSCI.22-03-00698.2002. PMC 6758498. PMID 11826099.
  • 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.

External links

  • 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
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See also: cytoskeletal defects