Search by BoMiProt ID - Bomi2324


Primary Information

BoMiProt ID Bomi2324
Protein Name Heat shock 70 kDa protein 1A
Organism Bos taurus
Uniprot IdQ27975
Milk FractionMFGM, Exosome
Ref Sequence Id NP_976067.3
Amino Acid Lenth 641
Molecular Weight 70259
Fasta Sequence https://www.uniprot.org/uniprot/Q27975.fasta
Gene Name HSPA1A
Gene Id 282254
Protein Existence Status Reviewed: Experimental evidence at protein level

Secondry 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
Significance of PTMs sensitive to heat stress and mainly responsible for mammary cell protection from heat stress
Linking IDs Bomi29
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.