Error
Your session has expired. Please click "Refresh" to refresh the page.
Nuclear Receptor Signaling Atlas
A research resource for the nuclear receptor signaling community
CARM1
Last updated January 31, 2014
Overview
NURSA Name
Coactivator-associated arginine methyltransferase-1
NURSA Symbol
CARM1
Synonyms
ARABIDOPSIS THALIANA PROTEIN ARGININE METHYLTRANSFERASE 4B; ATPRMT4B; Art4; Art4-PA; Art4-PB; CARM1; CARMER; CG5358; CG5358-PA; CG5358-PB more...
Synonyms
ARABIDOPSIS THALIANA PROTEIN ARGININE METHYLTRANSFERASE 4B; ATPRMT4B; Art4; Art4-PA; Art4-PB; CARM1; CARMER; CG5358; CG5358-PA; CG5358-PB; Carm1; DART4; Dmel\CG5358; PRMT4; PRMT4B; Prmt4; arginie methyl transferase 4; arginine methyl-transferase 4; arginine methyltransferase 4; carm1; coactivator Arg methyltransferase for Ecr/Usp; histone-arginine methyltransferase CARM1; protein arginine N-methyltransferase 4; protein arginine methyltransferase; protein arginine methyltransferase 4B; si:dkey-204f11.63; zgc:100805
Description
CARM1 is an arginine methyltransferase which targets transcriptional coactivators, including SRC-1 and CBP, to regulate transcription at their cognate promoters. It has been shown to function as a coregulator for several members of the nuclear receptor superfamily. CARM1 is broadly expressed in a variety of tissues, with peaks of expression in the central nervous system (corpus striatum, olfactory bulb, hypothalamus, pituitary), reproductive system (ovary, testis) and metabolic tissues (muscle, thyroid, aorta). CARM1 has been shown to be overexpressed in prostate cancer and maps to a genomic location influencing circulating levels of homocysteine and therefore susceptibility to vascular diseases. Homozygous null deletion of CARM1 results in perinatal mortality and defects in protein methylation.
Original References:
Chen D,Ma H,Hong H,Koh SS,Huang SM,Schurter BT, et al. (1999) Regulation of transcription by a protein methyltransferase. Science 28 2174-7 View Abstract | View Pubmed
View Pubmed

Abstract

Human
Gene
RNA
Protein
GO Terms
Post-Translational Modifications
Crystal Structures
Protein-Protein Interactions
Targeting miRNAs
Datasets
Reagents
Diseases
Clinical Trials
Animal Models
Drugs
Literature