HSPA8

Chr 11

heat shock protein family A (Hsp70) member 8

Also known as: HEL-33, HEL-S-72p, HSC54, HSC70, HSC71, HSP71, HSP73, HSPA10

NCBI Gene: 3312 ENSG00000109971 UniProt: P11142

The HSPA8 protein is a constitutively expressed heat shock cognate protein that functions as a molecular chaperone, facilitating protein folding, chaperone-mediated autophagy, and clathrin-coated vesicle uncoating. Mutations cause autosomal dominant neurodevelopmental disorders with intellectual disability and neurological features. This gene is highly constrained against loss-of-function variants, indicating that such mutations are likely to cause severe developmental consequences.

ResearchSummary from RefSeq, UniProt

This gene encodes a member of the heat shock protein 70 family, which contains both heat-inducible and constitutively expressed members. This protein belongs to the latter group, which are also referred to as heat-shock cognate proteins. It functions as a chaperone, and binds to nascent polypeptides to facilitate correct folding. It also functions as an ATPase in the disassembly of clathrin-coated vesicles during transport of membrane components through the cell. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2011]

ResearchGenerating clinical summary…

Clinical highlights

Interpreting a novel variant

This gene is strongly intolerant of loss-of-function variation in the population, so LoF variants warrant close attention. No curated mechanism annotation is available — see the mechanism card for the computational prediction and its caveats.Based on population constraint only.

Active trials

199

Pubs (1 yr)

—

P/LP submissions

—

P/LP missense

0.20

LOEUF· LoF intol.

LOF

Mechanism· predicted

Some data sources returned errors (1)