Basic Information
Name | Glutathione reductase (GR) (GRase) (EC 1.8.1.7) |
Uniprot ID | P41921 |
Systematic gene name | YPL091W |
Standard gene name | GLR1 |
Gene names | GLR1 YPL091W LPG17W |
Description from SGD | YPL091W GLR1 SGDID:S000006012, Chr XVI from 375502-376953, Genome Release 64-3-1, Verified ORF, "Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress" |
Protein length | 483 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MLSATKQTFR SLQIRTMSTN TKHYDYLVIG GGSGGVASAR RAASYGAKTL
LVEAKALGGT CVNVGCVPKK VMWYASDLAT RVSHANEYGL YQNLPLDKEH
LTFNWPEFKQ KRDAYVHRLN GIYQKNLEKE KVDVVFGWAR FNKDGNVEVQ
KRDNTTEVYS ANHILVATGG KAIFPENIPG FELGTDSDGF FRLEEQPKKV
VVVGAGYIGI ELAGVFHGLG SETHLVIRGE TVLRKFDECI QNTITDHYVK
EGINVHKLSK IVKVEKNVET DKLKIHMNDS KSIDDVDELI WTIGRKSHLG
MGSENVGIKL NSHDQIIADE YQNTNVPNIY SLGDVVGKVE LTPVAIAAGR
KLSNRLFGPE KFRNDKLDYE NVPSVIFSHP EAGSIGISEK EAIEKYGKEN
IKVYNSKFTA MYYAMLSEKS PTRYKIVCAG PNEKVVGLHI VGDSSAEILQ
GFGVAIKMGA TKADFDNCVA IHPTSAEELV TMR
LVEAKALGGT CVNVGCVPKK VMWYASDLAT RVSHANEYGL YQNLPLDKEH
LTFNWPEFKQ KRDAYVHRLN GIYQKNLEKE KVDVVFGWAR FNKDGNVEVQ
KRDNTTEVYS ANHILVATGG KAIFPENIPG FELGTDSDGF FRLEEQPKKV
VVVGAGYIGI ELAGVFHGLG SETHLVIRGE TVLRKFDECI QNTITDHYVK
EGINVHKLSK IVKVEKNVET DKLKIHMNDS KSIDDVDELI WTIGRKSHLG
MGSENVGIKL NSHDQIIADE YQNTNVPNIY SLGDVVGKVE LTPVAIAAGR
KLSNRLFGPE KFRNDKLDYE NVPSVIFSHP EAGSIGISEK EAIEKYGKEN
IKVYNSKFTA MYYAMLSEKS PTRYKIVCAG PNEKVVGLHI VGDSSAEILQ
GFGVAIKMGA TKADFDNCVA IHPTSAEELV TMR
Legend
- X Phoshorylation
- X Multiple modifications
- X K-acetylation
- X K-Succinylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[44, 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) |
[44, 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) |
[125, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[125, 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) |
[143, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[259, 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) |
[260, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |
[342, 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) |
[342, Phos] | Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications) |
[361, K-succ] | Frankovsky, J., Keresztesová, B., Bellová, J., et al. (2021). The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids. Journal of Biological Chemistry, 297(4): 101155. (Publication) (All modifications) |
[361, K-acetyl] | Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications) |
[396, 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) |
[396, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |
[402, K-succ] | Weinert, B.T., Schölz, C., Wagner, S.A., et al. (2013). Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Reports, 4(4), 842-851. (Publication) (All modifications) |
[407, 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) |
[420, 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) |
[462, 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) |
[475, 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) |
[475, 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) |
[475, Phos] | Albuquerque, C.P., Smolka, M.B., Payne, S.H., Bafna, V., Eng, J., Zhou, H. (2008). A multidimensional chromatography technology for in-depth phosphoproteome analysis. Molecular and Cellular Proteomics 7(7):1389-1396. (Publication) (All modifications) |
[475, Phos] | Frankovsky, J., Vozáriková, V., Nosek, J., Tomáška, Ľ. (2021a). Mitochondrial protein phosphorylation in yeast revisited.Mitochondrion 57:148-162. (Publication) (All modifications) |