"Genuine" Casein Kinase (Fam20C): The Mother of the Phosphosecretome

Giorgio Cozza, Vincent S. Tagliabracci, Jack E. Dixon, Lorenzo A. Pinna

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Scopus citations


Although several members of the kinome are able to phosphorylate casein in vitro, notably casein kinase 2 (CK2) and the members of the casein kinase 1 (CK1) subfamily, none of these enzymes are the bona fide casein kinase (Golgi casein kinase (G-CK)) whose activity was detected and partially purified from the Golgi apparatus of lactating mammary gland and milk. Although casein was the first protein shown to contain phosphate esterified to phosphoseryl residues, the sequences surrounding the phosphoseryl residues of casein fractions started being elucidated almost one century later in 1971. In the meantime, the amino acid sequences surrounding residues in fibrinogen had been elucidated, revealing the same pS-x-E motif, later also found in pepsin, corticotropin, ovalbumin, and in all casein fractions. Peptide (ß28-40) exhibits an unmatched selectivity among the huge repertoire of protein kinase peptide substrates being unaffected only by all the false "casein kinases," including CK1 and CK2.

Original languageEnglish (US)
Title of host publicationKinomics
Subtitle of host publicationApproaches and Applications
Number of pages16
ISBN (Electronic)9783527683031
ISBN (Print)9783527337651
StatePublished - Oct 1 2015


  • Casein kinase
  • Fam20C
  • PS-x-E motif
  • Peptide substrate
  • Phosphoproteins
  • Phosphosecretome

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


Dive into the research topics of '"Genuine" Casein Kinase (Fam20C): The Mother of the Phosphosecretome'. Together they form a unique fingerprint.

Cite this