Search by BoMiProt ID - Bomi293

Primary Information

BoMiProt ID Bomi293
Protein Name Heat shock protein beta-1
Organism Bos taurus
Uniprot IDQ3T149
Milk FractionMFGM, Exosome
Ref Sequence ID XP_005225172.1
Aminoacid Length 201
Molecular Weight 22393
FASTA Sequence Download
Gene Name HSPB1
Gene ID 516099
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Presence in other biological fluids/tissue/cells Ubiquitous, high levels in heart, striated and smooth muscles
Protein Function also known as sHSP 27conserved across species and are important in stress tolerance; exhibit chaperone-like activity in preventing aggregation of target proteins; may exhibit immunomodulatory and anti-inflammatory functions; predominantly heat-inducible; involved in diverse cellular functions such as stress tolerance, protein folding, protein degradation, maintaining cytoskeletal integrity, cell death, differentiation, cell cycle and signal transduction and development; exhibit cardio and neuroprotection, potent anti-apoptotic activity, pro-angiogenic property and anti-inflammatory property involving interactions with several clients; bovine αBcrystallin prevent aggregation of citrate synthase and α-glucosidase
Biochemical Properties bind Cu2+, and suppress generation of reactive oxygen species (ROS) ; Temperature-dependent conformational change in α-crystallin leading to the increased exposure of hydrophobic surfaces paralleled the increase in chaperone-like activity; undergoes thermally induced self-association, leading to increased oligomeric size, which correlated with increase in its chaperone-like activity; increase the refolding yields of citrate synthase and α-glucosidase upon refolding from their urea-denatured state
Significance in milk heat stress proteins in mamary gland
PTMs phosphorylated, especially under stress conditions - phosphorylation of serines(S), S15, S78, and S82 in human Hsp27;
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs sensitive to heat stress and mainly responsible for mammary cell protection from heat stress
Bibliography 1. Chowdary, T. K. et al. (2004) ‘Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity.’, The Biochemical journal, 381(Pt 2), pp. 379–87. doi: 10.1042/BJ20031958.
2. Fukuda, K. et al. (2011) ‘Biochemical, Proteomic, Structural, and Thermodynamic Characterizations of Integrin-linked Kinase (ILK)’, Journal of Biological Chemistry, 286(24), pp. 21886–21895. doi: 10.1074/jbc.M111.240093.
3. Jakob, U. et al. (1993) ‘Small heat shock proteins are molecular chaperones.’, The Journal of biological chemistry, 268(3), pp. 1517–20. Available at: http://www.ncbi.nlm.nih.gov/pubmed/8093612 (Accessed: 4 October 2019).
4. Raman, B. and Rao, C. M. (1994) ‘Chaperone-like activity and quaternary structure of alpha-crystallin.’, The Journal of biological chemistry, 269(44), pp. 27264–8. Available at: http://www.ncbi.nlm.nih.gov/pubmed/7961635 (Accessed: 4 October 2019).
5. Lelj-Garolla, B. and Mauk, A. G. (2006) ‘Self-association and Chaperone Activity of Hsp27 Are Thermally Activated’, Journal of Biological Chemistry, 281(12), pp. 8169–8174. doi: 10.1074/jbc.M512553200.
6. Landry, J. et al. (1992) ‘Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II.’, The Journal of biological chemistry, 267(2), pp. 794–803. Available at: http://www.ncbi.nlm.nih.gov/pubmed/1730670 (Accessed: 4 October 2019).
7. Rogalla, T. et al. (1999) ‘Regulation of Hsp27 Oligomerization, Chaperone Function, and Protective Activity against Oxidative Stress/Tumor Necrosis Factor α by Phosphorylation’, Journal of Biological Chemistry, 274(27), pp. 18947–18956. doi: 10.1074/jbc.274.27.18947.