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,
Phosphorylation
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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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. https://doi.org/10.1128/mcb.12.5.2186.
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. https://doi.org/10.1021/bi00359a023.
8. Chappells, T. G., Konforti, B. B., Schmids, S. L., & Rothmann, J. E. (1987). The ATPase Core of. 262(2), 746–751.