Xu ZC, Yang Y, Hebert SC (1996) Phosphorylation of the ATP-sensitive, inwardly rectifying K+ channel, ROMK, by cyclic AMP-dependent protein kinase. J Biol Chem 271, 9313-9 8621594

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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S44-p - ROMK (rat) ▲
Modsite: RQRARLVsKEGRCNI SwissProt Entrez-Gene Orthologous residues ROMK (human): S44‑p, ROMK (mouse): S25‑p, ROMK (rat): S44‑p, ROMK iso2 (rat): S25‑p Upstream Regulation Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes colforsin increase IBMX increase

S219-p - ROMK (rat) ▲
Modsite: RVANLRKsLLIGSHI SwissProt Entrez-Gene Orthologous residues ROMK (human): S219‑p, ROMK (mouse): S200‑p, ROMK (rat): S219‑p, ROMK iso2 (rat): S200‑p Upstream Regulation Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes colforsin increase IBMX increase

S313-p - ROMK (rat) ▲
Modsite: ATCQVRTsYVPEEVL SwissProt Entrez-Gene Orthologous residues ROMK (human): S313‑p, ROMK (mouse): S294‑p, ROMK (rat): S313‑p, ROMK iso2 (rat): S294‑p Upstream Regulation Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes colforsin increase IBMX increase

S25-p - ROMK iso2 (rat) ▲

Modsite: RQRARLVsKEGRCNI SwissProt Orthologous residues ROMK (human): S44‑p, ROMK (mouse): S25‑p, ROMK (rat): S44‑p, ROMK iso2 (rat): S25‑p Characterization Methods used to characterize site in vivo:  mutation of modification site, western blotting Relevant cell lines - cell types - tissues:  293 (epithelial), oocyte Cellular systems studied:  cell lines, primary cells Species studied:  frog, human Enzymes shown to modify site in vitro:  Type Enzyme KINASE PKACA (human) Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes KINASE PKACA (human) pharmacological activator of upstream enzyme, mutation in upstream enzyme recognition motif Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes colforsin increase IBMX increase Downstream Regulation Effect of modification (function):  activity, induced Comments:  phosphorylation of at least two serines necessary for channel activity

S200-p - ROMK iso2 (rat) ▲

Modsite: RVANLRKsLLIGSHI SwissProt Orthologous residues ROMK (human): S219‑p, ROMK (mouse): S200‑p, ROMK (rat): S219‑p, ROMK iso2 (rat): S200‑p Characterization Methods used to characterize site in vivo:  mutation of modification site, western blotting Relevant cell lines - cell types - tissues:  293 (epithelial), oocyte Cellular systems studied:  cell lines, primary cells Species studied:  frog, human Enzymes shown to modify site in vitro:  Type Enzyme KINASE PKACA (human) Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes KINASE PKACA (human) pharmacological activator of upstream enzyme, mutation in upstream enzyme recognition motif Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes colforsin increase IBMX increase Downstream Regulation Effect of modification (function):  activity, induced Comments:  phosphorylation of at least two serines necessary for channel activity

S294-p - ROMK iso2 (rat) ▲

Modsite: ATCQVRTsYVPEEVL SwissProt Orthologous residues ROMK (human): S313‑p, ROMK (mouse): S294‑p, ROMK (rat): S313‑p, ROMK iso2 (rat): S294‑p Characterization Methods used to characterize site in vivo:  mutation of modification site, western blotting Relevant cell lines - cell types - tissues:  293 (epithelial), oocyte Cellular systems studied:  cell lines, primary cells Species studied:  frog, human Enzymes shown to modify site in vitro:  Type Enzyme KINASE PKACA (human) Upstream Regulation Potential in vivo enzymes for site:  Type Enzyme Evidence Notes KINASE PKACA (human) pharmacological activator of upstream enzyme, mutation in upstream enzyme recognition motif Treatments, proteins and their effect on site modification:  Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes colforsin increase IBMX increase Downstream Regulation Effect of modification (function):  activity, induced Comments:  phosphorylation of at least two serines necessary for channel activity