\
logo
  Home | Contact us | Browse | Quick Search by UniProtKB ID, Keyword, PDBID

Menu:

Latest news:

Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

Read more...


Protein Name: Ubiquitin-like-conjugating enzyme ATG3

UniprotKB/SwissProt ID: Q9CPX6 (Q9CPX6)

Gene Name: Atg3

Organism: Mus musculus (Mouse)

Function: E2 conjugating enzyme that catalyzes the covalent conjugation of the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to the amino group of phosphatidylethanolamine (PE)-containing lipids in the membrane resulting in membrane-bound ATG8-like proteins which is one of the key steps in the development of autophagic isolation membranes during autophagosome formation (PubMed:18768753). Cycles back and forth between binding to ATG7 for loading with the ATG8-like proteins and binding to E3 enzyme, composed of ATG12, ATG5 and ATG16L1 to promote ATG8-like proteins lipidation (By similarity). Also play a role as a membrane curvature sensor that facilitates LC3/GABARAP lipidation by sensing local membrane stress associated with lipid-packing defects as occurs with high molar proportions of conical lipids or strident membrane curvature (PubMed:24747438). Interacts with negatively-charged membranes promoting membrane tethering and enhancing LC3/GABARAP lipidation (By similarity). Also acts as an autocatalytic E2-like enzyme by catalyzing the conjugation of ATG12 to itself in an ATG7-dependent manner, this complex thus formed, plays a role in mitochondrial homeostasis but not in autophagy (PubMed:20723759). ATG12-ATG3 conjugation promotes late endosome to lysosome trafficking and basal autophagosome maturation via its interaction with PDCD6IP (PubMed:25686249). ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation (PubMed:22024753). Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (PubMed:24089205)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR007135 Atg3/Atg10