Q9DCM2
Gene name |
Gstk1 |
Protein name |
Glutathione S-transferase kappa 1 |
Names |
GST 13-13, GST class-kappa, GSTK1-1, mGSTK1, Glutathione S-transferase subunit 13 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:76263 |
EC number |
2.5.1.18: Transferring alkyl or aryl groups, other than methyl groups |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9DCM2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9DCM2-F1 | Predicted | AlphaFoldDB |
16 variants for Q9DCM2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs37027716 | 7 | I>T | No | EVA | |
| rs3412481437 | 24 | E>D | No | EVA | |
| rs3388822311 | 53 | N>I | No | EVA | |
| rs3388818775 | 97 | I>L | No | EVA | |
| rs230901797 | 105 | T>S | No | EVA | |
| rs249658362 | 121 | I>L | No | EVA | |
| rs3388827581 | 126 | W>* | No | EVA | |
| rs259844809 | 136 | Q>P | No | EVA | |
| rs3396651914 | 150 | A>V | No | EVA | |
| rs260614520 | 154 | H>Q | No | EVA | |
| rs3388825683 | 180 | A>T | No | EVA | |
| rs3388793029 | 200 | S>A | No | EVA | |
| rs3388818754 | 208 | Y>C | No | EVA | |
| rs3388822269 | 217 | P>T | No | EVA | |
| rs212233803 | 222 | A>V | No | EVA | |
| rs3388819455 | 224 | A>T | No | EVA |
No associated diseases with Q9DCM2
1 regional properties for Q9DCM2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | DSBA-like thioredoxin domain | 8 - 210 | IPR001853 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.5.1.18 | Transferring alkyl or aryl groups, other than methyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
| peroxisome | A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| glutathione peroxidase activity | Catalysis of the reaction: 2 glutathione + hydrogen peroxide = oxidized glutathione + 2 H2O. |
| glutathione transferase activity | Catalysis of the reaction: R-X + glutathione = H-X + R-S-glutathione. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| epithelial cell differentiation | The process in which a relatively unspecialized cell acquires specialized features of an epithelial cell, any of the cells making up an epithelium. |
| glutathione metabolic process | The chemical reactions and pathways involving glutathione, the tripeptide glutamylcysteinylglycine, which acts as a coenzyme for some enzymes and as an antioxidant in the protection of sulfhydryl groups in enzymes and other proteins; it has a specific role in the reduction of hydrogen peroxide (H2O2) and oxidized ascorbate, and it participates in the gamma-glutamyl cycle. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGPAPRILEL | FYDVLSPYSW | LGFEVLCRYQ | HLWNIKLQLR | PTLIAGIMKD | SGNQPPAMVP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RKGQYIFKEI | PLLKQFFQVP | LNIPKDFFGE | TVKKGSINAM | RFLTTVSMEQ | PEMLEKVSRE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IWMRVWSRDE | DITEYQSILA | AAVKAGMSTA | QAQHFLEKIS | TQQVKNKLIE | NTDAACKYGA |
| 190 | 200 | 210 | 220 | ||
| FGLPTTVAHV | DGKTYMLFGS | DRLELLAYLL | GEKWMGPVPP | TANARL |