| UniProt ID | TRX2_YEAST | |
|---|---|---|
| UniProt AC | P22803 | |
| Protein Name | Thioredoxin-2 | |
| Gene Name | TRX2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 104 | |
| Subcellular Localization |
Cytoplasm . Golgi apparatus membrane Peripheral membrane protein . Nucleus . |
|
| Protein Description | Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress.. | |
| Protein Sequence | MVTQLKSASEYDSALASGDKLVVVDFFATWCGPCKMIAPMIEKFAEQYSDAAFYKLDVDEVSDVAQKAEVSSMPTLIFYKGGKEVTRVVGANPAAIKQAIASNV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 6 | Ubiquitination | --MVTQLKSASEYDS --CCCCCCCHHHHHH | 33.87 | 24961812 | |
| 6 | Succinylation | --MVTQLKSASEYDS --CCCCCCCHHHHHH | 33.87 | 23954790 | |
| 6 | 2-Hydroxyisobutyrylation | --MVTQLKSASEYDS --CCCCCCCHHHHHH | 33.87 | - | |
| 7 | Phosphorylation | -MVTQLKSASEYDSA -CCCCCCCHHHHHHH | 45.69 | 27017623 | |
| 9 | Phosphorylation | VTQLKSASEYDSALA CCCCCCHHHHHHHHH | 43.72 | 28889911 | |
| 43 | Acetylation | MIAPMIEKFAEQYSD HHHHHHHHHHHHHCC | 38.66 | 24489116 | |
| 55 | Ubiquitination | YSDAAFYKLDVDEVS HCCCCEEECCHHHHH | 31.58 | 24961812 | |
| 55 | Acetylation | YSDAAFYKLDVDEVS HCCCCEEECCHHHHH | 31.58 | 24489116 | |
| 62 | Phosphorylation | KLDVDEVSDVAQKAE ECCHHHHHHHHHHHH | 25.07 | 22369663 | |
| 67 | Ubiquitination | EVSDVAQKAEVSSMP HHHHHHHHHHHCCCC | 36.46 | 23749301 | |
| 71 | Phosphorylation | VAQKAEVSSMPTLIF HHHHHHHCCCCEEEE | 16.66 | 28889911 | |
| 72 | Phosphorylation | AQKAEVSSMPTLIFY HHHHHHCCCCEEEEE | 33.68 | 27017623 | |
| 80 | 2-Hydroxyisobutyrylation | MPTLIFYKGGKEVTR CCEEEEEECCCEEEE | 50.90 | - | |
| 80 | Acetylation | MPTLIFYKGGKEVTR CCEEEEEECCCEEEE | 50.90 | 24489116 | |
| 80 | Succinylation | MPTLIFYKGGKEVTR CCEEEEEECCCEEEE | 50.90 | 23954790 | |
| 83 | 2-Hydroxyisobutyrylation | LIFYKGGKEVTRVVG EEEEECCCEEEEEEC | 58.65 | - | |
| 97 | Acetylation | GANPAAIKQAIASNV CCCHHHHHHHHHHCC | 29.02 | 24489116 | |
| 97 | Ubiquitination | GANPAAIKQAIASNV CCCHHHHHHHHHHCC | 29.02 | 23749301 | |
| 97 | Succinylation | GANPAAIKQAIASNV CCCHHHHHHHHHHCC | 29.02 | 23954790 |
| 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 TRX2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRX2_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 TRX2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-62, AND MASSSPECTROMETRY. | |
