Marin O, et al. (2002) Structural features underlying the multisite phosphorylation of the A domain of the NF-AT4 transcription factor by protein kinase CK1. Biochemistry 41, 618-27 11781102

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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S165-p - NFAT4 (human) ▲
Modsite: RESSLsPsPASSISs SwissProt Entrez-Gene Orthologous residues NFAT4 (human): S165‑p, NFAT4 iso2 (human): S165‑p, NFAT4 (mouse): S165‑p, NFAT4 iso3 (mouse): S165‑p, NFAT4 (rat): S166‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK1A (rat) Comments:  Phosphorylation of S177 and S165 primes hierarachical phosphorylation of other serines of NFAT4 peptides.

S177-p - NFAT4 (human) ▲
Modsite: ISsRSWFsDAssCEs SwissProt Entrez-Gene Orthologous residues NFAT4 (human): S177‑p, NFAT4 iso2 (human): S177‑p, NFAT4 (mouse): S177‑p, NFAT4 iso3 (mouse): S177‑p, NFAT4 (rat): S178‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK1A (rat) Comments:  Phosphorylation of S177 and S165 primes hierarachical phosphorylation of other serines of NFAT4 peptides.

S180-p - NFAT4 (human) ▲
Modsite: RSWFsDAssCEsLsH SwissProt Entrez-Gene Orthologous residues NFAT4 (human): S180‑p, NFAT4 iso2 (human): S180‑p, NFAT4 (mouse): S180‑p, NFAT4 iso3 (mouse): S180‑p, NFAT4 (rat): S181‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK1A (rat) Comments:  Phosphorylation of S177 and S165 primes hierarachical phosphorylation of other serines of NFAT4 peptides.

S181-p - NFAT4 (human) ▲
Modsite: SWFsDAssCEsLsHI SwissProt Entrez-Gene Orthologous residues NFAT4 (human): S181‑p, NFAT4 iso2 (human): S181‑p, NFAT4 (mouse): S181‑p, NFAT4 iso3 (mouse): S181‑p, NFAT4 (rat): S182‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK1A (rat) Comments:  Phosphorylation of S177 and S165 primes hierarachical phosphorylation of other serines of NFAT4 peptides.

S184-p - NFAT4 (human) ▲
Modsite: sDAssCEsLsHIYDD SwissProt Entrez-Gene Orthologous residues NFAT4 (human): S184‑p, NFAT4 iso2 (human): S184‑p, NFAT4 (mouse): S184‑p, NFAT4 iso3 (mouse): S184‑p, NFAT4 (rat): S185‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK1A (rat) Comments:  Phosphorylation of S177 and S165 primes hierarachical phosphorylation of other serines of NFAT4 peptides.

S186-p - NFAT4 (human) ▲
Modsite: AssCEsLsHIYDDVD SwissProt Entrez-Gene Orthologous residues NFAT4 (human): S186‑p, NFAT4 iso2 (human): S186‑p, NFAT4 (mouse): S186‑p, NFAT4 iso3 (mouse): S186‑p, NFAT4 (rat): S187‑p Characterization Enzymes shown to modify site in vitro:  Type Enzyme KINASE CK1A (rat) Comments:  Phosphorylation of S177 and S165 primes hierarachical phosphorylation of other serines of NFAT4 peptides.