PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation

Journal of Biological Chemistry

Volumn 273, Issue 27, 1998, Pages 16935-16945

  Tang, Jie ^a,b   Gary, Jonathan D ^a   Clarke, Steven ^a   Herschman, Harvey R ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYBRID PROTEIN; PROTEIN ARGININE METHYLTRANSFERASE; RECOMBINANT PROTEIN;

ANIMAL CELL; ARTICLE; CELLULAR DISTRIBUTION; ENZYME ANALYSIS; ENZYME REGULATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; IMMUNOBLOTTING; IMMUNOFLUORESCENCE; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN METHYLATION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BIOPOLYMERS; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; DNA, COMPLEMENTARY; GLUTATHIONE TRANSFERASE; HUMANS; METHYLATION; MOLECULAR SEQUENCE DATA; OPEN READING FRAMES; PROTEIN-ARGININE N-METHYLTRANSFERASE; RATS; RECOMBINANT FUSION PROTEINS; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; SUBCELLULAR FRACTIONS; SUBSTRATE SPECIFICITY;

EID: 0032479171     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.27.16935     Document Type: Article

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