Curated Information
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Home > Curated Information Page > PubMed Id: 27105117
Keramisanou D, et al. (2016) Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37. Mol Cell 62, 260-71 27105117
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S13-p - CDC37 (human)
Modsite: VWDHIEVsDDEDETH SwissProt Entrez-Gene
Orthologous residues
CDC37 (human): S13‑p, CDC37 (mouse): S13‑p, CDC37 (rat): S13‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, western blotting
Disease tissue studied:  breast cancer
Relevant cell lines - cell types - tissues:  MCF-7 (breast cell)
Cellular systems studied:  cell lines
Species studied:  human
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Comments:  S13 phosphorylation does not impact recognition or affnity for BRAF. S13 affects chaperone cycle at a stage later than Cdc37 recognition.