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%2F00023736%3A_____%2F11%3A00008920" target="_blank" >RIV/00023736:_____/11:00008920 - isvavai.cz</a>
Result on the web
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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
Protein arginine methyltransferase 3 (PRMT3) is a cytosolic enzyme that catalyzes the formation of mono- and asymmetric dimethyl arginines, with ribosomal protein (RP) S2 as its main in vivo substrate. Defects in ribosome maturation are the hallmark of Diamond-Blackfan anemia (DBA). Sequencing of the PRMT3 gene in patients from the Czech DBA registry revealed a heterozygous mutation encoding the Tyr87Cys substitution. Although later analysis excluded this mutation as the cause of DBA in the patient, weanticipated that this substitution might be important for PRMT3 function. Indeed, biochemical analyses showed the importance of Tyr87 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
FD - Oncology and haematology
OECD FORD branch
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Project
<a href="/en/project/LC06044" target="_blank" >LC06044: Center for Experimental Hematology</a><br>
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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