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Article

Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain.

Journal of molecular biology - 12 Dec 2014

Liang Ruei-Yue, Chen Li, Ko Bo-Ting, Shen Yu-Han, Li Yen-Te, Chen Bo-Rong, Lin Kuan-Ting, Madura Kiran, Chuang Show-Mei

Abstract excerpt

Rad23 was identified as a DNA repair protein, although a role in protein degradation has been described. The protein degradation function of Rad23 contributes to cell cycle progression, stress response, endoplasmic reticulum proteolysis, and DNA repair. Rad23 binds the proteasome through a UbL (ubiquitin-like) domain and contains UBA (ubiquitin-associated) motifs that bind multiubiquitin chains. These domains...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 25311859
DOI: 10.1016/j.jmb.2014.10.004
PMCID: PMC4258468

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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Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain.PMID 25311859Read ↗

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