ATG12_HUMAN
ID ATG12_HUMAN Reviewed; 140 AA.
AC O94817; Q6PJV2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Ubiquitin-like protein ATG12;
DE AltName: Full=Autophagy-related protein 12;
DE Short=APG12-like;
GN Name=ATG12; Synonyms=APG12, APG12L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CONJUGATION TO ATG5, AND TISSUE
RP SPECIFICITY.
RX PubMed=9852036; DOI=10.1074/jbc.273.51.33889;
RA Mizushima N., Sugita H., Yoshimori T., Ohsumi Y.;
RT "A new protein conjugation system in human. The counterpart of the yeast
RT Apg12p conjugation system essential for autophagy.";
RL J. Biol. Chem. 273:33889-33892(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH ATG7, AND CONJUGATION TO ATG5.
RX PubMed=11096062; DOI=10.1074/jbc.c000752200;
RA Tanida I., Tanida-Miyake E., Ueno T., Kominami E.;
RT "The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-
RT activating enzyme for multiple substrates including human Apg12p, GATE-16,
RT GABARAP, and MAP-LC3.";
RL J. Biol. Chem. 276:1701-1706(2001).
RN [5]
RP INTERACTION WITH ATG3, CONJUGATION TO ATG5, AND FUNCTION.
RX PubMed=12207896; DOI=10.1016/s0006-291x(02)02057-0;
RA Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.;
RT "Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3
RT processing.";
RL Biochem. Biophys. Res. Commun. 296:1164-1170(2002).
RN [6]
RP INTERACTION WITH ATG3, AND CONJUGATION TO ATG5.
RX PubMed=11825910; DOI=10.1074/jbc.m200385200;
RA Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
RT "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
RT substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation
RT of hApg12p to hApg5p.";
RL J. Biol. Chem. 277:13739-13744(2002).
RN [7]
RP CONJUGATION TO ATG5.
RX PubMed=16963840; DOI=10.4161/auto.3270;
RA Shao Y., Gao Z., Feldman T., Jiang X.;
RT "Stimulation of ATG12-ATG5 conjugation by ribonucleic acid.";
RL Autophagy 3:10-16(2007).
RN [8]
RP INDUCTION.
RX PubMed=17457038; DOI=10.4161/auto.4239;
RA Prigione A., Cortopassi G.;
RT "Mitochondrial DNA deletions and chloramphenicol treatment stimulate the
RT autophagic transcript ATG12.";
RL Autophagy 3:377-380(2007).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ATG5; IFIH1; DHX58 AND
RP MAVS.
RX PubMed=17709747; DOI=10.1073/pnas.0704014104;
RA Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A., Xin K.Q.,
RA Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
RT "The Atg5-Atg12 conjugate associates with innate antiviral immune
RT responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
RN [10]
RP DOMAIN.
RX PubMed=18704115; DOI=10.1038/embor.2008.163;
RA Geng J., Klionsky D.J.;
RT "The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy.
RT 'Protein modifications: beyond the usual suspects' review series.";
RL EMBO Rep. 9:859-864(2008).
RN [11]
RP FUNCTION.
RX PubMed=19074260; DOI=10.1073/pnas.0810611105;
RA Kim P.K., Hailey D.W., Mullen R.T., Lippincott-Schwartz J.;
RT "Ubiquitin signals autophagic degradation of cytosolic proteins and
RT peroxisomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:20567-20574(2008).
RN [12]
RP FUNCTION.
RX PubMed=17999726; DOI=10.1111/j.1600-0854.2007.00677.x;
RA Fader C.M., Sanchez D., Furlan M., Colombo M.I.;
RT "Induction of autophagy promotes fusion of multivesicular bodies with
RT autophagic vacuoles in k562 cells.";
RL Traffic 9:230-250(2008).
RN [13]
RP INDUCTION.
RX PubMed=19473119; DOI=10.1111/j.1474-9726.2009.00487.x;
RA Kang H.T., Hwang E.S.;
RT "Nicotinamide enhances mitochondria quality through autophagy activation in
RT human cells.";
RL Aging Cell 8:426-438(2009).
RN [14]
RP FUNCTION.
RX PubMed=19164948; DOI=10.4161/auto.5.3.7663;
RA Terebiznik M.R., Raju D., Vazquez C.L., Torbricki K., Kulkarni R.,
RA Blanke S.R., Yoshimori T., Colombo M.I., Jones N.L.;
RT "Effect of Helicobacter pylori's vacuolating cytotoxin on the autophagy
RT pathway in gastric epithelial cells.";
RL Autophagy 5:370-379(2009).
RN [15]
RP ACETYLATION.
RX PubMed=19124466; DOI=10.1074/jbc.m807135200;
RA Lee I.H., Finkel T.;
RT "Regulation of autophagy by the p300 acetyltransferase.";
RL J. Biol. Chem. 284:6322-6328(2009).
RN [16]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=19666601; DOI=10.1073/pnas.0907344106;
RA Dreux M., Gastaminza P., Wieland S.F., Chisari F.V.;
RT "The autophagy machinery is required to initiate hepatitis C virus
RT replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:14046-14051(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP INTERACTION WITH TECPR1, AND SUBCELLULAR LOCATION.
RX PubMed=22342342; DOI=10.1016/j.molcel.2011.12.036;
RA Chen D., Fan W., Lu Y., Ding X., Chen S., Zhong Q.;
RT "A mammalian autophagosome maturation mechanism mediated by TECPR1 and the
RT Atg12-Atg5 conjugate.";
RL Mol. Cell 45:629-641(2012).
RN [19]
RP CONJUGATION TO ATG5.
RX PubMed=26812546; DOI=10.7554/elife.12245;
RA Kim M., Sandford E., Gatica D., Qiu Y., Liu X., Zheng Y., Schulman B.A.,
RA Xu J., Semple I., Ro S.H., Kim B., Mavioglu R.N., Tolun A., Jipa A.,
RA Takats S., Karpati M., Li J.Z., Yapici Z., Juhasz G., Lee J.H.,
RA Klionsky D.J., Burmeister M.;
RT "Mutation in ATG5 reduces autophagy and leads to ataxia with developmental
RT delay.";
RL Elife 5:0-0(2016).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 52-140 IN COMPLEX WITH ATG5 AND
RP ATG16L1, INTERACTION WITH ATG3, FUNCTION, AND MUTAGENESIS OF LYS-54;
RP VAL-62; GLY-63; LYS-72; TRP-73; PHE-108; ASP-113; CYS-122; PHE-123; ALA-138
RP AND TRP-139.
RX PubMed=23202584; DOI=10.1038/nsmb.2431;
RA Otomo C., Metlagel Z., Takaesu G., Otomo T.;
RT "Structure of the human ATG12-ATG5 conjugate required for LC3 lipidation in
RT autophagy.";
RL Nat. Struct. Mol. Biol. 20:59-66(2013).
CC -!- FUNCTION: Ubiquitin-like protein involved in autophagy vesicles
CC formation. Conjugation with ATG5 through a ubiquitin-like conjugating
CC system involving also ATG7 as an E1-like activating enzyme and ATG10 as
CC an E2-like conjugating enzyme, is essential for its function. The
CC ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for
CC lipidation of ATG8 family proteins and their association to the vesicle
CC membranes. {ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:17999726,
CC ECO:0000269|PubMed:19074260, ECO:0000269|PubMed:19164948,
CC ECO:0000269|PubMed:23202584}.
CC -!- FUNCTION: (Microbial infection) May act as a proviral factor. In
CC association with ATG5, negatively regulates the innate antiviral immune
CC response by impairing the type I IFN production pathway upon vesicular
CC stomatitis virus (VSV) infection (PubMed:17709747). Required for the
CC translation of incoming hepatitis C virus (HCV) RNA and, thereby, for
CC the initiation of HCV replication, but not required once infection is
CC established (PubMed:19666601). {ECO:0000269|PubMed:17709747,
CC ECO:0000269|PubMed:19666601}.
CC -!- SUBUNIT: Forms a conjugate with ATG5 (PubMed:11096062, PubMed:12207896,
CC PubMed:11825910, PubMed:17709747, PubMed:26812546, PubMed:23202584).
CC The ATG12-ATG5 conjugate forms a complex with several units of ATG16L1
CC (PubMed:23202584). Forms an 800-kDa complex composed of ATG12-ATG5 and
CC ATG16L2 (By similarity). Interacts with DHX58/RIG-1, IFIH1/MDA5 and
CC MAVS/IPS-1 in monomeric form as well as in ATG12-ATG5 conjugate. The
CC interaction with MAVS is further enhanced upon vesicular stomatitis
CC virus (VSV) infection (PubMed:17709747). Interacts with ATG3 and ATG7
CC (PubMed:11096062, PubMed:12207896, PubMed:11825910, PubMed:23202584).
CC Interacts with ATG10 (By similarity). Interacts with TECPR1
CC (PubMed:22342342). {ECO:0000250|UniProtKB:Q9CQY1,
CC ECO:0000269|PubMed:11096062, ECO:0000269|PubMed:11825910,
CC ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:17709747,
CC ECO:0000269|PubMed:22342342, ECO:0000269|PubMed:23202584,
CC ECO:0000269|PubMed:26812546}.
CC -!- INTERACTION:
CC O94817; Q9NT62: ATG3; NbExp=6; IntAct=EBI-746742, EBI-988094;
CC O94817; O43186: CRX; NbExp=3; IntAct=EBI-746742, EBI-748171;
CC O94817; Q9BTL4: IER2; NbExp=3; IntAct=EBI-746742, EBI-2806011;
CC O94817; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-746742, EBI-16439278;
CC O94817; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-746742, EBI-748601;
CC O94817; Q14140: SERTAD2; NbExp=3; IntAct=EBI-746742, EBI-2822051;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal
CC structure membrane {ECO:0000269|PubMed:22342342}; Peripheral membrane
CC protein {ECO:0000269|PubMed:22342342}. Note=TECPR1 recruits the ATG12-
CC ATG5 conjugate to the autolysosomal membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94817-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94817-4; Sequence=VSP_018104, VSP_018105;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9852036}.
CC -!- INDUCTION: Expression is induced by mitochondrial DNA deletions,
CC chloramphenicol and nicotinamide. {ECO:0000269|PubMed:17457038,
CC ECO:0000269|PubMed:19473119}.
CC -!- DOMAIN: Shares weak sequence similarity with ubiquitin family, but
CC contains an 'ubiquitin superfold' and the C-terminal Gly is required
CC for isopeptide linkage. {ECO:0000269|PubMed:18704115}.
CC -!- PTM: Acetylated by EP300. {ECO:0000269|PubMed:19124466}.
CC -!- MISCELLANEOUS: Small amount of ATG5-ATG12 conjugate is enough to
CC perform normal autophagy.
CC -!- SIMILARITY: Belongs to the ATG12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12266.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB017507; BAA36493.1; -; mRNA.
DR EMBL; AC026449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011033; AAH11033.1; -; mRNA.
DR EMBL; BC012266; AAH12266.2; ALT_INIT; mRNA.
DR CCDS; CCDS4122.2; -. [O94817-1]
DR CCDS; CCDS64222.1; -. [O94817-4]
DR RefSeq; NP_001264712.1; NM_001277783.1. [O94817-4]
DR RefSeq; NP_004698.3; NM_004707.3. [O94817-1]
DR PDB; 4GDK; X-ray; 2.70 A; A/D=52-140.
DR PDB; 4GDL; X-ray; 2.88 A; A=52-140.
DR PDB; 4NAW; X-ray; 2.20 A; A/E/I/M=52-140.
DR PDBsum; 4GDK; -.
DR PDBsum; 4GDL; -.
DR PDBsum; 4NAW; -.
DR AlphaFoldDB; O94817; -.
DR SMR; O94817; -.
DR BioGRID; 114587; 77.
DR ComplexPortal; CPX-200; ATG12-ATG5-ATG16L1 complex.
DR ComplexPortal; CPX-354; ATG12-ATG5-ATG16L2 complex.
DR ComplexPortal; CPX-356; ATG5-ATG12 complex.
DR ComplexPortal; CPX-358; ATG5-ATG12-TECPR1 complex.
DR DIP; DIP-46466N; -.
DR IntAct; O94817; 30.
DR STRING; 9606.ENSP00000425107; -.
DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
DR iPTMnet; O94817; -.
DR PhosphoSitePlus; O94817; -.
DR SwissPalm; O94817; -.
DR BioMuta; ATG12; -.
DR EPD; O94817; -.
DR jPOST; O94817; -.
DR MassIVE; O94817; -.
DR MaxQB; O94817; -.
DR PaxDb; O94817; -.
DR PeptideAtlas; O94817; -.
DR PRIDE; O94817; -.
DR ProteomicsDB; 50457; -. [O94817-1]
DR ProteomicsDB; 50458; -. [O94817-4]
DR Antibodypedia; 4593; 801 antibodies from 40 providers.
DR DNASU; 9140; -.
DR Ensembl; ENST00000500945.2; ENSP00000425164.1; ENSG00000145782.13. [O94817-4]
DR Ensembl; ENST00000509910.2; ENSP00000425107.1; ENSG00000145782.13. [O94817-1]
DR GeneID; 9140; -.
DR KEGG; hsa:9140; -.
DR MANE-Select; ENST00000509910.2; ENSP00000425107.1; NM_004707.4; NP_004698.3.
DR UCSC; uc003krh.4; human. [O94817-1]
DR CTD; 9140; -.
DR DisGeNET; 9140; -.
DR GeneCards; ATG12; -.
DR HGNC; HGNC:588; ATG12.
DR HPA; ENSG00000145782; Low tissue specificity.
DR MIM; 609608; gene.
DR neXtProt; NX_O94817; -.
DR OpenTargets; ENSG00000145782; -.
DR PharmGKB; PA24879; -.
DR VEuPathDB; HostDB:ENSG00000145782; -.
DR eggNOG; KOG3439; Eukaryota.
DR GeneTree; ENSGT00390000016654; -.
DR HOGENOM; CLU_106795_3_0_1; -.
DR InParanoid; O94817; -.
DR OMA; LFIYVHQ; -.
DR OrthoDB; 1525971at2759; -.
DR PhylomeDB; O94817; -.
DR TreeFam; TF325131; -.
DR PathwayCommons; O94817; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR SignaLink; O94817; -.
DR SIGNOR; O94817; -.
DR BioGRID-ORCS; 9140; 21 hits in 1087 CRISPR screens.
DR ChiTaRS; ATG12; human.
DR GeneWiki; ATG12; -.
DR GenomeRNAi; 9140; -.
DR Pharos; O94817; Tbio.
DR PRO; PR:O94817; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O94817; protein.
DR Bgee; ENSG00000145782; Expressed in calcaneal tendon and 214 other tissues.
DR ExpressionAtlas; O94817; baseline and differential.
DR Genevisible; O94817; HS.
DR GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IPI:ComplexPortal.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IC:ComplexPortal.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; IMP:ComplexPortal.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IDA:ComplexPortal.
DR GO; GO:0045824; P:negative regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0032480; P:negative regulation of type I interferon production; IEA:Ensembl.
DR GO; GO:1904973; P:positive regulation of viral translation; IDA:ComplexPortal.
DR GO; GO:0006497; P:protein lipidation; IDA:ComplexPortal.
DR GO; GO:1901096; P:regulation of autophagosome maturation; IMP:ComplexPortal.
DR InterPro; IPR007242; Atg12.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13385; PTHR13385; 1.
DR Pfam; PF04110; APG12; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autophagy; Cytoplasm;
KW Host-virus interaction; Isopeptide bond; Membrane; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..140
FT /note="Ubiquitin-like protein ATG12"
FT /id="PRO_0000212471"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 140
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-130 in ATG5)"
FT /evidence="ECO:0000269|PubMed:23202584"
FT VAR_SEQ 56..74
FT /note="DILLKAVGDTPIMKTKKWA -> YLCESVLCSFPRPRSWNSL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018104"
FT VAR_SEQ 75..140
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018105"
FT MUTAGEN 54
FT /note="K->D: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 62
FT /note="V->R: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 63
FT /note="G->D: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 72
FT /note="K->D: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 73
FT /note="W->A: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 108
FT /note="F->A,D,R: Impairs ATG12 stability."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 113
FT /note="D->V: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 122
FT /note="C->W: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 123
FT /note="F->D: Impairs ATG12 stability."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 138
FT /note="A->R: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT MUTAGEN 139
FT /note="W->F,Y: Impairs E3 activity of the ATG12-ATG5
FT conjugate."
FT /evidence="ECO:0000269|PubMed:23202584"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:4NAW"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4GDK"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:4NAW"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:4NAW"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:4GDK"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:4NAW"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:4NAW"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:4NAW"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:4NAW"
SQ SEQUENCE 140 AA; 15113 MW; 109258521C2D194F CRC64;
MAEEPQSVLQ LPTSIAAGGE GLTDVSPETT TPEPPSSAAV SPGTEEPAGD TKKKIDILLK
AVGDTPIMKT KKWAVERTRT IQGLIDFIKK FLKLVASEQL FIYVNQSFAP SPDQEVGTLY
ECFGSDGKLV LHYCKSQAWG
