HSPB1

Chr 7q11.23

heat shock protein family B (small) member 1

Aliases:: HSP27, HSP28, Hs.76067, Hsp25, CMT2F
MANE:: ENST00000248553.7

OMIM: 602195 ↗NCBI: 3315 ↗Ensembl ↗

Annotations refreshed 10 hours ago.

Predicted protein structure

AlphaFold predicted structure

HSPB1 · P04792

v62025-08-01

Predicted Aligned Error matrix for HSPB1 — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

68.9/ 100

Low

205 residues

Confidence breakdown

Very high(≥ 90)33%
Confident(70–90)15%
Low(50–70)24%
Very low(< 50)28%

Open interactive 3D viewer

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

Distal myopathies
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Hereditary neuropathy
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Hereditary neuropathy or pain disorder
MONOALLELIC, autosomal or pseudoautosomal, imprinted status unknown
Paediatric motor neuronopathies
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted
Adult onset neurodegenerative disorder
MONOALLELIC, autosomal or pseudoautosomal, NOT imprinted

Disease associations (Open Targets)

neuronopathy, distal hereditary motor, type 2B
0.81
Charcot-Marie-Tooth disease axonal type 2F
0.80
Autosomal dominant Charcot-Marie-Tooth disease type 2F
0.75
Charcot-Marie-Tooth disease
0.54
hereditary disease
0.51
distal hereditary motor neuropathy type 2
0.46
distal hereditary motor neuropathy
0.35
Charcot-Marie-Tooth disease type 4
0.14
breast cancer
0.13
prostate cancer
0.13

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

Heat shock protein beta-1

Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742)