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

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PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M312904200
P698PubMed publication ID15044439
P5875ResearchGate publication ID8657292

P50authorAdam FrankelQ43280576
P2093author name stringSteven Clarke
Tina Branscombe Miranda
Mark Miranda
P2860cites workProtein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3Q22253444
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificityQ24291936
Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alphaQ24298570
PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulationQ24310138
The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferaseQ24320461
Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequencesQ24336098
Negative regulation of transcription by the type II arginine methyltransferase PRMT5Q24522638
Gapped BLAST and PSI-BLAST: a new generation of protein database search programsQ24545170
The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteinsQ24548244
Crystal structure of the conserved core of protein arginine methyltransferase PRMT3Q24631369
A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1Q24652837
Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate PeptidesQ27641186
The predominant protein-arginine methyltransferase from Saccharomyces cerevisiaeQ27931102
Automated identification of putative methyltransferases from genomic open reading framesQ27940326
S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferaseQ27940350
Regulation of transcription by a protein methyltransferaseQ28138085
Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domainsQ28140712
Arginine methylation of STAT1 regulates its dephosphorylation by T cell protein tyrosine phosphataseQ28217313
Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient miceQ28586486
Biological significance of endogenous methylarginines that inhibit nitric oxide synthasesQ33847583
Analysis of the yeast arginine methyltransferase Hmt1p/Rmt1p and its in vivo function. Cofactor binding and substrate interactions.Q33888183
Endogenous methylarginines regulate neuronal nitric-oxide synthase and prevent excitotoxic injuryQ44045935
RNA and protein interactions modulated by protein arginine methylation.Q46021819
PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in ProteinsQ56227906
P433issue22
P407language of work or nameEnglishQ1860
P921main subjectregulation of protein bindingQ14762271
Protein arginine methyltransferase 7Q21131695
P304page(s)22902-22907
P577publication date2004-03-24
P1433published inJournal of Biological ChemistryQ867727
P1476titlePRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
P478volume279

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