Description: Homo sapiens tubulin, beta 2B class IIb (TUBB2B), mRNA. RefSeq Summary (NM_178012): The protein encoded by this gene is a beta isoform of tubulin, which binds GTP and is a major component of microtubules. This gene is highly similar to TUBB2A and TUBB2C. Defects in this gene are a cause of asymmetric polymicrogyria. [provided by RefSeq, Mar 2010]. Transcript (Including UTRs) Position: hg19 chr6:3,224,495-3,227,968 Size: 3,474 Total Exon Count: 4 Strand: - Coding Region Position: hg19 chr6:3,224,985-3,227,777 Size: 2,793 Coding Exon Count: 4
ID:TBB2B_HUMAN DESCRIPTION: RecName: Full=Tubulin beta-2B chain; FUNCTION: Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha-chain (By similarity). TUBB2B is implicated in neuronal migration. SUBUNIT: Dimer of alpha and beta chains (By similarity). INTERACTION: O00555:CACNA1A; NbExp=2; IntAct=EBI-355665, EBI-766279; SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity). TISSUE SPECIFICITY: High expression in brain. PTM: Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable). DISEASE: Defects in TUBB2B are a cause of polymicrogyria asymmetric (PMGA) [MIM:610031]. PMGA is a malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. SIMILARITY: Belongs to the tubulin family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q9BVA1
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
KEGG - Kyoto Encyclopedia of Genes and Genomes hsa04540 - Gap junction hsa05130 - Pathogenic Escherichia coli infection
Reactome (by CSHL, EBI, and GO)
Protein Q9BVA1 (Reactome details) participates in the following event(s):
R-HSA-389980 unfolded actin/tubulin associates with prefoldin R-HSA-389970 Actin/tubulin:prefoldin complex associates with CCT/TriC R-HSA-389954 Hydrolysis of ATP and release of tubulin folding intermediate from CCT/TriC R-HSA-389961 ADP is exchanged for ATP in the (ADP:CCT/TriC):tubulin complex R-HSA-389956 Beta-tubulin:GTP + Cofactor A -> Beta-tubulin:GTP: Cofactor A R-HSA-389969 Beta-tubulin:GTP + Cofactor D -> Beta-tubulin:GTP: Cofactor D R-HSA-389974 Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E:Cofactor C-> Beta-tubulin:GDP :alpha-tubulin:GTP heterodimer +Cofactor E+ Cofactor D+ Cofactor C+ Pi R-HSA-8955706 TTL ligates L-Tyr to the carboxy terminus of alpha-tubulin R-HSA-8955712 TTCP hydrolyzes the terminal L-Tyr residue from alpha-tubulin R-HSA-389955 Beta-tubulin:GTP: Cofactor A+ Cofactor D -> Beta-tubulin:GTP:Cofactor D + Cofactor A R-HSA-389976 Beta-tubulin:GTP:Cofactor D+alpha-tubulin:GTP:Cofactor E-> Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E R-HSA-389964 Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E+ Cofactor C-> Beta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E:Cofactor C R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC R-HSA-389958 Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC R-HSA-389977 Post-chaperonin tubulin folding pathway R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin R-HSA-390466 Chaperonin-mediated protein folding R-HSA-391251 Protein folding R-HSA-597592 Post-translational protein modification R-HSA-392499 Metabolism of proteins
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