Stat5a serine phosphorylation. Serine 779 is constitutively phosphorylated in the mammary gland, and serine 725 phosphorylation influences prolactin-stimulated in vitro DNA binding activity

Journal of Biological Chemistry

Volumn 275, Issue 14, 2000, Pages 10247-10255

  Beuvink, Iwan ^a   Hess, Daniel ^a   Flotow, Horst ^a,b   Hofsteenge, Jan ^a   Groner, Bernd ^a,c   Hynes, Nancy E ^a  

^a FRIEDRICH MIESCHER INSTITUTE FOR BIOMEDICAL RESEARCH   (Switzerland)

^b ROCHE PRODUCTS LTD   (United Kingdom)

^c INSTITUTE FOR TUMOR BIOLOGY AND EXPERIMENTAL THERAPY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BETA CASEIN; DNA; LUCIFERASE; PHOSPHATE; PHOSPHOPEPTIDE; PHOSPHORUS 32; PROLACTIN; SERINE; STAT5 PROTEIN; TYROSINE;

ANIMAL CELL; ARTICLE; DNA BINDING; MAMMARY GLAND; NONHUMAN; PEPTIDE ANALYSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; TRANSCRIPTION INITIATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; BRAIN; COS CELLS; DNA-BINDING PROTEINS; FEMALE; LUNG; MAMMARY GLANDS, ANIMAL; MICE; MILK PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MYOCARDIUM; PEPTIDE FRAGMENTS; PEPTIDE MAPPING; PHOSPHATES; PHOSPHOPEPTIDES; PHOSPHORYLATION; PHOSPHOSERINE; PROLACTIN; RECEPTORS, PROLACTIN; RECOMBINANT PROTEINS; SERINE; SPLEEN; STAT5 TRANSCRIPTION FACTOR; TRANS-ACTIVATORS; TRANSFECTION;

ANIMALIA;

EID: 0034615929     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.275.14.10247     Document Type: Article

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