ATG3
entrez
64422
canonical
uniprot
Q9NT62
canonical
ensembl
ENSG00000144848
resolver
ensp
ENSP00000283290
resolver
ensp
ENSP00000385943
resolver
genesymbol
ATG3
resolver
genesymbol_syn
APG3
resolver
genesymbol_syn
APG3L
resolver
hgnc
HGNC:20962
resolver
uniprot
C9JNW8
resolver
uniprot
Q6PKC5
resolver
uniprot
Q9H6L9
resolver
uniprot_entry
ATG3_HUMAN
resolver
uniprot_sec
C9JNW8
resolver
uniprot_sec
Q6PKC5
resolver
uniprot_sec
Q9H6L9
resolver
amino_acid_sequence
MQNVINTVKGKALEVAEYLTPVLKESKFKETGVITPEEFVAAGDHLVHHCPTWQWATGEELKVKAYLPTGKQFLVTKNVPCYKRCKQMEYSDELEAIIEEDDGDGGWVDTYHNTGITGITEAVKEITLENKDNIRLQDCSALCEEEEDEDEGEAADMEEYEESGLLETDEATLDTRKIVEACKAKTDAGGEDAILQTRTYDLYITYDKYYQTPRLWLFGYDEQRQPLTVEHMYEDISQDHVKKTVTIENHPHLPPPPMCSVHPCRHAEVMKKIIETVAEGGGELGVHMYLLIFLKFVQAVIPTIEYDYTRHFTM
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:Q9CPX6, ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:12890687, ECO:0000269|PubMed:16704426, ECO:0000269|PubMed:24186333, ECO:0000269|PubMed:24191030, ECO:0000269|PubMed:29142222, ECO:0000269|PubMed:33446636, ECO:0000269|PubMed:37252361}.
uniprot
proteins
mass_dalton
35864
uniprot
proteins
mutagenesis
MUTAGEN 8; /note="V->D: Significantly reduces ATG8-family conjugating enzyme activity; when associated with K-15. Decreases protein membrane interactions; when associated with K-15. Does not affect formation of the covalent thioester intermediate with MAP1LC3B; when associated with K-15."; /evidence="ECO:0000269|PubMed:33446636"; MUTAGEN 9; /note="K->D: Slightly decreases interaction with lipid monolayers; when associated with D-11. Slightly decreases insertion into lipid monolayers; when associated with D-11. Decreases affinity for monolayers containing cardiolipin (CL); when associated with D-11. Cancels selectivity for anionic phospholipids; when associated with D-11. Impairs binding to lipid bilayers; when associated with D-11. Impairs insertion into lipid bilayers; when associated with D-11. Does not induce vesicle tethering; when associated with D-11."; /evidence="ECO:0000269|PubMed:29142222"; MUTAGEN 11; /note="K->D: Slightly decreases interaction with lipid monolayers; when associated with D-9. Slightly decreases insertion into lipid monolayers; when associated with D-9. Decreases affinity for monolayers containing cardiolipin (CL); when associated with D-9. Cancels selectivity for anionic phospholipids; when associated with D-11. Impairs binding to lipid bilayers; when associated with D-11. Impairs insertion into lipid bilayers; when associated with D-11. Does not induce vesicle tethering; when associated with D-11."; /evidence="ECO:0000269|PubMed:29142222"; MUTAGEN 15; /note="V->K: Significantly reduces ATG8-family conjugating enzyme activity; when associated with D-8. Decreases protein membrane interactions; when associated with D-8. Does not affect formation of the covalent thioester intermediate with MAP1LC3B; when associated with D-8."; /evidence="ECO:0000269|PubMed:33446636"; MUTAGEN 21; /note="P->A: Impairs ATG8-family conjugating enzyme activity. Does not affect protein membrane interactions. Does not affect formation of the covalent thioester intermediate with MAP1LC3B. Partially rescues MAP1LC3B lipidation in cell lacking ATG3."; /evidence="ECO:0000269|PubMed:33446636"; MUTAGEN 23; /note="L->T: Severely reduces ATG8-family conjugating enzyme activity. Reduces of about 40% protein membrane interactions. Does not affect formation of the covalent thioester intermediate with MAP1LC3B. Completely fails to induce membrane-bound MAP1LC3B (MAP1LC3B-II) and autophagic flux when expressed in cell lacking ATG3."; /evidence="ECO:0000269|PubMed:33446636"; MUTAGEN 25; /note="E->K: Increases of about 30% more ATG8-family conjugating enzyme activity. Does not affect protein membrane interactions. Does not affect formation of the covalent thioester intermediate with MAP1LC3B."; /evidence="ECO:0000269|PubMed:33446636"; MUTAGEN 95; /note="E->A: Severely diminish GABARAP:ATG3 conjugation."; /evidence="ECO:0000269|PubMed:37252361"; MUTAGEN 97; /note="I->A: Severely diminish GABARAP:ATG3 conjugation."; /evidence="ECO:0000269|PubMed:37252361"; MUTAGEN 107; /note="W->A: Almost completely abrogates GABARAP:ATG3 conjugation."; /evidence="ECO:0000269|PubMed:37252361"; MUTAGEN 108; /note="V->A: Significantly reduces GABARAP:ATG3 conjugation."; /evidence="ECO:0000269|PubMed:37252361"; MUTAGEN 144..151; /note="EEEEDEDE->AAAAAAAA: Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. Severely decreases phosphatidylethanolamine (PE)-conjugated ATG8-like proteins formation."; /evidence="ECO:0000269|PubMed:24191030"; MUTAGEN 156; /note="D->A: Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. Impairs interaction with the complex ATG12:ATG5:ATG16L1; when associated with A-157. Impairs phosphatidylethanolamine (PE)-conjugated ATG8-like protein formation. Loss of phosphatidylethanolamine (PE)-conjugated ATG8-like proteins formation; when associated with A-157. Impairs interaction with ATG12:ATG5; when associated with A-157. Does not affect interaction with ATG7; when associated with A-157. Does not affect the formation of the ATG8-like protein:ATG3 intermediate complex; when associated with A-157. Affects modestly the ATG3-ATG7 interaction; when associated with A-157. Reduces the thioester-linkage formation with GABARAP; when associated with A-157."; /evidence="ECO:0000269|PubMed:24191030, ECO:0000269|PubMed:26043688"; MUTAGEN 157; /note="M->A: Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. Impairs interaction with the complex ATG12:ATG5:ATG16L1; when associated with A-156. Impairs phosphatidylethanolamine (PE)-conjugated ATG8-like proteins formation. Loss of phosphatidylethanolamine (PE)-conjugated ATG8-like proteins formation; when associated with A-156. Impairs interaction with ATG12:ATG5; when associated with A-156. Does not affect interaction with ATG7; when associated with A-156. Does not affect the formation of the ATG8-like protein:ATG3 intermediate complex; when associated with A-156. Affects modestly the ATG3-ATG7 interaction; when associated with A-156. Reduces the thioester-linkage formation with GABARAP; when associated with A-156."; /evidence="ECO:0000269|PubMed:24191030, ECO:0000269|PubMed:26043688"; MUTAGEN 160; /note="Y->A: Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1. Affects modestly the ATG3-ATG7 interaction. Reduces the thioester-linkage formation with GABARAP."; /evidence="ECO:0000269|PubMed:24191030, ECO:0000269|PubMed:26043688"; MUTAGEN 161; /note="E->A: Strongly decreases affinity for the complex ATG12:ATG5:ATG16L1."; /evidence="ECO:0000269|PubMed:24191030"; MUTAGEN 167; /note="E->A: Weakens the ATG3-ATG7 interaction. Reduces the thioester-linkage formation with GABARAP."; /evidence="ECO:0000269|PubMed:26043688"; MUTAGEN 169; /note="D->A: Weakens the ATG3-ATG7 interaction. Severely reduces the thioester-linkage formation with GABARAP."; /evidence="ECO:0000269|PubMed:26043688"; MUTAGEN 171; /note="A->A: Weakens the ATG3-ATG7 interaction. Reduces the thioester-linkage formation with GABARAP."; /evidence="ECO:0000269|PubMed:26043688"; MUTAGEN 172; /note="T->A: Weakens the ATG3-ATG7 interaction. Significantly reduces the thioester-linkage formation with GABARAP."; /evidence="ECO:0000269|PubMed:26043688"; MUTAGEN 173; /note="L->A: Weakens the ATG3-ATG7 interaction. Significantly reduces the thioester-linkage formation with GABARAP."; /evidence="ECO:0000269|PubMed:26043688"; MUTAGEN 264; /note="C->A: Does not affect interaction with ATG12:ATG5. Impairs MAP1LC3A lipidation. Impairs MAP1LC3B lipidation. Impairs ATG3:ATG8-like proteins thioester complex formation."; /evidence="ECO:0000269|PubMed:24191030, ECO:0000269|PubMed:37252361"; MUTAGEN 264; /note="C->S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and GABARAPL1/APG8L (substrate), a stable complex with an O-ester bond is formed."; /evidence="ECO:0000269|PubMed:11825910
uniprot
proteins
post_translational_modification
PTM: Cleaved by CASP8 upon death ligand binding such as tumor necrosis factor-alpha (PubMed:22644571). CASP8 cleavage blocks survival-related autophagy and favors apoptosis (PubMed:22644571). {ECO:0000269|PubMed:22644571}.; PTM: Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a role in regulation of mitochondrial homeostasis and cell death, while it is not involved in phosphatidylethanolamine-conjugation to ATG8-like proteins and autophagy. {ECO:0000250|UniProtKB:Q9CPX6}.
uniprot
proteins
protein_family
ATG3 family
uniprot
proteins
pubmed
11825910
uniprot
proteins
pubmed
12207896
uniprot
proteins
pubmed
12890687
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16704426
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19342671
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22170151
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22644571
uniprot
proteins
pubmed
24186333
uniprot
proteins
pubmed
24191030
uniprot
proteins
pubmed
26043688
uniprot
proteins
pubmed
29142222
uniprot
proteins
pubmed
33446636
uniprot
proteins
pubmed
37252361
uniprot
proteins
sequence_length
314
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11825910}.
uniprot
proteins