About: Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)     Goto   Sponge   NotDistinct   Permalink

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  • 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, we anticipated 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
  • 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, we anticipated 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 (en)
Title
  • Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)
  • Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3) (en)
skos:prefLabel
  • Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)
  • Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3) (en)
skos:notation
  • RIV/00023736:_____/11:00008920!RIV11-MZ0-00023736
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(LC06044), Z(MZ0UHKT2005)
http://linked.open...iv/cisloPeriodika
  • 2
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 236424
http://linked.open...ai/riv/idVysledku
  • RIV/00023736:_____/11:00008920
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • PRMT3; RPS2; methylation; Diamond-Blackfan anemia; DBA (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [CF8D07982F93]
http://linked.open...i/riv/nazevZdroje
  • Biochimica et Biophysica Acta, Complete Edition
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 1814
http://linked.open...iv/tvurceVysledku
  • Halada, P.
  • Petrák, Jiří
  • Pospíšilová, D.
  • Handrková, Helena
  • Čmejla, Radek
http://linked.open...ain/vavai/riv/wos
  • 000287067700002
http://linked.open...n/vavai/riv/zamer
issn
  • 0006-3002
number of pages
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