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Publication : Identification of the phosphorylation sites of the murine small heat shock protein hsp25.

First Author  Gaestel M Year  1991
Journal  J Biol Chem Volume  266
Issue  22 Pages  14721-4
PubMed ID  1860870 Mgi Jnum  J:41206
Mgi Id  MGI:893285 Doi  10.1016/s0021-9258(18)98746-6
Citation  Gaestel M, et al. (1991) Identification of the phosphorylation sites of the murine small heat shock protein hsp25. J Biol Chem 266(22):14721-4
abstractText  Native phosphorylated mouse small heat shock protein hsp25 from Ehrlich ascites tumor cells was isolated and the in vivo phosphorylation sites of the protein were determined. Furthermore, native hsp25 was phosphorylated by the endogenous kinase(s) in a cell-free system as well as recombinant hsp25 was phosphorylated in vitro by protein kinase C and catalytic subunit of cAMP-dependent protein kinase. The two major phosphorylation sites of native and recombinant hsp25 were determined as Ser-15 and Ser-86. There are no differences in the hsp25 phosphorylation sites phosphorylated by the protein kinase C, the catalytic subunit of cAMP-dependent protein kinase and the unknown intracellular kinase(s). The serine residues identified exist in all known small mammalian stress proteins and are located in the conserved kinase recognition sequence Arg-X-X-Ser.
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