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Article

Mutational analysis of the carboxy-terminal casein kinase II phosphorylation site in human c-myc.

Current topics in microbiology and immunology - 1 Jan 1990

Street A J, Blackwood E, Lüscher B, Eisenman R N

Abstract excerpt

Myc proteins are phosphorylated within two critical regions by casein kinase II (CKII): the central acidic domain and a carboxy-terminal region bordering the basic region-helix-loop-helix segment. In order to test whether the carboxy-terminal phosphorylation site was functionally important we introduced three types of mutations into this region. Two of the mutations would be expected to prevent phosphorylation...

Topics

Amino Acid Sequence
Animals
Casein Kinases
Cell Line
Cell Transformation, Neoplastic
Fusion Proteins, bcr-abl
Genes, myc
Humans
Mice
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphorylation

Protein Kinases

Rats

Source

Identifiers

PMID: 2073805
DOI: 10.1007/978-3-642-75889-8_31

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2073805-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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