Proteomics

Dataset Information

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USP9X phosphopeptide mapping - We previously identified the deubiquitylase USP9X as a G2/M-specific CDC14B interactor (PXD012732). The functional connection of these proteins has been further investigated by a quantitative comparison of USP9X phosphorylation in WT vs CDC14B-overexpressing HEK 293Tcells (ATCC® CRL-3216™). The approach identified USP9X serine 2563 as a specific CDC14B target. Phosphorylation at USP9XS2563 has been confirmed by in-house phosphospecific antibodies.


ABSTRACT: We previously identified the deubiquitylase USP9X as a G2/M-specific CDC14B interactor (PXD012732). The functional connection of these proteins has been further investigated by a quantitative comparison of USP9X phosphorylation in WT vs CDC14B-overexpressing HEK 293Tcells (ATCC® CRL-3216™). The approach identified USP9X serine 2563 as a specific CDC14B target. Phosphorylation at USP9XS2563 has been confirmed by in-house phosphospecific antibodies.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Christian Johannes Gloeckner  

LAB HEAD: Christian Johannes Gloeckner

PROVIDER: PXD012733 | Pride | 2020-03-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
GLO0029-S4-USP9x-FT-A1.raw Raw
GLO0029_txt.zip Other
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Publications


Regulation of mitosis secures cellular integrity and its failure critically contributes to the development, maintenance, and treatment resistance of cancer. In yeast, the dual phosphatase Cdc14 controls mitotic progression by antagonizing Cdk1-mediated protein phosphorylation. By contrast, specific mitotic functions of the mammalian Cdc14 orthologue CDC14B have remained largely elusive. Here, we find that CDC14B antagonizes CDK1-mediated activating mitotic phosphorylation of the deubiquitinase U  ...[more]

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