Primary Information
BoMiProt ID	Bomi29
Protein Name	Heat shock 70 kDa protein
Organism	Bos taurus
Uniprot ID	Q2TBX4
Milk Fraction	Whey
Ref Sequence ID	NP_001033594.1
Aminoacid Length	471
Molecular Weight	51920
FASTA Sequence	Download
Gene Name	HSPA13
Gene ID	505907
Protein Existence Status	Reviewed: Experimental evidence at transcript level
Secondary Information
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
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	(315-337)
DisProt Annotation
TM Helix Prediction	1TMH; (7-25)
Significance of PTMs	sensitive to heat stress and mainly responsible for mammary cell protection from heat stress
Linking IDs
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. 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. https://doi.org/10.1073/pnas.1300173110 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. https://doi.org/10.1007/bf00188611 4. Samali, A., & Cotter, T. G. (1996). Heat shock proteins increase resistance to apoptosis. Experimental Cell Research, 223(1), 163–170. https://doi.org/10.1006/excr.1996.0070. 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. https://doi.org/10.1152/ajpcell.1987.252.6.C640. 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.