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There are 15 genes in the human genome that encode proteins termed chaperonins with the HSPE1 encoded protein (chaperonin 10/Hsp10) being required as a co-chaperone for Hsp60 function.

Human Hsp60 was originally characterized as a mitochondrial chaperone involved in correct folding of mitochondrial proteins during their import into this organelle.

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In addition, there is the small heat shock protein family often referred to as the Hsp25 family or the HSPB family.Proteins that are classified as chaperonins are large (800-900 k Da) double-ring complexes that function by globally enclosing substrate proteins for folding.Proteins up to a size of around 60 k Da can be acted upon by the chaperonins.Improper folding and protein aggregation can lead to the formation of potentially toxic species.To reduce and prevent these negative outcomes, cells harbor a complex network of molecular chaperones whose functions are to promote efficient folding and to prevent protein aggregation.

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