MassIVE MSV000100123

Complete Public PXD071647

Proteomics reveals extensive phosphoregulation of outer kinetochore protein KNL1

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Description

The goal of this project was to utilize a proteomics approach to identify phosphorylation sites on native KNL1 purified from HEK293T/17 cells. KNL1 phosphorylation is known to be critical for activation of the spindle assembly checkpoint and recruitment of the fibrous corona in the presence of unattached kinetochores. We tested KNL1 phosphorylation in 4 different kinetochore-microtubule attachment states to identify additional sites that may be involved in regulating kinetochore function. [doi:10.25345/C5MP4W18K] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Kinetchore ; LC-MS/MS ; anti-FLAG immunoprecipitation ; DatasetType:Proteomics

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Principal Investigators:
(in alphabetical order) 		Susan Biggins, Fred Hutchinson Cancer Center, USA
Submitting User: FHproteomics
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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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