UniProt ID | AQP1_HUMAN | |
---|---|---|
UniProt AC | P29972 | |
Protein Name | Aquaporin-1 | |
Gene Name | AQP1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 269 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
Protein Description | Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.. | |
Protein Sequence | MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKVSLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAILSGITSSLTGNSLGRNDLADGVNSGQGLGIEIIGTLQLVLCVLATTDRRRRDLGGSAPLAIGLSVALGHLLAIDYTGCGINPARSFGSAVITHNFSNHWIFWVGPFIGGALAVLIYDFILAPRSSDLTDRVKVWTSGQVEEYDLDADDINSRVEMKPK | |
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 |
---|---|---|---|---|---|
42 | N-linked_Glycosylation | FKYPVGNNQTAVQDN CCCCCCCCCCCCCCC | 34.35 | UniProtKB CARBOHYD | |
157 | Phosphorylation | VLCVLATTDRRRRDL HHHHHHCCCHHHHHC | 23.15 | 22817900 | |
167 | Phosphorylation | RRRDLGGSAPLAIGL HHHHCCCCCCHHHHH | 25.55 | 25332170 | |
175 | Phosphorylation | APLAIGLSVALGHLL CCHHHHHHHHHHHHH | 10.51 | 25332170 | |
205 | N-linked_Glycosylation | GSAVITHNFSNHWIF CCEEEEECCCCCEEE | 33.13 | UniProtKB CARBOHYD | |
236 | O-linked_Glycosylation | FILAPRSSDLTDRVK HHHCCCCCCCCCCEE | 37.61 | 12623621 | |
236 | Phosphorylation | FILAPRSSDLTDRVK HHHCCCCCCCCCCEE | 37.61 | - | |
239 | Phosphorylation | APRSSDLTDRVKVWT CCCCCCCCCCEEEEC | 27.10 | 28857561 | |
246 | Phosphorylation | TDRVKVWTSGQVEEY CCCEEEECCCCEEEE | 26.43 | 23403867 | |
247 | Phosphorylation | DRVKVWTSGQVEEYD CCEEEECCCCEEEEE | 16.12 | 26657352 | |
253 | Phosphorylation | TSGQVEEYDLDADDI CCCCEEEEECCHHHH | 14.32 | 23403867 | |
262 | Phosphorylation | LDADDINSRVEMKPK CCHHHHHCCCCCCCC | 37.73 | 19664994 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
157 | T | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
157 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
157 | T | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
239 | T | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
239 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
239 | T | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AQP1_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 AQP1_HUMAN !! |
Kegg Disease | |
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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 | |
DB00819 | Acetazolamide |
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Phosphorylation | |
Reference | PubMed |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASSSPECTROMETRY. |