| UniProt ID | ACHA4_HUMAN | |
|---|---|---|
| UniProt AC | P43681 | |
| Protein Name | Neuronal acetylcholine receptor subunit alpha-4 | |
| Gene Name | CHRNA4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 627 | |
| Subcellular Localization |
Cell junction, synapse, postsynaptic cell membrane Multi-pass membrane protein. Cell membrane Multi-pass membrane protein. Cell membrane Lipid-anchor. |
|
| 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 permeable to sodium ions.. | |
| Protein Sequence | MELGGPGAPRLLPPLLLLLGTGLLRASSHVETRAHAEERLLKKLFSGYNKWSRPVANISDVVLVRFGLSIAQLIDVDEKNQMMTTNVWVKQEWHDYKLRWDPADYENVTSIRIPSELIWRPDIVLYNNADGDFAVTHLTKAHLFHDGRVQWTPPAIYKSSCSIDVTFFPFDQQNCTMKFGSWTYDKAKIDLVNMHSRVDQLDFWESGEWVIVDAVGTYNTRKYECCAEIYPDITYAFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPRTHTMPTWVRRVFLDIVPRLLLMKRPSVVKDNCRRLIESMHKMASAPRFWPEPEGEPPATSGTQSLHPPSPSFCVPLDVPAEPGPSCKSPSDQLPPQQPLEAEKASPHPSPGPCRPPHGTQAPGLAKARSLSVQHMSSPGEAVEGGVRCRSRSIQYCVPRDDAAPEADGQAAGALASRNTHSAELPPPDQPSPCKCTCKKEPSSVSPSATVKTRSTKAPPPHLPLSPALTRAVEGVQYIADHLKAEDTDFSVKEDWKYVAMVIDRIFLWMFIIVCLLGTVGLFLPPWLAGMI | |
| 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 |
|---|---|---|---|---|---|
| 10 | Methylation | LGGPGAPRLLPPLLL CCCCCHHHCHHHHHH | 48.61 | 18567405 | |
| 25 | Methylation | LLGTGLLRASSHVET HHHHCHHHHCCCHHH | 37.15 | 18567415 | |
| 33 | Methylation | ASSHVETRAHAEERL HCCCHHHHHHHHHHH | 15.74 | 18567425 | |
| 46 | Phosphorylation | RLLKKLFSGYNKWSR HHHHHHHCCCCCCCC | 51.29 | 24961811 | |
| 57 | N-linked_Glycosylation | KWSRPVANISDVVLV CCCCCCCCCCHHHHH | 34.23 | UniProtKB CARBOHYD | |
| 84 | Phosphorylation | DEKNQMMTTNVWVKQ CHHCCEEEEEEEECC | 15.18 | 30619164 | |
| 85 | Phosphorylation | EKNQMMTTNVWVKQE HHCCEEEEEEEECCC | 15.18 | 30619164 | |
| 107 | N-linked_Glycosylation | WDPADYENVTSIRIP CCHHHCCCCCEEECC | 35.82 | UniProtKB CARBOHYD | |
| 115 | Phosphorylation | VTSIRIPSELIWRPD CCEEECCHHHCCCCC | 42.54 | 27794612 | |
| 136 | Phosphorylation | ADGDFAVTHLTKAHL CCCCEEEEEECEEEE | 14.03 | 26437602 | |
| 174 | N-linked_Glycosylation | FFPFDQQNCTMKFGS EEECCCCCCEEEECE | 20.00 | UniProtKB CARBOHYD | |
| 196 | Phosphorylation | IDLVNMHSRVDQLDF EEEEECCCCCCCCCH | 24.19 | - | |
| 271 | S-palmitoylation | VFYLPSECGEKITLC HHHCCCCCCHHHHHH | 11.35 | - | |
| 334 | Phosphorylation | VLNVHHRSPRTHTMP HHCCCCCCCCCCCCC | 17.87 | 26074081 | |
| 337 | Phosphorylation | VHHRSPRTHTMPTWV CCCCCCCCCCCCHHH | 25.69 | 26074081 | |
| 339 | Phosphorylation | HRSPRTHTMPTWVRR CCCCCCCCCCHHHHH | 25.00 | 26074081 | |
| 342 | Phosphorylation | PRTHTMPTWVRRVFL CCCCCCCHHHHHHHH | 26.27 | 26074081 | |
| 362 | Phosphorylation | LLLMKRPSVVKDNCR HHHHCCCHHHHHHHH | 43.50 | 22817900 | |
| 424 | Phosphorylation | EPGPSCKSPSDQLPP CCCCCCCCHHHCCCC | 33.68 | - | |
| 465 | Phosphorylation | PGLAKARSLSVQHMS CCHHHHHHCEEEECC | 29.83 | 23532336 | |
| 467 | Phosphorylation | LAKARSLSVQHMSSP HHHHHHCEEEECCCC | 22.45 | 22817900 | |
| 488 | Phosphorylation | GVRCRSRSIQYCVPR CEEEECCEEEEEEEC | 18.45 | - | |
| 538 | Phosphorylation | CTCKKEPSSVSPSAT CEECCCCCCCCCCCE | 44.45 | - | |
| 539 | Phosphorylation | TCKKEPSSVSPSATV EECCCCCCCCCCCEE | 37.01 | - | |
| 541 | Phosphorylation | KKEPSSVSPSATVKT CCCCCCCCCCCEEEE | 18.32 | - | |
| 543 | Phosphorylation | EPSSVSPSATVKTRS CCCCCCCCCEEEECC | 29.12 | - | |
| 545 | Phosphorylation | SSVSPSATVKTRSTK CCCCCCCEEEECCCC | 27.20 | - | |
| 550 | Phosphorylation | SATVKTRSTKAPPPH CCEEEECCCCCCCCC | 39.22 | 22817900 | |
| 561 | Phosphorylation | PPPHLPLSPALTRAV CCCCCCCCHHHHHHH | 13.24 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 362 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 467 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
| 550 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ACHA4_HUMAN !! | ||||||
* 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 ACHA4_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| 1433F_HUMAN | YWHAH | physical | 11352901 | |
| UBQL1_MOUSE | Ubqln1 | physical | 16091357 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H00807 | Autosomal dominant nocturnal frontal lobe epilepsy (ADNFLE); Nocturnal frontal lobe epilepsy (NFLE) | |||||
| OMIM Disease | ||||||
| 600513 | Epilepsy, nocturnal frontal lobe, 1 (ENFL1) | |||||
| Kegg Drug | ||||||
| D00611 | Mecamylamine hydrochloride (USP); Inversine (TN) | |||||
| D00999 | Acetylcholine chloride (JP16/USP/INN); Miochol (TN) | |||||
| D02202 | Lobeline hydrochloride (JAN) | |||||
| D02204 | Hexamethonium bromide (JAN/INN); Hexamethonium bromide (TN) | |||||
| D02364 | Lobeline (INN) | |||||
| D02839 | Altinicline maleate (USAN) | |||||
| D06282 | Varenicline tartrate (USAN); Chantix (TN) | |||||
| D08138 | Lobeline sulfate; Smokeless (TN) | |||||
| D08669 | Varenicline (INN) | |||||
| D08935 | Ispronicline (INN/USAN) | |||||
| D08987 | Rivanicline galactarate (USAN) | |||||
| D09367 | Pozanicline (USAN); ABT-089 | |||||
| D09368 | Pozanicline tartrate (USAN) | |||||
| D09382 | Sofinicline (USAN) | |||||
| D09383 | Sofinicline benzenesulfonate (USAN) | |||||
| D10111 | Dexmecamylamine (USAN) | |||||
| D10112 | Dexmecamylamine hydrochloride (USAN) | |||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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