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Phosphorylation of Hsp90 on serine residues in the charged linker modulates binding to interacting proteins and has implications for overall Hsp90β conformation

ABSTRACT: Serine residues in the charged linker region of human Hsp90beta are highly phoshporylated in vivo. Mutation of these residues to alanines resulted in altered binding of many Hsp90beta interactors. This project contains the data and searches related to co-immunoprecipitation experiments with wild-type and mutant Hsp90beta, as well as input.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Manfredo Quadroni

LAB HEAD: Manfredo Quadroni

PROVIDER: PXD025873 | Pride | 2021-07-07

REPOSITORIES: Pride

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			Action	DRS
	190529_LW_11360.raw	Raw
	190529_LW_11361.raw	Raw
	190529_LW_11362.raw	Raw
	190529_LW_11363.raw	Raw
	190529_LW_11364.raw	Raw

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