An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination

Biochemical Journal

Volumn 469, Issue 3, 2015, Pages 455-467

  Puig Sàrries, Pilar ^a,b   Bijlmakers, Marie José ^a   Zuin, Alice ^a   Bichmann, Anne ^a   Pons, Miquel ^c   Crosas, Bernat ^a  

^a INSTITUT DE BIOLOGIA MOLECULAR DE BARCELONA   (Spain)

^b INSTITUT QUÍMIC DE SARRIÀ   (Spain)

^c UNIVERSITY OF BARCELONA   (Spain)

Author keywords

E3 ubiquitin ligase; Fold back model; Intrinsically disordered protein; Monoubiquitination; Polyubiquitin chain; Proteasome; Rpn10; Rsp5; Ubiquitin

Indexed keywords

INTRINSICALLY DISORDERED PROTEIN; POLYUBIQUITIN; PROTEASOME; REGULATOR PROTEIN; RPN10 PROTEIN; RSP5 PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG; RPN10 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; GENE MUTATION; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; RECEPTOR DOWN REGULATION; UBIQUITINATION; YEAST; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; METABOLISM; MOLECULAR GENETICS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT;

EUKARYOTA;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; MOLECULAR SEQUENCE DATA; PROTEASOME ENDOPEPTIDASE COMPLEX; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; UBIQUITIN; UBIQUITINATION;

EID: 84938614568     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141571     Document Type: Article

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