PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation - Wikidata - awgldk - TriplyDB

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

http://www.wikidata.org/entity/Q24303480

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Friend of Prmt1, a novel chromatin target of protein arginine methyltransferases Promiscuous modification of the nuclear poly(A)-binding protein by multiple protein-arginine methyltransferases does not affect the aggregation behavior TDRD3 is an effector molecule for arginine-methylated histone marks H3R42me2a is a histone modification with positive transcriptional effects Dysregulation of protein methyltransferases in human cancer: An emerging target class for anticancer therapy Arginine methyltransferases as novel therapeutic targets for breast cancer On WD40 proteins: propelling our knowledge of transcriptional control?A role for Set1/MLL-related components in epigenetic regulation of the Caenorhabditis elegans germ line The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance Crystal Structure of Arginine Methyltransferase 6 from Trypanosoma brucei Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro.Roles of protein arginine methyltransferases in the control of glucose metabolism Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1 PRMT4 is a novel coactivator of c-Myb-dependent transcription in haematopoietic cell lines beta-Catenin primes organizer gene expression by recruiting a histone H3 arginine 8 methyltransferase, Prmt2 Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor Protein arginine methylation in mammals: who, what, and why Readers of histone methylarginine marks.Quantitative proteomic analysis of histone modifications Thrombospondin-1 is a transcriptional repression target of PRMT6.Histone arginine methylation keeps RUNX1 target genes in an intermediate state.Histone arginine methylations: their roles in chromatin dynamics and transcriptional regulation.Epigenetics: an emerging player in gastric cancer Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition.Protein arginine methyltransferase 6 regulates multiple aspects of gene expression.Quantitative mass spectrometry of histones H3.2 and H3.3 in Suz12-deficient mouse embryonic stem cells reveals distinct, dynamic post-translational modifications at Lys-27 and Lys-36 TbPRMT6 is a type I protein arginine methyltransferase that contributes to cytokinesis in Trypanosoma brucei A gain-of-function mouse model identifies PRMT6 as a NF-κB coactivator.Characterization of the PRMT gene family in rice reveals conservation of arginine methylation.Trithorax group proteins: switching genes on and keeping them active.Cell cycle regulation by the PRMT6 arginine methyltransferase through repression of cyclin-dependent kinase inhibitors.Recruitment of Rpd3 to the telomere depends on the protein arginine methyltransferase Hmt1.Identification and characterization of new molecular partners for the protein arginine methyltransferase 6 (PRMT6).Dynamic protein methylation in chromatin biology.Distinct transcriptional outputs associated with mono- and dimethylated histone H3 arginine 2.Protein arginine methylation in parasitic protozoa.Status of epigenetic chromatin modification enzymes and esophageal squamous cell carcinoma risk in northeast Indian population.Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.The Arginine Methyltransferase PRMT6 Cooperates with Polycomb Proteins in Regulating HOXA Gene Expression.

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PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

http://www.wikidata.org/entity/Q24303480

description

2007 nî lūn-bûn

@nan

2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

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PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

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PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

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PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

@nl

type

label

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

@ast

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

@en

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

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PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

@nl

prefLabel

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

@ast

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

@en

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

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PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

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Genes & Development

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PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

@en

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Claudia Stein

http://www.w3.org/2001/XMLSchema#string

Dawin Hyllus

http://www.w3.org/2001/XMLSchema#string

Emile Schiltz

http://www.w3.org/2001/XMLSchema#string

James Hsieh

http://www.w3.org/2001/XMLSchema#string

Kristin Schnabel

http://www.w3.org/2001/XMLSchema#string

Uta-Maria Bauer

http://www.w3.org/2001/XMLSchema#string

Yali Dou

http://www.w3.org/2001/XMLSchema#string

P2860

Translating the Histone Code

The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity

Structure and catalytic mechanism of the human histone methyltransferase SET7/9

Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1

FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues

Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF

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

Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus

Arginine methylation regulates DNA polymerase beta

PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity

P304

3369-80

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scholarly article

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4771937

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10.1101/GAD.447007

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24

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21

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2007-12-15T00:00:00Z

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5769776

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18079182

http://www.w3.org/2001/XMLSchema#string

P921

histone methyltransferase activity (H2A-R3 specific)

Protein arginine methyltransferase 6

P932

2113036

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