Mutational analysis of the putative effector domain of the GTP-binding Ypt1 protein in yeast suggests specific regulation by a novel GAP activity.

doi:10.1002/j.1460-2075.1991.tb08010.x

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Article

Mutational analysis of the putative effector domain of the GTP-binding Ypt1 protein in yeast suggests specific regulation by a novel GAP activity.

The EMBO journal - 1 Apr 1991

Becker J, Tan T J, Trepte H H, Gallwitz D

Abstract excerpt

Ypt1p of Saccharomyces cerevisiae is a ras-related GTP-binding protein that fulfils an essential function in intracellular protein transport between the endoplasmic reticulum (ER) and the Golgi complex. Ypt proteins from yeasts and mammals that share an identical sequence in the region analogous to the ras effector domain are functionally interchangeable. We analyzed the function of the putative effector domain...

Topics

Amino Acid Sequence
Base Sequence
Cloning, Molecular
Escherichia coli
Fungal Proteins
GTP Phosphohydrolases
GTPase-Activating Proteins
Genes, Fungal
Glycoside Hydrolases
Kinetics
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Oligonucleotide Probes

Phenotype

Proteins

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Temperature

Source

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Identifiers

PMID: 2009858
DOI: 10.1002/j.1460-2075.1991.tb08010.x
PMCID: PMC452717

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2009858-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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