TUBA1B Knowpia

TUBA1B
Available structures
PDB	Ortholog 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
Aliases	TUBA1B, K-ALPHA-1, tubulin alpha 1b
External IDs	OMIM: 602530 MGI: 107804 HomoloGene: 134527 GeneCards: TUBA1B
Gene location (Human)
Chr.	Chromosome 12 (human)
End	49,131,397 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	98,832,446 bp
RNA expression pattern
	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
	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
	10376
	22143
	ENSG00000123416
	ENSMUSG00000023004
	P68363
	P05213
	NM_006082
	NM_011654
	NP_006073
	NP_035784
	Wikidata
View/Edit Human	View/Edit Mouse

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

Interactions edit

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 edit

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000123416 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000023004 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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.
^ 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.
^ "Entrez Gene: TUBA1B tubulin, alpha 1b".
^ 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.
^ "Anti-alpha Tubulin antibody [GT114] (GTX628802) | GeneTex".

Further reading edit

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.