UniProt ID | KCNJ2_MOUSE | |
---|---|---|
UniProt AC | P35561 | |
Protein Name | Inward rectifier potassium channel 2 | |
Gene Name | Kcnj2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 428 | |
Subcellular Localization |
Membrane Multi-pass membrane protein. Membrane Lipid-anchor . |
|
Protein Description | Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium.. | |
Protein Sequence | MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDTSKVSKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEEEDSENGVPESTSTDSPPGIDLHNQASVPLEPRPLRRESEI | |
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 |
---|---|---|---|---|---|
2 | Myristoylation | ------MGSVRTNRY ------CCCCCCCCE | - | ||
3 | Phosphorylation | -----MGSVRTNRYS -----CCCCCCCCEE | 23375375 | ||
6 | Phosphorylation | --MGSVRTNRYSIVS --CCCCCCCCEEEEE | 23375375 | ||
9 | Phosphorylation | GSVRTNRYSIVSSEE CCCCCCCEEEEECCC | 29899451 | ||
10 | Phosphorylation | SVRTNRYSIVSSEED CCCCCCEEEEECCCH | 22817900 | ||
13 | Phosphorylation | TNRYSIVSSEEDGMK CCCEEEEECCCHHHH | 19144319 | ||
14 | Phosphorylation | NRYSIVSSEEDGMKL CCEEEEECCCHHHHH | 21183079 | ||
76 | S-nitrosylation | LADIFTTCVDIRWRW HHHHHHHHHHHHHHH | - | ||
76 | S-nitrosocysteine | LADIFTTCVDIRWRW HHHHHHHHHHHHHHH | - | ||
242 | Phosphorylation | RITSEGEYIPLDQID CCCCCCCEEEHHHEE | - | ||
336 | Phosphorylation | VLFEEKHYYKVDYSR EECEEEEEEEEEHHH | 25367039 | ||
337 | Phosphorylation | LFEEKHYYKVDYSRF ECEEEEEEEEEHHHC | 25367039 | ||
338 | Ubiquitination | FEEKHYYKVDYSRFH CEEEEEEEEEHHHCC | 22790023 | ||
346 | Ubiquitination | VDYSRFHKTYEVPNT EEHHHCCCEEECCCC | 22790023 | ||
347 | Phosphorylation | DYSRFHKTYEVPNTP EHHHCCCEEECCCCC | - | ||
348 | Phosphorylation | YSRFHKTYEVPNTPL HHHCCCEEECCCCCC | - | ||
391 | Phosphorylation | SKEEEEDSENGVPES CHHHHHCCCCCCCCC | 23737553 | ||
398 | Phosphorylation | SENGVPESTSTDSPP CCCCCCCCCCCCCCC | 23737553 | ||
399 | Phosphorylation | ENGVPESTSTDSPPG CCCCCCCCCCCCCCC | 23737553 | ||
400 | Phosphorylation | NGVPESTSTDSPPGI CCCCCCCCCCCCCCC | 23737553 | ||
401 | Phosphorylation | GVPESTSTDSPPGID CCCCCCCCCCCCCCC | 23737553 | ||
403 | Phosphorylation | PESTSTDSPPGIDLH CCCCCCCCCCCCCCC | 23737553 |
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 KCNJ2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KCNJ2_MOUSE !! |
* 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 KCNJ2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of KCNJ2_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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