Q8CGR7
Gene name |
Upp2 |
Protein name |
Uridine phosphorylase 2 |
Names |
UPase 2, UrdPase 2, Liver-specific uridine phosphorylase, L-UrdPase |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:76654 |
EC number |
2.4.2.3: Pentosyltransferases |
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 Q8CGR7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8CGR7-F1 | Predicted | AlphaFoldDB |
18 variants for Q8CGR7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388556173 | 10 | R>K | No | EVA | |
| rs27907017 | 12 | M>I | No | EVA | |
| rs260358219 | 12 | M>T | No | EVA | |
| rs27906979 | 26 | Y>S | No | EVA | |
| rs3388547053 | 31 | Y>F | No | EVA | |
| rs246820048 | 83 | R>Q | No | EVA | |
| rs3388550408 | 109 | V>M | No | EVA | |
| rs27906909 | 136 | H>R | No | EVA | |
| rs3388550470 | 149 | G>V | No | EVA | |
| rs3388556098 | 155 | P>L | No | EVA | |
| rs27906881 | 158 | V>I | No | EVA | |
| rs3388556079 | 179 | D>E | No | EVA | |
| rs3388556897 | 234 | S>L | No | EVA | |
| rs3388544553 | 234 | S>T | No | EVA | |
| rs3391655927 | 247 | R>G | No | EVA | |
| rs3388544471 | 277 | T>K | No | EVA | |
| rs3388556082 | 299 | Q>L | No | EVA | |
| rs3388556102 | 311 | K>N | No | EVA |
No associated diseases with Q8CGR7
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.2.3 | Pentosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| type III intermediate filament | A type of intermediate filament, typically made up of one or more of the proteins vimentin, desmin, glial fibrillary acidic protein (GFAP), and peripherin. Unlike the keratins, the type III proteins can form both homo- and heteropolymeric IF filaments. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| deoxyuridine phosphorylase activity | Catalysis of the reaction: deoxyuridine + phosphate = uracil + deoxy-D-ribose 1-phosphate. |
| identical protein binding | Binding to an identical protein or proteins. |
| uridine phosphorylase activity | Catalysis of the reaction: uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| CMP catabolic process | The chemical reactions and pathways resulting in the breakdown of CMP, cytidine monophosphate. |
| dCMP catabolic process | The chemical reactions and pathways resulting in the breakdown of dCMP, deoxycytidine monophosphate. |
| UMP catabolic process | The chemical reactions and pathways resulting in the breakdown of UMP, uridine monophosphate. |
| UMP salvage | Any process which produces UMP, uridine monophosphate, from derivatives of it (e.g. cytidine, uridine, cytosine) without de novo synthesis. |
| uridine catabolic process | The chemical reactions and pathways resulting in the breakdown of uridine, uracil riboside, a ribonucleoside very widely distributed but occurring almost entirely as phosphoric esters in ribonucleotides and ribonucleic acids. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| O95045 | UPP2 | Uridine phosphorylase 2 | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASILPASNR | SMRPDKNTYE | RKRSVYVKNP | YLEGMDEDIL | YHLDLGTKTH | NLPAMFGDVK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FVCVGGSPNR | MKAFAQFMHK | ELRLEGDGED | IEDICAGTDR | YCMFKTGPVL | SVSHGMGIPS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ISIMLHELIK | LLHHAHCCDV | TIIRIGTSGG | IGIAPGSVVI | TDTAVDSFFK | PRFEQVILDN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VVTRSTELDK | ELANDLFNCS | REIPNVPTLI | GHTMCTYDFY | EGQGRLDGAL | CSFSREKKLD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YLKRAYRAGV | RNIEMESTVF | AAMCGLCGLR | AAVVCVTLLD | RLESDQINLS | HDVLVEYQQR |
| 310 | |||||
| PQLLISNFIK | KQLGLCDQMS |