UniProt ID | KAT3_ARATH | |
---|---|---|
UniProt AC | P92960 | |
Protein Name | Potassium channel KAT3 | |
Gene Name | KAT3 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 662 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | Probable modulatory (alpha) subunit of inward-rectifying potassium channels. Could mediate potassium uptake from the soil solution by plant roots in association with AKT1.. | |
Protein Sequence | MSTTTTEARSPLPLLLRRGRSSTALSASTAEARSPLSILQFRRRSSKDVRNITSVSSSLLPAFGTFIEDDNPSSKPFIVLHFDRRYRLWELFLVILVGYSAWASLFELAFEKAAEGALLTIDLVVDFFFAVDIILTFFVSYLDNTTYLNVTDHKLIAKRYLKSVAFVMDVASTLPIQFIYKTITGDVGRGQAFGFLNLLRLWRLRRVAELFKRLEKDAHFNYFVIRVIKLLCVTIFWIHLAGCILYWIAYHYPRPTDTWIGSQVEDFKERSVWLGYTYSMYWSIVTLTTVGYGDLHAVNSREKTFNMFYMLFNIGLTSYIIGIMTNLVVHGALRTFAMRSAINDILRYTSKNRLPDTMREQMLAHMQLKFKTAELRQEEVLQDLPKAIRSSINQHLFRSIIEEAYLFKGFPEGLLVQLVSQIQAEYFPPKMEIILQNEIPTDFYVIVSGGVDIIASKGVSEQVLAKLGPGSMAGEIGVVFNIPQPFTVRTRRLSQVIRIGHHKFKEMVQSDNDVDAKMIIANFMTYLKGLNDELKKEIPFLRDLLDDADAQVQETVQSEETPQSNDEEIVTVSRHENGQIEERRREGVPKRVIIHGQAPPNQDNKNNGDSNGRLIILPDSIQLLFDLAEKKLGKRGSTIAMADGAHVEQIDALRENDHLYIF | |
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 |
---|---|---|---|---|---|
21 | Phosphorylation | LLLRRGRSSTALSAS HHHHCCCCCCCCCCC | 34.56 | 30407730 | |
22 | Phosphorylation | LLRRGRSSTALSAST HHHCCCCCCCCCCCC | 19.15 | 30407730 | |
23 | Phosphorylation | LRRGRSSTALSASTA HHCCCCCCCCCCCCH | 32.63 | 30589143 | |
26 | Phosphorylation | GRSSTALSASTAEAR CCCCCCCCCCCHHHC | 20.08 | 30407730 | |
28 | Phosphorylation | SSTALSASTAEARSP CCCCCCCCCHHHCCC | 25.44 | 30407730 | |
29 | Phosphorylation | STALSASTAEARSPL CCCCCCCCHHHCCCC | 28.38 | 30407730 | |
34 | Phosphorylation | ASTAEARSPLSILQF CCCHHHCCCCHHHHH | 36.92 | 26811356 | |
53 | Phosphorylation | SKDVRNITSVSSSLL CCCCHHCHHHCCCHH | 26.99 | 23776212 | |
54 | Phosphorylation | KDVRNITSVSSSLLP CCCHHCHHHCCCHHH | 19.06 | 23776212 | |
56 | Phosphorylation | VRNITSVSSSLLPAF CHHCHHHCCCHHHHH | 17.61 | 23776212 | |
57 | Phosphorylation | RNITSVSSSLLPAFG HHCHHHCCCHHHHHC | 23.89 | 23776212 | |
58 | Phosphorylation | NITSVSSSLLPAFGT HCHHHCCCHHHHHCC | 26.81 | 23776212 | |
65 | Phosphorylation | SLLPAFGTFIEDDNP CHHHHHCCEECCCCC | 18.26 | 23776212 | |
73 | Phosphorylation | FIEDDNPSSKPFIVL EECCCCCCCCCEEEE | 58.19 | 23776212 | |
74 | Phosphorylation | IEDDNPSSKPFIVLH ECCCCCCCCCEEEEE | 45.68 | 23776212 |
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 KAT3_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KAT3_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 KAT3_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AKT1_ARATH | KT1 | physical | 12678562 | |
SY121_ARATH | SYP121 | physical | 19794113 | |
SY121_ARATH | SYP121 | physical | 20884800 | |
GONS1_ARATH | GONST1 | physical | 22737156 | |
AKT1_ARATH | KT1 | physical | 19509299 | |
UBC34_ARATH | UBC34 | physical | 24833385 | |
CNIH1_ARATH | AT3G12180 | physical | 24833385 | |
PPA3_ARATH | PAP3 | physical | 24833385 | |
VA721_ARATH | VAMP721 | physical | 26002867 | |
VA722_ARATH | SAR1 | physical | 26002867 | |
VA724_ARATH | VAMP724 | physical | 26002867 | |
VA726_ARATH | VAMP726 | physical | 26002867 | |
VA727_ARATH | VAMP727 | physical | 26002867 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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