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Autophagy protein 5 (APG5-like) (Apoptosis-specific protein)

 ATG5_HUMAN              Reviewed;         275 AA.
Q9H1Y0; O60875; Q5JVR2; Q68DI4; Q9H2B8; Q9HCZ7;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
16-NOV-2001, sequence version 2.
12-SEP-2018, entry version 163.
RecName: Full=Autophagy protein 5;
AltName: Full=APG5-like;
AltName: Full=Apoptosis-specific protein;
Name=ATG5; Synonyms=APG5L, ASP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Fetal liver;
PubMed=9563500; DOI=10.1016/S0014-5793(98)00266-X;
Hammond E.M., Brunet C.L., Johnson G.D., Parkhill J., Milner A.E.,
Brady G., Gregory C.D., Grand R.J.A.;
"Homology between a human apoptosis specific protein and the product
of APG5, a gene involved in autophagy in yeast.";
FEBS Lett. 425:391-395(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Chen Y., Piao Y.J., Jiang Y.;
"A novel splicing isoform of human APG5.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
TISSUE=Fetal brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Endometrium, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION IN APOPTOSIS.
PubMed=7796880; DOI=10.1006/excr.1995.1177;
Grand R.J.A., Milner A.E., Mustoe T., Johnson G.D., Owen D.,
Grant M.L., Gregory C.D.;
"A novel protein expressed in mammalian cells undergoing apoptosis.";
Exp. Cell Res. 218:439-451(1995).
[7]
CONJUGATION TO ATG12 AT LYS-130, AND MUTAGENESIS OF LYS-130.
PubMed=9852036; DOI=10.1074/jbc.273.51.33889;
Mizushima N., Sugita H., Yoshimori T., Ohsumi Y.;
"A new protein conjugation system in human. The counterpart of the
yeast Apg12p conjugation system essential for autophagy.";
J. Biol. Chem. 273:33889-33892(1998).
[8]
CONJUGATION TO ATG12.
PubMed=11096062; DOI=10.1074/jbc.C000752200;
Tanida I., Tanida-Miyake E., Ueno T., Kominami E.;
"The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-
activating enzyme for multiple substrates including human Apg12p,
GATE-16, GABARAP, and MAP-LC3.";
J. Biol. Chem. 276:1701-1706(2001).
[9]
CONJUGATION TO ATG12, AND SUBCELLULAR LOCATION.
TISSUE=Embryonic stem cell;
PubMed=11266458; DOI=10.1083/jcb.152.4.657;
Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y.,
Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.;
"Dissection of autophagosome formation using Apg5-deficient mouse
embryonic stem cells.";
J. Cell Biol. 152:657-668(2001).
[10]
INTERACTION WITH ATG3, CONJUGATION TO ATG12, AND FUNCTION.
PubMed=12207896; DOI=10.1016/S0006-291X(02)02057-0;
Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.;
"Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3
processing.";
Biochem. Biophys. Res. Commun. 296:1164-1170(2002).
[11]
INTERACTION WITH ATG3, AND CONJUGATION TO ATG12.
PubMed=11825910; DOI=10.1074/jbc.M200385200;
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the
conjugation of hApg12p to hApg5p.";
J. Biol. Chem. 277:13739-13744(2002).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FADD.
PubMed=15778222; DOI=10.1074/jbc.M413934200;
Pyo J.O., Jang M.H., Kwon Y.K., Lee H.J., Jun J.I., Woo H.N.,
Cho D.H., Choi B., Lee H., Kim J.H., Mizushima N., Oshumi Y.,
Jung Y.K.;
"Essential roles of Atg5 and FADD in autophagic cell death: dissection
of autophagic cell death into vacuole formation and cell death.";
J. Biol. Chem. 280:20722-20729(2005).
[13]
CONJUGATION TO ATG12.
PubMed=16963840; DOI=10.4161/auto.3270;
Shao Y., Gao Z., Feldman T., Jiang X.;
"Stimulation of ATG12-ATG5 conjugation by ribonucleic acid.";
Autophagy 3:10-16(2007).
[14]
FUNCTION IN VIRAL INFECTION, INTERACTION WITH ATG12; DHX58; IFIH1 AND
MAVS, MUTAGENESIS OF LYS-130, AND SUBCELLULAR LOCATION.
PubMed=17709747; DOI=10.1073/pnas.0704014104;
Jounai N., Takeshita F., Kobiyama K., Sawano A., Miyawaki A.,
Xin K.Q., Ishii K.J., Kawai T., Akira S., Suzuki K., Okuda K.;
"The Atg5-Atg12 conjugate associates with innate antiviral immune
responses.";
Proc. Natl. Acad. Sci. U.S.A. 104:14050-14055(2007).
[15]
ACETYLATION BY EP300.
PubMed=19124466; DOI=10.1074/jbc.M807135200;
Lee I.H., Finkel T.;
"Regulation of autophagy by the p300 acetyltransferase.";
J. Biol. Chem. 284:6322-6328(2009).
[16]
FUNCTION IN VIRAL REPLICATION.
PubMed=19666601; DOI=10.1073/pnas.0907344106;
Dreux M., Gastaminza P., Wieland S.F., Chisari F.V.;
"The autophagy machinery is required to initiate hepatitis C virus
replication.";
Proc. Natl. Acad. Sci. U.S.A. 106:14046-14051(2009).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HEPATITIS C VIRUS
PROTEIN NS5B.
PubMed=20580051; DOI=10.1016/j.virol.2010.05.032;
Guevin C., Manna D., Belanger C., Konan K.V., Mak P., Labonte P.;
"Autophagy protein ATG5 interacts transiently with the hepatitis C
virus RNA polymerase (NS5B) early during infection.";
Virology 405:1-7(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
INTERACTION WITH TECPR1.
PubMed=21575909; DOI=10.1016/j.chom.2011.04.010;
Ogawa M., Yoshikawa Y., Kobayashi T., Mimuro H., Fukumatsu M.,
Kiga K., Piao Z., Ashida H., Yoshida M., Kakuta S., Koyama T.,
Goto Y., Nagatake T., Nagai S., Kiyono H., Kawalec M., Reichhart J.M.,
Sasakawa C.;
"A Tecpr1-dependent selective autophagy pathway targets bacterial
pathogens.";
Cell Host Microbe 9:376-389(2011).
[20]
FUNCTION.
PubMed=22170153; DOI=10.4161/auto.8.1.18174;
Mai S., Muster B., Bereiter-Hahn J., Jendrach M.;
"Autophagy proteins LC3B, ATG5 and ATG12 participate in quality
control after mitochondrial damage and influence lifespan.";
Autophagy 8:47-62(2012).
[21]
INTERACTION WITH TECPR1.
PubMed=22342342; DOI=10.1016/j.molcel.2011.12.036;
Chen D., Fan W., Lu Y., Ding X., Chen S., Zhong Q.;
"A mammalian autophagosome maturation mechanism mediated by TECPR1 and
the Atg12-Atg5 conjugate.";
Mol. Cell 45:629-641(2012).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN CONJUGATION WITH ATG12.
PubMed=23202584; DOI=10.1038/nsmb.2431;
Otomo C., Metlagel Z., Takaesu G., Otomo T.;
"Structure of the human ATG12-ATG5 conjugate required for LC3
lipidation in autophagy.";
Nat. Struct. Mol. Biol. 20:59-66(2013).
[24]
VARIANT [LARGE SCALE ANALYSIS] MET-58.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[25]
VARIANT SCAR25 ASP-122, CHARACTERIZATION OF VARIANT SCAR25 ASP-122,
FUNCTION, AND CONJUGATION TO ATG12.
PubMed=26812546; DOI=10.7554/eLife.12245;
Kim M., Sandford E., Gatica D., Qiu Y., Liu X., Zheng Y.,
Schulman B.A., Xu J., Semple I., Ro S.H., Kim B., Mavioglu R.N.,
Tolun A., Jipa A., Takats S., Karpati M., Li J.Z., Yapici Z.,
Juhasz G., Lee J.H., Klionsky D.J., Burmeister M.;
"Mutation in ATG5 reduces autophagy and leads to ataxia with
developmental delay.";
Elife 5:0-0(2016).
-!- FUNCTION: Involved in autophagic vesicle formation. Conjugation
with ATG12, through a ubiquitin-like conjugating system involving
ATG7 as an E1-like activating enzyme and ATG10 as an E2-like
conjugating enzyme, is essential for its function. The ATG12-ATG5
conjugate acts as an E3-like enzyme which is required for
lipidation of ATG8 family proteins and their association to the
vesicle membranes. Involved in mitochondrial quality control after
oxidative damage, and in subsequent cellular longevity. Plays a
critical role in multiple aspects of lymphocyte development and is
essential for both B and T lymphocyte survival and proliferation.
Required for optimal processing and presentation of antigens for
MHC II. Involved in the maintenance of axon morphology and
membrane structures, as well as in normal adipocyte
differentiation. Promotes primary ciliogenesis through removal of
OFD1 from centriolar satellites and degradation of IFT20 via the
autophagic pathway. {ECO:0000250|UniProtKB:Q99J83,
ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:20580051,
ECO:0000269|PubMed:22170153, ECO:0000269|PubMed:26812546}.
-!- FUNCTION: May play an important role in the apoptotic process,
possibly within the modified cytoskeleton. Its expression is a
relatively late event in the apoptotic process, occurring
downstream of caspase activity. Plays a crucial role in IFN-gamma-
induced autophagic cell death by interacting with FADD.
{ECO:0000269|PubMed:15778222, ECO:0000269|PubMed:7796880}.
-!- FUNCTION: (Microbial infection) May act as a proviral factor. In
association with ATG12, negatively regulates the innate antiviral
immune response by impairing the type I IFN production pathway
upon vesicular stomatitis virus (VSV) infection (PubMed:17709747).
Required for the translation of incoming hepatitis C virus (HCV)
RNA and, thereby, for initiation of HCV replication, but not
required once infection is established (PubMed:19666601).
{ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:19666601}.
-!- SUBUNIT: Forms a conjugate with ATG12 (PubMed:12207896,
PubMed:11825910, PubMed:17709747, PubMed:26812546). The ATG5-ATG12
conjugate forms a complex with several units of ATG16L. Interacts
with TECPR1; the interaction is direct and does not take place
when ATG16L is associated with the ATG5-ATG12 conjugate
(PubMed:21575909, PubMed:22342342). Interacts with DHX58/RIG-1,
IFIH1/MDA5 and MAVS/IPS-1 in monomeric form as well as in ATG12-
ATG5 conjugate form. The interaction with MAVS is further enhanced
upon vesicular stomatitis virus (VSV) infection (PubMed:17709747).
Interacts with ATG3 (PubMed:12207896, PubMed:11825910). Interacts
with ATG7 and ATG10 (By similarity). Interacts with FADD
(PubMed:15778222). {ECO:0000250|UniProtKB:Q99J83,
ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:12207896,
ECO:0000269|PubMed:15778222, ECO:0000269|PubMed:17709747,
ECO:0000269|PubMed:21575909, ECO:0000269|PubMed:22342342,
ECO:0000269|PubMed:26812546}.
-!- SUBUNIT: (Microbial infection) Interacts transiently interacts
with hepatitis C virus (HCV) protein NS5B during HCV infection.
{ECO:0000269|PubMed:20580051}.
-!- INTERACTION:
Q676U5:ATG16L1; NbExp=7; IntAct=EBI-1047414, EBI-535909;
Q8C0J2-3:Atg16l1 (xeno); NbExp=2; IntAct=EBI-1047414, EBI-16029274;
Q8WUD4:CCDC12; NbExp=3; IntAct=EBI-1047414, EBI-2557572;
O95786-1:DDX58; NbExp=4; IntAct=EBI-1047414, EBI-15577823;
O95166:GABARAP; NbExp=2; IntAct=EBI-1047414, EBI-712001;
Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-1047414, EBI-373144;
Q7Z434-1:MAVS; NbExp=4; IntAct=EBI-1047414, EBI-15577799;
Q8TDY2:RB1CC1; NbExp=3; IntAct=EBI-1047414, EBI-1047793;
Q7Z6L1:TECPR1; NbExp=8; IntAct=EBI-1047414, EBI-2946676;
Q8IZQ1:WDFY3; NbExp=7; IntAct=EBI-1047414, EBI-1569256;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17709747}.
Preautophagosomal structure membrane; Peripheral membrane protein.
Note=Colocalizes with nonmuscle actin. The conjugate detaches from
the membrane immediately before or after autophagosome formation
is completed (By similarity). Localizes also to discrete punctae
along the ciliary axoneme and to the base of the ciliary axoneme.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=Q9H1Y0-1; Sequence=Displayed;
Name=Short; Synonyms=APG5beta;
IsoId=Q9H1Y0-2; Sequence=VSP_003791;
-!- TISSUE SPECIFICITY: Ubiquitous. The mRNA is present at similar
levels in viable and apoptotic cells, whereas the protein is
dramatically highly expressed in apoptotic cells.
-!- INDUCTION: By apoptotic stimuli.
-!- PTM: Conjugated to ATG12; which is essential for autophagy, but is
not required for association with isolation membrane.
-!- PTM: Acetylated by EP300. {ECO:0000269|PubMed:19124466}.
-!- DISEASE: Spinocerebellar ataxia, autosomal recessive, 25 (SCAR25)
[MIM:617584]: A form of spinocerebellar ataxia, a clinically and
genetically heterogeneous group of cerebellar disorders due to
degeneration of the cerebellum with variable involvement of the
brainstem and spinal cord. SCAR25 patients manifest delayed
psychomotor development with delayed walking, truncal ataxia,
dysmetria, and nystagmus, Cerebellar hypoplasia is seen on brain
imaging. {ECO:0000269|PubMed:26812546}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ATG5 family. {ECO:0000305}.
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EMBL; Y11588; CAA72327.1; -; mRNA.
EMBL; AF293841; AAG44955.1; -; mRNA.
EMBL; CR749386; CAH18236.1; -; mRNA.
EMBL; AL022067; CAI42297.1; -; Genomic_DNA.
EMBL; AL133509; CAI42297.1; JOINED; Genomic_DNA.
EMBL; AL138917; CAI42297.1; JOINED; Genomic_DNA.
EMBL; AL022067; CAI42298.1; -; Genomic_DNA.
EMBL; AL133509; CAI42298.1; JOINED; Genomic_DNA.
EMBL; AL138917; CAI42298.1; JOINED; Genomic_DNA.
EMBL; AL133509; CAC19459.2; -; Genomic_DNA.
EMBL; AL022067; CAC19459.2; JOINED; Genomic_DNA.
EMBL; AL138917; CAC19459.2; JOINED; Genomic_DNA.
EMBL; AL133509; CAI42831.1; -; Genomic_DNA.
EMBL; AL022067; CAI42831.1; JOINED; Genomic_DNA.
EMBL; AL138917; CAI42831.1; JOINED; Genomic_DNA.
EMBL; AL138917; CAI20313.1; -; Genomic_DNA.
EMBL; AL133509; CAI20313.1; JOINED; Genomic_DNA.
EMBL; AL022067; CAI20313.1; JOINED; Genomic_DNA.
EMBL; AL138917; CAI20314.1; -; Genomic_DNA.
EMBL; AL022067; CAI20314.1; JOINED; Genomic_DNA.
EMBL; AL133509; CAI20314.1; JOINED; Genomic_DNA.
EMBL; BC002699; AAH02699.1; -; mRNA.
EMBL; BC093011; AAH93011.1; -; mRNA.
CCDS; CCDS5055.1; -. [Q9H1Y0-1]
CCDS; CCDS69159.1; -. [Q9H1Y0-2]
RefSeq; NP_001273035.1; NM_001286106.1. [Q9H1Y0-1]
RefSeq; NP_001273036.1; NM_001286107.1. [Q9H1Y0-2]
RefSeq; NP_001273037.1; NM_001286108.1.
RefSeq; NP_001273040.1; NM_001286111.1.
RefSeq; NP_004840.1; NM_004849.3. [Q9H1Y0-1]
UniGene; Hs.486063; -.
PDB; 4GDK; X-ray; 2.70 A; B/E=1-275.
PDB; 4GDL; X-ray; 2.88 A; B=1-275.
PDB; 4NAW; X-ray; 2.20 A; B/F/J/N=1-275.
PDB; 4TQ0; X-ray; 2.70 A; A/C/E=1-275.
PDB; 4TQ1; X-ray; 1.80 A; A=1-275.
PDB; 5D7G; X-ray; 3.00 A; A/C/E/G=1-275.
PDB; 5NPV; X-ray; 3.10 A; A/C=1-275.
PDB; 5NPW; X-ray; 3.10 A; A/C/E/G=1-275.
PDBsum; 4GDK; -.
PDBsum; 4GDL; -.
PDBsum; 4NAW; -.
PDBsum; 4TQ0; -.
PDBsum; 4TQ1; -.
PDBsum; 5D7G; -.
PDBsum; 5NPV; -.
PDBsum; 5NPW; -.
ProteinModelPortal; Q9H1Y0; -.
SMR; Q9H1Y0; -.
BioGrid; 114859; 41.
ComplexPortal; CPX-200; ATG12-ATG5-ATG16L1 complex.
ComplexPortal; CPX-354; ATG12-ATG5-ATG16L2 complex.
ComplexPortal; CPX-356; ATG5-ATG12 complex.
ComplexPortal; CPX-358; ATG5-ATG12-TECPR1 complex.
DIP; DIP-29758N; -.
IntAct; Q9H1Y0; 52.
MINT; Q9H1Y0; -.
STRING; 9606.ENSP00000343313; -.
iPTMnet; Q9H1Y0; -.
PhosphoSitePlus; Q9H1Y0; -.
DMDM; 17366828; -.
EPD; Q9H1Y0; -.
MaxQB; Q9H1Y0; -.
PaxDb; Q9H1Y0; -.
PeptideAtlas; Q9H1Y0; -.
PRIDE; Q9H1Y0; -.
ProteomicsDB; 80456; -.
ProteomicsDB; 80457; -. [Q9H1Y0-2]
DNASU; 9474; -.
Ensembl; ENST00000343245; ENSP00000343313; ENSG00000057663. [Q9H1Y0-1]
Ensembl; ENST00000369076; ENSP00000358072; ENSG00000057663. [Q9H1Y0-1]
Ensembl; ENST00000635758; ENSP00000490493; ENSG00000057663. [Q9H1Y0-2]
GeneID; 9474; -.
KEGG; hsa:9474; -.
UCSC; uc003prf.4; human. [Q9H1Y0-1]
CTD; 9474; -.
DisGeNET; 9474; -.
EuPathDB; HostDB:ENSG00000057663.12; -.
GeneCards; ATG5; -.
HGNC; HGNC:589; ATG5.
HPA; CAB034432; -.
HPA; CAB037309; -.
HPA; HPA042973; -.
MalaCards; ATG5; -.
MIM; 604261; gene.
MIM; 617584; phenotype.
neXtProt; NX_Q9H1Y0; -.
OpenTargets; ENSG00000057663; -.
PharmGKB; PA24880; -.
eggNOG; KOG2976; Eukaryota.
eggNOG; ENOG410XQ71; LUCA.
GeneTree; ENSGT00390000004766; -.
HOGENOM; HOG000007893; -.
HOVERGEN; HBG018731; -.
InParanoid; Q9H1Y0; -.
KO; K08339; -.
OMA; WHYPIGV; -.
OrthoDB; EOG091G0JU7; -.
PhylomeDB; Q9H1Y0; -.
TreeFam; TF314415; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-5205685; Pink/Parkin Mediated Mitophagy.
Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
SIGNOR; Q9H1Y0; -.
ChiTaRS; ATG5; human.
GeneWiki; ATG5; -.
GenomeRNAi; 9474; -.
PRO; PR:Q9H1Y0; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000057663; Expressed in 225 organ(s), highest expression level in colonic mucosa.
CleanEx; HS_ATG5; -.
ExpressionAtlas; Q9H1Y0; baseline and differential.
Genevisible; Q9H1Y0; HS.
GO; GO:0034274; C:Atg12-Atg5-Atg16 complex; IBA:GO_Central.
GO; GO:0005776; C:autophagosome; IDA:MGI.
GO; GO:0005930; C:axoneme; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0044233; C:ER-mitochondrion membrane contact site; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB.
GO; GO:0035973; P:aggrephagy; IMP:ParkinsonsUK-UCL.
GO; GO:0019883; P:antigen processing and presentation of endogenous antigen; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:UniProtKB.
GO; GO:0075044; P:autophagy of host cells involved in interaction with symbiont; IGI:UniProtKB.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
GO; GO:0006501; P:C-terminal protein lipidation; IBA:GO_Central.
GO; GO:0019725; P:cellular homeostasis; IEA:Ensembl.
GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central.
GO; GO:0071500; P:cellular response to nitrosative stress; IEA:Ensembl.
GO; GO:0060047; P:heart contraction; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0060548; P:negative regulation of cell death; IMP:MGI.
GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; IEA:Ensembl.
GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0039689; P:negative stranded viral RNA replication; IEA:Ensembl.
GO; GO:0045060; P:negative thymic T cell selection; IEA:Ensembl.
GO; GO:0048840; P:otolith development; IEA:Ensembl.
GO; GO:0070257; P:positive regulation of mucus secretion; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; IEA:Ensembl.
GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
GO; GO:0002739; P:regulation of cytokine secretion involved in immune response; IEA:Ensembl.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009620; P:response to fungus; IEA:Ensembl.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
GO; GO:0055015; P:ventricular cardiac muscle cell development; IEA:Ensembl.
InterPro; IPR007239; Atg5.
PANTHER; PTHR13040; PTHR13040; 1.
Pfam; PF04106; APG5; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis; Autophagy;
Complete proteome; Cytoplasm; Disease mutation; Immunity;
Isopeptide bond; Membrane; Neurodegeneration; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 275 Autophagy protein 5.
/FTId=PRO_0000218994.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ATG12).
{ECO:0000305}.
VAR_SEQ 1 79 MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPR
VSYLTLVTDKVKKHFQKVMRQEDISEIWFEYEGTPLKW ->
M (in isoform Short).
{ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.2}.
/FTId=VSP_003791.
VARIANT 58 58 K -> M (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036243.
VARIANT 122 122 E -> D (in SCAR25; reduced conjugation to
ATG12; decrease in autophagy activity;
dbSNP:rs1131692265).
{ECO:0000269|PubMed:26812546}.
/FTId=VAR_079274.
MUTAGEN 130 130 K->R: Loss of conjugaction with ATG12.
Does affect interaction with DHX58, nor
with MAVS. {ECO:0000269|PubMed:17709747,
ECO:0000269|PubMed:9852036}.
CONFLICT 79 79 W -> M (in Ref. 4; CAC19459).
{ECO:0000305}.
HELIX 4 12 {ECO:0000244|PDB:4TQ1}.
STRAND 15 22 {ECO:0000244|PDB:4TQ1}.
STRAND 24 26 {ECO:0000244|PDB:5NPV}.
STRAND 28 30 {ECO:0000244|PDB:4GDL}.
STRAND 35 40 {ECO:0000244|PDB:4TQ1}.
HELIX 45 48 {ECO:0000244|PDB:4TQ1}.
HELIX 50 57 {ECO:0000244|PDB:4TQ1}.
HELIX 62 64 {ECO:0000244|PDB:4NAW}.
STRAND 69 72 {ECO:0000244|PDB:4TQ1}.
HELIX 83 91 {ECO:0000244|PDB:4TQ1}.
STRAND 92 94 {ECO:0000244|PDB:5D7G}.
STRAND 96 103 {ECO:0000244|PDB:4TQ1}.
TURN 109 111 {ECO:0000244|PDB:4TQ1}.
STRAND 113 115 {ECO:0000244|PDB:5NPV}.
HELIX 118 137 {ECO:0000244|PDB:4TQ1}.
HELIX 140 144 {ECO:0000244|PDB:4TQ1}.
HELIX 147 158 {ECO:0000244|PDB:4TQ1}.
HELIX 162 172 {ECO:0000244|PDB:4TQ1}.
HELIX 177 179 {ECO:0000244|PDB:4TQ0}.
STRAND 187 192 {ECO:0000244|PDB:4TQ1}.
STRAND 194 196 {ECO:0000244|PDB:4TQ1}.
STRAND 208 210 {ECO:0000244|PDB:4GDL}.
HELIX 215 222 {ECO:0000244|PDB:4TQ1}.
HELIX 224 226 {ECO:0000244|PDB:4TQ1}.
TURN 229 231 {ECO:0000244|PDB:4TQ1}.
STRAND 232 240 {ECO:0000244|PDB:4TQ1}.
HELIX 251 257 {ECO:0000244|PDB:4TQ1}.
STRAND 265 270 {ECO:0000244|PDB:4TQ1}.
SEQUENCE 275 AA; 32447 MW; C33A1E0B3C1DBE5C CRC64;
MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD KVKKHFQKVM
RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI TVHFKSFPEK DLLHCPSKDA
IEAHFMSCMK EADALKHKSQ VINEMQKKDH KQLWMGLQND RFDQFWAINR KLMEYPAEEN
GFRYIPFRIY QTTTERPFIQ KLFRPVAADG QLHTLGDLLK EVCPSAIDPE DGEKKNQVMI
HGIEPMLETP LQWLSEHLSY PDNFLHISII PQPTD


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