A novel p53 phosphorylation site within the MDM2 ubiquitination signal: I. Phosphorylation at SER269 in vivo is linked to inactivation of p53 function

Journal of Biological Chemistry

Volumn 285, Issue 48, 2010, Pages 37762-37772

  Fraser, Jennifer A ^a   Vojtesek, Borivoj ^b   Hupp, Ted R ^a  

^a UNIVERSITY OF EDINBURGH   (United Kingdom)

^b MASARYK MEMORIAL CANCER INSTITUTE   (Czech Republic)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION FUNCTIONS; DNA-BINDING DOMAIN; DOCKING SITES; DYNAMIC EQUILIBRIA; HUMAN TUMOR CELLS; IN-VITRO; IN-VIVO; P53 FUNCTION; P53 PROTEIN; PEPTIDE LIBRARY; PHOSPHORYLATION SITES; UBIQUITINATION;

ALLERGIES; BINDING ENERGY; MONOCLONAL ANTIBODIES; PEPTIDES; SURFACE PLASMON RESONANCE;

PHOSPHORYLATION;

DNA; EPITOPE; MONOCLONAL ANTIBODY; PROTEIN MDM2; PROTEIN P53; SERINE;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; EMBRYO; ENZYME SPECIFICITY; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; MOLECULAR DOCKING; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; SIGNAL TRANSDUCTION; TRANSCRIPTION INITIATION; UBIQUITINATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; CELL LINE, TUMOR; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PHOSPHORYLATION; PROTEIN BINDING; PROTO-ONCOGENE PROTEINS C-MDM2; SERINE; TUMOR SUPPRESSOR PROTEIN P53; UBIQUITINATION;

EID: 78549274413     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.143099     Document Type: Article

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