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Article

Autophosphorylation of purified c-Src at its primary negative regulation site.

The Journal of biological chemistry - 27 Oct 1995

Osusky M, Taylor S J, Shalloway D

Abstract excerpt

The phosphorylating and transforming activities of c-Src are negatively regulated by phosphorylation at Tyr-527 near its carboxyl terminus. Previous studies have indicated that c-Src preferentially autophosphorylates Tyr-416, a residue in the middle of the catalytic domain, in vitro, and that Tyr-527 is phosphorylated by the carboxyl-terminal Src kinase, Csk. However, indirect evidence suggests that c-Src may...

Topics

Escherichia coli
Mutation
Phosphorylation
Phosphotyrosine
Proto-Oncogene Proteins pp60(c-src)
Recombinant Proteins
Tyrosine

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 7592753
DOI: 10.1074/jbc.270.43.25729

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7592753-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Autophosphorylation of purified c-Src at its primary negative regulation site.PMID 7592753Read ↗

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A new strategy to produce active human Src from bacteria for biochemical study of its regulation.Semantic proximity Read ↗

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Activation of human pp60c-src.Semantic proximity Read ↗

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