Ubiquitin-conjugating enzyme (original) (raw)

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Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.

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dbo:abstract Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell. (en) ユビキチン結合酵素(ユビキチンけつごうこうそ、英: ubiquitin-conjugating enzyme)はE2酵素(E2 enzyme)としても知られ、タンパク質をプロテアソームを介した分解の標的とするユビキチン化反応の2番目の段階を担う。稀にubiquitin-carrier enzymeと呼ばれることもある。ユビキチン化は、標的タンパク質のリジン残基へ、76アミノ酸の小さなタンパク質ユビキチンを共有結合によって接着する過程である。タンパク質に対して1つのユビキチン分子によるタグ付けがなされると、さらなるユビキチン化によってポリユビキチン鎖が形成される。ポリユビキチン鎖はプロテアソームの19S調節粒子によって認識され、ATP依存的な標的タンパク質のアンフォールディングが引き起こされる。それによってポリペプチド鎖はプロテアソームの20Sコア粒子を通過できるようになり、そこでプロテアーゼが標的タンパク質を短いペプチド断片へ分解し、リサイクルされる。 (ja)
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dbp:interpro IPR000608 (en)
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dbp:name Ubiquitin—protein ligase (en) Ubiquitin-conjugating enzyme, E2 (en)
dbp:pfam PF00179 (en)
dbp:prosite PDOC00163 (en)
dbp:smart SM00212 (en)
dbp:symbol UBQ-conjugat_E2 (en)
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rdfs:comment Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell. (en) ユビキチン結合酵素(ユビキチンけつごうこうそ、英: ubiquitin-conjugating enzyme)はE2酵素(E2 enzyme)としても知られ、タンパク質をプロテアソームを介した分解の標的とするユビキチン化反応の2番目の段階を担う。稀にubiquitin-carrier enzymeと呼ばれることもある。ユビキチン化は、標的タンパク質のリジン残基へ、76アミノ酸の小さなタンパク質ユビキチンを共有結合によって接着する過程である。タンパク質に対して1つのユビキチン分子によるタグ付けがなされると、さらなるユビキチン化によってポリユビキチン鎖が形成される。ポリユビキチン鎖はプロテアソームの19S調節粒子によって認識され、ATP依存的な標的タンパク質のアンフォールディングが引き起こされる。それによってポリペプチド鎖はプロテアソームの20Sコア粒子を通過できるようになり、そこでプロテアーゼが標的タンパク質を短いペプチド断片へ分解し、リサイクルされる。 (ja)
rdfs:label ユビキチン結合酵素 (ja) Ubiquitin-conjugating enzyme (en)
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