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Q9H1Y0

- ATG5_HUMAN

UniProt

Q9H1Y0 - ATG5_HUMAN

Protein

Autophagy protein 5

Gene

ATG5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (16 Nov 2001)
      Previous versions | rss
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    Functioni

    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. The ATG12-ATG5 conjugate also negatively regulates the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 and MAVS. Also plays a role in translation or delivery of incoming viral RNA to the translation apparatus. 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.
    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.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. autophagic vacuole assembly Source: UniProtKB
    3. autophagy Source: UniProtKB
    4. blood vessel remodeling Source: Ensembl
    5. heart contraction Source: Ensembl
    6. innate immune response Source: Reactome
    7. negative regulation of apoptotic process Source: Ensembl
    8. negative regulation of protein ubiquitination Source: Ensembl
    9. negative regulation of type I interferon production Source: Reactome
    10. otolith development Source: Ensembl
    11. post-translational protein modification Source: UniProtKB
    12. regulation of cilium assembly Source: UniProtKB
    13. regulation of cytokine secretion involved in immune response Source: Ensembl
    14. response to drug Source: Ensembl
    15. response to fungus Source: Ensembl
    16. vasodilation Source: Ensembl
    17. ventricular cardiac muscle cell development Source: Ensembl

    Keywords - Biological processi

    Apoptosis, Autophagy, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_25271. Negative regulators of RIG-I/MDA5 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Autophagy protein 5
    Alternative name(s):
    APG5-like
    Apoptosis-specific protein
    Gene namesi
    Name:ATG5
    Synonyms:APG5L, ASP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:589. ATG5.

    Subcellular locationi

    Cytoplasm. 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.By similarity

    GO - Cellular componenti

    1. autophagic vacuole Source: MGI
    2. axoneme Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. membrane Source: MGI
    5. pre-autophagosomal structure membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi130 – 1301K → R: Loss of conjugation. 1 Publication

    Organism-specific databases

    PharmGKBiPA24880.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 275275Autophagy protein 5PRO_0000218994Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Cross-linki130 – 130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)Curated

    Post-translational modificationi

    Conjugated to ATG12; which is essential for autophagy, but is not required for association with isolation membrane.
    Acetylated by EP300.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9H1Y0.
    PaxDbiQ9H1Y0.
    PRIDEiQ9H1Y0.

    PTM databases

    PhosphoSiteiQ9H1Y0.

    Expressioni

    Tissue specificityi

    Ubiquitous. The mRNA is present at similar levels in viable and apoptotic cells, whereas the protein is dramatically highly expressed in apoptotic cells.

    Inductioni

    By apoptotic stimuli.

    Gene expression databases

    ArrayExpressiQ9H1Y0.
    BgeeiQ9H1Y0.
    CleanExiHS_ATG5.
    GenevestigatoriQ9H1Y0.

    Organism-specific databases

    HPAiCAB034432.
    CAB037309.
    HPA042973.

    Interactioni

    Subunit structurei

    Forms a conjugate with ATG12. 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. ATG12-ATG5 interacts with MAVS, MGA and RARRES3. Interacts with ATG3, ATG7 and ATG10. Interacts with FADD. Interacts transiently interacts with hepatitis C virus (HCV) protein NS5B during HCV infection.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPO951662EBI-1047414,EBI-712001
    MAP1LC3BQ9GZQ82EBI-1047414,EBI-373144
    TECPR1Q7Z6L16EBI-1047414,EBI-2946676
    WDFY3Q8IZQ17EBI-1047414,EBI-1569256

    Protein-protein interaction databases

    BioGridi114859. 18 interactions.
    DIPiDIP-29758N.
    IntActiQ9H1Y0. 33 interactions.
    STRINGi9606.ENSP00000343313.

    Structurei

    Secondary structure

    1
    275
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1210
    Beta strandi15 – 228
    Beta strandi28 – 303
    Beta strandi35 – 406
    Helixi45 – 484
    Helixi50 – 578
    Helixi62 – 643
    Beta strandi69 – 724
    Helixi83 – 908
    Turni91 – 933
    Beta strandi96 – 1038
    Turni109 – 1113
    Helixi118 – 13720
    Helixi140 – 1445
    Helixi147 – 15812
    Helixi162 – 17211
    Beta strandi179 – 1813
    Beta strandi187 – 1904
    Beta strandi194 – 1974
    Beta strandi208 – 2103
    Helixi215 – 2228
    Helixi224 – 2263
    Beta strandi236 – 2405
    Helixi251 – 2577
    Beta strandi265 – 2717

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GDKX-ray2.70B/E1-275[»]
    4GDLX-ray2.88B1-275[»]
    4NAWX-ray2.20B/F/J/N1-275[»]
    ProteinModelPortaliQ9H1Y0.
    SMRiQ9H1Y0. Positions 3-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ATG5 family.Curated

    Phylogenomic databases

    eggNOGiNOG271554.
    HOGENOMiHOG000007893.
    HOVERGENiHBG018731.
    InParanoidiQ9H1Y0.
    KOiK08339.
    OMAiHYPIGVL.
    OrthoDBiEOG72C50T.
    PhylomeDBiQ9H1Y0.
    TreeFamiTF314415.

    Family and domain databases

    InterProiIPR007239. Atg5.
    [Graphical view]
    PANTHERiPTHR13040. PTHR13040. 1 hit.
    PfamiPF04106. APG5. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q9H1Y0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTDDKDVLRD VWFGRIPTCF TLYQDEITER EAEPYYLLLP RVSYLTLVTD    50
    KVKKHFQKVM RQEDISEIWF EYEGTPLKWH YPIGLLFDLL ASSSALPWNI 100
    TVHFKSFPEK DLLHCPSKDA IEAHFMSCMK EADALKHKSQ VINEMQKKDH 150
    KQLWMGLQND RFDQFWAINR KLMEYPAEEN GFRYIPFRIY QTTTERPFIQ 200
    KLFRPVAADG QLHTLGDLLK EVCPSAIDPE DGEKKNQVMI HGIEPMLETP 250
    LQWLSEHLSY PDNFLHISII PQPTD 275
    Length:275
    Mass (Da):32,447
    Last modified:November 16, 2001 - v2
    Checksum:iC33A1E0B3C1DBE5C
    GO
    Isoform Short (identifier: Q9H1Y0-2) [UniParc]FASTAAdd to Basket

    Also known as: APG5beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-79: MTDDKDVLRD...FEYEGTPLKW → M

    Show »
    Length:197
    Mass (Da):22,931
    Checksum:i05FC581F6EABB753
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti79 – 791W → M in CAC19459. (PubMed:14574404)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 581K → M in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036243

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7979MTDDK…TPLKW → M in isoform Short. 2 PublicationsVSP_003791Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11588 mRNA. Translation: CAA72327.1.
    AF293841 mRNA. Translation: AAG44955.1.
    CR749386 mRNA. Translation: CAH18236.1.
    AL022067, AL133509, AL138917 Genomic DNA. Translation: CAI42297.1.
    AL022067, AL133509, AL138917 Genomic DNA. Translation: CAI42298.1.
    AL133509, AL022067, AL138917 Genomic DNA. Translation: CAC19459.2.
    AL133509, AL022067, AL138917 Genomic DNA. Translation: CAI42831.1.
    AL138917, AL133509, AL022067 Genomic DNA. Translation: CAI20313.1.
    AL138917, AL022067, AL133509 Genomic DNA. Translation: CAI20314.1.
    BC002699 mRNA. Translation: AAH02699.1.
    BC093011 mRNA. Translation: AAH93011.1.
    CCDSiCCDS5055.1. [Q9H1Y0-1]
    CCDS69159.1. [Q9H1Y0-2]
    RefSeqiNP_001273035.1. NM_001286106.1. [Q9H1Y0-1]
    NP_001273036.1. NM_001286107.1. [Q9H1Y0-2]
    NP_001273037.1. NM_001286108.1.
    NP_001273040.1. NM_001286111.1.
    NP_004840.1. NM_004849.3. [Q9H1Y0-1]
    UniGeneiHs.486063.

    Genome annotation databases

    EnsembliENST00000343245; ENSP00000343313; ENSG00000057663. [Q9H1Y0-1]
    ENST00000369070; ENSP00000358066; ENSG00000057663. [Q9H1Y0-2]
    ENST00000369076; ENSP00000358072; ENSG00000057663. [Q9H1Y0-1]
    GeneIDi9474.
    KEGGihsa:9474.
    UCSCiuc003prf.3. human. [Q9H1Y0-1]
    uc003prg.3. human. [Q9H1Y0-2]

    Polymorphism databases

    DMDMi17366828.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11588 mRNA. Translation: CAA72327.1 .
    AF293841 mRNA. Translation: AAG44955.1 .
    CR749386 mRNA. Translation: CAH18236.1 .
    AL022067 , AL133509 , AL138917 Genomic DNA. Translation: CAI42297.1 .
    AL022067 , AL133509 , AL138917 Genomic DNA. Translation: CAI42298.1 .
    AL133509 , AL022067 , AL138917 Genomic DNA. Translation: CAC19459.2 .
    AL133509 , AL022067 , AL138917 Genomic DNA. Translation: CAI42831.1 .
    AL138917 , AL133509 , AL022067 Genomic DNA. Translation: CAI20313.1 .
    AL138917 , AL022067 , AL133509 Genomic DNA. Translation: CAI20314.1 .
    BC002699 mRNA. Translation: AAH02699.1 .
    BC093011 mRNA. Translation: AAH93011.1 .
    CCDSi CCDS5055.1. [Q9H1Y0-1 ]
    CCDS69159.1. [Q9H1Y0-2 ]
    RefSeqi NP_001273035.1. NM_001286106.1. [Q9H1Y0-1 ]
    NP_001273036.1. NM_001286107.1. [Q9H1Y0-2 ]
    NP_001273037.1. NM_001286108.1.
    NP_001273040.1. NM_001286111.1.
    NP_004840.1. NM_004849.3. [Q9H1Y0-1 ]
    UniGenei Hs.486063.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GDK X-ray 2.70 B/E 1-275 [» ]
    4GDL X-ray 2.88 B 1-275 [» ]
    4NAW X-ray 2.20 B/F/J/N 1-275 [» ]
    ProteinModelPortali Q9H1Y0.
    SMRi Q9H1Y0. Positions 3-275.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114859. 18 interactions.
    DIPi DIP-29758N.
    IntActi Q9H1Y0. 33 interactions.
    STRINGi 9606.ENSP00000343313.

    PTM databases

    PhosphoSitei Q9H1Y0.

    Polymorphism databases

    DMDMi 17366828.

    Proteomic databases

    MaxQBi Q9H1Y0.
    PaxDbi Q9H1Y0.
    PRIDEi Q9H1Y0.

    Protocols and materials databases

    DNASUi 9474.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343245 ; ENSP00000343313 ; ENSG00000057663 . [Q9H1Y0-1 ]
    ENST00000369070 ; ENSP00000358066 ; ENSG00000057663 . [Q9H1Y0-2 ]
    ENST00000369076 ; ENSP00000358072 ; ENSG00000057663 . [Q9H1Y0-1 ]
    GeneIDi 9474.
    KEGGi hsa:9474.
    UCSCi uc003prf.3. human. [Q9H1Y0-1 ]
    uc003prg.3. human. [Q9H1Y0-2 ]

    Organism-specific databases

    CTDi 9474.
    GeneCardsi GC06M106632.
    HGNCi HGNC:589. ATG5.
    HPAi CAB034432.
    CAB037309.
    HPA042973.
    MIMi 604261. gene.
    neXtProti NX_Q9H1Y0.
    PharmGKBi PA24880.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271554.
    HOGENOMi HOG000007893.
    HOVERGENi HBG018731.
    InParanoidi Q9H1Y0.
    KOi K08339.
    OMAi HYPIGVL.
    OrthoDBi EOG72C50T.
    PhylomeDBi Q9H1Y0.
    TreeFami TF314415.

    Enzyme and pathway databases

    Reactomei REACT_25271. Negative regulators of RIG-I/MDA5 signaling.

    Miscellaneous databases

    ChiTaRSi ATG5. human.
    GeneWikii ATG5.
    GenomeRNAii 9474.
    NextBioi 35504.
    PROi Q9H1Y0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H1Y0.
    Bgeei Q9H1Y0.
    CleanExi HS_ATG5.
    Genevestigatori Q9H1Y0.

    Family and domain databases

    InterProi IPR007239. Atg5.
    [Graphical view ]
    PANTHERi PTHR13040. PTHR13040. 1 hit.
    Pfami PF04106. APG5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Homology between a human apoptosis specific protein and the product of APG5, a gene involved in autophagy in yeast."
      Hammond E.M., Brunet C.L., Johnson G.D., Parkhill J., Milner A.E., Brady G., Gregory C.D., Grand R.J.A.
      FEBS Lett. 425:391-395(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Fetal liver.
    2. "A novel splicing isoform of human APG5."
      Chen Y., Piao Y.J., Jiang Y.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
      Tissue: Fetal brain.
    4. "The DNA sequence and analysis of human chromosome 6."
      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.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Endometrium and Placenta.
    6. "A novel protein expressed in mammalian cells undergoing apoptosis."
      Grand R.J.A., Milner A.E., Mustoe T., Johnson G.D., Owen D., Grant M.L., Gregory C.D.
      Exp. Cell Res. 218:439-451(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN APOPTOSIS.
    7. "A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy."
      Mizushima N., Sugita H., Yoshimori T., Ohsumi Y.
      J. Biol. Chem. 273:33889-33892(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CONJUGATION TO ATG12 AT LYS-130, MUTAGENESIS OF LYS-130.
    8. "The human homolog of Saccharomyces cerevisiae Apg7p is a Protein-activating enzyme for multiple substrates including human Apg12p, GATE-16, GABARAP, and MAP-LC3."
      Tanida I., Tanida-Miyake E., Ueno T., Kominami E.
      J. Biol. Chem. 276:1701-1706(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CONJUGATION TO ATG12.
    9. "Dissection of autophagosome formation using Apg5-deficient mouse embryonic stem cells."
      Mizushima N., Yamamoto A., Hatano M., Kobayashi Y., Kabeya Y., Suzuki K., Tokuhisa T., Ohsumi Y., Yoshimori T.
      J. Cell Biol. 152:657-668(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CONJUGATION TO ATG12, SUBCELLULAR LOCATION.
      Tissue: Embryonic stem cell.
    10. "Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3 processing."
      Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.
      Biochem. Biophys. Res. Commun. 296:1164-1170(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATG3, CONJUGATION TO ATG12, FUNCTION.
    11. "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."
      Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.
      J. Biol. Chem. 277:13739-13744(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATG3, CONJUGATION TO ATG12.
    12. "Essential roles of Atg5 and FADD in autophagic cell death: dissection of autophagic cell death into vacuole formation and cell death."
      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.
      J. Biol. Chem. 280:20722-20729(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FADD.
    13. "Stimulation of ATG12-ATG5 conjugation by ribonucleic acid."
      Shao Y., Gao Z., Feldman T., Jiang X.
      Autophagy 3:10-16(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CONJUGATION TO ATG12.
    14. Cited for: FUNCTION IN INNATE IMMUNE RESPONSE, INTERACTION WITH MAVS; MGA AND RARRES3.
    15. "Regulation of autophagy by the p300 acetyltransferase."
      Lee I.H., Finkel T.
      J. Biol. Chem. 284:6322-6328(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION BY EP300.
    16. "Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection."
      Guevin C., Manna D., Belanger C., Konan K.V., Mak P., Labonte P.
      Virology 405:1-7(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HEPATITIS C VIRUS PROTEIN NS5B.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: INTERACTION WITH TECPR1.
    19. "Autophagy proteins LC3B, ATG5 and ATG12 participate in quality control after mitochondrial damage and influence lifespan."
      Mai S., Muster B., Bereiter-Hahn J., Jendrach M.
      Autophagy 8:47-62(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "A mammalian autophagosome maturation mechanism mediated by TECPR1 and the Atg12-Atg5 conjugate."
      Chen D., Fan W., Lu Y., Ding X., Chen S., Zhong Q.
      Mol. Cell 45:629-641(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TECPR1.
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Structure of the human ATG12-ATG5 conjugate required for LC3 lipidation in autophagy."
      Otomo C., Metlagel Z., Takaesu G., Otomo T.
      Nat. Struct. Mol. Biol. 20:59-66(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN CONJUGATION WITH ATG12.
    23. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-58.

    Entry informationi

    Entry nameiATG5_HUMAN
    AccessioniPrimary (citable) accession number: Q9H1Y0
    Secondary accession number(s): O60875
    , Q5JVR2, Q68DI4, Q9H2B8, Q9HCZ7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: November 16, 2001
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3