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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | The TCP-1 protein [ , ] (Tailless Complex Polypeptide 1) was first identified in mice where it is especially abundant in testis but present in all cell types. It has since been found and characterised in many other animal species, as well as in yeast, plants and protists. TCP-1 is a highly conserved protein of about 60kDa (556 to 560 residues) which participates in a hetero-oligomeric 900kDa double-torus shaped particle [] with 6 to 8 other different subunits. These subunits, the chaperonin containing TCP-1 (CCT) subunit beta, gamma, delta, epsilon, zeta and eta are evolutionary related to TCP-1 itself [, ]. The CCT is known to act as a molecular chaperone for tubulin, actin and probably some other proteins.The CCT subunits are highly related to archaebacterial counterparts:TF55 and TF56 [ ], a molecular chaperone from Sulfolobus shibatae. TF55 has ATPase activity, is known to bind unfolded polypeptides and forms a oligomeric complex of two stacked nine-membered rings.Thermosome [ ], from Thermoplasma acidophilum. The thermosome is composed of two subunits (alpha and beta) and also seems to be a chaperone with ATPase activity. It forms an oligomeric complex of eight-membered rings.The TCP-1 family of proteins are weakly, but significantly [ ], related to the cpn60/groEL chaperonin family (see ). | Name | Chaperonin TCP-1, conserved site |
| Short Name | Chaperonin_TCP-1_CS | Type | Conserved_site |
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