Ubiquitin-mediated degradation of Rpn4 is controlled by a phosphorylation-dependent ubiquitylation signal

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1773, Issue 11, 2007, Pages 1672-1680

  Ju, Donghong ^a   Xu, Haiming ^a   Wang, Xiaogang ^a   Xie, Youming ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Proteasome; Protein degradation; Protein phosphorylation; Rpn4; Ubiquitin; Ubr2

Indexed keywords

PROTEASOME; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR RNP4; UBIQUITIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SACCHAROMYCES CEREVISIAE; UBIQUITINATION;

AMINO ACID SEQUENCE; DNA-BINDING PROTEINS; MOLECULAR SEQUENCE DATA; NAD; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SERINE; SIGNAL TRANSDUCTION; TRANSCRIPTION FACTORS; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

SACCHAROMYCES CEREVISIAE;

EID: 35548985701     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2007.04.012     Document Type: Article

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