Primary Information
BoMiProt ID	Bomi63
Protein Name	Heat shock protein HSP 90-alpha
Organism	Bos taurus
Uniprot ID	Q76LV2
Milk Fraction	Whey, MFGM, Exosome
Ref Sequence ID	NP_001012688.1
Aminoacid Length	733
Molecular Weight	84731
FASTA Sequence	Download
Gene Name	HSP90AA1
Gene ID	281832
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Protein Function	regulates efficient transport of peptides from the proteasome to MHC1; 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; ubiquitous expression of hsp70, hsp90, calreticulin and gp96 in cells essentially ensures that the MHC I presentation pathway remains functional in all nucleated cells; Hsp70 and hsp90 form heteromultimeric complexes in the cytosol with other co-chaperones; Hsp90 and hsp70 are intimately involved in the extrusion of antigens from the endosomes to the cytosol through a putative pore structure;protection of human monocytes from hydrogen peroxideinduced toxicity; guinea pig gastric mucosal cells from ethanol damage
Biochemical Properties	cytosolic HSP; Hsp90 has been shown to physically associate with the proteasome, and in certain instances replace the PA28 subunits; inhibitor is 17-AAG
Significance in milk	heat stress proteins in mamary gland
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	225-279,700-733
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
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.