Histone-arginine methyltransferase CARM1 (Protein name
), CARM1_MOUSE from NCBI database.
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General Annotation
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Gene name:
Carm1(Prmt4);
Protein name:
Histone-arginine methyltransferase CARM1;
Alternative:
Protein arginine N-methyltransferase 4;Coactivator-associated arginine methyltransferase 1;
Organism:
Mouse (Mus musculus).
General Annotation
Sub Unit:
Homodimer. Interacts with NR1H4. Interacts with SNRPC (By similarity). Interacts with the C-terminus of NCOA2/GRIP1, NCO3/ACTR and NCOA1/SRC1. Part of a complex consisting of CARM1, EP300/P300 and NCOA2/GRIP1. Interacts with FLII, TP53, myogenic factor MEF2, EP300/P300, TRIM24, CREBBP and CTNNB1. Interacts with RELA. Identified in a complex containing CARM1, TRIM24 and NCOA2/GRIP1. Interacts with NCOA3/SRC3.
Function:
Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability. Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activates transcription via chromatin remodeling. During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription. During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C. During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B. Acts as coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue. Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors. Also seems to be involved in p53/TP53 transcriptional activation. Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation. Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs.
Subcellular Location:
Nucleus
Cytoplasm
Mainly nuclear during the G1, S and G2 phases of the cell cycle. Cytoplasmic during mitosis, after breakup of the nuclear membrane.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);MUTAGENESIS OF 189-VAL--ASP-191;FUNCTION;TISSUE SPECIFICITY;METHYLATION OF HISTONE H3;INTERACTION WITH NCOA1; NCOA2 AND NCOA3
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2);NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-608 (ISOFORM 1)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-608 (ISOFORM 1)
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Cited for: FUNCTION IN METHYLATION OF HISTONE H3;CATALYTIC ACTIVITY
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Cited for: FUNCTION;METHYLATION OF EP300 AND CREBBP;MUTAGENESIS OF 189-VAL--ASP-191;INTERACTION WITH EP300 AND CREBBP
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Cited for: FUNCTION;SUBCELLULAR LOCATION;DEVELOPMENTAL STAGE;INTERACTION WITH MEF2C
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Cited for: FUNCTION;MUTAGENESIS OF GLU-267;INTERACTION WITH CTNNB1
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Cited for: FUNCTION;IDENTIFICATION IN A COMPLEX WITH EP300 AND NCOA2;MUTAGENESIS OF GLU-267
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Cited for: FUNCTION;DISRUPTION PHENOTYPE;METHYLATION OF PABPC1
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Cited for: METHYLATION OF HISTONE H3;FUNCTION;INTERACTION WITH RELA
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Cited for: FUNCTION;INTERACTION WITH TRIM24;IDENTIFICATION IN A COMPLEX WITH TRIM24 AND NCOA2
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Cited for: FUNCTION;CATALYTIC ACTIVITY;SUBUNIT;INTERACTION WITH EP300 AND NCOA3;SUBCELLULAR LOCATION;MUTAGENESIS OF TYR-154; SER-217 AND SER-229;PHOSPHORYLATION AT SER-217
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Cited for: FUNCTION;CATALYTIC ACTIVITY;DISRUPTION PHENOTYPE;SUBUNIT;MUTAGENESIS OF ARG-169 AND TYR-173
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Cited for: METHYLATION AT ARG-551;FUNCTION;CATALYTIC ACTIVITY;MUTAGENESIS OF ARG-551;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-490 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE;CATALYTIC ACTIVITY;FUNCTION;INTERACTION WITH NCOA2/GRIP1;ENZYME REGULATION;SUBUNIT