A conserved deubiquitinating enzyme uses intrinsically disordered regions to scaffold multiple protein interaction sites

Journal of Biological Chemistry

Volumn 290, Issue 33, 2015, Pages 20601-20612

  Reed, Benjamin J ^a   Locke, Melissa N ^a   Gardner, Richard G ^a  

^a UNIVERSITY OF WASHINGTON SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME ACTIVITY; ENZYMES; SCAFFOLDS (BIOLOGY);

DEUBIQUITINATING ENZYMES; IDENTIFICATION OF PROTEINS; INTRINSICALLY DISORDERED REGIONS; MULTIPLE CONFORMATIONS; PROTEIN INTERACTION; PROTEIN INTERACTION SITES; PROTEIN MODIFICATIONS; THREE-DIMENSIONAL STRUCTURE;

PROTEINS;

DEUBIQUITINASE; FUNGAL PROTEIN; UBP10 PROTEIN; UNCLASSIFIED DRUG; USP36 PROTEIN; INTRINSICALLY DISORDERED PROTEIN; NUCLEAR PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN THIOLESTERASE; UBP10 PROTEIN, S CEREVISIAE;

ARTICLE; BINDING SITE; BIOGENESIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME STRUCTURE; GENE SILENCING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN INTRINSICALLY DISORDERED REGION; PROTEIN MOTIF; REGULATORY MECHANISM; RIBOSOME; SEQUENCE HOMOLOGY; UBIQUITINATION; CHEMISTRY; ENZYMOLOGY; HUMAN; METABOLISM; SACCHAROMYCES CEREVISIAE;

BINDING SITES; CATALYTIC DOMAIN; HUMANS; INTRINSICALLY DISORDERED PROTEINS; NUCLEAR PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN THIOLESTERASE;

EID: 84939641748     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.650952     Document Type: Article

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