PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain. (Q40863473)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10931850%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

title

PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain (English)

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9 November 2019

1

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9 November 2019

author name string

S Clarke

series ordinal

2

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9 November 2019

language of work or name

English

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publication date

1 October 2000

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Journal of Biological Chemistry

9 November 2019

number of pages

9

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based on heuristic

inferred from page(s)

published in

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9 November 2019

volume

275

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9 November 2019

issue

42

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9 November 2019

page(s)

32974-32982

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Identification of N(G)-methylarginine residues in human heterogeneous RNP protein A1: Phe/Gly-Gly-Gly-Arg-Gly-Gly-Gly/Phe is a preferred recognition motif

9 November 2019

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Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23.

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Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62

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Arginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domains

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Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3

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Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3

21 January 2018

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A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export

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The essential yeast RNA binding protein Np13p is methylated

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RNase treatment of yeast and mammalian cell extracts affects in vitro substrate methylation by type I protein arginine N-methyltransferases.

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The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase

21 January 2018

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

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The predominant protein-arginine methyltransferase from Saccharomyces cerevisiae

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A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins

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PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells

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Regulation of transcription by a protein methyltransferase

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Specific Enzymic Methylation of an Arginine in the Experimental Allergic Encephalomyelitis Protein from Human Myelin

21 January 2018

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Predicted folding of beta-structure in myelin basic protein.

21 January 2018

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The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies

21 January 2018

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The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity

21 January 2018

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Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase

21 January 2018

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In vivo and in vitro arginine methylation of RNA-binding proteins

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A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor

21 January 2018

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Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene

21 January 2018

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Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)

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A human protein selected for interference with Ras function interacts directly with Ras and competes with Raf1

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

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Zinc fingers are sticking together

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