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A protein family that has been portrays as peptide binding protein involved in antigen processing exist in manifold subcellular sites such as plasma membrane,mitochondria,endoplasmic reticulum and cytosol.


Mortalin gene is mapped on chromosome 5q31.1 with 17 exons that contains N-terminal 46 amino acids signal peptide which undergoes calcium-dependent autophosphorylation and is highly conserved heat-shock chaperone. It is translated in the cytoplasm and transported into mitochondria which consist of two functional domains such as ATPase N-terminal nucleotide-binding domain and C-terminal substrate binding domain wherein the biological activities of each domain is necessary for general and specialized functions.

Mortalin is a protein related to the heat shock proteinhsp70 that differentially distributed in normal and cancerous cell depending on its different subcellular niche and binding partner that is likely to carry out various functions relevant to cell survival, control of proliferation and stress response.

Mortalin minor alterations in expression may lead to serious biological consequences including neurodegeneration in which the coupling of stress with destruction of the chaperone system causes premature aging, a biological processed typified by a general and progressive decline in metabolic processes affecting tissues that exhibit an elevated rate of oxygen utilization in the brain.

Gene name: HSPA9

Protein name: Stress-70 protein, mitochondrial


75 kDa glucose-regulated protein




See also:

Heat-shock protein