UniProt ID | GSHR_YEAST | |
---|---|---|
UniProt AC | P41921 | |
Protein Name | Glutathione reductase | |
Gene Name | GLR1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 483 | |
Subcellular Localization | Cytoplasm. | |
Protein Description | Maintains high levels of reduced glutathione in the cytosol.. | |
Protein Sequence | MLSATKQTFRSLQIRTMSTNTKHYDYLVIGGGSGGVASARRAASYGAKTLLVEAKALGGTCVNVGCVPKKVMWYASDLATRVSHANEYGLYQNLPLDKEHLTFNWPEFKQKRDAYVHRLNGIYQKNLEKEKVDVVFGWARFNKDGNVEVQKRDNTTEVYSANHILVATGGKAIFPENIPGFELGTDSDGFFRLEEQPKKVVVVGAGYIGIELAGVFHGLGSETHLVIRGETVLRKFDECIQNTITDHYVKEGINVHKLSKIVKVEKNVETDKLKIHMNDSKSIDDVDELIWTIGRKSHLGMGSENVGIKLNSHDQIIADEYQNTNVPNIYSLGDVVGKVELTPVAIAAGRKLSNRLFGPEKFRNDKLDYENVPSVIFSHPEAGSIGISEKEAIEKYGKENIKVYNSKFTAMYYAMLSEKSPTRYKIVCAGPNEKVVGLHIVGDSSAEILQGFGVAIKMGATKADFDNCVAIHPTSAEELVTMR | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MLSATKQT -------CCCCHHHH | 6.35 | 22814378 | |
2 (in isoform 2) | Acetylation | - | 4.85 | 22814378 | |
48 | Acetylation | RAASYGAKTLLVEAK HHHHCCCCEEEEEHH | 35.03 | 24489116 | |
125 | Ubiquitination | RLNGIYQKNLEKEKV HHCCHHHHCCCHHCC | 46.67 | 23749301 | |
125 | Acetylation | RLNGIYQKNLEKEKV HHCCHHHHCCCHHCC | 46.67 | 24489116 | |
143 | Acetylation | FGWARFNKDGNVEVQ EEEEEECCCCCEEEE | 65.39 | 22865919 | |
235 | Acetylation | RGETVLRKFDECIQN CCHHHHHHHHHHHHH | 53.67 | 24489116 | |
266 | 2-Hydroxyisobutyrylation | SKIVKVEKNVETDKL HHEEEEECCCCCCEE | 70.09 | - | |
342 | Phosphorylation | VVGKVELTPVAIAAG CCEEEECCHHHHHHC | 11.38 | 25752575 | |
361 | Acetylation | NRLFGPEKFRNDKLD HCCCCCHHHCCCCCC | 53.40 | 24489116 | |
366 | Acetylation | PEKFRNDKLDYENVP CHHHCCCCCCCCCCC | 46.97 | 24489116 | |
395 | Acetylation | SEKEAIEKYGKENIK CHHHHHHHHCHHCCE | 53.87 | 24489116 | |
396 | Phosphorylation | EKEAIEKYGKENIKV HHHHHHHHCHHCCEE | 22.20 | 21126336 | |
402 | Succinylation | KYGKENIKVYNSKFT HHCHHCCEEECHHHH | 50.69 | 23954790 | |
402 | Ubiquitination | KYGKENIKVYNSKFT HHCHHCCEEECHHHH | 50.69 | 22817900 | |
407 | Ubiquitination | NIKVYNSKFTAMYYA CCEEECHHHHHHHHH | 43.00 | 23749301 | |
462 | Ubiquitination | AIKMGATKADFDNCV EEEECCCHHCCCCCE | 45.48 | 23749301 | |
474 | Phosphorylation | NCVAIHPTSAEELVT CCEEECCCCHHHHHH | 26.80 | 30377154 | |
475 | Phosphorylation | CVAIHPTSAEELVTM CEEECCCCHHHHHHC | 37.83 | 28889911 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of GSHR_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GSHR_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of GSHR_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASSSPECTROMETRY. |