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P40344 (ATG3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Autophagy-related protein 3
Alternative name(s):
Autophagy-related E2-like conjugation enzyme ATG3
Gene names
Name:ATG3
Synonyms:APG3, AUT1
Ordered Locus Names:YNR007C
ORF Names:N2040
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as 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. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.27 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35

Enzyme regulation

ATG12-ATG5 induces reorientation of the ATG3 structure, increasing conjugation activity of ATG3. Ref.34

Subunit structure

Monomer. Interacts with ATG8 through an intermediate thioester bond between Cys-234 and the C-terminal Gly of ATG8. Also interacts with the 40 amino acid C-terminal region of the E1-like ATG7 enzyme. Interacts also with the ATG12-ATG5 conjugate. Ref.8 Ref.10 Ref.12 Ref.20 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.34 Ref.35

Subcellular location

Cytoplasm Ref.11 Ref.14.

Induction

Expression is increased during filamentous growth and controlled by the RSF2 transcription factor. Ref.19 Ref.26 Ref.34

Domain

The N-teminal region (residues 1-7) is involved in phosphatidylethanolamine-binding and is required for ATG8-PE conjugation. Ref.25 Ref.27 Ref.35

The flexible region (FR) is required for ATG7-binding. Ref.25 Ref.27 Ref.35

The handle region (HR) contains the ATG8 interaction motif (AIM) and mediates binding to ATG8. It is crucial for the cytoplasm-to-vacuole targeting pathway. Ref.25 Ref.27 Ref.35

Post-translational modification

Acetylated by NuA4 complex acetyltransferase ESA1 at Lys-19 and Lys-48. Acetylation regulates autophagy by controlling ATG8 interaction and lipidation. Deacetylated by histone deacetylase RPD3. Ref.24 Ref.33

Miscellaneous

Present with 3610 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ATG3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATG7P388624EBI-3381,EBI-2677
ATG8P381823EBI-3381,EBI-2684

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Autophagy-related protein 3
PRO_0000213586

Regions

Region1 – 77PE-binding
Region83 – 16381Flexible region
Region238 – 28548Handle region
Motif270 – 2734ATG8 interaction motif (AIM)

Sites

Active site2341Glycyl thioester intermediate Potential

Amino acid modifications

Modified residue191N6-acetyllysine; by ESA1 Ref.33
Modified residue481N6-acetyllysine; by ESA1 Ref.33

Experimental info

Mutagenesis2131T → A: Decreases ATG8-PE comjugation and autophagy. Ref.34
Mutagenesis2341C → A: Loss of interaction with ATG8 and defect in autophagy and Cvt pathway. Ref.8 Ref.16
Mutagenesis2341C → S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG3 (E2-like enzyme) and ATG8 (substrate), a stable complex with an O-ester bond is formed. Ref.8 Ref.16
Mutagenesis2701W → A: Decreases interaction with ATG8. Ref.27
Mutagenesis2721D → A: Decreases interaction with ATG8. Ref.27
Mutagenesis2731L → A: Decreases interaction with ATG8. Ref.27

Secondary structure

.................................... 310
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P40344 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 52CCFB216B18CF0C

FASTA31035,887
        10         20         30         40         50         60 
MIRSTLSSWR EYLTPITHKS TFLTTGQITP EEFVQAGDYL CHMFPTWKWN EESSDISYRD 

        70         80         90        100        110        120 
FLPKNKQFLI IRKVPCDKRA EQCVEVEGPD VIMKGFAEDG DEDDVLEYIG SETEHVQSTP 

       130        140        150        160        170        180 
AGGTKDSSID DIDELIQDME IKEEDENDDT EEFNAKGGLA KDMAQERYYD LYIAYSTSYR 

       190        200        210        220        230        240 
VPKMYIVGFN SNGSPLSPEQ MFEDISADYR TKTATIEKLP FYKNSVLSVS IHPCKHANVM 

       250        260        270        280        290        300 
KILLDKVRVV RQRRRKELQE EQELDGVGDW EDLQDDIDDS LRVDQYLIVF LKFITSVTPS 

       310 
IQHDYTMEGW 

« Hide

References

« Hide 'large scale' references
[1]"AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae."
Schlumpberger M., Schaeffeler E., Straub M., Bredschneider M., Wolf D.H., Thumm M.
J. Bacteriol. 179:1068-1076(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Twelve open reading frames revealed in the 23.6 kb segment flanking the centromere on the Saccharomyces cerevisiae chromosome XIV right arm."
Verhasselt P., Aert R., Voet M., Volckaert G.
Yeast 10:1355-1361(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. expand/collapse author list , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae."
Tsukada M., Ohsumi Y.
FEBS Lett. 333:169-174(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Isolation of autophagocytosis mutants of Saccharomyces cerevisiae."
Thumm M., Egner R., Koch B., Schlumpberger M., Straub M., Veenhuis M., Wolf D.H.
FEBS Lett. 349:275-280(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The breakdown of autophagic vesicles inside the vacuole depends on Aut4p."
Suriapranata I., Epple U.D., Bernreuther D., Bredschneider M., Sovarasteanu K., Thumm M.
J. Cell Sci. 113:4025-4033(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"A ubiquitin-like system mediates protein lipidation."
Ichimura Y., Kirisako T., Takao T., Satomi Y., Shimonishi Y., Ishihara N., Mizushima N., Tanida I., Kominami E., Ohsumi M., Noda T., Ohsumi Y.
Nature 408:488-492(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG8, MUTAGENESIS OF CYS-234.
[9]"The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation."
Suzuki K., Kirisako T., Kamada Y., Mizushima N., Noda T., Ohsumi Y.
EMBO J. 20:5971-5981(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The C-terminal region of an Apg7p/Cvt2p is required for homodimerization and is essential for its E1 activity and E1-E2 complex formation."
Komatsu M., Tanida I., Ueno T., Ohsumi M., Ohsumi Y., Kominami E.
J. Biol. Chem. 276:9846-9854(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG7.
[11]"Membrane recruitment of Aut7p in the autophagy and cytoplasm to vacuole targeting pathways requires Aut1p, Aut2p, and the autophagy conjugation complex."
Kim J., Huang W.-P., Klionsky D.J.
J. Cell Biol. 152:51-64(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"The carboxyl terminal 17 amino acids within Apg7 are essential for Apg8 lipidation, but not for Apg12 conjugation."
Yamazaki-Sato H., Tanida I., Ueno T., Kominami E.
FEBS Lett. 551:71-77(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG7.
[13]"A unified nomenclature for yeast autophagy-related genes."
Klionsky D.J., Cregg J.M., Dunn W.A. Jr., Emr S.D., Sakai Y., Sandoval I.V., Sibirny A., Subramani S., Thumm M., Veenhuis M., Ohsumi Y.
Dev. Cell 5:539-545(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[14]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[15]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[16]"In vivo and in vitro reconstitution of atg8 conjugation essential for autophagy."
Ichimura Y., Imamura Y., Emoto K., Umeda M., Noda T., Ohsumi Y.
J. Biol. Chem. 279:40584-40592(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF CYS-234.
[17]"Crystallization and preliminary X-ray analysis of Atg3."
Yamada Y., Suzuki N.N., Fujioka Y., Ichimura Y., Ohsumi Y., Inagaki F.
Acta Crystallogr. F 62:1016-1017(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CRYSTALLIZATION.
[18]"Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion."
Nakatogawa H., Ichimura Y., Ohsumi Y.
Cell 130:165-178(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[19]"An interrelationship between autophagy and filamentous growth in budding yeast."
Ma J., Jin R., Jia X., Dobry C.J., Wang L., Reggiori F., Zhu J., Kumar A.
Genetics 177:205-214(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[20]"The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy."
Hanada T., Noda N.N., Satomi Y., Ichimura Y., Fujioka Y., Takao T., Inagaki F., Ohsumi Y.
J. Biol. Chem. 282:37298-37302(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THE ATG12-ATG5 CONJUGATE.
[21]"Physiological pH and acidic phospholipids contribute to substrate specificity in lipidation of Atg8."
Oh-oka K., Nakatogawa H., Ohsumi Y.
J. Biol. Chem. 283:21847-21852(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"In vivo reconstitution of autophagy in Saccharomyces cerevisiae."
Cao Y., Cheong H., Song H., Klionsky D.J.
J. Cell Biol. 182:703-713(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"Piecemeal microautophagy of the nucleus requires the core macroautophagy genes."
Krick R., Muehe Y., Prick T., Bremer S., Schlotterhose P., Eskelinen E.L., Millen J., Goldfarb D.S., Thumm M.
Mol. Biol. Cell 19:4492-4505(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis."
Lin Y.Y., Lu J.Y., Zhang J., Walter W., Dang W., Wan J., Tao S.C., Qian J., Zhao Y., Boeke J.D., Berger S.L., Zhu H.
Cell 136:1073-1084(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION BY THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
[25]"The amino-terminal region of Atg3 is essential for association with phosphatidylethanolamine in Atg8 lipidation."
Hanada T., Satomi Y., Takao T., Ohsumi Y.
FEBS Lett. 583:1078-1083(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG8, LIPIDATION, DOMAIN.
[26]"Rsf1p is required for an efficient metabolic shift from fermentative to glycerol-based respiratory growth in S. cerevisiae."
Roberts G.G. III, Hudson A.P.
Yeast 26:95-110(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[27]"Autophagy-related protein 8 (Atg8) family interacting motif in Atg3 mediates the Atg3-Atg8 interaction and is crucial for the cytoplasm-to-vacuole targeting pathway."
Yamaguchi M., Noda N.N., Nakatogawa H., Kumeta H., Ohsumi Y., Inagaki F.
J. Biol. Chem. 285:29599-29607(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ATG8, DOMAIN, MUTAGENESIS OF TRP-270; ASP-272 AND LEU-273.
[28]"Purification and characterization of a ubiquitin-like system for autophagosome formation."
Bae J.Y., Park H.H.
J. Microbiol. Biotechnol. 20:1647-1652(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[29]"Structural basis of Atg8 activation by a homodimeric E1, Atg7."
Noda N.N., Satoo K., Fujioka Y., Kumeta H., Ogura K., Nakatogawa H., Ohsumi Y., Inagaki F.
Mol. Cell 44:462-475(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG7 AND ATG8.
[30]"Insights into noncanonical E1 enzyme activation from the structure of autophagic E1 Atg7 with Atg8."
Hong S.B., Kim B.W., Lee K.E., Kim S.W., Jeon H., Kim J., Song H.K.
Nat. Struct. Mol. Biol. 18:1323-1330(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATG7.
[31]"Atg4 recycles inappropriately lipidated Atg8 to promote autophagosome biogenesis."
Nakatogawa H., Ishii J., Asai E., Ohsumi Y.
Autophagy 8:177-186(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[32]"A late form of nucleophagy in Saccharomyces cerevisiae."
Mijaljica D., Prescott M., Devenish R.J.
PLoS ONE 7:E40013-E40013(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[33]"Function and molecular mechanism of acetylation in autophagy regulation."
Yi C., Ma M., Ran L., Zheng J., Tong J., Zhu J., Ma C., Sun Y., Zhang S., Feng W., Zhu L., Le Y., Gong X., Yan X., Hong B., Jiang F.J., Xie Z., Miao D., Deng H., Yu L.
Science 336:474-477(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-19 AND LYS-48, DEACETYLATION BY RPD3, FUNCTION.
[34]"Atg12-Atg5 conjugate enhances E2 activity of Atg3 by rearranging its catalytic site."
Sakoh-Nakatogawa M., Matoba K., Asai E., Kirisako H., Ishii J., Noda N.N., Inagaki F., Nakatogawa H., Ohsumi Y.
Nat. Struct. Mol. Biol. 20:433-439(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-213, INTERACTION WITH THE ATG12-ATG5 CONJUGATE, ENZYME REGULATION.
[35]"The crystal structure of Atg3, an autophagy-related ubiquitin carrier protein (E2) enzyme that mediates Atg8 lipidation."
Yamada Y., Suzuki N.N., Hanada T., Ichimura Y., Kumeta H., Fujioka Y., Ohsumi Y., Inagaki F.
J. Biol. Chem. 282:8036-8043(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, DOMAIN, INTERACTION WITH ATG7 AND ATG8.
[36]"Atg8 transfer from Atg7 to Atg3: a distinctive E1-E2 architecture and mechanism in the autophagy pathway."
Taherbhoy A.M., Tait S.W., Kaiser S.E., Williams A.H., Deng A., Nourse A., Hammel M., Kurinov I., Rock C.O., Green D.R., Schulman B.A.
Mol. Cell 44:451-461(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 128-144 IN COMPLEX WITH ATG7.
[37]"Noncanonical E2 recruitment by the autophagy E1 revealed by Atg7-Atg3 and Atg7-Atg10 structures."
Kaiser S.E., Mao K., Taherbhoy A.M., Yu S., Olszewski J.L., Duda D.M., Kurinov I., Deng A., Fenn T.D., Klionsky D.J., Schulman B.A.
Nat. Struct. Mol. Biol. 19:1242-1249(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ATG7.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77395 Genomic DNA. Translation: CAA54575.1.
Z71622 Genomic DNA. Translation: CAA96284.1.
BK006947 Genomic DNA. Translation: DAA10548.1.
PIRS45130.
RefSeqNP_014404.3. NM_001183184.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DYTX-ray2.50A1-310[»]
3T7GX-ray2.08C/D128-144[»]
4GSLX-ray2.70C/D1-310[»]
ProteinModelPortalP40344.
SMRP40344. Positions 21-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35832. 99 interactions.
DIPDIP-1190N.
IntActP40344. 10 interactions.
MINTMINT-389035.
STRING4932.YNR007C.

Proteomic databases

MaxQBP40344.
PaxDbP40344.
PeptideAtlasP40344.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNR007C; YNR007C; YNR007C.
GeneID855741.
KEGGsce:YNR007C.

Organism-specific databases

CYGDYNR007c.
SGDS000005290. ATG3.

Phylogenomic databases

eggNOGNOG237080.
GeneTreeENSGT00390000010308.
HOGENOMHOG000234613.
KOK08343.
OMANEQQGHA.
OrthoDBEOG7KWSTW.

Enzyme and pathway databases

BioCycYEAST:G3O-33325-MONOMER.

Gene expression databases

GenevestigatorP40344.

Family and domain databases

InterProIPR007135. Autophagy-rel_prot_3.
IPR019461. Autophagy-rel_prot_3_C.
IPR007134. Autophagy-rel_prot_3_N.
[Graphical view]
PfamPF03987. Autophagy_act_C. 1 hit.
PF10381. Autophagy_Cterm. 1 hit.
PF03986. Autophagy_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP40344.
NextBio980136.
PROP40344.

Entry information

Entry nameATG3_YEAST
AccessionPrimary (citable) accession number: P40344
Secondary accession number(s): D6W1I2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references