| UniProt ID | GLO2_YEAST | |
|---|---|---|
| UniProt AC | Q05584 | |
| Protein Name | Hydroxyacylglutathione hydrolase, cytoplasmic isozyme | |
| Gene Name | GLO2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 274 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.. | |
| Protein Sequence | MQVKSIKMRWESGGVNYCYLLSDSKNKKSWLIDPAEPPEVLPELTEDEKISVEAIVNTHHHYDHADGNADILKYLKEKNPTSKVEVIGGSKDCPKVTIIPENLKKLHLGDLEITCIRTPCHTRDSICYYVKDPTTDERCIFTGDTLFTAGCGRFFEGTGEEMDIALNNSILETVGRQNWSKTRVYPGHEYTSDNVKFVRKIYPQVGENKALDELEQFCSKHEVTAGRFTLKDEVEFNPFMRLEDPKVQKAAGDTNNSWDRAQIMDKLRAMKNRM | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MQVKSIKMRWES ---CCCEEEEEEEEC | 28.69 | 21126336 | |
| 12 | Phosphorylation | SIKMRWESGGVNYCY EEEEEEECCCCCEEE | 33.61 | 23749301 | |
| 17 | Phosphorylation | WESGGVNYCYLLSDS EECCCCCEEEEEECC | 4.69 | 23749301 | |
| 22 | Phosphorylation | VNYCYLLSDSKNKKS CCEEEEEECCCCCCE | 36.92 | 23749301 | |
| 24 | Phosphorylation | YCYLLSDSKNKKSWL EEEEEECCCCCCEEE | 34.45 | 23749301 | |
| 104 | Acetylation | TIIPENLKKLHLGDL EECCCCCCCCCCCCC | 65.94 | 24489116 | |
| 131 | Acetylation | DSICYYVKDPTTDER CCEEEEEECCCCCCC | 41.70 | 24489116 | |
| 131 | Ubiquitination | DSICYYVKDPTTDER CCEEEEEECCCCCCC | 41.70 | 23749301 | |
| 148 | Phosphorylation | FTGDTLFTAGCGRFF EECCEEEECCCCCCC | 25.83 | 19779198 | |
| 158 | Phosphorylation | CGRFFEGTGEEMDIA CCCCCCCCCCHHHHH | 33.93 | 19779198 | |
| 169 | Phosphorylation | MDIALNNSILETVGR HHHHHHCCHHHHHCC | 27.72 | 27017623 | |
| 173 | Phosphorylation | LNNSILETVGRQNWS HHCCHHHHHCCCCCC | 25.47 | 19779198 | |
| 196 | Acetylation | EYTSDNVKFVRKIYP CCCCCCHHHHHHHHH | 44.38 | 24489116 | |
| 220 | Acetylation | ELEQFCSKHEVTAGR HHHHHHHHCCCCCCC | 44.99 | 24489116 | |
| 249 | Ubiquitination | LEDPKVQKAAGDTNN CCCHHHHHHCCCCCC | 43.10 | 23749301 | |
| 254 | Phosphorylation | VQKAAGDTNNSWDRA HHHHCCCCCCCCHHH | 35.07 | 22369663 | |
| 257 | Phosphorylation | AAGDTNNSWDRAQIM HCCCCCCCCHHHHHH | 32.21 | 22369663 | |
| 266 | Acetylation | DRAQIMDKLRAMKNR HHHHHHHHHHHHHHC | 23.61 | 24489116 |
| 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 GLO2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GLO2_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 GLO2_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TRX1_YEAST | TRX1 | physical | 16554755 | |
| HSV2_YEAST | HSV2 | physical | 18467557 | |
| THDH_YEAST | ILV1 | genetic | 21623372 |
| 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-257, AND MASSSPECTROMETRY. | |