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Article

Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins.

The EMBO journal - 24 Mar 2004

Hettema Ewald H, Valdez-Taubas Javier, Pelham Hugh R B

Abstract excerpt

Membrane proteins destined for the vacuolar or lysosomal lumen are typically ubiquitinated, the ubiquitin serving as a targeting signal for the multivesicular body pathway. The RING-domain ubiquitin ligase Tul1 is an integral membrane protein that modifies the yeast vacuolar enzyme carboxypeptidase S (Cps1), the polyphosphatase Ppn1/Phm5 and other proteins containing exposed hydrophilic residues within their...

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Share to Carboxypeptidases
Share to Endosomal Sorting Complexes Required for Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Fungal

Share to Ion Transport

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Share to Saccharomyces cerevisiae Proteins

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Source

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Identifiers

PMID: 14988731
DOI: 10.1038/sj.emboj.7600137
PMCID: PMC381411

Genes

NEDD4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Bsd2 binds the ubiquitin ligase Rsp5 and mediates the ubiquitination of transmembrane proteins.PMID 14988731Read ↗

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