Ubiquitin-conjugating enzyme E2 L3

Basic Information
Short Name	UbcH7, UBE2L3, Ubiquitin-protein ligase L3
UNP ID	P68036
Organism	Homo sapiens
Cys Site	Cys86
Family/Domain	Ubiquitin-conjugating enzyme family
Known Ligand	Ligand list
Function Type	Ubiquitinase/Deubiquitinase, 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)
UBE2L3 expressed in 226 organ(s), highest expression level in C1 segment of cervical spinal cord.
The reaction of UBE2L3:

S-ubiquitinyl-[E1]-L-cysteine + [E2]-L-cysteine = [E1]-L-cysteine + S-ubiquitinyl-[E2]-L-cysteine.

PMID: 27002218

Cys Function & Property

Cys87 is the active site of UBE2N, which could form a glycyl thioester intermediate during the catalysis.

• Hydrophobic property:

• SASA：

Cys87: 32.715 A^2

Protein Sequence

MAASRRLMKE LEEIRKCGMK NFRNIQVDEA NLLTWQGLIV PDNPPYDKGA
FRIEINFPAE YPFKPPKITF KTKIYHPNID EKGQVCLPVI SAENWKPATK
TDQVIQSLIA LVNDPQPEHP LRADLAEEYS KDRKKFCKNA EEFTKKYGEK
RPVD

Structural Information

• Known structures with covalent ligands:
  

Unknown

• Protein structure:

Related Pathway

• Ubiquitin mediated proteolysis
  
• Parkinson disease
  

Experimental Evidence

MALDI-TOF/MS, Tryptic Digest

Reference

1. 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. 23441730