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UniProtKB/Swiss-Prot entry Q9NT62


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ATG3_HUMAN
Primary accession number Q9NT62
Secondary accession numbers Q6PKC5 Q9H6L9
Integrated into Swiss-Prot on March 15, 2005
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 48)
Name and origin of the protein
Protein name Autophagy-related protein 3
Synonyms APG3-like
hApg3
Protein PC3-96
Gene name
Name: ATG3
Synonyms: APG3, APG3L
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF CYS-264, SUBCELLULAR LOCATION, CHARACTERIZATION, AND INTERACTION WITH ATG7 AND ATG12.
TISSUE=Brain;
DOI=10.1074/jbc.M200385200; PubMed=11825910 [NCBI, ExPASy, EBI, Israel, Japan]
Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
"Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation of hApg12p to hApg5p.";
J. Biol. Chem. 277:13739-13744(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
Wu B.X., Li Y., Laser M., Crosson C.E., Hazard E.S. III, Ma J.X.;
"Cloning and characterization of human PC3-96 gene.";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
The German cDNA consortium;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-314 (ISOFORM 2).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-18, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
Comments
  • FUNCTION: GABARAPL1 (GABARAPL2 or GABARAP or MAP1LC3)-modifier protein conjugating enzyme involved in its E2-like covalent binding to PE. ATG7 (E1-like enzyme) facilitates this reaction by forming an E1-E2 complex with ATG3 (E2-like enzyme). Preferred substrate is MAP1LC3A. Formation of the GABARAPL1-PE conjugate is essential for autophagy.
  • SUBUNIT: Interacts with ATG7 and ATG12. The complex, composed of ATG3 and ATG7, plays a role in the conjugation of ATG12 to ATG5.
  • INTERACTION:
    P60520:GABARAPL2; NbExp=1; IntAct=EBI-988094, EBI-720116;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9NT62-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9NT62-2
    Note: No experimental confirmation available. Ref.4 (AAH02830) isoform 2 sequence differs from that shown due to a frameshift in position 311.
    Features which should be applied to build the isoform sequence: VSP_013037.
  • TISSUE SPECIFICITY: Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta.
  • SIMILARITY: Belongs to the ATG3 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB079384; BAB90843.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF202092; AAG35611.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL137515; CAB70781.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002830; AAH02830.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC024221; AAH24221.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK025778; BAB15237.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T46276; T46276.
RefSeq NP_071933.2; -.
UniGene Hs.477126
3D structure databases
ModBase Q9NT62.
Protein-protein interaction databases
IntAct Q9NT62; -.
PTM databases
PhosphoSite Q9NT62; -.
Organism-specific databases
H-InvDB HIX0003548; -.
HGNC HGNC:20962; ATG3.
GeneLynx ATG3; Homo sapiens.
GenAtlas ATG3.
MIM 609606; gene. [NCBI / EBI]
PharmGKB PA134883444; -.
GeneCards Q9NT62.
Gene expression databases
ArrayExpress Q9NT62; -.
CleanEx HS_ATG3; -.
GermOnline ENSG00000144848; Homo sapiens.
Ontologies
GO
GO:0000153; Cellular component: cytoplasmic ubiquitin ligase complex (inferred from physical interaction from MGI).
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0019899; Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0019787; Molecular function: small conjugating protein ligase activity (inferred from direct assay from MGI).
GO:0006914; Biological process: autophagy (inferred from sequence or structural similarity from UniProtKB).
GO:0016567; Biological process: protein ubiquitination (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR007135; Autophagy_C.
IPR007134; Autophagy_N.
Graphical view of domain structure.
Pfam PF03987; Autophagy_C; 1.
PF03986; Autophagy_N; 1.
Pfam graphical view of domain structure.
BLOCKS Q9NT62.
Genome annotation databases
Ensembl ENSG00000144848; Homo sapiens. [Contig view]
GeneID 64422; -.
KEGG hsa:64422; -.
Phylogenomic databases
HOGENOM Q9NT62; -.
HOVERGEN Q9NT62; -.
Other
LinkHub Q9NT62; -.
SOURCE ATG3; Homo sapiens.
ProtoNet Q9NT62.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Autophagy; Cytoplasm; Phosphoprotein; Protein transport; Transport; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   314  314     Autophagy-related protein 3. PRO_0000213569
ACT_SITE   264   264        Glycyl thioester intermediate (Potential). 
MOD_RES   18    18        Phosphotyrosine. 
VAR_SEQ   290   314        LLIFLKFVQAVIPTIEYDYTRHFTM -> PSLYVRLVAKWLLTIFFLRNLV (in isoform 2). VSP_013037
MUTAGEN   264   264        C->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. 
Sequence information
Length: 314 AA [This is the length of the unprocessed precursor] Molecular weight: 35864 Da [This is the MW of the unprocessed precursor] CRC64: 40EFE88DB5FE3EAB [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWQWATGEE 

        70         80         90        100        110        120 
LKVKAYLPTG KQFLVTKNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT YHNTGITGIT 

       130        140        150        160        170        180 
EAVKEITLEN KDNIRLQDCS ALCEEEEDED EGEAADMEEY EESGLLETDE ATLDTRKIVE 

       190        200        210        220        230        240 
ACKAKTDAGG EDAILQTRTY DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH 

       250        260        270        280        290        300 
VKKTVTIENH PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV 

       310 
IPTIEYDYTR HFTM 

Q9NT62 in FASTA format

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