Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9NT62

- ATG3_HUMAN

UniProt

Q9NT62 - ATG3_HUMAN

Protein

Ubiquitin-like-conjugating enzyme ATG3

Gene

ATG3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8-like proteins from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8-like proteins. The formation of the ATG8-phosphatidylethanolamine conjugates is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). Preferred substrate is MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei169 – 1702Cleavage; by CASP8
    Active sitei264 – 2641Glycyl thioester intermediate1 Publication

    GO - Molecular functioni

    1. Atg12 ligase activity Source: UniProtKB
    2. Atg8 ligase activity Source: UniProtKB
    3. enzyme binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. small conjugating protein ligase activity Source: MGI

    GO - Biological processi

    1. autophagic vacuole assembly Source: UniProtKB
    2. cellular protein modification process Source: MGI
    3. mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
    4. mitochondrion degradation Source: RefGenome
    5. nucleophagy Source: RefGenome
    6. protein targeting to membrane Source: UniProtKB
    7. protein ubiquitination Source: UniProtKB
    8. regulation of cilium assembly Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Autophagy, Protein transport, Transport, Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like-conjugating enzyme ATG3 (EC:6.3.2.-)
    Alternative name(s):
    Autophagy-related protein 3
    Short name:
    APG3-like
    Short name:
    hApg3
    Protein PC3-96
    Gene namesi
    Name:ATG3
    Synonyms:APG3, APG3L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:20962. ATG3.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasmic ubiquitin ligase complex Source: MGI
    2. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi264 – 2641C → S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and GABARAPL1/APG8L (substrate), a stable complex with an O-ester bond is formed. 1 Publication

    Organism-specific databases

    PharmGKBiPA134883444.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 314314Ubiquitin-like-conjugating enzyme ATG3PRO_0000213569Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Cross-linki243 – 243Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)By similarity

    Post-translational modificationi

    Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a role in regulation of mitochondrial homeostasis and cell death, while it is not involved in PE-conjugation to ATG8-like proteins and autophagy.
    Cleaved by CASP8 upon death ligand binding such as tumor necrosis factor-alpha. CASP8 cleavage blocks survival-related autophagy and favors apoptosis.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NT62.
    PaxDbiQ9NT62.
    PRIDEiQ9NT62.

    PTM databases

    PhosphoSiteiQ9NT62.

    Expressioni

    Tissue specificityi

    Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta.1 Publication

    Gene expression databases

    ArrayExpressiQ9NT62.
    BgeeiQ9NT62.
    CleanExiHS_ATG3.
    GenevestigatoriQ9NT62.

    Organism-specific databases

    HPAiCAB037260.

    Interactioni

    Subunit structurei

    Interacts with ATG7 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5. Interacts with FNBP1L.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPO951665EBI-988094,EBI-712001
    GABARAPL1Q9H0R83EBI-988094,EBI-746969
    GABARAPL2P605205EBI-988094,EBI-720116
    MAP1LC3BQ9GZQ87EBI-988094,EBI-373144
    TECPR1Q7Z6L13EBI-988094,EBI-2946676

    Protein-protein interaction databases

    BioGridi122171. 32 interactions.
    DIPiDIP-35052N.
    IntActiQ9NT62. 20 interactions.
    STRINGi9606.ENSP00000283290.

    Structurei

    Secondary structure

    1
    314
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi157 – 1637

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NAWX-ray2.20D/H/L/P140-170[»]
    ProteinModelPortaliQ9NT62.
    SMRiQ9NT62. Positions 28-84, 193-309.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi166 – 1694Caspase cleavage motif LETD

    Sequence similaritiesi

    Belongs to the ATG3 family.Curated

    Phylogenomic databases

    eggNOGiNOG237080.
    HOGENOMiHOG000234613.
    HOVERGENiHBG080876.
    InParanoidiQ9NT62.
    KOiK08343.
    OMAiADEWVET.
    OrthoDBiEOG7VMP5R.
    PhylomeDBiQ9NT62.
    TreeFamiTF105903.

    Family and domain databases

    InterProiIPR007135. Autophagy-rel_prot_3.
    IPR019461. Autophagy-rel_prot_3_C.
    IPR007134. Autophagy-rel_prot_3_N.
    [Graphical view]
    PfamiPF03987. Autophagy_act_C. 1 hit.
    PF10381. Autophagy_Cterm. 1 hit.
    PF03986. Autophagy_N. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NT62-1) [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

    MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC    50
    PTWQWATGEE LKVKAYLPTG KQFLVTKNVP CYKRCKQMEY SDELEAIIEE 100
    DDGDGGWVDT YHNTGITGIT EAVKEITLEN KDNIRLQDCS ALCEEEEDED 150
    EGEAADMEEY EESGLLETDE ATLDTRKIVE ACKAKTDAGG EDAILQTRTY 200
    DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH VKKTVTIENH 250
    PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV 300
    IPTIEYDYTR HFTM 314
    Length:314
    Mass (Da):35,864
    Last modified:October 1, 2000 - v1
    Checksum:i40EFE88DB5FE3EAB
    GO
    Isoform 2 (identifier: Q9NT62-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         290-314: LLIFLKFVQAVIPTIEYDYTRHFTM → PSLYVRLVAKWLLTIFFLRNLV

    Note: No experimental confirmation available.Curated

    Show »
    Length:311
    Mass (Da):35,467
    Checksum:iF15A9F8BCBD021A1
    GO

    Sequence cautioni

    The sequence AAH02830.1 differs from that shown. Reason: Frameshift at position 290.
    Isoform 2 : The sequence AAH02830.1 differs from that shown. Reason: Frameshift at position 311.
    The sequence BAB15237.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei290 – 31425LLIFL…RHFTM → PSLYVRLVAKWLLTIFFLRN LV in isoform 2. 2 PublicationsVSP_013037Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079384 mRNA. Translation: BAB90843.1.
    AF202092 mRNA. Translation: AAG35611.1.
    AL137515 mRNA. Translation: CAB70781.1.
    BC002830 mRNA. Translation: AAH02830.1. Frameshift.
    BC024221 mRNA. Translation: AAH24221.1.
    AK025778 mRNA. Translation: BAB15237.1. Different initiation.
    CCDSiCCDS2966.1. [Q9NT62-1]
    CCDS63721.1. [Q9NT62-2]
    PIRiT46276.
    RefSeqiNP_001265641.1. NM_001278712.1. [Q9NT62-2]
    NP_071933.2. NM_022488.4. [Q9NT62-1]
    UniGeneiHs.477126.

    Genome annotation databases

    EnsembliENST00000283290; ENSP00000283290; ENSG00000144848. [Q9NT62-1]
    ENST00000402314; ENSP00000385943; ENSG00000144848. [Q9NT62-2]
    GeneIDi64422.
    KEGGihsa:64422.
    UCSCiuc003dzc.3. human. [Q9NT62-2]
    uc003dzd.3. human. [Q9NT62-1]

    Polymorphism databases

    DMDMi61212142.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB079384 mRNA. Translation: BAB90843.1 .
    AF202092 mRNA. Translation: AAG35611.1 .
    AL137515 mRNA. Translation: CAB70781.1 .
    BC002830 mRNA. Translation: AAH02830.1 . Frameshift.
    BC024221 mRNA. Translation: AAH24221.1 .
    AK025778 mRNA. Translation: BAB15237.1 . Different initiation.
    CCDSi CCDS2966.1. [Q9NT62-1 ]
    CCDS63721.1. [Q9NT62-2 ]
    PIRi T46276.
    RefSeqi NP_001265641.1. NM_001278712.1. [Q9NT62-2 ]
    NP_071933.2. NM_022488.4. [Q9NT62-1 ]
    UniGenei Hs.477126.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NAW X-ray 2.20 D/H/L/P 140-170 [» ]
    ProteinModelPortali Q9NT62.
    SMRi Q9NT62. Positions 28-84, 193-309.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122171. 32 interactions.
    DIPi DIP-35052N.
    IntActi Q9NT62. 20 interactions.
    STRINGi 9606.ENSP00000283290.

    PTM databases

    PhosphoSitei Q9NT62.

    Polymorphism databases

    DMDMi 61212142.

    Proteomic databases

    MaxQBi Q9NT62.
    PaxDbi Q9NT62.
    PRIDEi Q9NT62.

    Protocols and materials databases

    DNASUi 64422.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000283290 ; ENSP00000283290 ; ENSG00000144848 . [Q9NT62-1 ]
    ENST00000402314 ; ENSP00000385943 ; ENSG00000144848 . [Q9NT62-2 ]
    GeneIDi 64422.
    KEGGi hsa:64422.
    UCSCi uc003dzc.3. human. [Q9NT62-2 ]
    uc003dzd.3. human. [Q9NT62-1 ]

    Organism-specific databases

    CTDi 64422.
    GeneCardsi GC03M112251.
    HGNCi HGNC:20962. ATG3.
    HPAi CAB037260.
    MIMi 609606. gene.
    neXtProti NX_Q9NT62.
    PharmGKBi PA134883444.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG237080.
    HOGENOMi HOG000234613.
    HOVERGENi HBG080876.
    InParanoidi Q9NT62.
    KOi K08343.
    OMAi ADEWVET.
    OrthoDBi EOG7VMP5R.
    PhylomeDBi Q9NT62.
    TreeFami TF105903.

    Miscellaneous databases

    GenomeRNAii 64422.
    NextBioi 66413.
    PROi Q9NT62.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NT62.
    Bgeei Q9NT62.
    CleanExi HS_ATG3.
    Genevestigatori Q9NT62.

    Family and domain databases

    InterProi IPR007135. Autophagy-rel_prot_3.
    IPR019461. Autophagy-rel_prot_3_C.
    IPR007134. Autophagy-rel_prot_3_N.
    [Graphical view ]
    Pfami PF03987. Autophagy_act_C. 1 hit.
    PF10381. Autophagy_Cterm. 1 hit.
    PF03986. Autophagy_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF CYS-264, SUBCELLULAR LOCATION, FUNCTION, ACTIVE SITE, INTERACTION WITH ATG7 AND ATG12.
      Tissue: Brain.
    2. "Cloning and characterization of human PC3-96 gene."
      Wu B.X., Li Y., Laser M., Crosson C.E., Hazard E.S. III, Ma J.X.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Retina.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORMS 1 AND 2).
      Tissue: Lung and Lymph.
    5. "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] OF 118-314 (ISOFORM 2).
    6. "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: FUNCTION, INTERACTION WITH THE ATG12-ATG5 CONJUGATE.
    7. "The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation, facilitates MAP-LC3 modification."
      Nemoto T., Tanida I., Tanida-Miyake E., Minematsu-Ikeguchi N., Yokota M., Ohsumi M., Ueno T., Kominami E.
      J. Biol. Chem. 278:39517-39526(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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.
    11. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "A novel hybrid yeast-human network analysis reveals an essential role for FNBP1L in antibacterial autophagy."
      Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J., Podolsky D.K., Xavier R.J.
      J. Immunol. 182:4917-4930(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FNBP1L.
    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, INTERACTION WITH ATG12.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Cleavage of Atg3 protein by caspase-8 regulates autophagy during receptor-activated cell death."
      Oral O., Oz-Arslan D., Itah Z., Naghavi A., Deveci R., Karacali S., Gozuacik D.
      Apoptosis 17:810-820(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, CLEAVAGE BY CASP8.
    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: INTERACTION WITH ATG3 AND ATG12.
    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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiATG3_HUMAN
    AccessioniPrimary (citable) accession number: Q9NT62
    Secondary accession number(s): Q6PKC5, Q9H6L9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 15, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 109 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

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3