|Protein Name||Heat shock 70 kDa protein|
|Ref Sequence Id||NP_001033594.1|
|Amino Acid Lenth||471|
|Protein Existence Status||Reviewed: Experimental evidence at transcript level|
|Presence in other biological fluids/tissue/cells||cytosol, mitochondria, endoplasmic reticulum, and nucleus|
|Protein Function||bind ATP; molecular chaperone normal unstressed cells; role in modifying antigen presentation; glial-axon transfer proteins; interact directly with fatty acids - interaction may be part of their mode of binding to cell membranes; resist noxious stimuli both in vitro and in vivo; protection of human monocytes from hydrogen peroxideinduced toxicity; guinea pig gastric mucosal cells from ethanol damage|
|Biochemical Properties||b-sheet structures are the most hydrophobic parts of HSC-70 and thus are likely to be involved in the binding of hydrophobic peptides; changes in resting pHi neither affect the baseline levels of HSP-70 nor alter the ability of heat shock to induce HSP-70 as found in human A-431 cells;|
|Significance in milk||heat stress proteins in mamary gland|
|PTMs||O glycosylation was found in HSP6, a member of HSP 70 family; presence of N-acetyl glucosamine|
|Significance of PTMs||sensitive to heat stress and mainly responsible for mammary cell protection from heat stress|
|Linking IDs||Bomi2324 Bomi546 Bomi2327|
|Bibliography||1. Ichiyanagi, T., Imai, T., Kajiwara, C., Mizukami, S., Nakai, A., Nakayama, T., & Udono, H. (2010). Essential role of endogenous heat shock protein 90 of dendritic cells in antigen cross-presentation. Journal of Immunology (Baltimore, Md. : 1950), 185(5), 2693–2700. https://doi.org/10.4049/jimmunol.1000821. |
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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.