Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiae.

Molecular biology of the cell - 1 Jul 2002

Sato Ken, Nakano Akihiko

Abstract excerpt

The yeast open reading frame YLR080w/EMP46 encodes a homolog of the Golgi protein Emp47p. These two proteins are 45% identical and have a single transmembrane domain in their C-terminal regions and a carbohydrate recognition domain signature in the N-terminal region. The C-terminal tail of Emp46p includes a dilysine signal. This protein is localized to Golgi membranes at steady state by subcellular fractionation...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Fractionation
Share to COP-Coated Vesicles

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum

Share to Glycoproteins

Share to Golgi Apparatus

Share to Protein Sorting Signals

Share to Tyrosine

Share to Vesicular Transport Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 12134087
DOI: 10.1091/mbc.e02-01-0027
PMCID: PMC117331

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Emp47p and its close homolog Emp46p have a tyrosine-containing endoplasmic reticulum exit signal and function in glycoprotein secretion in Saccharomyces cerevisiae.PMID 12134087Read ↗

Structures of the carbohydrate recognition domain of Ca2+-independent cargo receptors Emp46p and Emp47p.Semantic proximity Read ↗

The Golgi-localization of yeast Emp47p depends on its di-lysine motif but is not affected by the ret1-1 mutation in alpha-COP.Semantic proximity Read ↗

The Sec20/Tip20p complex is involved in ER retrieval of dilysine-tagged proteins.Semantic proximity Read ↗

Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome.Semantic proximity Read ↗

Erp1p and Erp2p, partners for Emp24p and Erv25p in a yeast p24 complex.Semantic proximity Read ↗

Proteolytic function of GPI-anchored plasma membrane protease Yps1p in the yeast vacuole and Golgi.Semantic proximity Read ↗

The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system.Semantic proximity Read ↗

The yeast inositol polyphosphate 5-phosphatase Inp54p localizes to the endoplasmic reticulum via a C-terminal hydrophobic anchoring tail: regulation of secretion from the endoplasmic reticulum.Semantic proximity Read ↗

Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments.Semantic proximity Read ↗

Exo70p mediates the secretion of specific exocytic vesicles at early stages of the cell cycle for polarized cell growth.Semantic proximity Read ↗

Identification of the essential EPE1 gene involved in retention of secreted proteins on the cell surface of Saccharomyces cerevisiae cells.Semantic proximity Read ↗

Eps1, a novel PDI-related protein involved in ER quality control in yeast.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.