Search Results

Overview

Uniprot IDQ9NT62
Protein NameUbiquitin-like-conjugating enzyme ATG3
Gene NameATG3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
11 VINTVKGKALEVAEY
183 RKIVEACKAKTDAGG
185 IVEACKAKTDAGGED

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:24191030, PubMed:33446636, PubMed:37252361). 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 (PubMed:11825910, PubMed:12207896, PubMed:12890687, PubMed:16704426, PubMed:24186333). Also plays 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 (By similarity). Interacts with negatively-charged membranes promoting membrane tethering and enhancing LC3/GABARAP lipidation (PubMed:29142222). 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 (By similarity). ATG12-ATG3 conjugation promotes late endosome to lysosome trafficking and basal autophagosome maturation via its interaction with PDCD6IP (By similarity). 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 (By similarity). Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (By similarity)

Protein Sequence

10 MQNVINTVKG 20 KALEVAEYLT 30 PVLKESKFKE 40 TGVITPEEFV 50 AAGDHLVHHC 60 PTWQWATGEE 70 LKVKAYLPTG 80 KQFLVTKNVP 90 CYKRCKQMEY 100 SDELEAIIEE 110 DDGDGGWVDT 120 YHNTGITGIT 130 EAVKEITLEN 140 KDNIRLQDCS 150 ALCEEEEDED 160 EGEAADMEEY 170 EESGLLETDE 180 ATLDTRKIVE 190 ACKAKTDAGG 200 EDAILQTRTY 210 DLYITYDKYY 220 QTPRLWLFGY 230 DEQRQPLTVE 240 HMYEDISQDH 250 VKKTVTIENH 260 PHLPPPPMCS 270 VHPCRHAEVM 280 KKIIETVAEG 290 GGELGVHMYL 300 LIFLKFVQAV 310 IPTIEYDYTR HFTM

Gene Ontology

Classification GO ID Description
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0019787 ubiquitin-like protein transferase activity
Cellular Component GO:0034274 Atg12-Atg5-Atg16 complex
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0000407 phagophore assembly site
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0019777 Atg12 transferase activity
Molecular Function GO:0141046 Atg8-family conjugating enzyme activity
Molecular Function GO:0019776 Atg8-family ligase activity
Biological Process GO:0000045 autophagosome assembly
Biological Process GO:0000422 autophagy of mitochondrion
Biological Process GO:0061723 glycophagy
Biological Process GO:0043653 mitochondrial fragmentation involved in apoptotic process
Biological Process GO:0044804 nucleophagy
Biological Process GO:0006612 protein targeting to membrane
Biological Process GO:0015031 protein transport
Biological Process GO:0016567 protein ubiquitination
Biological Process GO:1902017 regulation of cilium assembly

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.