| UniProt ID | ASIC3_HUMAN | |
|---|---|---|
| UniProt AC | Q9UHC3 | |
| Protein Name | Acid-sensing ion channel 3 | |
| Gene Name | ASIC3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 531 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein. Cytoplasm. Cell surface expression may be stabilized by interaction with LIN7B and cytoplasmic retention by interaction with DLG4. In part cytoplasmic in cochlea cells (By similarity).. |
|
| Protein Description | Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties.. | |
| Protein Sequence | MKPTSGPEEARRPASDIRVFASNCSMHGLGHVFGPGSLSLRRGMWAAAVVLSVATFLYQVAERVRYYREFHHQTALDERESHRLIFPAVTLCNINPLRRSRLTPNDLHWAGSALLGLDPAEHAAFLRALGRPPAPPGFMPSPTFDMAQLYARAGHSLDDMLLDCRFRGQPCGPENFTTIFTRMGKCYTFNSGADGAELLTTTRGGMGNGLDIMLDVQQEEYLPVWRDNEETPFEVGIRVQIHSQEEPPIIDQLGLGVSPGYQTFVSCQQQQLSFLPPPWGDCSSASLNPNYEPEPSDPLGSPSPSPSPPYTLMGCRLACETRYVARKCGCRMVYMPGDVPVCSPQQYKNCAHPAIDAMLRKDSCACPNPCASTRYAKELSMVRIPSRAAARFLARKLNRSEAYIAENVLALDIFFEALNYETVEQKKAYEMSELLGDIGGQMGLFIGASLLTILEILDYLCEVFRDKVLGYFWNRQHSQRHSSTNLLQEGLGSHRTQVPHLSLGPRPPTPPCAVTKTLSASHRTCYLVTQL | |
| 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 |
|---|---|---|---|---|---|
| 5 | Phosphorylation | ---MKPTSGPEEARR ---CCCCCCHHHHCC | 61.96 | 9886053 | |
| 37 | Phosphorylation | GHVFGPGSLSLRRGM CCCCCCCCHHHHHHH | 20.23 | 22167270 | |
| 39 | Phosphorylation | VFGPGSLSLRRGMWA CCCCCCHHHHHHHHH | 22.87 | 22167270 | |
| 175 | N-linked_Glycosylation | GQPCGPENFTTIFTR CCCCCCCCCEEEEEE | 42.57 | 9886053 | |
| 175 | N-linked_Glycosylation | GQPCGPENFTTIFTR CCCCCCCCCEEEEEE | 42.57 | UniProtKB CARBOHYD | |
| 364 (in isoform 4) | Phosphorylation | - | 6.92 | 24114839 | |
| 370 (in isoform 4) | Phosphorylation | - | 6.25 | 24114839 | |
| 375 | Phosphorylation | NPCASTRYAKELSMV CCCCCHHHHHHHCCC | 23.32 | 17693683 | |
| 380 | Phosphorylation | TRYAKELSMVRIPSR HHHHHHHCCCCCCHH | 19.14 | 22964224 | |
| 386 | Phosphorylation | LSMVRIPSRAAARFL HCCCCCCHHHHHHHH | 31.98 | 20363803 | |
| 398 | N-linked_Glycosylation | RFLARKLNRSEAYIA HHHHHHCCCCHHHHH | 48.76 | 9886053 | |
| 398 | N-linked_Glycosylation | RFLARKLNRSEAYIA HHHHHHCCCCHHHHH | 48.76 | 9886053 | |
| 429 | Phosphorylation | TVEQKKAYEMSELLG HHHHHHHHHHHHHHH | 22.50 | - | |
| 478 | Phosphorylation | YFWNRQHSQRHSSTN HHCCCHHHHCCCHHH | 22.14 | 9886053 | |
| 484 (in isoform 2) | Phosphorylation | - | 32.66 | - | |
| 487 (in isoform 2) | Phosphorylation | - | 4.77 | - | |
| 488 (in isoform 2) | Phosphorylation | - | 45.97 | - | |
| 491 (in isoform 2) | Phosphorylation | - | 6.64 | 9886053 | |
| 493 | Phosphorylation | LLQEGLGSHRTQVPH HHHHCCCCCCCCCCC | 18.16 | 9886053 | |
| 521 (in isoform 3) | Phosphorylation | - | 15.32 | - |
| 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 ASIC3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASIC3_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 ASIC3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| MAGI1_HUMAN | MAGI1 | physical | 15317815 | |
| GOPC_HUMAN | GOPC | physical | 15317815 | |
| LIN7B_HUMAN | LIN7B | physical | 15317815 | |
| DLG4_HUMAN | DLG4 | physical | 15317815 |
| 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. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-375, AND MASSSPECTROMETRY. | |
