Ubiquitin conjugating enzyme: Difference between revisions
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<StructureSection load=' | <StructureSection load='3ptf' size='350' side='right' caption='Structure of human ubiquitin conjugating enzyme E2 (green) complex with ubiquitin (deepskyblue) (PDB entry [[3ptf]])' scene='55/551219/Cv/1'> | ||
== Function == | |||
'''Ubiquitin conjugating enzyme''' (Ubc) or '''E2 enzyme''' catalyzes the second step in the ubiquitination of a protein tagged to be degraded by the proteasome. Ubiquitin activating enzyme (E1) and ATP produce a C-terminal acyl adenylated ubiquitin molecule which binds to ubiquitin conjugating enzyme (Ubc) cysteine. The Ubc then binds to ubiquitin ligase (E3) via a conserved binding region. E3 catalyzes the transfer of ubiquitin from the Ubc-ubiquitin complex to a lysine residue of the target protein. Ubc13 makes a catalytically active heterodimer with MMS2. | '''Ubiquitin conjugating enzyme''' (Ubc) or '''E2 enzyme''' catalyzes the second step in the ubiquitination of a protein tagged to be degraded by the proteasome. Ubiquitin activating enzyme (E1) and ATP produce a C-terminal acyl adenylated ubiquitin molecule which binds to ubiquitin conjugating enzyme (E2) (Ubc) cysteine<ref>PMID:19549727</ref>. The Ubc then binds to ubiquitin ligase (E3) via a conserved binding region. E3 catalyzes the transfer of ubiquitin from the Ubc-ubiquitin complex to a lysine residue of the target protein. Ubc13 makes a catalytically active heterodimer with MMS2<ref>PMID:16980971</ref>.<br /> | ||
*'''UBC2''' is required for silencing in yeast<ref>PMID:9343433</ref>.<br /> | |||
*'''UBC4 UBC5''' mediate selective degradation of short-lived and abnormal proteins<ref>PMID:2154373</ref>.<br /> | |||
*'''UBC6 and UBC J2''' participate in ER-associated protein degradation<ref>PMID:12082160</ref>.<br /> | |||
*'''UBC7 or UBC13''' is key in the process of tagging target proteins with Lys63-linked polyubiquitin<ref>PMID:16862162</ref>.<br /> For more details on Ubc13 see [[UBC13 MMS2]].<br /> | |||
*'''UBC8''' is interferon-inducible<ref>PMID:15485925</ref>.<br /> | |||
*'''UBC9''' or [[SUMO conjugating enzyme Ubc9]] is required for sumoylation<ref>PMID:24706591</ref>.<br /> For more details on Ubc9 see [[SUMO conjugating enzyme Ubc9]].<br /> | |||
*'''UBC16''' conjugates ubiquitin to its N-terminus and to that of the small ubiquitin-like modifier SUMO<ref>PMID:23560854</ref>.<br /> | |||
*'''UBC D2,D3,Q1''' functions in the ubiquitination of the tumor suppressor p53<ref>PMID:25987028</ref>.<br /> | |||
*'''UBC G2''' functions in identification and degradation of misfolded proteins in the endoplasmic reticulum.<br /> | |||
*'''UBC H''' acts on histones and cytoskeletal proteins<ref>PMID:19922136</ref>.<br /> | |||
*'''UBC K,R1''' preferentially catalyses the formation of ubiquitin chain links to proteasome-bound proteins to Lys48<ref>PMID:26592444</ref>.<br /> | |||
*'''UBC S''' preferentially catalyses the formation of ubiquitin chain links of Lys11 to histones <ref>PMID:28525740</ref>.<br /> | |||
*'''UBC T''' acts in the Fanconi anemia pathway which is required for the efficient repair of damaged DNA<ref>PMID:16916645</ref>.<br /> | |||
*'''UBC Z''' is required for FAT10 conjugation (post-translational modification analogous to ubiquitination)<ref>PMID:26555268</ref>.<br /> | |||
*'''UBC Hip-2''' mediates amyloid-β neurotoxicity<ref>PMID:14527403</ref>.<br /> | |||
*'''UBC Uev-1''' is a variant of UBC which lacks its enzymatic activity<ref>PMID:9418904</ref>.<br /> | |||
==Disease== | |||
UBC13 is required for metastatic spread and lung colonizationin breast cancer<ref>PMID:25189770</ref>.<br /> | |||
'' | == Structural highlights == | ||
The active site of Ubc contains a cysteine residue. The <scene name='55/551219/Cv/4'>ubiquitin surface which interacts with Ubc</scene><ref>PMID:21396940</ref>. | |||
==[[3D structures of ubiquitin conjugating enzyme]]== | |||
</StructureSection> | |||
==References== | |||
<references /> | |||
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