Q5ZJU3
Gene name |
ASNS (RCJMB04_15l3) |
Protein name |
Asparagine synthetase [glutamine-hydrolyzing] |
Names |
Glutamine-dependent asparagine synthetase |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:420574 |
EC number |
6.3.5.4: Carbon--nitrogen ligases with glutamine as amido-N-donor |
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 Q5ZJU3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5ZJU3-F1 | Predicted | AlphaFoldDB |
7 variants for Q5ZJU3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs312748911 | 47 | F>S | No | Ensembl | |
| rs730889010 | 48 | H>P | No | Ensembl | |
| rs737830635 | 64 | V>G | No | Ensembl | |
| rs741548800 | 99 | E>G | No | Ensembl | |
| rs10724145 | 103 | H>Y | No | Ensembl | |
| rs10727702 | 197 | V>A | No | Ensembl | |
| rs314516960 | 542 | V>G | No | Ensembl |
No associated diseases with Q5ZJU3
3 regional properties for Q5ZJU3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Clathrin adaptor, mu subunit, conserved site | 157 - 177 | IPR018240-1 |
| conserved_site | Clathrin adaptor, mu subunit, conserved site | 253 - 267 | IPR018240-2 |
| domain | Mu homology domain | 157 - 421 | IPR028565 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.5.4 | Carbon--nitrogen ligases with glutamine as amido-N-donor |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| asparagine synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: ATP + L-aspartate + L-glutamine = AMP + diphosphate + L-asparagine + L-glutamate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| asparagine biosynthetic process | The chemical reactions and pathways resulting in the formation of asparagine, 2-amino-3-carbamoylpropanoic acid. |
| cellular response to glucose starvation | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of glucose. |
| glutamine metabolic process | The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid. |
| L-asparagine biosynthetic process | The chemical reactions and pathways resulting in the formation of asparagine, (2S)-2-amino-3-carbamoylpropanoic acid. |
| negative regulation of apoptotic process | Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. |
| positive regulation of mitotic cell cycle | Any process that activates or increases the rate or extent of progression through the mitotic cell cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MCGIWALFGS | DECLSVQCLS | AMKIAHRGPD | AFRFENVNGF | TNCCFGFHRL | AVVDQLYGMQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PIRVKKFPYL | WLCYNGEIYN | FKQLQEQFGF | EYQTLVDGEV | ILHLYNRGGI | EQTASMLDGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FAFILLDTAN | RKVFLARDTY | GVRPLFKVLT | DDGFLGVCSE | AKGLINLKHS | TSLFPKVEPF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LPGHYEVLDL | KPSGKVVSVE | VVKFHSYKDE | PLHAACDTVG | NLPSGFDLET | VKSNIRVLFE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NAVRKRLMAH | RRIGCLLSGG | LDSSLVAAVL | LKLMKEMNIK | YPLQTFAIGM | ENSPDLLAAR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KVAAHIGSEH | HEVIFNSEEG | IQAVEEVIFS | LETYDITTVR | ASIGMYLVSK | YIRKKTDSVV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IFSGEGSDEL | TQGYIYFHKA | PSPEEAAEES | ERLLKELYLF | DVLRADRTTA | AHGLELRVPF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LDHRFTSYYL | SLPAELRIPK | NGIEKYLLRQ | SFEDSNLLPK | EILWRPKEAF | SDGIASVKKS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| WFSILQDYID | QQVDDLLLEK | AAEKYPFNPP | RTKESYYYRQ | IFEKHYPGRS | SWLPHYWMPR |
| 550 | 560 | ||||
| WVEATDPSAR | TLKHYKSAIQ | E |