The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer

EMBO Journal

Volumn 16, Issue 18, 1997, Pages 5509-5519

  Johnson, Erica S ^b   Schwienhorst, Ingrid ^a   Dohmen, R Jürgen ^a   Blobel, Günter ^b  

^a HEINRICH HEINE UNIVERSITY   (Germany)

^b ROCKEFELLER UNIVERSITY   (United States)

Author keywords

Aos1p; Post translational modification; Uba2p; Ubiquitin activating enzyme; Yeast

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; GLYCINE; UBIQUITIN;

ARTICLE; BACTERIAL GENE; CARBOXY TERMINAL SEQUENCE; CELL VIABILITY; CONJUGATION; CONTROLLED STUDY; GENE ACTIVATION; GENE FUNCTION; LETHALITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; RNA TRANSLATION; SACCHAROMYCES CEREVISIAE;

ALLELES; AMINO ACID SEQUENCE; BINDING SITES; CELL SURVIVAL; DIMERIZATION; FUNGAL PROTEINS; GENETIC COMPLEMENTATION TEST; GLYCINE; HUMANS; LIGASES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECEPTORS, ESTROGEN; RECOMBINANT FUSION PROTEINS; REPRESSOR PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE ALIGNMENT; SMALL UBIQUITIN-RELATED MODIFIER PROTEINS; UBIQUITIN-ACTIVATING ENZYMES; UBIQUITIN-PROTEIN LIGASES; UBIQUITINS;

BACTERIA (MICROORGANISMS); MAMMALIA; SACCHAROMYCES CEREVISIAE;

EID: 0030794729     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.18.5509     Document Type: Article

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