Basic Information
Name | Ubiquitin-like modifier-activating enzyme ATG7 (ATG12-activating enzyme E1 ATG7) (Autophagy-related protein 7) (Cytoplasm to vacuole targeting protein 2) |
Uniprot ID | P38862 |
Systematic gene name | YHR171W |
Standard gene name | ATG7 |
Gene names | ATG7 APG7 CVT2 YHR171W |
Description from SGD | YHR171W ATG7 SGDID:S000001214, Chr VIII from 445713-447605, Genome Release 64-3-1, Verified ORF, "Autophagy-related protein and dual specificity member of the E1 family; mediates the attachment of Atg12p to Atg5p and Atg8p to phosphatidylethanolamine which are required steps in autophagosome formation; E1 enzymes are also known as ubiquitin-activating enzymes; involved in methionine restriction extension of chronological lifespan in an autophagy-dependent manner" |
Protein length | 630 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MSSERVLSYA PAFKSFLDTS FFQELSRLKL DVLKLDSTCQ PLTVNLDLHN
IPKSADQVPL FLTNRSFEKH NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL
FLHQRALECW EDGIKDINKC VSFVIISFAD LKKYRFYYWL GVPCFQRPSS
TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV CILDADDEIV NYDKCIIRKT
KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI IRQNEGSFAL
NATFASIDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ
SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK
ITFVDNGTVS YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK
LSIPMIGHKL VNEEAQHKDF DRLRALIKEH DIIFLLVDSR ESRWLPSLLS
NIENKTVINA ALGFDSYLVM RHGNRDEQSS KQLGCYFCHD VVAPTDSLTD
RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT VLGDIPHQIR
GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE
ISGLSVIKQE VERLGNDVFE WEDDESDEIA
IPKSADQVPL FLTNRSFEKH NNKRTNEVPL QGSIFNFNVL DEFKNLDKQL
FLHQRALECW EDGIKDINKC VSFVIISFAD LKKYRFYYWL GVPCFQRPSS
TVLHVRPEPS LKGLFSKCQK WFDVNYSKWV CILDADDEIV NYDKCIIRKT
KVLAIRDTST MENVPSALTK NFLSVLQYDV PDLIDFKLLI IRQNEGSFAL
NATFASIDPQ SSSSNPDMKV SGWERNVQGK LAPRVVDLSS LLDPLKIADQ
SVDLNLKLMK WRILPDLNLD IIKNTKVLLL GAGTLGCYVS RALIAWGVRK
ITFVDNGTVS YSNPVRQALY NFEDCGKPKA ELAAASLKRI FPLMDATGVK
LSIPMIGHKL VNEEAQHKDF DRLRALIKEH DIIFLLVDSR ESRWLPSLLS
NIENKTVINA ALGFDSYLVM RHGNRDEQSS KQLGCYFCHD VVAPTDSLTD
RTLDQMCTVT RPGVAMMASS LAVELMTSLL QTKYSGSETT VLGDIPHQIR
GFLHNFSILK LETPAYEHCP ACSPKVIEAF TDLGWEFVKK ALEHPLYLEE
ISGLSVIKQE VERLGNDVFE WEDDESDEIA
Legend
- X Phoshorylation
- X SUMOylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[447, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[450, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |
[608, SUMO] | Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications) |
[626, Phos] | Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications) |