View source for Ubiquitin-conjugating enzyme E2 L3

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{{#invoke:InfoboxforTarget|run|UbcH7, UBE2L3, Ubiquitin-protein ligase L3|[https://www.uniprot.org/uniprot/P68036 P68036]|Homo sapiens|Cys86|[http://pfam.xfam.org/family/PF00179 Ubiquitin-conjugating enzyme family]|[[:Category:Ubiquitin-conjugating enzyme E2 L3|Ligand list]]|Ubiquitinase/Deubiquitinase,<br/>Post-translational Modification}}
==Summary==

===Protein Function ===
Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PRKN and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down-regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis. (From Uniprot)<br/>
UBE2L3 expressed in 226 organ(s), highest expression level in C1 segment of cervical spinal cord. <br/>
The reaction of UBE2L3: <br/>
<div align="center">S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.</div>
[[File:571-function-UB.jpg|center|1000px]]
<div align="center">PMID: 27002218</div>

===Cys Function & Property===
Cys87 is the active site of UBE2N, which could form a glycyl thioester intermediate during the catalysis.<br/>

* Hydrophobic property:
:[[File:525-hydro.png||600px]]
* SASA：
:Cys87: 32.715 A^2

==Protein Sequence==
<font face="Courier">
MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA <br/>
FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQV<span style="background:#ffff00">'''C'''</span>LPVI SAENWKPATK <br/>
TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK <br/>
RPVD <br/> 
</font>

==Structural Information==
*Known structures with covalent ligands: <br/>
:Unknown<br/>

*Protein structure:
[[File:525.png|center|800px]]

==Related Pathway==
*[https://www.genome.jp/kegg-bin/show_pathway?ko04120 Ubiquitin mediated proteolysis] <br/>
*[https://www.genome.jp/kegg-bin/show_pathway?ko05012 Parkinson disease] <br/>

==Experimental Evidence==
:MALDI-TOF/MS, Tryptic Digest 

==Reference==
# Strickson S, Campbell D G, Emmerich C H, et al. '''The anti-inflammatory drug BAY 11-7082 suppresses the MyD88-dependent signalling network by targeting the ubiquitin system[J].''' Biochemical Journal, 2013, 451(3): 427-437. [https://www.ncbi.nlm.nih.gov/pubmed/?term=23441730 23441730]<br/> 

[[Category:Targets|Targets]]
[[Category:Homo sapiens|Homo sapiens]]
[[Category:Ubiquitinase/Deubiquitinase|Ubiquitinase/Deubiquitinase]]
[[Category:Post-translational Modification|Post-translational Modification]]
[[Category:Ubiquitin-conjugating enzyme family|Ubiquitin-conjugating enzyme family]]
[[Category:Ubiquitin mediated proteolysis|Ubiquitin mediated proteolysis]]
[[Category:Parkinson disease|Parkinson disease]]