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O95352

- ATG7_HUMAN

UniProt

O95352 - ATG7_HUMAN

Protein

Ubiquitin-like modifier-activating enzyme ATG7

Gene

ATG7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Plays also a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei572 – 5721Glycyl thioester intermediateBy similarity

    GO - Molecular functioni

    1. Atg12 activating enzyme activity Source: UniProtKB
    2. Atg8 activating enzyme Source: RefGenome
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. transcription factor binding Source: UniProtKB
    6. ubiquitin activating enzyme activity Source: ProtInc

    GO - Biological processi

    1. adult walking behavior Source: Ensembl
    2. cardiac muscle cell development Source: Ensembl
    3. cellular amino acid metabolic process Source: Ensembl
    4. cellular protein modification process Source: ProtInc
    5. cellular response to hyperoxia Source: UniProtKB
    6. cellular response to nitrogen starvation Source: RefGenome
    7. cellular response to starvation Source: UniProtKB
    8. central nervous system neuron axonogenesis Source: Ensembl
    9. cerebellar Purkinje cell layer development Source: Ensembl
    10. cerebral cortex development Source: Ensembl
    11. C-terminal protein lipidation Source: RefGenome
    12. late nucleophagy Source: RefGenome
    13. liver development Source: Ensembl
    14. membrane fusion Source: ProtInc
    15. mitochondrion degradation Source: RefGenome
    16. negative regulation of apoptotic process Source: Ensembl
    17. neurological system process Source: Ensembl
    18. organelle organization Source: Ensembl
    19. piecemeal microautophagy of nucleus Source: RefGenome
    20. positive regulation of apoptotic process Source: UniProtKB
    21. positive regulation of autophagy Source: UniProtKB
    22. positive regulation of macroautophagy Source: BHF-UCL
    23. positive regulation of protein catabolic process Source: UniProtKB
    24. positive regulation of protein modification process Source: MGI
    25. post-embryonic development Source: Ensembl
    26. protein catabolic process Source: RefGenome
    27. protein lipidation Source: MGI
    28. protein modification by small protein conjugation Source: RefGenome
    29. protein transport Source: UniProtKB-KW
    30. protein ubiquitination Source: GOC
    31. pyramidal neuron development Source: Ensembl
    32. regulation of protein ubiquitination Source: Ensembl

    Keywords - Biological processi

    Autophagy, Protein transport, Transport, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like modifier-activating enzyme ATG7
    Alternative name(s):
    ATG12-activating enzyme E1 ATG7
    Autophagy-related protein 7
    Short name:
    APG7-like
    Short name:
    hAGP7
    Ubiquitin-activating enzyme E1-like protein
    Gene namesi
    Name:ATG7
    Synonyms:APG7L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:16935. ATG7.

    Subcellular locationi

    Cytoplasm By similarity. Preautophagosomal structure By similarity
    Note: Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme.By similarity

    GO - Cellular componenti

    1. axoneme Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: RefGenome
    4. pre-autophagosomal structure Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151F → D: Impairs conjugation activity; when associated with D-16 and D-17. 1 Publication
    Mutagenesisi16 – 161A → D: Impairs conjugation activity; when associated with D-15 and D-17. 1 Publication
    Mutagenesisi17 – 171P → D: Impairs conjugation activity; when associated with D-15 and D-16. 1 Publication

    Organism-specific databases

    PharmGKBiPA134983397.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 703702Ubiquitin-like modifier-activating enzyme ATG7PRO_0000212806Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Post-translational modificationi

    Acetylated by EP300.3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO95352.
    PaxDbiO95352.
    PRIDEiO95352.

    PTM databases

    PhosphoSiteiO95352.

    Expressioni

    Tissue specificityi

    Widely expressed, especially in kidney, liver, lymph nodes and bone marrow.1 Publication

    Inductioni

    Expression is up-regulated by the transcription factor HSF1.1 Publication

    Gene expression databases

    ArrayExpressiO95352.
    BgeeiO95352.
    CleanExiHS_ATG7.
    GenevestigatoriO95352.

    Organism-specific databases

    HPAiCAB018771.
    HPA007639.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with ATG3 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. Forms intermediate conjugates with ATG8-like proteins such as GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A. Interacts with EP300 acetyltransferase. Interacts with FOXO1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EEF1DP296922EBI-987834,EBI-358607
    GABARAPO951668EBI-987834,EBI-712001
    GABARAPL1Q9H0R86EBI-987834,EBI-746969
    GABARAPL2P605207EBI-987834,EBI-720116
    IRF2P143162EBI-987834,EBI-2866589
    MAP1LC3BQ9GZQ87EBI-987834,EBI-373144

    Protein-protein interaction databases

    BioGridi115787. 43 interactions.
    DIPiDIP-29759N.
    IntActiO95352. 14 interactions.
    STRINGi9606.ENSP00000346437.

    Structurei

    3D structure databases

    ProteinModelPortaliO95352.
    SMRiO95352. Positions 13-690.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi15 – 173FAP motif

    Domaini

    The C-terminal part of the protein is essential for the dimerization and interaction with ATG3 and ATG12.By similarity
    The N-terminal FAP motif (residues 15 to 17) is essential for the formation of the ATG89-PE and ATG5-ATG12 conjugates.1 Publication

    Sequence similaritiesi

    Belongs to the ATG7 family.Curated

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000162379.
    HOVERGENiHBG080877.
    InParanoidiO95352.
    KOiK08337.
    OMAiLGCQVAR.
    OrthoDBiEOG7X0VGG.
    PhylomeDBiO95352.
    TreeFamiTF105689.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006285. Atg7.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view]
    PANTHERiPTHR10953:SF3. PTHR10953:SF3. 1 hit.
    PfamiPF00899. ThiF. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 2 hits.
    TIGRFAMsiTIGR01381. E1_like_apg7. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95352-1) [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

    MAAATGDPGL SKLQFAPFSS ALDVGFWHEL TQKKLNEYRL DEAPKDIKGY    50
    YYNGDSAGLP ARLTLEFSAF DMSAPTPARC CPAIGTLYNT NTLESFKTAD 100
    KKLLLEQAAN EIWESIKSGT ALENPVLLNK FLLLTFADLK KYHFYYWFCY 150
    PALCLPESLP LIQGPVGLDQ RFSLKQIEAL ECAYDNLCQT EGVTALPYFL 200
    IKYDENMVLV SLLKHYSDFF QGQRTKITIG VYDPCNLAQY PGWPLRNFLV 250
    LAAHRWSSSF QSVEVVCFRD RTMQGARDVA HSIIFEVKLP EMAFSPDCPK 300
    AVGWEKNQKG GMGPRMVNLS ECMDPKRLAE SSVDLNLKLM CWRLVPTLDL 350
    DKVVSVKCLL LGAGTLGCNV ARTLMGWGVR HITFVDNAKI SYSNPVRQPL 400
    YEFEDCLGGG KPKALAAADR LQKIFPGVNA RGFNMSIPMP GHPVNFSSVT 450
    LEQARRDVEQ LEQLIESHDV VFLLMDTRES RWLPAVIAAS KRKLVINAAL 500
    GFDTFVVMRH GLKKPKQQGA GDLCPNHPVA SADLLGSSLF ANIPGYKLGC 550
    YFCNDVVAPG DSTRDRTLDQ QCTVSRPGLA VIAGALAVEL MVSVLQHPEG 600
    GYAIASSSDD RMNEPPTSLG LVPHQIRGFL SRFDNVLPVS LAFDKCTACS 650
    SKVLDQYERE GFNFLAKVFN SSHSFLEDLT GLTLLHQETQ AAEIWDMSDD 700
    ETI 703
    Length:703
    Mass (Da):77,960
    Last modified:May 1, 1999 - v1
    Checksum:iABBD1A29A6C58356
    GO
    Isoform 2 (identifier: O95352-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         626-652: Missing.

    Show »
    Length:676
    Mass (Da):75,002
    Checksum:i184E1A7A3B989524
    GO
    Isoform 3 (identifier: O95352-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         138-176: Missing.
         653-693: Missing.

    Show »
    Length:623
    Mass (Da):68,618
    Checksum:i2186C29D24B11D6E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101V → A in BAG64682. (PubMed:14702039)Curated
    Sequence conflicti346 – 3461P → L in BAG64682. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti471 – 4711V → A.
    Corresponds to variant rs36117895 [ dbSNP | Ensembl ].
    VAR_053014

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei138 – 17639Missing in isoform 3. 1 PublicationVSP_045206Add
    BLAST
    Alternative sequencei626 – 65227Missing in isoform 2. 1 PublicationVSP_013205Add
    BLAST
    Alternative sequencei653 – 69341Missing in isoform 3. 1 PublicationVSP_045207Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF094516 mRNA. Translation: AAC69630.1.
    AK303694 mRNA. Translation: BAG64682.1.
    AC020750 Genomic DNA. No translation available.
    AC022001 Genomic DNA. No translation available.
    AC026185 Genomic DNA. No translation available.
    AC083855 Genomic DNA. No translation available.
    BC000091 mRNA. Translation: AAH00091.1.
    AL122075 mRNA. Translation: CAB59250.1.
    CCDSiCCDS2605.1. [O95352-1]
    CCDS46752.1. [O95352-2]
    CCDS46753.1. [O95352-3]
    PIRiT34556.
    RefSeqiNP_001129503.2. NM_001136031.2. [O95352-2]
    NP_001138384.1. NM_001144912.1. [O95352-3]
    NP_006386.1. NM_006395.2. [O95352-1]
    UniGeneiHs.38032.

    Genome annotation databases

    EnsembliENST00000354449; ENSP00000346437; ENSG00000197548. [O95352-1]
    ENST00000354956; ENSP00000347042; ENSG00000197548. [O95352-2]
    ENST00000446450; ENSP00000412580; ENSG00000197548. [O95352-3]
    GeneIDi10533.
    KEGGihsa:10533.
    UCSCiuc003bwc.3. human. [O95352-1]
    uc003bwd.3. human. [O95352-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF094516 mRNA. Translation: AAC69630.1 .
    AK303694 mRNA. Translation: BAG64682.1 .
    AC020750 Genomic DNA. No translation available.
    AC022001 Genomic DNA. No translation available.
    AC026185 Genomic DNA. No translation available.
    AC083855 Genomic DNA. No translation available.
    BC000091 mRNA. Translation: AAH00091.1 .
    AL122075 mRNA. Translation: CAB59250.1 .
    CCDSi CCDS2605.1. [O95352-1 ]
    CCDS46752.1. [O95352-2 ]
    CCDS46753.1. [O95352-3 ]
    PIRi T34556.
    RefSeqi NP_001129503.2. NM_001136031.2. [O95352-2 ]
    NP_001138384.1. NM_001144912.1. [O95352-3 ]
    NP_006386.1. NM_006395.2. [O95352-1 ]
    UniGenei Hs.38032.

    3D structure databases

    ProteinModelPortali O95352.
    SMRi O95352. Positions 13-690.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115787. 43 interactions.
    DIPi DIP-29759N.
    IntActi O95352. 14 interactions.
    STRINGi 9606.ENSP00000346437.

    Chemistry

    ChEMBLi CHEMBL2321621.

    PTM databases

    PhosphoSitei O95352.

    Proteomic databases

    MaxQBi O95352.
    PaxDbi O95352.
    PRIDEi O95352.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354449 ; ENSP00000346437 ; ENSG00000197548 . [O95352-1 ]
    ENST00000354956 ; ENSP00000347042 ; ENSG00000197548 . [O95352-2 ]
    ENST00000446450 ; ENSP00000412580 ; ENSG00000197548 . [O95352-3 ]
    GeneIDi 10533.
    KEGGi hsa:10533.
    UCSCi uc003bwc.3. human. [O95352-1 ]
    uc003bwd.3. human. [O95352-2 ]

    Organism-specific databases

    CTDi 10533.
    GeneCardsi GC03P011313.
    HGNCi HGNC:16935. ATG7.
    HPAi CAB018771.
    HPA007639.
    MIMi 608760. gene.
    neXtProti NX_O95352.
    PharmGKBi PA134983397.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000162379.
    HOVERGENi HBG080877.
    InParanoidi O95352.
    KOi K08337.
    OMAi LGCQVAR.
    OrthoDBi EOG7X0VGG.
    PhylomeDBi O95352.
    TreeFami TF105689.

    Enzyme and pathway databases

    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    GeneWikii ATG7.
    GenomeRNAii 10533.
    NextBioi 39961.
    PROi O95352.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95352.
    Bgeei O95352.
    CleanExi HS_ATG7.
    Genevestigatori O95352.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR006285. Atg7.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view ]
    PANTHERi PTHR10953:SF3. PTHR10953:SF3. 1 hit.
    Pfami PF00899. ThiF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 2 hits.
    TIGRFAMsi TIGR01381. E1_like_apg7. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Glucose-induced autophagy of peroxisomes in Pichia pastoris requires a unique E1-like protein."
      Yuan W., Stromhaug P.E., Dunn W.A. Jr.
      Mol. Biol. Cell 10:1353-1366(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Kidney.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 2).
      Tissue: Placenta.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 179-703 (ISOFORM 1).
      Tissue: Testis.
    6. "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: FUNCTION, SUBUNIT, INTERACTION WITH ATG12; GABARAP; GABARAPL2 AND MAP1LC3A.
    7. "Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p homologs."
      Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H., Ueno T., Kominami E.
      Biochem. Biophys. Res. Commun. 292:256-262(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "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 AND ATG12.
      Tissue: Brain.
    9. "Phosphatidylserine in addition to phosphatidylethanolamine is an in vitro target of the mammalian Atg8 modifiers, LC3, GABARAP, and GATE-16."
      Sou Y.S., Tanida I., Komatsu M., Ueno T., Kominami E.
      J. Biol. Chem. 281:3017-3024(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GABARAP; GABARAPL2 AND MAP1LC3A.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "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, INTERACTION WITH EP300.
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Cytosolic FoxO1 is essential for the induction of autophagy and tumour suppressor activity."
      Zhao Y., Yang J., Liao W., Liu X., Zhang H., Wang S., Wang D., Feng J., Yu L., Zhu W.G.
      Nat. Cell Biol. 12:665-675(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXO1.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is essential for the E2-substrate reaction of LC3 lipidation."
      Tanida I., Yamasaki M., Komatsu M., Ueno T.
      Autophagy 8:88-97(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PHE-15; ALA-16 AND PRO-17.
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Heat shock factor 1 (HSF1) controls chemoresistance and autophagy through transcriptional regulation of autophagy-related protein 7 (ATG7)."
      Desai S., Liu Z., Yao J., Patel N., Chen J., Wu Y., Ahn E.E., Fodstad O., Tan M.
      J. Biol. Chem. 288:9165-9176(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiATG7_HUMAN
    AccessioniPrimary (citable) accession number: O95352
    Secondary accession number(s): B4E170
    , E9PB95, Q7L8L0, Q9BWP2, Q9UFH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3