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Article

Acidic residues at the carboxyl terminus of p60c-src are required for regulation of tyrosine kinase activity and transformation.

The New biologist - 1 Sept 1990

MacAuley A, Cooper J A

Abstract excerpt

Protein phosphorylation sites act to transduce signals into changes in enzymatic activity, representing a point of interaction within a regulatory pathway. The amino acid sequence surrounding a phosphorylation site may well have several functions, including recognition by an appropriate kinase. B...

Topics

Amino Acid Sequence
Animals
Base Sequence
DNA
Humans
Molecular Sequence Data
Mutation
Peptide Mapping
Protein-Tyrosine Kinases
Proto-Oncogene Mas
Proto-Oncogene Proteins pp60(c-src)
Sequence Homology, Nucleic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Transformation, Genetic

Source

Identifiers

PMID: 1703788

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1703788-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Acidic residues at the carboxyl terminus of p60c-src are required for regulation of tyrosine kinase activity and transformation.PMID 1703788Read ↗

Regulation of the oncogenic activity of the cellular src protein requires the correct spacing between the kinase domain and the C-terminal phosphorylated tyrosine (Tyr-527).Semantic proximity Read ↗

Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src.Semantic proximity Read ↗

The amino-terminal region of pp60c-src has a modulatory role and contains multiple sites of tyrosine phosphorylation.Semantic proximity Read ↗

Analysis of mutant forms of the c-src gene product containing a phenylalanine substitution for tyrosine 416.Semantic proximity Read ↗

Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain.Semantic proximity Read ↗

Phosphorylation of Src mutants at Tyr 527 in fibroblasts does not correlate with in vitro phosphorylation by CSK.Semantic proximity Read ↗

Mutational activation of pp60(c-src) leads to a tumorigenic phenotype in a preneoplastic Syrian hamster embryo cell line.Semantic proximity Read ↗

Autophosphorylation of purified c-Src at its primary negative regulation site.Semantic proximity Read ↗

Autophosphorylation is required for high kinase activity and efficient transformation ability of proteins encoded by host range alleles of v-src.Semantic proximity Read ↗

Highly conserved amino acids in the SH2 and catalytic domains of v-src are altered in naturally occurring, transformation-defective alleles.Semantic proximity Read ↗

The amino terminus of polyomavirus middle T antigen is required for transformation.Semantic proximity Read ↗

pp60c-src binding to polyomavirus middle T-antigen (MT) requires residues 185 to 210 of the MT sequence.Semantic proximity Read ↗

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