Reviewed, UniProtKB/Swiss-Prot Q9NT62 (ATG3_HUMAN)

Names and origin

Protein names

Recommended name:
    Autophagy-related protein 3
Alternative name(s):
    APG3-like
      Short name=hApg3
    Protein PC3-96

Gene names

Name:	ATG3
Synonyms:	APG3, APG3L

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1
Subcellular location	Cytoplasm Ref.1.
Tissue specificity	Widely expressed, with a highest expression in heart, skeletal muscle, kidney, liver and placenta. Ref.1
Sequence similarities	Belongs to the ATG3 family.

Ontologies

Keywords
Biological process	Autophagy Protein transport Transport Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	autophagic vacuole assembly Inferred from sequence or structural similarity. Source: UniProtKB modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein targeting to membrane Inferred from sequence or structural similarity. Source: UniProtKB protein ubiquitination Ref.1 Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasmic ubiquitin ligase complex Ref.1 Inferred from physical interaction. Source: MGI cytosol Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	enzyme binding Ref.1 Inferred from physical interaction. Source: UniProtKB small conjugating protein ligase activity Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAPL2	P60520	1	EBI-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

Note: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 314	314	Autophagy-related protein 3		PRO_0000213569
Sites
	Active site	264	1	Glycyl thioester intermediate Potential
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.8
	Modified residue	18	1	Phosphotyrosine Ref.6
Natural variations
	Alternative sequence	290 – 314	25	LLIFL…RHFTM → PSLYVRLVAKWLLTIFFLRN LV in isoform 2.		VSP_013037
Experimental info
	Mutagenesis	264	1	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. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 40EFE88DB5FE3EAB	FASTA	314	35,864
	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
	Isoform 2. Checksum: F15A9F8BCBD021A1	FASTA	311	35,467
	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 GGELGVHMYP SLYVRLVAKW 310 LLTIFFLRNL V

References

	« Hide 'large scale' referencesShow '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 full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] 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. , 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.
[7]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[8]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00022254. IPI00449201.
PIR	T46276.
RefSeq	NP_071933.2.
UniGene	Hs.477126
3D structure databases
SMR	Q9NT62. Positions 27-309.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NT62. 6 interactions.
STRING	Q9NT62.
PTM databases
PhosphoSite	Q9NT62.
Proteomic databases
PRIDE	Q9NT62.
Genome annotation databases
Ensembl	ENST00000283290; ENSP00000283290; ENSG00000144848; Homo sapiens. [Genome view]
GeneID	64422.
KEGG	hsa:64422.
UCSC	uc003dzc.2. human. uc003dzd.1. human.
Organism-specific databases
CTD	64422.
GeneCards	GC03M113735.
H-InvDB	HIX0003548.
HGNC	HGNC:20962. ATG3.
MIM	609606. gene.
PharmGKB	PA134883444.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10145.
HOGENOM	HBG602769.
HOVERGEN	Q9NT62.
InParanoid	Q9NT62.
OMA	YHNTGIA.
OrthoDB	EOG9WWV4X.
PhylomeDB	Q9NT62.
Gene expression databases
ArrayExpress	Q9NT62.
Bgee	Q9NT62.
CleanEx	HS_ATG3.
Genevestigator	Q9NT62.
GermOnline	ENSG00000144848. Homo sapiens.
Family and domain databases
InterPro	IPR007135. Autophagy-rel_prot_3. IPR019461. Autophagy-rel_prot_3_C. IPR007134. Autophagy-rel_prot_3_N. [Graphical view]
Pfam	PF03987. Autophagy_act_C. 1 hit. PF10381. Autophagy_Cterm. 1 hit. PF03986. Autophagy_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	66413.
SOURCE	Search...

Entry information

Entry name

ATG3_HUMAN

Accession

Primary (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:	January 19, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.