Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F11%3A8913" target="_blank" >RIV/00216208:11110/11:8913 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/11:00371328 RIV/61989592:15110/11:10225409
Result on the web
<a href="http://dx.doi.org/10.1016/j.bbapap.2010.10.011" target="_blank" >http://dx.doi.org/10.1016/j.bbapap.2010.10.011</a>
DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)
Original language description
Sequencing of the PRMT3 gene in patients from the Czech DBA registry revealed a heterozygous mutation encoding the Tyr87Cys substitution. To address the impact of the mutation and putative Tyr87 phosphorylation on PRMT3 properties, we constructed two additional PRMT3 variants, Tyr87Phe and Tyr87Glu PRMT3, mimicking non-phosphorylated and phosphorylated Tyr87, respectively and studied their activity. In conclusion, Tyr87 is important for the interaction between PRMT3 and RPS2 and for its full enzymatic activity
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EB - Genetics and molecular biology
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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