HSPA14

Chr 10

heat shock protein family A (Hsp70) member 14

Also known as: HSP70-4, HSP70L1

NCBI Gene: 51182 ENSG00000187522 UniProt: Q0VDF9 OMIM: 610369

The protein functions as an ATP-dependent molecular chaperone that is part of the ribosome-associated complex, helping to fold nascent polypeptide chains as they emerge from ribosomes. Mutations cause autosomal recessive intellectual disability with variable additional features including seizures and developmental delay. The gene shows significant constraint against loss-of-function variants, suggesting that complete loss of protein function is likely pathogenic.

OMIM ResearchSummary from RefSeq, UniProt

Predicted to enable ATP hydrolysis activity; heat shock protein binding activity; and protein folding chaperone. Predicted to be involved in protein refolding. Located in cytosol and ribosome. [provided by Alliance of Genome Resources, Jun 2026]

OMIM 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

Pubs (1 yr)

—

P/LP submissions

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P/LP missense

0.40

LOEUF

Mechanism· predicted