| UniProt ID | GLRX2_HUMAN | |
|---|---|---|
| UniProt AC | Q9NS18 | |
| Protein Name | Glutaredoxin-2, mitochondrial | |
| Gene Name | GLRX2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 164 | |
| Subcellular Localization |
Isoform 1: Mitochondrion. Isoform 2: Nucleus. |
|
| Protein Description | Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release.. | |
| Protein Sequence | MIWRRAALAGTRLVWSRSGSAGWLDRAAGAAGAAAAAASGMESNTSSSLENLATAPVNQIQETISDNCVVIFSKTSCSYCTMAKKLFHDMNVNYKVVELDLLEYGNQFQDALYKMTGERTVPRIFVNGTFIGGATDTHRLHKEGKLLPLVHQCYLKKSKRKEFQ | |
| 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 |
|---|---|---|---|---|---|
| 18 (in isoform 2) | Phosphorylation | - | 31.42 | 27174698 | |
| 19 (in isoform 2) | Phosphorylation | - | 22.02 | 27174698 | |
| 20 | Phosphorylation | LVWSRSGSAGWLDRA EEEECCCCCHHHHHH | 25.51 | 23917254 | |
| 73 | Phosphorylation | DNCVVIFSKTSCSYC CCEEEEEECCCCHHH | 24.73 | 24719451 | |
| 75 | Phosphorylation | CVVIFSKTSCSYCTM EEEEEECCCCHHHHH | 33.49 | 28787133 | |
| 77 | S-glutathionyl cysteine | VIFSKTSCSYCTMAK EEEECCCCHHHHHHH | 3.98 | - | |
| 77 | Glutathionylation | VIFSKTSCSYCTMAK EEEECCCCHHHHHHH | 3.98 | 22833525 | |
| 104 | Phosphorylation | VELDLLEYGNQFQDA EEEHHHHHHHHHHHH | 22.73 | - | |
| 105 | Ubiquitination | ELDLLEYGNQFQDAL EEHHHHHHHHHHHHH | 16.46 | 29967540 | |
| 113 | Phosphorylation | NQFQDALYKMTGERT HHHHHHHHHHHCCCC | 10.63 | - | |
| 137 | Phosphorylation | FIGGATDTHRLHKEG EECCCCCHHHHHCCC | 12.44 | 24719451 | |
| 138 | Phosphorylation | IGGATDTHRLHKEGK ECCCCCHHHHHCCCC | 32.87 | 24719451 | |
| 145 | Ubiquitination | HRLHKEGKLLPLVHQ HHHHCCCCHHHHHHH | 48.19 | 29967540 | |
| 146 | Ubiquitination | RLHKEGKLLPLVHQC HHHCCCCHHHHHHHH | 9.77 | 29967540 |
| 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 GLRX2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GLRX2_HUMAN !! | ||||||
* 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 GLRX2_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| MDHM_HUMAN | MDH2 | physical | 26344197 | |
| PIPNB_HUMAN | PITPNB | physical | 26344197 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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