Source:http://linkedlifedata.com/resource/pubmed/id/11724789
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
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| pubmed:dateCreated |
2002-1-28
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| pubmed:abstractText |
Protein arginine methylation is a prevalent posttranslational modification in eukaryotic cells that has been implicated in signal transduction, the metabolism of nascent pre-RNA, and the transcriptional activation processes. In searching the human genome for protein arginine N-methyltransferase (PRMT) family members, a novel gene has been found on chromosome 1 that encodes for an apparent methyltransferase, PRMT6. The polypeptide chain of PRMT6 is 41.9 kDa consisting of a catalytic core sequence common to other PRMT enzymes. Expressed as a glutathione S-transferase fusion protein, PRMT6 demonstrates type I PRMT activity, capable of forming both omega-N(G)-monomethylarginine and asymmetric omega-N(G),N(G)-dimethylarginine derivatives on the recombinant glycine- and arginine-rich substrate in a processive manner with a specific activity of 144 pmol methyl groups transferred min(-1) mg(-1) enzyme. A comparison of substrate specificity reveals that PRMT6 is functionally distinct from two previously characterized type I enzymes, PRMT1 and PRMT4. In addition, PRMT6 displays automethylation activity; it is the first PRMT to do so. This novel human PRMT, which resides solely in the nucleus when fused to the green fluorescent protein, joins a family of enzymes with diverse functions within cells.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Arginine...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
277
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3537-43
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:11724789-Amino Acid Sequence,
pubmed-meshheading:11724789-Blotting, Northern,
pubmed-meshheading:11724789-Catalytic Domain,
pubmed-meshheading:11724789-Cell Nucleus,
pubmed-meshheading:11724789-Chromosome Mapping,
pubmed-meshheading:11724789-Chromosomes, Human, Pair 1,
pubmed-meshheading:11724789-Genome, Human,
pubmed-meshheading:11724789-Glutathione Transferase,
pubmed-meshheading:11724789-Humans,
pubmed-meshheading:11724789-Isoenzymes,
pubmed-meshheading:11724789-Kinetics,
pubmed-meshheading:11724789-Molecular Sequence Data,
pubmed-meshheading:11724789-Nuclear Proteins,
pubmed-meshheading:11724789-Organ Specificity,
pubmed-meshheading:11724789-Protein Processing, Post-Translational,
pubmed-meshheading:11724789-Protein-Arginine N-Methyltransferases,
pubmed-meshheading:11724789-Recombinant Fusion Proteins,
pubmed-meshheading:11724789-Sequence Alignment,
pubmed-meshheading:11724789-Sequence Homology, Amino Acid,
pubmed-meshheading:11724789-Substrate Specificity,
pubmed-meshheading:11724789-Transcriptional Activation
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| pubmed:year |
2002
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| pubmed:articleTitle |
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity.
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| pubmed:affiliation |
University of Texas M. D. Anderson Cancer Center, Science Park Research Division, Smithville, Texas 78957, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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