Search by BoMiProt ID - Bomi291

Primary Information

BoMiProt ID Bomi291
Protein Name Heat shock protein 105 kDa
Organism Bos taurus
Uniprot IDQ0IIM3
Milk FractionMFGM, Exosome
Ref Sequence ID NP_001068770.1
Aminoacid Length 859
Molecular Weight 96726
FASTA Sequence Download
Gene Name HSPH1
Gene ID 507165
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Presence in other biological fluids/tissue/cells 105-kDa heat-shock protein (HSP105) as a mammalian high molecular mass heat-shock protein in human, mouse, and rat cells; moderately expressed in adrenal, spleen, liver, lung, and heart; Small amounts of HSP105 are expressed in the kidney, stomach, muscle, testis, and lens. However, in brain HSP105-a was characteristically highly expressed over HSP105-b
Protein Function induced in various tissues of rat after whole-body hyperthermia; HSP105 level of HSP10S increased markedly in the embryos from gestational day (GD) 9 to 11, then decreased gradually by GD 14; plays important roles in mouse embryogenesis; prevent the aggregation of heat-denatured proteins in vitro;
Biochemical Properties HSPI05 is composed of two isoforms with slightly different isoelectric points with slightly different isoelectric points, acidic and basic isoforms; mRNA was also induced by azetidine-2-carboxylic acid, sodium arsenite, zinc sulfate, and cupric sulfate;
Significance in milk heat stress proteins in mamary gland
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions 515-585,797-859
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
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2. French, J. B., Zhao, H., An, S., Niessen, S., Deng, Y., Cravatt, B. F., & Benkovic, S. J. (2013). Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome. Proceedings of the National Academy of Sciences of the United States of America, 110(7), 2528–2533.
3. Srivastava, P. K., Udono, H., Blachere, N. E., & Li, Z. (1994). Heat shock proteins transfer peptides during antigen processing and CTL priming. Immunogenetics, 39(2), 93–98.
4. Samali, A., & Cotter, T. G. (1996). Heat shock proteins increase resistance to apoptosis. Experimental Cell Research, 223(1), 163–170.
5. Polla, B. S., Healy, A. M., Wojno, W. C., & Krane, S. M. (1987). Hormone 1 alpha,25-dihydroxyvitamin D3 modulates heat shock response in monocytes. The American Journal of Physiology, 252(6 Pt 1), C640-9.
6. Shi, Y., & Thomas, J. O. (1992). The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Molecular and Cellular Biology, 12(5), 2186–2192.
7. Guidon, P. T., & Hightower, L. E. (1986). Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins. Biochemistry, 25(11), 3231–3239.
8. Chappells, T. G., Konforti, B. B., Schmids, S. L., & Rothmann, J. E. (1987). The ATPase Core of. 262(2), 746–751.