The in vitro phosphorylation of the co-chaperone mSTI1 by cell cycle kinases substantiates a predicted casein kinase II-p34(cdc2)-NLS(CcN) motif

Biological Chemistry

Volumn 381, Issue 11, 2000, Pages 1133-1138

  Longshaw, V M ^a   Dirr, H W ^a   Blatch, G L ^a   Lassle, M ^a  

^a WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

Author keywords

Cell cycle; Heat shock protein; Nuclear localization; Stress protein

Indexed keywords

CASEIN KINASE II; CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEIN KINASE; STRESS INDUCIBLE PROTEIN 1; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL CYCLE; CONTROLLED STUDY; ENZYME SUBSTRATE; IN VITRO STUDY; MOUSE; NONHUMAN; NUCLEAR LOCALIZATION SIGNAL; PREDICTION; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CASEIN KINASE II; CDC2 PROTEIN KINASE; CELL CYCLE; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; MICE; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; NUCLEAR LOCALIZATION SIGNALS; PHOSPHOPROTEINS; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; RECOMBINANT FUSION PROTEINS;

EID: 0034535451     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2000.139     Document Type: Article

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