|Protein Name||Heat shock 70 kDa protein 1A|
|Milk Fraction||MFGM, Exosome|
|Ref Sequence Id||NP_976067.3|
|Amino Acid Lenth||641|
|Protein Existence Status||Reviewed: Experimental evidence at protein 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|
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