Difference between revisions of "Ubiquitin-conjugating enzyme E2 D3"

From Cysteinome
Jump to: navigation, search
(Created page with "{| align="left" | __TOC__ |} {{#invoke:InfoboxforTarget|run|UBE2D3|[https://www.uniprot.org/uniprot/P61077 P61077]|Homo sapiens|Cys85|[http://pfam.xfam.org/family/PF00179...")
 
(Protein Function)
Line 7: Line 7:
 
===Protein Function ===
 
===Protein Function ===
 
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. <br/>
 
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. <br/>
[[File:571-function-UB.jpg|center|800px]]
+
[[File:571-function-UB.jpg|center|1000px]]
 
<div align="center">PMID: 27002218</div>
 
<div align="center">PMID: 27002218</div>
  

Revision as of 02:24, 19 August 2019

Basic Information
Short Name UBE2D3
UNP ID P61077
Organism Homo sapiens
Cys Site Cys85
Family/Domain Ubiquitin-conjugating enzyme family
Known Ligand Ligand list
Function Type Post-translational Modification, Ubiquitinase/Deubiquitinase

Summary

Protein Function

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.

571-function-UB.jpg
PMID: 27002218

Cys Function & Property

Cys85 is the active site of UBE2D3, act as a glycyl thioester intermediate.

  • Hydrophobic property:
571-hydro.png
  • SASA:
Cys85: 22.494 A^2

Protein Sequence

MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF
FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS
KVLLSICSLL CDPNPDDPLV PEIARIYKTD RDKYNRISRE WTQKYAM

Structural Information

  • Known structure with covalent ligand:
Unknown
  • Protein structure:
571.png

Related Pathway

Experimental Evidence

LC-CID-MS/MS, Tryptic Digest

Reference

  1. Liu L, Hua Y, Wang D, et al. A sesquiterpene lactone from a medicinal herb inhibits proinflammatory activity of TNF-α by inhibiting ubiquitin-conjugating enzyme UbcH5[J]. Chemistry & biology, 2014, 21(10): 1341-1350. 25200604