Cheusova T, et al. (2006) Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction. Genes Dev 20, 1800-16 16818610

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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S680-p - MUSK (mouse) ▲

Modsite: TVCSLSHsDLSTRAR SwissProt Entrez-Gene Orthologous residues MUSK (human): S681‑p, MUSK (mouse): S680‑p, MUSK (rat): S680‑p Characterization Methods used to characterize site in vivo:  mutation of modification site Relevant cell lines - cell types - tissues:  C2C12 (myoblast) Cellular systems studied:  cell lines Species studied:  mouse Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK2A1 (human) Downstream Regulation Comments:  formation of regular AChR clusters

S697-p - MUSK (mouse) ▲

Modsite: SPGPPPLsCAEQLCI SwissProt Entrez-Gene Orthologous residues MUSK (human): S698‑p, MUSK (mouse): S697‑p, MUSK (rat): S697‑p Characterization Methods used to characterize site in vivo:  mutation of modification site Relevant cell lines - cell types - tissues:  C2C12 (myoblast) Cellular systems studied:  cell lines Species studied:  mouse Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK2A1 (human) Downstream Regulation Comments:  formation of regular AChR clusters