HSP27 Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins. Belongs to the small heat shock protein (HSP20) family. Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein; Motility/polarity/chemotaxis
Cellular Component: 
Reference #:  P15991 (UniProtKB)
Alt. Names/Synonyms: heat shock 27 kDa protein; Heat shock protein beta-1; heat-shock protein beta-1; HSP 27; HSP27; HspB1
Gene Symbols: HSPB1
Molecular weight: 23,419 Da
Basal Isoelectric point: 6.23  Predict pI for various phosphorylation states
CST Pathways:  Inhibition of Apoptosis  |  Regulation of P38 MAPKs
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HSP27

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB