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Article

Identification of the site of interaction of the 14-3-3 protein with phosphorylated tryptophan hydroxylase.

The Journal of biological chemistry - 1 Dec 1995

Ichimura T, Uchiyama J, Kunihiro O, Ito M, Horigome T, Omata S, Shinkai F, Kaji H, Isobe T

Abstract excerpt

The 14-3-3 protein family plays a role in a wide variety of cell signaling processes including monoamine synthesis, exocytosis, and cell cycle regulation, but the structural requirements for the activity of this protein family are not known. We have previously shown that the 14-3-3 protein binds with and activates phosphorylated tryptophan hydroxylase (TPH, the rate-limiting enzyme in the biosynthesis of...

Topics

14-3-3 Proteins
Amino Acid Sequence
Animals
Base Sequence
DNA, Complementary
Escherichia coli
Molecular Sequence Data
Mutation
Phosphorylation
Proteins
Rats

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Sequence Homology, Amino Acid

Tryptophan Hydroxylase

Tyrosine 3-Monooxygenase

Source

Identifiers

PMID: 7499362
DOI: 10.1074/jbc.270.48.28515

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7499362-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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