Probable molecular chaperone that assists the folding of proteins upon ATP hydrolysis (PubMed:20080638). Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638). May play a role in protein processing in limb, cardiac and reproductive system development. May play a role in cytokinesis (PubMed:28753627). Component of a complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8 (PubMed:20080638). Interacts with STUB1 (PubMed:18094050). Interacts with BBS2 (via coiled coil domain) (PubMed:20080638). Interacts with CCDC28B (PubMed:16327777). Interacts with BBS12 (PubMed:26900326). Interacts with SMARCC1, a component of the SWI/SNF complexes; the interaction takes place predominantly in the cytoplasm and may modulate SMARCC1 location (PubMed:28753627). Interacts with DLEC1 (PubMed:33144677). The majority of the protein resides within the pericentriolar material (PCM), a proteinaceous tube surrounding centrioles. During interphase, the protein is confined to the lateral surfaces of the PCM but during mitosis it relocalizes throughout the PCM and is found at the intercellular bridge. The MKSS protein is highly mobile and rapidly shuttles between the cytosol and centrosome. Widely expressed in adult and fetal tissues. The substrate-binding apical domain region is sufficient for centrosomal association. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Belongs to the TCP-1 chaperonin family. Retina International's Scientific Newsletter