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HSP20
Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. Belongs to the small heat shock protein (HSP20) family. Note: This description may include information from UniProtKB.
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| Protein type: Chaperone; Heat shock protein |
| Chromosomal Location of rat Ortholog: 1q21 |
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Cellular Component:
cytoplasm; cytosol; extracellular region; mitochondrion; nuclear speck; nucleus
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Molecular Function:
protein folding chaperone; protein homodimerization activity; protein kinase binding; protein-folding chaperone binding; structural constituent of eye lens; unfolded protein binding
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Biological Process:
chaperone-mediated protein folding; negative regulation of apoptotic process; negative regulation of cardiac muscle cell apoptotic process; positive regulation of angiogenesis; protein refolding; response to heat
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Reference #:
P97541
(UniProtKB)
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Alt. Names/Synonyms: Heat shock 20 kDa-like protein p20; heat shock 20-kDa protein; Heat shock protein beta-6; heat shock protein, alpha-crystallin-related, B6; Hsp20; HspB6; p20
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Gene Symbols: Hspb6
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Molecular weight:
17,505 Da
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Basal Isoelectric point:
6.05
Predict pI for various phosphorylation states
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Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology®
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