Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a shared component of mammalian histone H3K4 methyltransferase complexes

Journal of Biological Chemistry

Volumn 286, Issue 14, 2011, Pages 12234-12244

  Butler, Jill S ^a,b   Zurita Lopez, Cecilia I ^c   Clarke, Steven G ^c   Bedford, Mark T ^a,b   Dent, Sharon Y R ^a,b  

^a UNIVERSITY OF TEXAS   (United States)

^b UNIVERSITY OF TEXAS MD ANDERSON CANCER CENTER   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE RESIDUE; ENZYME COMPLEXES; HISTONE PROTEINS; IN-CELL; IN-VITRO; METHYLTRANSFERASES; ONCOPROTEINS; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN-ARGININE METHYLTRANSFERASE; SHARED COMPONENTS; TRIMETHYLATION;

ARGININE; ENZYMES; MAMMALS;

AMINO ACIDS;

ARGININE; HISTONE H3; HISTONE H3K4; HISTONE LYSINE METHYLTRANSFERASE; METHYLTRANSFERASE; METHYLTRANSFERASE ASH2L; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 5; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; IN VITRO STUDY; MOLECULAR INTERACTION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN METHYLATION; PROTEIN PROCESSING;

BLOTTING, WESTERN; CELL LINE; CELL LINE, TUMOR; DNA-BINDING PROTEINS; HELA CELLS; HISTONE-LYSINE N-METHYLTRANSFERASE; HUMANS; IMMUNOPRECIPITATION; METHYLATION; NUCLEAR PROTEINS; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN-ARGININE N-METHYLTRANSFERASES; REPRESSOR PROTEINS; TRANSCRIPTION FACTORS;

MAMMALIA;

EID: 79953314028     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.202416     Document Type: Article

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