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Q9D906

- ATG7_MOUSE

UniProt

Q9D906 - ATG7_MOUSE

Protein

Ubiquitin-like modifier-activating enzyme ATG7

Gene

Atg7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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.13 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei567 – 5671Glycyl thioester intermediateCurated

    GO - Molecular functioni

    1. Atg12 activating enzyme activity Source: UniProtKB
    2. Atg8 activating enzyme Source: RefGenome
    3. protein binding Source: MGI
    4. ubiquitin activating enzyme activity Source: MGI

    GO - Biological processi

    1. adult walking behavior Source: MGI
    2. autophagy Source: MGI
    3. cardiac muscle cell development Source: MGI
    4. cellular amino acid metabolic process Source: MGI
    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: MGI
    9. cerebellar Purkinje cell layer development Source: MGI
    10. cerebral cortex development Source: MGI
    11. C-terminal protein lipidation Source: RefGenome
    12. late nucleophagy Source: RefGenome
    13. liver development Source: MGI
    14. macroautophagy Source: RefGenome
    15. membrane organization Source: MGI
    16. mitochondrion degradation Source: RefGenome
    17. mitochondrion organization Source: MGI
    18. negative regulation of apoptotic process Source: MGI
    19. negative stranded viral RNA replication Source: MGI
    20. neurological system process Source: MGI
    21. neuron projection development Source: MGI
    22. organelle organization Source: MGI
    23. piecemeal microautophagy of nucleus Source: RefGenome
    24. positive regulation of apoptotic process Source: UniProtKB
    25. positive regulation of autophagy Source: UniProtKB
    26. positive regulation of mucus secretion Source: MGI
    27. positive regulation of protein catabolic process Source: UniProtKB
    28. positive regulation of protein modification process Source: MGI
    29. post-embryonic development Source: MGI
    30. protein catabolic process Source: MGI
    31. protein lipidation Source: MGI
    32. protein modification by small protein conjugation Source: MGI
    33. protein transport Source: UniProtKB-KW
    34. protein ubiquitination Source: GOC
    35. pyramidal neuron development Source: MGI
    36. regulation of protein ubiquitination Source: MGI
    37. response to starvation Source: MGI

    Keywords - Biological processi

    Autophagy, Protein transport, Transport, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_199115. 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:
    mAGP7
    Ubiquitin-activating enzyme E1-like protein
    Gene namesi
    Name:Atg7
    Synonyms:Apg7l
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1921494. 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.1 Publication

    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

    Disruption phenotypei

    Leads to hepatomegaly in liver and accumulation of abnormal organelles in hepatic cells.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi567 – 5671C → S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG7 (E1-like enzyme) and GABARAPL1 (MAP1LC3, GABARAP or GABARAPL; substrates), a stable complex with an O-ester bond is formed. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 698698Ubiquitin-like modifier-activating enzyme ATG7PRO_0000212807Add
    BLAST

    Post-translational modificationi

    Acetylated by EP300.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9D906.
    PaxDbiQ9D906.
    PRIDEiQ9D906.

    PTM databases

    PhosphoSiteiQ9D906.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiQ9D906.
    CleanExiMM_ATG7.
    GenevestigatoriQ9D906.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with ATG3, FOXO1 and EP300 acetyltransferase. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. Interacts with FOXO1 By similarity. Forms intermediate conjugates with ATG8 family proteins such as GABARAP, GABARAPL1, GABARAPL2, MAP1LC3A, or GABARAPL1. Interacts with ATG12.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi216602. 6 interactions.
    IntActiQ9D906. 2 interactions.
    MINTiMINT-4615793.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D906.
    SMRiQ9D906. Positions 9-685.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi11 – 133FAP 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 11 to 13) is essential for the formation of the ATG89-PE and ATG5-ATG12 conjugates.By similarity

    Sequence similaritiesi

    Belongs to the ATG7 family.Curated

    Phylogenomic databases

    eggNOGiCOG0476.
    GeneTreeiENSGT00390000017509.
    HOGENOMiHOG000162379.
    HOVERGENiHBG080877.
    InParanoidiQ9D906.
    KOiK08337.
    OrthoDBiEOG7X0VGG.
    PhylomeDBiQ9D906.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q9D906-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDPGLAKLQ FAPFNSALDV GFWHELTQKK LNEYRLDEAP KDIKGYYYNG    50
    DSAGLPTRLT LEFSAFDMSA STPAHCCPAM GTLHNTNTLE AFKTADKKLL 100
    LEQSANEIWE AIKSGAALEN PMLLNKFLLL TFADLKKYHF YYWFCCPALC 150
    LPESIPLIRG PVSLDQRLSP KQIQALEHAY DDLCRAEGVT ALPYFLFKYD 200
    DDTVLVSLLK HYSDFFQGQR TKITVGVYDP CNLAQYPGWP LRNFLVLAAH 250
    RWSGSFQSVE VLCFRDRTMQ GARDVTHSII FEVKLPEMAF SPDCPKAVGW 300
    EKNQKGGMGP RMVNLSGCMD PKRLAESSVD LNLKLMCWRL VPTLDLDKVV 350
    SVKCLLLGAG TLGCNVARTL MGWGVRHVTF VDNAKISYSN PVRQPLYEFE 400
    DCLGGGKPKA LAAAERLQKI FPGVNARGFN MSIPMPGHPV NFSDVTMEQA 450
    RRDVEQLEQL IDNHDVIFLL MDTRESRWLP TVIAASKRKL VINAALGFDT 500
    FVVMRHGLKK PKQQGAGDLC PSHLVAPADL GSSLFANIPG YKLGCYFCND 550
    VVAPGDSTRD RTLDQQCTVS RPGLAVIAGA LAVELMVSVL QHPEGGYAIA 600
    SSSDDRMNEP PTSLGLVPHQ IRGFLSRFDN VLPVSLAFDK CTACSPKVLD 650
    QYEREGFTFL AKVFNSSHSF LEDLTGLTLL HQETQAAEIW DMSDEETV 698
    Length:698
    Mass (Da):77,520
    Last modified:June 1, 2001 - v1
    Checksum:i79D94EA7464C6ADB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221F → L in BAC10416. (PubMed:11890701)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079385 mRNA. Translation: BAC10416.1.
    AK007484 mRNA. Translation: BAB25060.1.
    AK035604 mRNA. Translation: BAC29122.1.
    AK161133 mRNA. Translation: BAE36208.1.
    AK170769 mRNA. Translation: BAE42018.1.
    AK172272 mRNA. Translation: BAE42917.1.
    BC058597 mRNA. Translation: AAH58597.1.
    CCDSiCCDS39598.1.
    RefSeqiNP_001240646.1. NM_001253717.1.
    NP_001240647.1. NM_001253718.1.
    NP_083111.1. NM_028835.4.
    XP_006506772.1. XM_006506709.1.
    XP_006506773.1. XM_006506710.1.
    UniGeneiMm.275332.

    Genome annotation databases

    EnsembliENSMUST00000032457; ENSMUSP00000032457; ENSMUSG00000030314.
    ENSMUST00000182793; ENSMUSP00000138137; ENSMUSG00000030314.
    ENSMUST00000182902; ENSMUSP00000138651; ENSMUSG00000030314.
    GeneIDi74244.
    KEGGimmu:74244.
    UCSCiuc009dhz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079385 mRNA. Translation: BAC10416.1 .
    AK007484 mRNA. Translation: BAB25060.1 .
    AK035604 mRNA. Translation: BAC29122.1 .
    AK161133 mRNA. Translation: BAE36208.1 .
    AK170769 mRNA. Translation: BAE42018.1 .
    AK172272 mRNA. Translation: BAE42917.1 .
    BC058597 mRNA. Translation: AAH58597.1 .
    CCDSi CCDS39598.1.
    RefSeqi NP_001240646.1. NM_001253717.1.
    NP_001240647.1. NM_001253718.1.
    NP_083111.1. NM_028835.4.
    XP_006506772.1. XM_006506709.1.
    XP_006506773.1. XM_006506710.1.
    UniGenei Mm.275332.

    3D structure databases

    ProteinModelPortali Q9D906.
    SMRi Q9D906. Positions 9-685.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 216602. 6 interactions.
    IntActi Q9D906. 2 interactions.
    MINTi MINT-4615793.

    PTM databases

    PhosphoSitei Q9D906.

    Proteomic databases

    MaxQBi Q9D906.
    PaxDbi Q9D906.
    PRIDEi Q9D906.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032457 ; ENSMUSP00000032457 ; ENSMUSG00000030314 .
    ENSMUST00000182793 ; ENSMUSP00000138137 ; ENSMUSG00000030314 .
    ENSMUST00000182902 ; ENSMUSP00000138651 ; ENSMUSG00000030314 .
    GeneIDi 74244.
    KEGGi mmu:74244.
    UCSCi uc009dhz.2. mouse.

    Organism-specific databases

    CTDi 10533.
    MGIi MGI:1921494. Atg7.

    Phylogenomic databases

    eggNOGi COG0476.
    GeneTreei ENSGT00390000017509.
    HOGENOMi HOG000162379.
    HOVERGENi HBG080877.
    InParanoidi Q9D906.
    KOi K08337.
    OrthoDBi EOG7X0VGG.
    PhylomeDBi Q9D906.
    TreeFami TF105689.

    Enzyme and pathway databases

    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi ATG7. mouse.
    NextBioi 340222.
    PROi Q9D906.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D906.
    CleanExi MM_ATG7.
    Genevestigatori Q9D906.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN GABARAPL1-ATG7 INTERMEDIATE CONJUGATE FORMATION, TISSUE SPECIFICITY, INTERACTION WITH ATG12, MUTAGENESIS OF CYS-567.
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Pancreas, Spleen and Urinary bladder.
    3. "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].
      Tissue: Eye.
    4. "Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated yeast two-hybrid method."
      Mizushima N., Yoshimori T., Ohsumi Y.
      FEBS Lett. 532:450-454(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATG10 AND ATG12.
    5. "Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8."
      Yu L., Alva A., Su H., Dutt P., Freundt E., Welsh S., Baehrecke E.H., Lenardo M.J.
      Science 304:1500-1502(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice."
      Komatsu M., Waguri S., Ueno T., Iwata J., Murata S., Tanida I., Ezaki J., Mizushima N., Ohsumi Y., Uchiyama Y., Kominami E., Tanaka K., Chiba T.
      J. Cell Biol. 169:425-434(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation mediated by human Atg4B, Atg7 and Atg3."
      Tanida I., Sou Y.S., Minematsu-Ikeguchi N., Ueno T., Kominami E.
      FEBS J. 273:2553-2562(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GABARAPL1.
    8. "Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration."
      Komatsu M., Wang Q.J., Holstein G.R., Friedrich V.L. Jr., Iwata J., Kominami E., Chait B.T., Tanaka K., Yue Z.
      Proc. Natl. Acad. Sci. U.S.A. 104:14489-14494(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation."
      Zhang J., Randall M.S., Loyd M.R., Dorsey F.C., Kundu M., Cleveland J.L., Ney P.A.
      Blood 114:157-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: SUBCELLULAR LOCATION.
    11. Cited for: FUNCTION.
    12. "Adipose-specific deletion of autophagy-related gene 7 (atg7) in mice reveals a role in adipogenesis."
      Zhang Y., Goldman S., Baerga R., Zhao Y., Komatsu M., Jin S.
      Proc. Natl. Acad. Sci. U.S.A. 106:19860-19865(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell death."
      Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C., Debnath J.
      Cell 142:590-600(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Atg7 induces basal autophagy and rescues autophagic deficiency in CryABR120G cardiomyocytes."
      Pattison J.S., Osinska H., Robbins J.
      Circ. Res. 109:151-160(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. Cited for: FUNCTION.
    16. "Lack of intestinal epithelial atg7 affects paneth cell granule formation but does not compromise immune homeostasis in the gut."
      Wittkopf N., Gunther C., Martini E., Waldner M., Amann K.U., Neurath M.F., Becker C.
      Clin. Dev. Immunol. 2012:278059-278059(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Atg7 modulates p53 activity to regulate cell cycle and survival during metabolic stress."
      Lee I.H., Kawai Y., Fergusson M.M., Rovira I.I., Bishop A.J., Motoyama N., Cao L., Finkel T.
      Science 336:225-228(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiATG7_MOUSE
    AccessioniPrimary (citable) accession number: Q9D906
    Secondary accession number(s): Q3TCD9, Q8K4Q5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3