Gagnon KB, England R, Delpire E (2007) A single binding motif is required for SPAK activation of the Na-K-2Cl cotransporter. Cell Physiol Biochem 20, 131-42 17595523

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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T205-p - NKCC1 (mouse) ▲

Modsite: TNtYYLRtFGHNtMD SwissProt Entrez-Gene Orthologous residues NKCC1 (human): T212‑p, NKCC1 iso3 (human): T212‑p, NKCC1 (mouse): T205‑p, NKCC1 (rat): T203‑p Characterization Methods used to characterize site in vivo:  mutation of modification site Relevant cell lines - cell types - tissues:  oocyte Cellular systems studied:  primary cells Species studied:  frog Enzymes shown to modify site in vitro:  Type Enzyme KINASE STLK3 (human) Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes KINASE STLK3 (human) co-immunoprecipitation, transfection of wild-type enzyme, mutation in upstream enzyme recognition motif, modification site within consensus motif Downstream Regulation Effect of modification (function):  activity, induced

T210-p - NKCC1 (mouse) ▲

Modsite: LRtFGHNtMDAVPRI SwissProt Entrez-Gene Orthologous residues NKCC1 (human): T217‑p, NKCC1 iso3 (human): T217‑p, NKCC1 (mouse): T210‑p, NKCC1 (rat): T208‑p Characterization Methods used to characterize site in vivo:  mutation of modification site Relevant cell lines - cell types - tissues:  oocyte Cellular systems studied:  primary cells Species studied:  frog Enzymes shown to modify site in vitro:  Type Enzyme KINASE STLK3 (human)