The human chaperonin system, Hsp60/Hsp10, is essential for maintaining protein homeostasis and is found mainly in mitochondria. Hsp60 forms a bowl-shaped structure that provides an enclosed environment for protein folding, while its co-chaperone, Hsp10, acts as a cap to seal the barrel. This coordinated process is crucial for the proper folding of many unfolded or misfolded proteins, making the Hsp60/Hsp10 complex an indispensable chaperone system. Changes in their expression levels have been linked to diseases such as neurodegenerative disorders and cancer. Although Hsp60 has gained increasing attention, its co-chaperone Hsp10 remains relatively underexplored and has often been assumed to play a passive role. However, emerging studies challenge this view, suggesting that Hsp10 alone may exert regulatory functions within the chaperonin cycle. Here, we present the near-complete NMR backbone assignment of the 102-residue human Hsp10, laying the groundwork for future investigations into its structure, interactions, and roles in facilitating protein folding and preventing aggregation.