| dbo:abstract
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- Fosforylace proteinů je posttranslační modifikace proteinů, ve kterých je aminokyselinový zbytek fosforylován pomocí protein kinázy přidáním kovalentně navázané fosfátové skupiny. Fosforylace mění strukturní konformaci proteinu, což způsobuje jeho aktivaci, deaktivaci nebo změnu jeho funkce. Reverzní reakce fosforylace se nazývá defosforylace a je katalyzována proteinem fosfatázou. Protein kinázy a fosfatázy fungují nezávisle a v rovnováze pro regulaci funkcí proteinů. Nejčastěji fosforylované aminokyseliny jsou serin, threonin a tyrosin u eukaryot a histidin u prokaryot a rostlin, kde hrají důležitou a dobře popsanou roli v signalizačních dráhách a metabolismu. Nicméně, mnoho jiných aminokyselin může být v buňkách také fosforylovaných, včetně argininu, lysinu, kyseliny asparagové, kyseliny glutamové a cysteinu. (cs)
- Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become either activated or deactivated, or otherwise modifying its function. Approximately 13000 human proteins have sites that are phosphorylated. The reverse reaction of phosphorylation is called dephosphorylation, and is catalyzed by protein phosphatases. Protein kinases and phosphatases work independently and in a balance to regulate the function of proteins. The amino acids most commonly phosphorylated are serine, threonine, tyrosine in eukaryotes, and also histidine in prokaryotes and plants (though it is now known to be common in humans). These phosphorylations play important and well-characterized roles in signaling pathways and metabolism. However, other amino acids can also be phosphorylated post-translationally, including arginine, lysine, aspartic acid, glutamic acid and cysteine, and these phosphorylated amino acids have recently been identified to be present in human cell extracts and fixed human cells using a combination of antibody-based analysis (for pHis) and mass spectrometry (for all other amino acids). Protein phosphorylation was first reported in 1906 by Phoebus Levene at the Rockefeller Institute for Medical Research with the discovery of phosphorylated vitellin. However, it was nearly 50 years until the enzymatic phosphorylation of proteins by protein kinases was discovered. (en)
- 단백질 인산화(蛋白質 燐酸化, 영어: protein phosphorylation)는 아미노산 잔기가 공유 결합된 인산기의 추가로 단백질 키네이스에 의해 인산화되는 단백질의 가역적인 번역 후 변형 과정이다. 인산화는 단백질의 입체 구조를 변화시켜 단백질을 활성화시키거나 비활성화시키며, 또는 단백질의 기능을 변형시킨다. 사람 단백질들 중 약 13,000가지의 단백질에는 인산화되는 부위를 가지고 있다. (ko)
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| rdfs:comment
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- 단백질 인산화(蛋白質 燐酸化, 영어: protein phosphorylation)는 아미노산 잔기가 공유 결합된 인산기의 추가로 단백질 키네이스에 의해 인산화되는 단백질의 가역적인 번역 후 변형 과정이다. 인산화는 단백질의 입체 구조를 변화시켜 단백질을 활성화시키거나 비활성화시키며, 또는 단백질의 기능을 변형시킨다. 사람 단백질들 중 약 13,000가지의 단백질에는 인산화되는 부위를 가지고 있다. (ko)
- Fosforylace proteinů je posttranslační modifikace proteinů, ve kterých je aminokyselinový zbytek fosforylován pomocí protein kinázy přidáním kovalentně navázané fosfátové skupiny. Fosforylace mění strukturní konformaci proteinu, což způsobuje jeho aktivaci, deaktivaci nebo změnu jeho funkce. Reverzní reakce fosforylace se nazývá defosforylace a je katalyzována proteinem fosfatázou. Protein kinázy a fosfatázy fungují nezávisle a v rovnováze pro regulaci funkcí proteinů. Nejčastěji fosforylované aminokyseliny jsou serin, threonin a tyrosin u eukaryot a histidin u prokaryot a rostlin, kde hrají důležitou a dobře popsanou roli v signalizačních dráhách a metabolismu. Nicméně, mnoho jiných aminokyselin může být v buňkách také fosforylovaných, včetně argininu, lysinu, kyseliny asparagové, kyseli (cs)
- Protein phosphorylation is a reversible post-translational modification of proteins in which an amino acid residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Phosphorylation alters the structural conformation of a protein, causing it to become either activated or deactivated, or otherwise modifying its function. Approximately 13000 human proteins have sites that are phosphorylated. (en)
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