UniProt ID | PIP27_ARATH | |
---|---|---|
UniProt AC | P93004 | |
Protein Name | Aquaporin PIP2-7 | |
Gene Name | PIP2-7 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 280 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein . |
|
Protein Description | Water channel required to facilitate the transport of water across cell membrane. May be involved in the osmoregulation in plants under high osmotic stress such as under a high salt condition.. | |
Protein Sequence | MSKEVSEEGKTHHGKDYVDPPPAPLLDMGELKSWSFYRALIAEFIATLLFLYVTVATVIGHKKQTGPCDGVGLLGIAWAFGGMIFVLVYCTAGISGGHINPAVTFGLFLARKVSLVRALGYMIAQCLGAICGVGFVKAFMKTPYNTLGGGANTVADGYSKGTALGAEIIGTFVLVYTVFSATDPKRSARDSHIPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNNEKAWDDQWIFWVGPFLGALAAAAYHQYILRASAIKALGSFRSNATN | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MSKEVSEE -------CCHHCCCC | 13.41 | - | |
2 | Phosphorylation | ------MSKEVSEEG ------CCHHCCCCC | 37.21 | 25561503 | |
3 | "N6,N6-dimethyllysine" | -----MSKEVSEEGK -----CCHHCCCCCC | 61.92 | - | |
3 | Methylation | -----MSKEVSEEGK -----CCHHCCCCCC | 61.92 | - | |
6 | Phosphorylation | --MSKEVSEEGKTHH --CCHHCCCCCCCCC | 30.90 | 19880383 | |
11 | Phosphorylation | EVSEEGKTHHGKDYV HCCCCCCCCCCCCCC | 29.93 | 25561503 | |
266 | Phosphorylation | HQYILRASAIKALGS HHHHHHHHHHHHHHH | 24.88 | 19376835 | |
273 | Phosphorylation | SAIKALGSFRSNATN HHHHHHHHHHHCCCC | 20.52 | 30291188 | |
276 | Phosphorylation | KALGSFRSNATN--- HHHHHHHHCCCC--- | 28.89 | 19880383 | |
279 | Phosphorylation | GSFRSNATN------ HHHHHCCCC------ | 45.79 | 19880383 |
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 PIP27_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PIP27_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 PIP27_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NAC89_ARATH | NAC089 | physical | 21798944 | |
SY121_ARATH | SYP121 | physical | 25082856 | |
SYP61_ARATH | SYP61 | physical | 25082856 | |
PIP27_ARATH | PIP3 | physical | 25082856 | |
TSPO_ARATH | TSPO | physical | 25538184 | |
PIP15_ARATH | PIP1;5 | physical | 24833385 | |
UTR2_ARATH | UTR2 | physical | 24833385 | |
HHP2_ARATH | HHP2 | physical | 24833385 | |
HHP4_ARATH | HHP4 | physical | 24833385 | |
PIP14_ARATH | PIP1;4 | physical | 24833385 | |
UBC34_ARATH | UBC34 | physical | 24833385 | |
ACBP6_ARATH | ACBP6 | physical | 24833385 | |
PIP22_ARATH | PIP2B | physical | 24833385 | |
ELIP2_ARATH | ELIP2 | physical | 24833385 | |
HSDD3_ARATH | AT2G43420 | physical | 24833385 | |
CP21D_ARATH | AT3G66654 | physical | 24833385 | |
BETL2_ARATH | AT1G29060 | physical | 24833385 | |
VAP21_ARATH | AT5G47180 | physical | 24833385 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-276 ANDTHR-279, AND MASS SPECTROMETRY. | |
"Novel subsets of the Arabidopsis plasmalemma phosphoproteome identifyphosphorylation sites in secondary active transporters."; Hem S., Rofidal V., Sommerer N., Rossignol M.; Biochem. Biophys. Res. Commun. 363:375-380(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-276 ANDTHR-279, AND MASS 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-273, AND MASSSPECTROMETRY. |