InterPro : IPR023123

Name  Tubulin, C-terminal Short Name  Tubulin_C
Type  Domain Description  Microtubules are polymers of tubulin, a dimer of two 55kDa subunits, designated alpha and beta [, ]. Within the microtubule lattice, alpha-beta heterodimers associate in a head-to-tail fashion, giving rise to microtubule polarity. Fluorescent labelling studies have suggested that tubulin is oriented in microtubules with beta-tubulin toward the plus end [].For maximal rate and extent of polymerisation into microtubules, tubulin requires GTP. Two molecules of GTP are bound at different sites, termed N and E. At the E (Exchangeable) site, GTP is hydrolysed during incorporationinto the microtubule. Close to the E site is an invariant region rich inglycine residues, which is found in both chains and is thought to controlaccess of the nucleotide to its binding site [].Most species, excepting simple eukaryotes, express a variety of closely-related alpha- and beta-isotypes. A third family member, gamma tubulin, hasalso been identified in a number of species. Gamma tubulin is found at microtubule-organising centres, such as the spindle poles or the centrosome, suggesting that it is involved in minus-end nucleation of microtubule assembly [].This entry represents the extreme C-terminal structural domain of both alpha and beta tubulin. It forms a helix hairpin [].
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6 Publications

First Author Title Year Journal Volume Pages
Cleveland DW Molecular biology and genetics of tubulin. 1985 Annu Rev Biochem 54 331-65
Joshi HC Gamma-tubulin: the hub of cellular microtubule assemblies. 1993 Bioessays 15 637-43
Joshi HC Diversity among tubulin subunits: toward what functional end? 1990 Cell Motil Cytoskeleton 16 159-63
Hesse J Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate. 1987 J Biol Chem 262 15472-5
Mitchison TJ Localization of an exchangeable GTP binding site at the plus end of microtubules. 1993 Science 261 1044-7
Gigant B The 4 A X-ray structure of a tubulin:stathmin-like domain complex. 2000 Cell 102 809-16



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)