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P38862

- ATG7_YEAST

UniProt

P38862 - ATG7_YEAST

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Protein

Ubiquitin-like modifier-activating enzyme ATG7

Gene

ATG7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. 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. Plays a role in the regulation of filamentous growth and chronological longevity.21 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei507 – 5071Glycyl thioester intermediate

GO - Molecular functioni

  1. Atg12 activating enzyme activity Source: SGD
  2. Atg8 activating enzyme Source: SGD

GO - Biological processi

  1. autophagy Source: SGD
  2. C-terminal protein lipidation Source: SGD
  3. CVT pathway Source: SGD
  4. late nucleophagy Source: SGD
  5. macroautophagy Source: SGD
  6. mitochondrion degradation Source: SGD
  7. piecemeal microautophagy of nucleus Source: SGD
  8. protein modification by small protein conjugation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-31205-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like modifier-activating enzyme ATG7
Alternative name(s):
ATG12-activating enzyme E1 ATG7
Autophagy-related protein 7
Cytoplasm to vacuole targeting protein 2
Gene namesi
Name:ATG7
Synonyms:APG7, CVT2
Ordered Locus Names:YHR171W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

CYGDiYHR171w.
SGDiS000001214. ATG7.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. extrinsic component of pre-autophagosomal structure membrane Source: UniProtKB
  3. membrane Source: SGD
  4. pre-autophagosomal structure Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi333 – 3331G → A: Loss of interaction with ATG8 and ATG12, and no more ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. 2 Publications
Mutagenesisi443 – 4431R → A: Loss of interaction with ATG8. 1 Publication
Mutagenesisi466 – 4661S → A: Loss of interaction with ATG8; when associated with F-486 and A-490. 1 Publication
Mutagenesisi486 – 4861Y → F: Loss of interaction with ATG8; when associated with A-466 and A-490. 1 Publication
Mutagenesisi490 – 4901D → A: Loss of interaction with ATG8; when associated with A-466 and F-486. 1 Publication
Mutagenesisi507 – 5071C → A: Loss of interaction with ATG8 and ATG12 and no more formation of ATG12-ATG5 conjugate. Defect in Cvt pathway and autophagy. 3 Publications
Mutagenesisi507 – 5071C → S: Instead of the formation of an intermediate complex with a thiol ester bond between ATG7 (E1-like enzyme) and ATG8 (substrate) or between ATG7 and ATG12 (substrate), a stable complex with an O-ester bond is formed. No more formation of ATG12-ATG5 conjugate. 3 Publications
Mutagenesisi550 – 5501R → A: Loss of interaction with ATG8. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 630630Ubiquitin-like modifier-activating enzyme ATG7PRO_0000212822Add
BLAST

Proteomic databases

MaxQBiP38862.
PaxDbiP38862.

Expressioni

Gene expression databases

GenevestigatoriP38862.

Interactioni

Subunit structurei

Homodimer. Interacts with ATG8 through a thioester bond between Cys-507 and the C-terminal 'Gly-116' of ATG8 and with ATG12 through a thioester bond between Cys-507 and the C-terminal 'Gly-186' of ATG12. Interacts also with ATG3.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG12P383163EBI-2677,EBI-2692
ATG3P403444EBI-2677,EBI-3381
ATG8P381823EBI-2677,EBI-2684

Protein-protein interaction databases

BioGridi36605. 40 interactions.
DIPiDIP-1196N.
IntActiP38862. 6 interactions.
MINTiMINT-388374.
STRINGi4932.YHR171W.

Structurei

Secondary structure

1
630
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 176
Helixi19 – 2911
Turni32 – 343
Beta strandi36 – 4611
Beta strandi48 – 503
Beta strandi56 – 627
Helixi64 – 674
Beta strandi68 – 703
Beta strandi78 – 8912
Helixi90 – 956
Helixi98 – 11316
Helixi117 – 1193
Beta strandi123 – 1308
Turni131 – 1344
Beta strandi135 – 14814
Beta strandi151 – 1577
Helixi159 – 1646
Helixi165 – 17410
Beta strandi179 – 1835
Beta strandi189 – 1913
Helixi194 – 2007
Beta strandi202 – 2065
Helixi219 – 22911
Beta strandi235 – 2417
Beta strandi243 – 2453
Beta strandi248 – 2569
Beta strandi263 – 2653
Beta strandi269 – 2735
Beta strandi279 – 2813
Beta strandi284 – 2874
Helixi289 – 2913
Helixi294 – 31219
Helixi319 – 3235
Beta strandi326 – 3305
Helixi334 – 34512
Beta strandi350 – 3545
Turni364 – 3663
Helixi372 – 3743
Beta strandi376 – 3783
Helixi379 – 39012
Beta strandi391 – 3933
Beta strandi395 – 3995
Helixi413 – 42917
Beta strandi431 – 4355
Beta strandi438 – 4403
Helixi441 – 4433
Helixi444 – 4529
Beta strandi456 – 4627
Beta strandi464 – 4718
Helixi486 – 4894
Beta strandi490 – 4923
Beta strandi494 – 4963
Turni498 – 5003
Helixi504 – 5085
Helixi513 – 52917
Beta strandi537 – 5404
Beta strandi547 – 5526
Turni553 – 5564
Beta strandi557 – 5615
Turni570 – 5723
Helixi574 – 58310
Helixi585 – 5939
Helixi595 – 6028
Helixi604 – 6129
Helixi616 – 6183
Helixi627 – 6293

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LI5NMR-B601-630[»]
3RUIX-ray1.91A293-630[»]
3RUJX-ray2.10A1-294[»]
3T7EX-ray2.25A289-630[»]
3T7FX-ray1.89A1-289[»]
3T7GX-ray2.08A/B1-289[»]
3T7HX-ray1.60A/B1-289[»]
3VH1X-ray3.00A1-595[»]
3VH2X-ray3.30A1-613[»]
3VH3X-ray2.00A295-630[»]
3VH4X-ray2.65A295-630[»]
4GSJX-ray1.70A1-289[»]
4GSKX-ray2.90A/B1-613[»]
4GSLX-ray2.70A/B1-613[»]
ProteinModelPortaliP38862.
SMRiP38862. Positions 1-630.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38862.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni591 – 63040HomodimerizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi331 – 3366GXGXXG motif

Domaini

The C-terminal 40 residues are required for homodimerization, as well as the interactions with ATG3, ATG8 and ATG12; and the C-terminal 17 residues are required for the ATG8 lipidation.
The GxGxxG motif is important for the function, possibly through binding with ATP.

Sequence similaritiesi

Belongs to the ATG7 family.Curated

Phylogenomic databases

eggNOGiCOG0476.
GeneTreeiENSGT00390000017509.
HOGENOMiHOG000162379.
InParanoidiP38862.
KOiK08337.
OMAiIPMIGHP.
OrthoDBiEOG7WHHK1.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR006285. Atg7.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view]
PANTHERiPTHR10953:SF3. PTHR10953:SF3. 1 hit.
PfamiPF00899. ThiF. 1 hit.
[Graphical view]
SUPFAMiSSF69572. SSF69572. 1 hit.
TIGRFAMsiTIGR01381. E1_like_apg7. 1 hit.

Sequencei

Sequence statusi: Complete.

P38862-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSERVLSYA PAFKSFLDTS FFQELSRLKL DVLKLDSTCQ PLTVNLDLHN
60 70 80 90 100
IPKSADQVPL FLTNRSFEKH NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL
110 120 130 140 150
FLHQRALECW EDGIKDINKC VSFVIISFAD LKKYRFYYWL GVPCFQRPSS
160 170 180 190 200
TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV CILDADDEIV NYDKCIIRKT
210 220 230 240 250
KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI IRQNEGSFAL
260 270 280 290 300
NATFASIDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ
310 320 330 340 350
SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK
360 370 380 390 400
ITFVDNGTVS YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK
410 420 430 440 450
LSIPMIGHKL VNEEAQHKDF DRLRALIKEH DIIFLLVDSR ESRWLPSLLS
460 470 480 490 500
NIENKTVINA ALGFDSYLVM RHGNRDEQSS KQLGCYFCHD VVAPTDSLTD
510 520 530 540 550
RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT VLGDIPHQIR
560 570 580 590 600
GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE
610 620 630
ISGLSVIKQE VERLGNDVFE WEDDESDEIA
Length:630
Mass (Da):71,428
Last modified:February 1, 1995 - v1
Checksum:i561EEC94F0ED57F5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB017925 Genomic DNA. Translation: BAA33474.1.
U00027 Genomic DNA. Translation: AAB68016.1.
BK006934 Genomic DNA. Translation: DAA06864.1.
PIRiS48910.
RefSeqiNP_012041.1. NM_001179302.1.

Genome annotation databases

EnsemblFungiiYHR171W; YHR171W; YHR171W.
GeneIDi856576.
KEGGisce:YHR171W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB017925 Genomic DNA. Translation: BAA33474.1 .
U00027 Genomic DNA. Translation: AAB68016.1 .
BK006934 Genomic DNA. Translation: DAA06864.1 .
PIRi S48910.
RefSeqi NP_012041.1. NM_001179302.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LI5 NMR - B 601-630 [» ]
3RUI X-ray 1.91 A 293-630 [» ]
3RUJ X-ray 2.10 A 1-294 [» ]
3T7E X-ray 2.25 A 289-630 [» ]
3T7F X-ray 1.89 A 1-289 [» ]
3T7G X-ray 2.08 A/B 1-289 [» ]
3T7H X-ray 1.60 A/B 1-289 [» ]
3VH1 X-ray 3.00 A 1-595 [» ]
3VH2 X-ray 3.30 A 1-613 [» ]
3VH3 X-ray 2.00 A 295-630 [» ]
3VH4 X-ray 2.65 A 295-630 [» ]
4GSJ X-ray 1.70 A 1-289 [» ]
4GSK X-ray 2.90 A/B 1-613 [» ]
4GSL X-ray 2.70 A/B 1-613 [» ]
ProteinModelPortali P38862.
SMRi P38862. Positions 1-630.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36605. 40 interactions.
DIPi DIP-1196N.
IntActi P38862. 6 interactions.
MINTi MINT-388374.
STRINGi 4932.YHR171W.

Proteomic databases

MaxQBi P38862.
PaxDbi P38862.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YHR171W ; YHR171W ; YHR171W .
GeneIDi 856576.
KEGGi sce:YHR171W.

Organism-specific databases

CYGDi YHR171w.
SGDi S000001214. ATG7.

Phylogenomic databases

eggNOGi COG0476.
GeneTreei ENSGT00390000017509.
HOGENOMi HOG000162379.
InParanoidi P38862.
KOi K08337.
OMAi IPMIGHP.
OrthoDBi EOG7WHHK1.

Enzyme and pathway databases

BioCyci YEAST:G3O-31205-MONOMER.

Miscellaneous databases

EvolutionaryTracei P38862.
NextBioi 982432.
PROi P38862.

Gene expression databases

Genevestigatori P38862.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR006285. Atg7.
IPR009036. Molybdenum_cofac_synth_MoeB.
IPR016040. NAD(P)-bd_dom.
IPR000594. ThiF_NAD_FAD-bd.
[Graphical view ]
PANTHERi PTHR10953:SF3. PTHR10953:SF3. 1 hit.
Pfami PF00899. ThiF. 1 hit.
[Graphical view ]
SUPFAMi SSF69572. SSF69572. 1 hit.
TIGRFAMsi TIGR01381. E1_like_apg7. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: ATCC 26109 / X2180.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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.
  5. "Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway."
    Harding T.M., Morano K.A., Scott S.V., Klionsky D.J.
    J. Cell Biol. 131:591-602(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Apg7p/Cvt2p is required for the cytoplasm-to-vacuole targeting, macroautophagy, and peroxisome degradation pathways."
    Kim J., Dalton V.M., Eggerton K.P., Scott S.V., Klionsky D.J.
    Mol. Biol. Cell 10:1337-1351(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Apg7p/Cvt2p: a novel protein-activating enzyme essential for autophagy."
    Tanida I., Mizushima N., Kiyooka M., Ohsumi M., Ueno T., Ohsumi Y., Kominami E.
    Mol. Biol. Cell 10:1367-1379(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATG12, MUTAGENESIS OF GLY-333 AND CYS-507.
  8. Cited for: FUNCTION, INTERACTION WITH ATG8, MUTAGENESIS OF GLY-333 AND CYS-507.
  9. "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: HOMODIMERIZATION, INTERACTION WITH ATG3; ATG8 AND ATG12.
  10. "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.
  11. Cited for: NOMENCLATURE.
  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.
  13. "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-507.
  14. "Structure-function relationship of Atg12, a ubiquitin-like modifier essential for autophagy."
    Hanada T., Ohsumi Y.
    Autophagy 1:110-118(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG12.
  15. "Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation."
    Onodera J., Ohsumi Y.
    J. Biol. Chem. 280:31582-31586(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "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.
  17. "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: FUNCTION.
  18. "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: INTERACTION WITH ATG3.
  19. "Localization of autophagy-related proteins in yeast using a versatile plasmid-based resource of fluorescent protein fusions."
    Ma J., Bharucha N., Dobry C.J., Frisch R.L., Lawson S., Kumar A.
    Autophagy 4:792-800(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  20. "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, INTERACTION WITH ATG8.
  21. "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.
  22. "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.
  23. "Autophagy and amino acid homeostasis are required for chronological longevity in Saccharomyces cerevisiae."
    Alvers A.L., Fishwick L.K., Wood M.S., Hu D., Chung H.S., Dunn W.A. Jr., Aris J.P.
    Aging Cell 8:353-369(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae."
    Kageyama T., Suzuki K., Ohsumi Y.
    Biochem. Biophys. Res. Commun. 378:551-557(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "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.
  26. Cited for: FUNCTION.
  27. "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.
  28. "Mitochondrial degradation during starvation is selective and temporally distinct from bulk autophagy in yeast."
    Eiyama A., Kondo-Okamoto N., Okamoto K.
    FEBS Lett. 587:1787-1792(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  29. "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 (1.60 ANGSTROMS).
  30. "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: STRUCTURE BY NMR OF 601-630 IN COMPLEX WITH ATG8, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ARG8, FUNCTION, MUTAGENESIS OF ARG-443; SER-466; TYR-486; ASP-490 AND ARG-550.
  31. "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: X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH ATG8, INTERACTION WITH ATG3.
  32. "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 (1.7 ANGSTROMS) OF 1-613 IN COMPLEX WITH ATG3 AND ATG10.

Entry informationi

Entry nameiATG7_YEAST
AccessioniPrimary (citable) accession number: P38862
Secondary accession number(s): D3DLC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

External Data

Dasty 3