| UniProt ID | PIP22_ARATH | |
|---|---|---|
| UniProt AC | P43287 | |
| Protein Name | Aquaporin PIP2-2 | |
| Gene Name | PIP2-2 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 285 | |
| Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
| Protein Description | Water channel required to facilitate the transport of water across cell membrane. Plays an predominant role in root water uptake process in conditions of reduced transpiration, and in osmotic fluid transport. Its function is impaired by Hg(2+). Inhibited by cytosolic acidosis which occurs during anoxia in roots.. | |
| Protein Sequence | MAKDVEGPEGFQTRDYEDPPPTPFFDADELTKWSLYRAVIAEFVATLLFLYITVLTVIGYKIQSDTKAGGVDCGGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLIRAVLYMVAQCLGAICGVGFVKAFQSSYYDRYGGGANSLADGYNTGTGLAAEIIGTFVLVYTVFSATDPKRNARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNKSKPWDDHWIFWVGPFIGAAIAAFYHQFVLRASGSKSLGSFRSAANV | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MAKDVEGP -------CCCCCCCC | 10.63 | - | |
| 2 | Acetylation | ------MAKDVEGPE ------CCCCCCCCC | 19.43 | - | |
| 3 | "N6,N6-dimethyllysine" | -----MAKDVEGPEG -----CCCCCCCCCC | 62.09 | - | |
| 3 | Methylation | -----MAKDVEGPEG -----CCCCCCCCCC | 62.09 | 16839310 | |
| 22 | Phosphorylation | DYEDPPPTPFFDADE CCCCCCCCCCCCHHH | 38.20 | 23111157 | |
| 275 | Phosphorylation | LRASGSKSLGSFRSA HHHCCCCCCCCHHHC | 39.39 | 23776212 | |
| 278 | Phosphorylation | SGSKSLGSFRSAANV CCCCCCCCHHHCCCC | 23.84 | 30291188 | |
| 281 | Phosphorylation | KSLGSFRSAANV--- CCCCCHHHCCCC--- | 29.71 | 30291188 |
| 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 PIP22_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PIP22_ARATH !! | ||||||
* 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 PIP22_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CHX9_ARATH | CHX9 | physical | 21423366 | |
| EPFL6_ARATH | CHAL | physical | 21423366 | |
| PIP21_ARATH | PIP2A | physical | 21423366 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Methylation | |
| Reference | PubMed |
| "Methylation of aquaporins in plant plasma membrane."; Santoni V., Verdoucq L., Sommerer N., Vinh J., Pflieger D., Maurel C.; Biochem. J. 400:189-197(2006). Cited for: METHYLATION AT LYS-3, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis."; Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.; Mol. Cell. Proteomics 6:1711-1726(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-281, ANDMASS SPECTROMETRY. | |
| "Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Plant Cell 16:2394-2405(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-281, ANDMASS SPECTROMETRY. | |
