Information on EC 2.1.1.125 - histone-arginine N-methyltransferase

at pH 8.0 and 30°C

0.61

eIF4A1

702248

0.17

eIF4A1-S

702248

0.08

eIF4A1-Y

702248

0.17

FYSGFNSKPRGRVYATSWY

at pH 8.0 and 30°C

2.2

FYSGFNSRAKGRVYATSWY

at pH 8.0 and 30°C

3.6

FYSGFNSRARGRVYATSWY

at pH 8.0 and 30°C

FYSGFNSRGKGRVYATSWY

at pH 8.0 and 30°C

FYSGFNSRGRGRVYATSWY

at pH 8.0 and 30°C

0.15 - 7.4

FYSGFNSRPAGRVYATSWY

2 entries

0.14

FYSGFNSRPKGRVYATSWY

at pH 8.0 and 30°C

0.54

FYSGFNSRPRGAVYATSVY

at pH 8.0 and 30°C

FYSGFNSRPRGKVYATSVY

at pH 8.0 and 30°C

FYSGFNSRPRGRVYATSWY

at pH 8.0 and 30°C

GGRGGFGARGGFGGRGGFG

at pH 8.0 and 30°C

4.3

GGRGGFGGRGGFGGRGGFG

at pH 8.0 and 30°C

GGRGGFGPRGGFGGRGGFG

at pH 8.0 and 30°C

0.934

histone H4 peptide PfH4-21-arginine

Plasmodium falciparum

pH 7.5, 37°C

702131

histone H4-arginine

at 30°C and pH 8.0

0.013 - 4.5

N-acetyl-GGRGGFGGRGGFGGRGGFGG

4 entries

6.6

N-acetyl-SFRGKGGKGLGKGGAKRHRKV

isoform PRMT1, pH and temperature not specified in the publication

2.17

N-acetyl-SGmeRGKGGKGLGKGGAKRHRKV

in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C

14.3

N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK

at 30°C and pH 8.0

21.2

N-acetyl-SGRGKGGKGLGKGGAKRHRK

at 30°C and pH 8.0

0.48 - 7.3

N-acetyl-SGRGKGGKGLGKGGAKRHRKV

2 entries

9.9

N-acetyl-SGRGRGGKGLGKGGAKRHRKV

isoform PRMT1, pH and temperature not specified in the publication

26.7

N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK

at 30°C and pH 8.0

270

nuclear poly(A)-binding protein 1-arginine

at pH 8.0 and 30°C

2.5 - 3.5

S-adenosyl-L-methionine

2 entries

0.15

WGGYSmeRGGYGGW

in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C

0.061

WGGYSRGGYGGW

in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C

additional information

Michaelis-Menten kinetics, kcat/Km for S-adenosyl-L-methionine is almost 2000fold higher for PRMT1 than for PRMT2, and the kcat/Km for histone H4 is nearly 600fold higher

702134

0.15

FYSGFNSRPAGRVYATSWY

at pH 8.0 and 30°C

7.4

FYSGFNSRPAGRVYATSWY

at pH 8.0 and 30°C

0.013

N-acetyl-GGRGGFGGRGGFGGRGGFGG

mutant enzyme M48A, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C

0.46

N-acetyl-GGRGGFGGRGGFGGRGGFGG

mutant enzyme M155A, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C

1.7

N-acetyl-GGRGGFGGRGGFGGRGGFGG

mutant enzyme M48L, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C

4.5

N-acetyl-GGRGGFGGRGGFGGRGGFGG

wild type enzyme, in 50 mM sodium phosphate buffer, pH 7.5, at 23°C

0.48

N-acetyl-SGRGKGGKGLGKGGAKRHRKV

in 50 mM HEPES (pH 8.0), 50 mM NaCl, 1 mM EDTA, and 0.5 mM dithiothreitol, at 37°C

7.3

N-acetyl-SGRGKGGKGLGKGGAKRHRKV

isoform PRMT1, pH and temperature not specified in the publication

2.5

S-adenosyl-L-methionine

using N-acetyl-SGRGKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK as cosubstrate, at 30°C and pH 8.0

3.5

S-adenosyl-L-methionine

using N-acetyl-SGRme1GKGGKG-2,3-diaminopropionic acid-(fluoresceinyl)GKGGAKRHRK as cosubstrate, at 30°C and pH 8.0

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

7 entries

physiological function

23 entries

malfunction

causal role of the elevated symmetric methylation of H3R8 and H4R3 at the RBL2 promoter in transformed B-lymphocyte pathology

688977

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

719469

malfunction

isoform PRMT7 knockdown causes a significant decrease in enzyme recruitment and hsitone H2A-arginine 3/histone H4-arginine 3 methylation

720039

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

720581

malfunction

mutations of protein arginine methyltransferase 10 result in a late-flowering phenotype

720960

malfunction

PRMT5 deficiency is associated with late flowering. Mutation of PRMT5 leads to widespread splicing defects

720902

malfunction

silencing PRMT5 expression strongly inhibits proliferation of lung adenocarcinoma cells

718797

physiological function

Mus musculus

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

704652

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

704604

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

703144

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

704794

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

704703

physiological function

Caenorhabditis elegans

PRMT-5 negatively regulates DNA damage-induced apoptosis

706414

physiological function

PRMT1 acts as a transcriptional co-activator

702134

physiological function

Xenopus laevis

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

705701

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

706095

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

704639

physiological function

PRMT2 acts as a transcriptional co-activator

702134

physiological function

PRMT5 and DNMT3A function cooperatively in gene silencing, DNMT3A binds specifically to histone H4R3me2s, overview

705870

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

706494

physiological function

Mus musculus

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

705690

physiological function

proper epigenetic modification of chromatin by protein arginine methyltransferases, PRMTs, is crucial for normal cell growth and health

688977

physiological function

protein arginine methylation by PRMT5 plays a role in ZNF224-mediated transcriptional repression, overview

704575

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

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

719469

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

720039

physiological function

methylation of Kaposi sarcoma-associated herpesvirus latency-associated nuclear antigen by PRMT1 antagonizes viral reactivation

720047

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

720581

physiological function

protein arginine methyltransferase 5 is essential for growth of lung cancer cells

718797

physiological function