ID:TBA3E_HUMAN DESCRIPTION: RecName: Full=Tubulin alpha-3E chain; AltName: Full=Alpha-tubulin 3E; 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). PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively (By similarity). 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). PTM: Acetylation of alpha-tubulins at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity). 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 Q6PEY2
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
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.
BC057811 - Homo sapiens tubulin, alpha 3e, mRNA (cDNA clone MGC:71743 IMAGE:5298532), complete cds. AK131043 - Homo sapiens cDNA FLJ29009 fis, clone TST03907, highly similar to TUBULIN ALPHA-3/ALPHA-7 CHAIN. JD404484 - Sequence 385508 from Patent EP1572962. HQ448482 - Synthetic construct Homo sapiens clone IMAGE:100071914; CCSB010893_01 tubulin, alpha 3e (TUBA3E) gene, encodes complete protein. KJ899981 - Synthetic construct Homo sapiens clone ccsbBroadEn_09375 TUBA3E gene, encodes complete protein. CU691250 - Synthetic construct Homo sapiens gateway clone IMAGE:100021198 5' read TUBA3E mRNA. JD461826 - Sequence 442850 from Patent EP1572962.
Biochemical and Signaling Pathways
Reactome (by CSHL, EBI, and GO)
Protein Q6PEY2 (Reactome details) participates in the following event(s):
R-HSA-389972 alpha-tubulin:GTP + Cofactor B -> alpha-tubulin:GTP: Cofactor B R-HSA-389978 alpha-tubulin:GTP + Cofactor E -> alpha-tubulin:GTP:Cofactor E 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-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-8955712 TTCP hydrolyzes the terminal L-Tyr residue from alpha-tubulin R-HSA-8955706 TTL ligates L-Tyr to the carboxy terminus of alpha-tubulin R-HSA-389963 alpha-tubulin:GTP:Cofactor B +Cofactor E -> alpha-tubulin:GTP: Cofactor E +Cofactor B 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-389977 Post-chaperonin tubulin folding pathway R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin R-HSA-391251 Protein folding R-HSA-389958 Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding R-HSA-597592 Post-translational protein modification R-HSA-392499 Metabolism of proteins R-HSA-390466 Chaperonin-mediated protein folding
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
