UniProt ID | ASIC2_HUMAN | |
---|---|---|
UniProt AC | Q16515 | |
Protein Name | Acid-sensing ion channel 2 {ECO:0000303|PubMed:10842183} | |
Gene Name | ASIC2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 512 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. Localized at the plasma membrane of neurons, in the soma and punctated peripheral processes.. |
|
Protein Description | Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li(+) and K(+). Generates a biphasic current with a fast inactivating and a slow sustained phase. Heteromeric channel assembly seems to modulate.. | |
Protein Sequence | MDLKESPSEGSLQPSSIQIFANTSTLHGIRHIFVYGPLTIRRVLWAVAFVGSLGLLLVESSERVSYYFSYQHVTKVDEVVAQSLVFPAVTLCNLNGFRFSRLTTNDLYHAGELLALLDVNLQIPDPHLADPSVLEALRQKANFKHYKPKQFSMLEFLHRVGHDLKDMMLYCKFKGQECGHQDFTTVFTKYGKCYMFNSGEDGKPLLTTVKGGTGNGLEIMLDIQQDEYLPIWGETEETTFEAGVKVQIHSQSEPPFIQELGFGVAPGFQTFVATQEQRLTYLPPPWGECRSSEMGLDFFPVYSITACRIDCETRYIVENCNCRMVHMPGDAPFCTPEQHKECAEPALGLLAEKDSNYCLCRTPCNLTRYNKELSMVKIPSKTSAKYLEKKFNKSEKYISENILVLDIFFEALNYETIEQKKAYEVAALLGDIGGQMGLFIGASILTILELFDYIYELIKEKLLDLLGKEEDEGSHDENVSTCDTMPNHSETISHTVNVPLQTTLGTLEEIAC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
8 | Phosphorylation | MDLKESPSEGSLQPS CCCCCCCCCCCCCCC | 64.96 | 25332170 | |
11 | Phosphorylation | KESPSEGSLQPSSIQ CCCCCCCCCCCCEEE | 21.56 | - | |
39 | Phosphorylation | IFVYGPLTIRRVLWA EEEECCHHHHHHHHH | 18.64 | 12399460 | |
134 (in isoform 2) | Phosphorylation | - | 3.60 | - | |
357 | Phosphorylation | LAEKDSNYCLCRTPC HHHCCCCEEEECCCC | 7.25 | - | |
365 | N-linked_Glycosylation | CLCRTPCNLTRYNKE EEECCCCCCCCCCCC | 45.72 | UniProtKB CARBOHYD | |
380 | Phosphorylation | LSMVKIPSKTSAKYL CCEEECCCHHHHHHH | 52.63 | 24719451 | |
392 | N-linked_Glycosylation | KYLEKKFNKSEKYIS HHHHHHCCCCHHCCC | 56.68 | UniProtKB CARBOHYD |
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 ASIC2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASIC2_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 ASIC2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ASIC3_HUMAN | ASIC3 | physical | 10842183 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...