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Information on EC 2.1.1.125 - histone-arginine N-methyltransferase
for references in articles please use BRENDA:EC2.1.1.125
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Please check here for current data: EC 2.1.1.319
Please check here for current data: EC 2.1.1.319
deleted, now covered by EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, EC 2.1.1.321, type III protein arginine methyltransferase and EC 2.1.1.322, type IV protein arginine methyltransferase
EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.125 histone-arginine N-methyltransferase
IUBMB Comments
The enzyme forms the Nω-monomethyl- and Nω,Nω′-dimethyl, but not the Nω,Nω-dimethyl-arginine derivatives. The name protein methylase I is misleading since it has been used for a number of enzymes with different specificities.
topHighest Expressing Human Cell Lines
Cell Line Links
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
malfunction
physiological function
malfunction
-
causal role of the elevated symmetric methylation of H3R8 and H4R3 at the RBL2 promoter in transformed B-lymphocyte pathology
malfunction
-
isoform PRMT2 silencing can enhance 17beta-estradiol-induced proliferation by regulating E2F1 expression and E2F1-responsive genes in estrogen receptor alpha-positive breast cancer cells
malfunction
-
isoform PRMT7 knockdown causes a significant decrease in enzyme recruitment and hsitone H2A-arginine 3/histone H4-arginine 3 methylation
malfunction
-
PRMT5 deficiency is associated with late flowering. Mutation of PRMT5 leads to widespread splicing defects
malfunction
-
knockdown of PRMT6 disrupts oestrogen-stimulated transcription of endogenous GREB1 and progesterone receptor in MCF-7 breast cancer cells. Knockdown of PRMT6 increases the exon inclusion:skipping ratio of alternatively spliced exons in endogenous vascular endothelial growth factor and spleen tyrosine kinase RNA transcripts in both the presence and absence of oestrogen
malfunction
-
mutations of protein arginine methyltransferase 10 result in a late-flowering phenotype
malfunction
-
silencing PRMT5 expression strongly inhibits proliferation of lung adenocarcinoma cells
physiological function
-
key role of PRMT5 and the two methylated histones in regulating rRNA promoter activity, PRMT5 functions as a transcriptional repressor of genes transcribed by RNA polymerase II
physiological function
-
involvement of protein argininemethyltransferases PRMT1 and CARM1 in p53 and p300 coactivator functions, analysis, overview. Distinct mechanisms for PRMT1 and p300, ectopic p53s. The results of recruitment of p300, PRMT1, and CARM1
physiological function
-
PRMT1 functions transiently as a coactivator in thyroid hormone receptor-mediated transcription by enhancing thyroid hormone receptor-T3 responsive element binding, PRMT1 has tissue-specific roles in regulating the rate of metamorphosis, overview
physiological function
-
proper epigenetic modification of chromatin by protein arginine methyltransferases, PRMTs, is crucial for normal cell growth and health
physiological function
-
Prmt5 is required for early-gene expression but dispensable for late-gene expression. Carm1/Prmt4 is required for late- but not for early-gene expression. Prmt5 is required for skeletal muscle differentiation at the early stages of myogenesis, while Carm1/Prmt4 at late genes is required to facilitate SWI/SNF chromatin-remodeling enzyme interaction and remodeling at late-gene loci
physiological function
-
PRMT5 and DNMT3A function cooperatively in gene silencing, DNMT3A binds specifically to histone H4R3me2s, overview
physiological function
-
PRMT-5 negatively regulates DNA damage-induced apoptosis
physiological function
-
PRMT1 is involved as effector in DNA damage signaling and epigenetic gene expression. Role of PRMT1, the major asymmetric arginine methyltransferase, in cellular processes and its link to human diseases, overview
physiological function
-
PRMT5 is a type II protein arginine methyltransferase that, in winter-annual strains, is required for epigenetic silencing of FLC, a member of a clade of floral repressors, and for the vernalization-mediated histone modifications characteristic of the vernalized state, overview. Arginine methylation of FLC chromatin is part of the histone code that is required for mitotic stability of the vernalized state
physiological function
-
PRMT1 is required for the transcriptional activity of the pregnane X receptor, PXR, a ligand-dependent transcription factor, regulating gene expression of enzymes and transporters involved in xenobiotic/drug metabolism. PXR has a reciprocal effect on thePRMT1 functions by regulating its cellular compartmentalization as well as its substrate specificity. The PXR ligand-binding domain is responsible for PXR-PRMT1 ligand-dependent interaction
physiological function
-
protein arginine methylation by PRMT5 plays a role in ZNF224-mediated transcriptional repression, overview
physiological function
-
CARM1 is a dual functional coregulator that facilitates transcription initiation by methylation of Arg17 and Arg26 of histone H3 and also dictates the subsequent coactivator complex disassembly by methylation of the steroid receptor coactivator family coactivators and p300/cAMP-response element-binding protein-binding protein. CARM1 function is regulated by phosphorylation at Ser217
physiological function
-
methylation of Arg17 in histone H3 by CARM1 plays a role in expression of p21, a p53-responsive gene and in the tumor suppressor function promoter-specific context, overview. CARM1 also is a secondary coactivator of several nuclear receptors. And CARM1 interacts with other chromatin-modifying enzymes such as p300/CBP and PRMT1 to bring about cooperative transcriptional activation of p53-responsive genes, overview
physiological function
-
CARM1 functions as a rather general transcriptional coactivator, much like p300/CBP. A possible scaffolding role for CARM1, that is a component of the nucleosomal methylation activator complex
physiological function
-
isoform PRMT2 and its splice variants may directly modulate estrogen receptor alpha signaling and play a role in the progression of breast cancer. Overexpression of PRMT2 variant mRNA in breast cancer is associated with estrogen receptor alpha positivity
physiological function
-
isoform PRMT7 regulates response to DNA damage and confers resistance to DNA-damaging agents. The enzyme interacts with BRG1-hSWI/SNF, targets histone H2A-arginine 3 and histone H4-arginine 3, and represses expression of POLD1. PRMT7 and BRG1 co-localize and are enriched at target DNA repair genes
physiological function
-
increased PRMT1 activity is associated with breast cancer (e.g., increased estrogen receptor alpha signaling) and heart disease (e.g., decreased nitric oxide production)
physiological function
-
methylation of Kaposi sarcoma-associated herpesvirus latency-associated nuclear antigen by PRMT1 antagonizes viral reactivation
physiological function
-
PRMT6 significantly increases the activity of estrogen receptor alpha, estrogen receptor beta, glucocorticoid receptor, and progesterone receptor by about 1.5, 2.1, 1.7 and 3.7fold, respectively. PRMT6 acts as a coactivator for steroid hormone receptors rather than a general transcription enhancer. PRMT6 enhances transcriptional activation with CARM1 in the presence of SRC-1. PRMT6 mediates oestrogen-dependent proliferation and regulates alternative splicing
physiological function
-
the methyltransferase activity of PRMT10 is essential for repressing flowering locus C expression and promoting flowering in Arabidopsis
physiological function
-
protein arginine methyltransferase 5 is essential for growth of lung cancer cells
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CARM1_HUMAN
608
0
65854
Swiss-Prot
other Location (Reliability: 3)
ANM6_HUMAN
375
0
41938
Swiss-Prot
other Location (Reliability: 3)
CARM1_MOUSE
608
0
65854
Swiss-Prot
Mitochondrion (Reliability: 1)
ANM5_CAEEL
734
0
83292
Swiss-Prot
other Location (Reliability: 2)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
construction of PRMT1 and CARM1 single and double knockouts in siRNA-treated HeLa cells, the mutations affect the expression of diverse other genes, expression analysis and phenotypes, overview
-
in vivo PRMT5 overexpression is caused by the altered expression of the PRMT5-specific microRNAs 19a, 25, 32, 92, 92b, and 96 and results in the increased global symmetric methylation of H3R8 and H4R3
-
through its interaction with the estrogen receptoralpha, peroxisome proliferator-activated receptor, progesterone receptor, and the retinoic acid receptor, PRMT2 shows a ligand-dependent increase in transcriptional activity
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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