Q3V1L4
Gene name |
Nt5c2 |
Protein name |
Cytosolic purine 5'-nucleotidase |
Names |
Cytosolic nucleoside phosphotransferase 5'N |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:76952 |
EC number |
2.7.1.77: Phosphotransferases with an alcohol group as acceptor |
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 Q3V1L4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3V1L4-F1 | Predicted | AlphaFoldDB |
31 variants for Q3V1L4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389545449 | 12 | A>V | No | EVA | |
| rs3389452647 | 24 | L>V | No | EVA | |
| rs3389560539 | 27 | Y>H | No | EVA | |
| rs3389523844 | 49 | F>L | No | EVA | |
| rs3389538379 | 117 | N>K | No | EVA | |
| rs3389511483 | 141 | F>C | No | EVA | |
| rs3389540955 | 181 | C>Y | No | EVA | |
| rs3389493146 | 296 | F>L | No | EVA | |
| rs3389555834 | 300 | T>I | No | EVA | |
| rs3389493214 | 303 | R>S | No | EVA | |
| rs3389555870 | 328 | S>L | No | EVA | |
| rs3389511479 | 337 | D>E | No | EVA | |
| rs3389493202 | 338 | L>* | No | EVA | |
| rs3389548834 | 338 | L>R | No | EVA | |
| rs3389554643 | 366 | W>E | No | EVA | |
| rs3389546221 | 388 | L>F | No | EVA | |
| rs3389544840 | 399 | L>S | No | EVA | |
| rs3389523818 | 402 | L>F | No | EVA | |
| rs3389545447 | 416 | I>V | No | EVA | |
| rs3409130078 | 431 | D>A | No | EVA | |
| rs3409304939 | 431 | D>Y | No | EVA | |
| rs3389540942 | 439 | S>I | No | EVA | |
| rs3409513977 | 466 | I>T | No | EVA | |
| rs3389538418 | 493 | T>M | No | EVA | |
| rs3389523748 | 505 | A>V | No | EVA | |
| rs3409217848 | 513 | D>A | No | EVA | |
| rs3407306630 | 513 | D>Y | No | EVA | |
| rs3409130099 | 514 | F>L | No | EVA | |
| rs3408254295 | 516 | D>A | No | EVA | |
| rs3409329443 | 516 | D>Y | No | EVA | |
| rs3389511481 | 522 | H>Y | No | EVA |
No associated diseases with Q3V1L4
No regional properties for Q3V1L4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q3V1L4 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.77 | Phosphotransferases with an alcohol group as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 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. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| 5'-nucleotidase activity | Catalysis of the reaction: a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| GMP 5'-nucleotidase activity | Catalysis of the reaction: 5'-GMP + H2O = guanosine + phosphate. |
| identical protein binding | Binding to an identical protein or proteins. |
| IMP 5'-nucleotidase activity | Catalysis of the reaction: 5'-IMP + H2O = inosine + phosphate. |
| metal ion binding | Binding to a metal ion. |
| nucleoside phosphotransferase activity | Catalysis of the reaction: a nucleotide + a 2'-deoxynucleoside = a nucleoside + a 2'-deoxynucleoside 5'-monophosphate. |
| XMP 5'-nucleosidase activity | Catalysis of the reaction: 5'XMP + H20 = phosphate + xanthosine. |
10 GO annotations of biological process
| Name | Definition |
|---|---|
| adenosine metabolic process | The chemical reactions and pathways involving adenosine, adenine riboside, a ribonucleoside found widely distributed in cells of every type as the free nucleoside and in combination in nucleic acids and various nucleoside coenzymes. |
| allantoin metabolic process | The chemical reactions and pathways involving allantoin, (2,5-dioxo-4-imidazolidinyl)urea, an intermediate or end product of purine catabolism. |
| dGMP catabolic process | The chemical reactions and pathways resulting in the breakdown of dGMP, deoxyguanosine monophosphate (2'-deoxyguanosine 5'-phosphate). |
| dGMP metabolic process | The chemical reactions and pathways involving dGMP, deoxyguanosine monophosphate (2'-deoxyguanosine 5'-phosphate). |
| GMP catabolic process | The chemical reactions and pathways resulting in the breakdown of GMP, guanosine monophosphate. |
| GMP catabolic process to guanine | The chemical reactions and pathways resulting in the breakdown of guanosine monophosphate into other compounds, including guanine. |
| GMP metabolic process | The chemical reactions and pathways involving GMP, guanosine monophosphate. |
| IMP catabolic process | The chemical reactions and pathways resulting in the breakdown of IMP, inosine monophosphate. |
| IMP metabolic process | The chemical reactions and pathways involving IMP, inosine monophosphate. |
| nucleotide phosphorylation | The process of introducing one or more phosphate groups into a nucleotide to produce a phosphorylated nucleoside. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTSWSDRLQ | NAADVPANMD | KHALKKYRRE | AYHRVFVNRS | LAMEKIKCFG | FDMDYTLAVY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KSPEYESLGF | ELTVERLVSI | GYPQELLSFA | YDSTFPTRGL | VFDTLYGNLL | KVDAYGNLLV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CAHGFNFIRG | PETREQYPNK | FIQRDDTERF | YILNTLFNLP | ETYLLACLVD | FFTNCPRYTS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CDTGFKDGDL | FMSYRSMFQD | VRDAVDWVHY | KGSLKEKTVE | NLEKYVVKDG | KLPLLLSRMK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EVGKVFLATN | SDYKYTDKIM | TYLFDFPHGP | KPGSSHRPWQ | SYFDLILVDA | RKPLFFGEGT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VLRQVDTKTG | KLKIGTYTGP | LQHGIVYSGG | SSDTICDLLG | AKGKDILYIG | DHIFGDILKS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KKRQGWRTFL | VIPELAQELH | VWTDKSSLFE | ELQSLDIFLA | ELYKHLDSSS | NERPDISSIQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RRIKKVTHDM | DMCYGMMGSL | FRSGSRQTLF | ASQVMRYADL | YAASFINLLY | YPFSYLFRAA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HVLMPHESTV | EHTHVDINEM | ESPLATRNRT | SVDFKDTDYK | RHQLTRSISE | IKPPNLFPLA |
| 550 | |||||
| PQEITHCHDE | DDDEEEEEEE |