| UniProt ID | ACHA_MOUSE | |
|---|---|---|
| UniProt AC | P04756 | |
| Protein Name | Acetylcholine receptor subunit alpha | |
| Gene Name | Chrna1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 457 | |
| Subcellular Localization |
Cell junction, synapse, postsynaptic cell membrane Multi-pass membrane protein. Cell membrane Multi-pass membrane protein. |
|
| Protein Description | After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.. | |
| Protein Sequence | MELSTVLLLLGLCSAGLVLGSEHETRLVAKLFEDYSSVVRPVEDHREIVQVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDVVLYNNADGDFAIVKFTKVLLDYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKEARGWKHWVFYSCCPTTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTSLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHIMPEWVRKVFIDTIPNIMFFSTMKRPSRDKQEKRIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGVKYIAETMKSDQESNNAAEEWKYVAMVMDHILLGVFMLVCLIGTLAVFAGRLIELHQQG | |
| 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 |
|---|---|---|---|---|---|
| 124 | Ubiquitination | DGDFAIVKFTKVLLD CCCEEEEEEEEEHHH | 41.00 | - | |
| 161 | N-linked_Glycosylation | HFPFDEQNCSMKLGT ECCCCCCCCEEEEEE | 20.13 | 17643119 | |
| 369 | Phosphorylation | FTEDIDISDISGKPG EECCCCHHHCCCCCC | 25.74 | 22817900 | |
| 372 | Phosphorylation | DIDISDISGKPGPPP CCCHHHCCCCCCCCC | 45.84 | 20415495 |
| 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 ACHA_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACHA_MOUSE !! | ||||||
* 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 ACHA_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| ACHA_MOUSE | Chrna1 | physical | 22956146 | |
| ACTN1_MOUSE | Actn1 | physical | 22956146 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Crystal structure of the extracellular domain of nAChR alpha1 boundto alpha-bungarotoxin at 1.94 A resolution."; Dellisanti C.D., Yao Y., Stroud J.C., Wang Z.Z., Chen L.; Nat. Neurosci. 10:953-962(2007). Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 21-231 IN COMPLEX WITHALPHA-BUNGAROTOXIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-161. | |