HSPA9
Description
The HSPA9 (heat shock protein family A (Hsp70) member 9) is a protein-coding gene located on chromosome 5.
HSPA9, also known as mortalin or mitochondrial 70 kDa heat shock protein (mtHsp70), is a protein encoded by the HSPA9 gene in humans. It belongs to the heat shock protein 70 family, which includes both heat-inducible and constitutively expressed members. HSPA9 is a heat-shock cognate protein involved in controlling cell proliferation and may act as a chaperone. It interacts with proteins like FGF1 and P53. Mutations in HSPA9 can lead to a syndrome called EVEN-PLUS, characterized by a combination of congenital malformations.
HSPA9 is a chaperone protein that plays a key role in the formation of mitochondrial iron-sulfur clusters (ISCs). It interacts with and stabilizes proteins involved in ISC assembly, including FXN, NFU1, NFS1, and ISCU. This regulation of ISC assembly is crucial for erythropoiesis. HSPA9 might also be involved in cell cycle control by interacting with and promoting the degradation of TP53. Additionally, it may contribute to cell proliferation and aging.
HSPA9 is also known as CRP40, CSA, EVPLS, GRP-75, GRP75, HEL-S-124m, HSPA9B, MOT, MOT2, MTHSP75, PBP74, SAAN, SIDBA4.
