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Reviewed, UniProtKB/Swiss-Prot Q9NT62 (ATG3_HUMAN)

Last modified September 2, 2008. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Autophagy-related protein 3
Alternative name(s):
    APG3-like
      Short name=hApg3
    Protein PC3-96
Gene names
Name: ATG3
Synonyms: APG3, APG3L
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (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 structure

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

Subcellular location

Cytoplasm.

Tissue specificity

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

Sequence similarities

Belongs to the ATG3 family.

Ontologies

Keywords

   Biological processAutophagy
Protein transport
Transport
Ubl conjugation pathway
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processautophagy Ref.1

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination Ref.1

Inferred from direct assay. Source: UniProtKB

   Cellular componentcytosol Ref.1

Inferred from direct assay. Source: UniProtKB

   Molecular functionenzyme binding Ref.1

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GABARAPL2P605201EBI-988094,EBI-720116

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NT62-1)

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.
Isoform 2 (identifier: Q9NT62-2)

The sequence of this isoform differs from the canonical sequence as follows:
     290-314: LLIFLKFVQAVIPTIEYDYTRHFTM → PSLYVRLVAKWLLTIFFLRNLV
Notes: No experimental confirmation available. Ref.4 (AAH02830) isoform 2 sequence differs from that shown due to a frameshift in position 311.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 314314Autophagy-related protein 3

Sites

Active site2641Glycyl thioester intermediate Potential

Amino acid modifications

Modified residue181Phosphotyrosine

Natural variations

Alternative sequence290 – 31425LLIFL…RHFTM → PSLYVRLVAKWLLTIFFLRN LV in isoform 2.

Experimental info

Mutagenesis2641C → 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

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 40EFE88DB5FE3EAB

FASTA31435,864
        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 

« Hide

Isoform 2 [UniParc].

Checksum: F15A9F8BCBD021A1
Show »

31135,467

References

« Hide 'large scale' references
[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: 11825910] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF CYS-264, SUBCELLULAR LOCATION, CHARACTERIZATION, 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]The German cDNA consortium
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-314 (ISOFORM 2).
[6]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-18, MASS SPECTROMETRY.

Cross-references

Sequence databases

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.
PIRT46276.
RefSeqNP_071933.2.
UniGeneHs.477126

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NT62.

PTM databases

PhosphoSiteQ9NT62.

Genome annotation databases

EnsemblENSG00000144848. Homo sapiens. [Contig view]
GeneID64422.
KEGGhsa:64422.

Organism-specific databases

H-InvDBHIX0003548.
HGNCHGNC:20962. ATG3.
MIM609606. gene.
PharmGKBPA134883444.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ9NT62.
HOVERGENQ9NT62.

Gene expression databases

ArrayExpressQ9NT62.
CleanExHS_ATG3.
GermOnlineENSG00000144848. Homo sapiens.

Family and domain databases

InterProIPR007135. Autophagy_C.
IPR007134. Autophagy_N.
[Graphical view]
PfamPF03987. Autophagy_C. 1 hit.
PF03986. Autophagy_N. 1 hit.
[Graphical view]
ProDomQ9NT62.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubQ9NT62.
SOURCESearch...
ProtoNetSearch...

Entry information

Entry nameATG3_HUMAN
AccessionPrimary (citable) accession number: Q9NT62
Secondary accession number(s): Q6PKC5, Q9H6L9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 1, 2000
Last modified: September 2, 2008
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents