Basic Information
Name | 3-keto-steroid reductase (EC 1.1.1.270) |
Uniprot ID | Q12452 |
Systematic gene name | YLR100W |
Standard gene name | ERG27 |
Gene names | ERG27 YLR100W |
Description from SGD | YLR100W ERG27 SGDID:S000004090, Chr XII from 341810-342853, Genome Release 64-3-1, Verified ORF, "3-keto sterol reductase; catalyzes the last of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants are sterol auxotrophs; mutation is functionally complemented by human HSD17B7" |
Protein length | 347 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MNRKVAIVTG TNSNLGLNIV FRLIETEDTN VRLTIVVTSR TLPRVQEVIN
QIKDFYNKSG RVEDLEIDFD YLLVDFTNMV SVLNAYYDIN KKYRAINYLF
VNAAQGIFDG IDWIGAVKEV FTNPLEAVTN PTYKIQLVGV KSKDDMGLIF
QANVFGPYYF ISKILPQLTR GKAYIVWISS IMSDPKYLSL NDIELLKTNA
SYEGSKRLVD LLHLATYKDL KKLGINQYVV QPGIFTSHSF SEYLNFFTYF
GMLCLFYLAR LLGSPWHNID GYKAANAPVY VTRLANPNFE KQDVKYGSAT
SRDGMPYIKT QEIDPTGMSD VFAYIQKKKL EWDEKLKDQI VETRTPI
QIKDFYNKSG RVEDLEIDFD YLLVDFTNMV SVLNAYYDIN KKYRAINYLF
VNAAQGIFDG IDWIGAVKEV FTNPLEAVTN PTYKIQLVGV KSKDDMGLIF
QANVFGPYYF ISKILPQLTR GKAYIVWISS IMSDPKYLSL NDIELLKTNA
SYEGSKRLVD LLHLATYKDL KKLGINQYVV QPGIFTSHSF SEYLNFFTYF
GMLCLFYLAR LLGSPWHNID GYKAANAPVY VTRLANPNFE KQDVKYGSAT
SRDGMPYIKT QEIDPTGMSD VFAYIQKKKL EWDEKLKDQI VETRTPI
Legend
- X Ubiquitination
- X Phoshorylation
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[134, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[291, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[295, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[309, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[337, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[343, 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) |
[343, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[343, Phos] | Holt, L.J., Tuch, B.B., Villén, J., Johnson, A.D., Gygi, S.P., Morgan, D.O. (2009). Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution. Science 325(5948): 1682-1686. (Publication) (All modifications) |
[343, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[345, 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) |
[345, Phos] | Vlastaridis P, Kyriakidou P, Chaliotis A, et al (2017) Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes. GigaScience 6:1–11. (Publication) (All modifications) |
[345, Phos] | Bai Y, Chen B, Li M, et al (2017) FPD: A comprehensive phosphorylation database in fungi. Fungal Biology 121:869–875. (Publication) (All modifications) |
[345, Phos] | MacGilvray, M.E., Shishkova, E., Place, M., Wagner, E.R., Coon, J.J., Gasch, A.P. (2020). Phosphoproteome response to dithiothreitol reveals unique versus shared features of Saccharomyces cerevisiae stress responses. Journal of Proteome Research 19(8): 3405-3417. (Publication) (All modifications) |
[345, Phos] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[345, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |