Eswaran J, et al. (2008) Structure of the human protein kinase MPSK1 reveals an atypical activation loop architecture. Structure 16, 115-24 18184589

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.

Click on the protein name to open the protein page, and on the RSD number to open the site page.

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T101-p - DRG1 (human) ▲
Modsite: yEFTTLTtVPGVIRY SwissProt Entrez-Gene Orthologous residues DRG1 (human): T101‑p, DRG1 (mouse): T101‑p, DRG1 (rat): T101‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE MPSK1 (human)

T185-p - MPSK1 (human) ▲
Modsite: EGSRQALtLQDWAAQ SwissProt Entrez-Gene Orthologous residues MPSK1 (human): T185‑p, MPSK1 (mouse): A185‑p, MPSK1 (rat): A185‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE MPSK1 (human)

S197-p - MPSK1 (human) ▲
Modsite: AAQRCTIsyRAPELF SwissProt Entrez-Gene Orthologous residues MPSK1 (human): S197‑p, MPSK1 (mouse): S197‑p, MPSK1 (rat): S197‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE MPSK1 (human)

Y198-p - MPSK1 (human) ▲
Modsite: AQRCTIsyRAPELFS SwissProt Entrez-Gene Orthologous residues MPSK1 (human): Y198‑p, MPSK1 (mouse): Y198‑p, MPSK1 (rat): Y198‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE MPSK1 (human)