ID:TBB6_HUMAN DESCRIPTION: RecName: Full=Tubulin beta-6 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). SUBUNIT: Dimer of alpha and beta chains (By similarity). SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity). TISSUE SPECIFICITY: Ubiquitous. Maximal expression in breast and lung, where it represents around 10% of all beta-tubulins. Largely decreased expression in most cancerous tissues. DOMAIN: The highly acidic C-terminal region may bind cations such as calcium. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. 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). 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 Q9BUF5
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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.
AK311364 - Homo sapiens cDNA, FLJ18406. AK092677 - Homo sapiens cDNA FLJ35358 fis, clone PUAEN2000497, highly similar to Tubulin beta-6 chain. AK001295 - Homo sapiens cDNA FLJ10433 fis, clone NT2RP1000478, highly similar to Tubulin beta-6 chain. AK304616 - Homo sapiens cDNA FLJ52847 complete cds, highly similar to Tubulin beta-6 chain. AK022340 - Homo sapiens cDNA FLJ12278 fis, clone MAMMA1001735, highly similar to TUBULIN BETA-5 CHAIN. AK098440 - Homo sapiens cDNA FLJ25574 fis, clone JTH07516, highly similar to TUBULIN BETA-5 CHAIN. BC002654 - Homo sapiens tubulin, beta 6, mRNA (cDNA clone MGC:4083 IMAGE:3605559), complete cds. AK298196 - Homo sapiens cDNA FLJ52712 complete cds, highly similar to Tubulin beta-6 chain. BC039717 - Homo sapiens mRNA similar to tubulin beta-5 (cDNA clone IMAGE:5745167). AB590145 - Synthetic construct DNA, clone: pFN21AE1530, Homo sapiens TUBB6 gene for tubulin, beta 6, without stop codon, in Flexi system. DQ896394 - Synthetic construct Homo sapiens clone IMAGE:100010854; FLH193926.01L; RZPDo839D0769D tubulin, beta 6 (TUBB6) gene, encodes complete protein. DQ893486 - Synthetic construct clone IMAGE:100006116; FLH193930.01X; RZPDo839D0779D tubulin, beta 6 (TUBB6) gene, encodes complete protein. KJ895010 - Synthetic construct Homo sapiens clone ccsbBroadEn_04404 TUBB6 gene, encodes complete protein. JD474669 - Sequence 455693 from Patent EP1572962. JD150169 - Sequence 131193 from Patent EP1572962. JD552405 - Sequence 533429 from Patent EP1572962. JD204264 - Sequence 185288 from Patent EP1572962. JD361339 - Sequence 342363 from Patent EP1572962.
Biochemical and Signaling Pathways
Reactome (by CSHL, EBI, and GO)
Protein Q9BUF5 (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