TCP1β also known as TCP1 beta, CCT2 is a crucial subunit of the chaperonin containing TCP-1 (CCT) complex, which is essential for proper folding of cytosolic proteins, particularly actins and tubulins. Located in the eukaryotic cytosol, CCT complex comprises eight distinct subunits, each encoded by different genes, and maintains cellular function and integrity. TCP1β′s role in protein folding is particularly important, as misfolded proteins can lead to cellular dysfunction and various diseases. TCP1β was initially identified in mice, where studies linked this protein to tail-less and embryonic lethal phenotypes, and homologous sequences appear in several other species, highlighting evolutionary significance. Studies of TCP1β in yeast demonstrate molecular chaperone activity for actin and tubulin, underscoring this protein′s critical role in cellular processes across different organisms.