Ubiquitin conjugating enzyme: Difference between revisions

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<StructureSection load='1z2u' size='350' side='right' caption='Structure of ubiquitin conjugating enzyme 2 comlex with butanediol and Cl- (green), Na+ (purple) ions (PDB entry [[1z2u]])' scene=''>
<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 />


== 3D Structures of ubiquitin conjugating enzyme ==
*'''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 />


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
==Disease==


[[2aak]] – AtUbc – ''Arabidopsis thaliana''  <BR />
UBC13 is required for metastatic spread and lung colonizationin breast cancer<ref>PMID:25189770</ref>.<br />
[[2e2c]] – Ubc – ''Spisula solidissima''  <BR />
[[1q34]] – CeUbc – ''Caenorhabidis elegans''  <BR />
[[2qcq]], [[1fzy]] – yUbc – yeast  <BR />
[[1jas]] – hUbc – human  <BR />
[[2fo3]] – Ubc – ''Plasmodium vivax''  <BR />
[[2h2y]] – PfUbc – ''Plasmodium falciparum''  <BR />
[[1fxt]] – yUbc + ubiquitin  <BR />


'''Ubc1'''
== 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>


[[1tte]] – yUbc  (mutant) <BR />
==References==
[[2aak]] – AtUbc <BR />
<references />
[[1z3d]] – CeUbc  <BR />
 
'''Ubc2'''
 
[[1ayz]] – yUbc  <BR />
[[1z2u]] – CeUbc  <BR />
 
'''Ubc4'''
 
[[1qcq]] – yUbc  <BR />
[[4ii2]] – Ubc  (mutant) + E1 + ATP – fission yeast<BR />
 
'''Ubc5'''
 
[[2esk]], [[2c4o]], [[2clw]], [[3l1y]], [[3tgd]], [[2c4p]], [[1x23]] – hUbc  <BR />
[[2eso]], [[2esp]], [[2esq]] – hUbc (mutant)<BR />
[[1w4u]] – hUbc - NMR<BR />
 
''Ubc5 complexes''
 
[[1ur6]] – hUbc + Cnot4 - NMR<BR />
[[3eb6]] – Ubc + baculoviral IAP repeat-containing protein- frog<BR />
[[4auq]] – hUbc (mutant) + baculoviral IAP repeat-containing protein + ubiquitin<BR />
[[3ptf]], [[4ddg]], [[4ddi]] – hUbc + ubiquitin<BR />
[[2fuh]] – hUbc + ubiquitin - NMR<BR />
[[3a33]], [[3ugb]] – hUbc (mutant) + ubiquitin<BR />
[[3jvz]], [[3jw0]] – hUbc (mutant) + E3 NEDD4-2 + ubiquitin<BR />
[[4ap4]] – hUbc + E3 Rnf4 + ubiquitin<BR />
[[3oj4]] – hUbc + tumor necrosis factor α-induced protein 3 + ubiquitin<BR />
[[4a49]] – hUbc + E3 Cbl <BR />
[[4a4b]], [[4a4c]] – hUbc + E3 Cbl + ZAP-70 peptide<BR />
[[3l1z]] – hUbc + ubiquitin conjugating factor<BR />
[[3rpg]] – hUbc + E3 Ring2 + polycomb complex protein Bmi-1 <BR />
[[3zni]] – hUbc + ubiquitin + + E3 Cbl + ZAP-70 peptide <BR />
 
'''Ubc6'''
 
[[4jjq]] – hUbc + ubiquitin carboxyl terminal hydrolase <BR />
 
'''Ubc7'''
 
[[2ucz]] – yUbc  <BR />
[[2awf]], [[2cyx]] – hUbc  <BR />
[[1c4z]] – hUbc + E3 HECT domain <BR />
[[1fbv]] – hUbc + E3 Cbl + ZAP-70 peptide<BR />
[[4jqu]] – hUbc + U7BR  <BR />
[[3sqv]] – hUbc + secreted effector protein <BR />
[[3sy2]] – hUbc + E3 Sopa <BR />
 
'''Ubc8'''
 
[[1y6l]], [[1wzw]] – hUbc  <BR />
[[2kjh]] – hUbc + ubiuqitin <BR />
 
'''Ubc9'''
 
See [[SUMO conjugating enzyme Ubc9]]
 
'''Ubc10'''
 
[[1i7k]] – hUbc (mutant)  <BR />
 
'''Ubc12 (NEDD8 conjugating enzyme)'''
 
[[3o2u]] – yUbc <BR />
[[1tt5]] – hUbc + E1 Uba3, APPBP1 subunits  <BR />
[[1y8x]] – hUbc + E1 NEDD8 <BR />
[[2nvu]] – hUbc + E1 NEDD8 + NEDD8<BR />
[[3tdu]] – hUbc + cullin-1 + Dcn1-like protein <BR />
[[4gao]] – hUbc + Dcn1-like protein <BR />
[[3tdi]] – hUbc + defective in cullin neddylation protein <BR />
 
'''Ubc13'''
 
[[1jbb]] – yUbc  <BR />
[[1jat]] – yUbc/Mms2  <BR />
[[1j74]] – hMms2  <BR />
[[1j7d]] – hUbc/Mms2  <BR />
[[4fh1]] – hUbc (mutant) <BR />
 
[[2c2v]] – hUbc + CHIP + Uev1a  <BR />
[[3hct]], [[3hcu]] – hUbc + TNF receptor associated factor 6  <BR />
[[4dhi]] – CeUbc + OTUB1  <BR />
[[4dhi]], [[4dhz]] – hUbc + OTUB1 + ubiquitin + ubiquitin aldehyde <BR />
[[4epo]] – hUbc/Mms2 + E3 Rnf8 <BR />
[[3von]] – hUbc/Mms2 + OTUB1 <BR />
[[1zgu]] – hMms2 + ubiquitin - NMR <BR />
[[2gmi]] – hUbc/Mms2 (mutant) + ubiquitin <BR />
[[4ip3]], [[3w31]] – hUbc + Orf169b <BR />
[[2oxq]] – Ubc + CHIP U-box - zebrafish<BR />
 
'''Ubc B'''
 
[[2y4w]] – hUbc - NMR <BR />
 
'''Ubc D1'''
 
[[2hyo]] – hUbc + E3 Mylip <BR />
 
'''Ubc E1'''
 
[[3bzh]] – hUbc  <BR />
 
'''Ubc G2'''
 
[[3fsh]] – hUbc + autocrine motility factor receptor <BR />
[[2kly]] – hUbc - NMR<BR />
 
'''Ubc H'''
 
[[2z5d]] – hUbc  <BR />
 
'''Ubc J2'''
 
[[2f4w]] – hUbc  <BR />
 
'''Ubc Q'''
 
[[2qgx]] – hUbc  <BR />
 
'''Ubc R1'''
 
[[3rz3]] – hUbc + inhibitor <BR />
 
'''Ubc S'''
 
[[1zdn]] – hUbc  <BR />
 
'''Ubc Uev-1'''
 
[[2a4d]] – hUbc catalytic domain <BR />
[[2hlw]] – hUbc catalytic domain - NMR<BR />
[[3e95]] – PfUbc + ubiquitin carrier protein <BR />
 
'''Ubc E2-25KDa (Huntington interacting protein 2 HIP-2)'''
 
[[1yla]], [[2bep]] – hHIP-2  <BR />
[[3e46]] – hHIP-2 (mutant)  <BR />
[[2bf8]] – hHIP-2 + SUMO  <BR />
[[2o25]] – hHIP-2 + Ubc9  <BR />
[[3f92]] – hHIP-2/azorectase (mutant)  <BR />
[[3k9o]], [[3k9p]] – hHIP-2 + ubiquitin  <BR />
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, David A Taves