Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
1 to 4 of 4  Show
  1. 1
    "The complete primary structure of protein kinase C -- the major phorbol ester receptor."
    Parker P.J., Coussens L., Totty N., Rhee L., Young S., Chen E., Stabel S., Waterfield M.D., Ullrich A.
    Science 233:853-859(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Category: Sequences.
    Tissue: Brain.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    "The molecular heterogeneity of protein kinase C and its implications for cellular regulation."
    Nishizuka Y.
    Nature 334:661-665(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4 other entries.

  3. 3
    "Identification of the phosphorylated region responsible for the permissive activation of protein kinase C."
    Cazaubon S.M., Parker P.J.
    J. Biol. Chem. 268:17559-17563(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-494; THR-495 AND THR-497, PHOSPHORYLATION AT THR-494; THR-495 AND THR-497.
    Category: Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).
  4. 4
    "Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase-resistant state."
    Bornancin F., Parker P.J.
    J. Biol. Chem. 272:3544-3549(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-657.
    Category: PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).
1 to 4 of 4  Show

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health