Purification notesab111552 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
FunctionMediates the voltage-dependent potassium ion permeability of excitable membranes. Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient.
Sequence similaritiesBelongs to the potassium channel family. B (Shab) (TC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily.
DomainThe segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. The tail may be important in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
Post-translational modificationsHighly phosphorylated on serine residues in the C-terminal. Differential phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-656 and Ser-720 as well as the N-terminal Ser-15 are all regulated by calcineurin-mediated dephosphorylation. Particularly, Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/ dephosphorylation activities. Tyr-128 can be dephosphorylated by PTPalpha and cyt-PTPepsilon. Phosphorylation levels on Ser-607 are supersensitive to neuronal activity. Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5. Levels then increase to reach adult levels by P14. Phosphorylation levels on Ser-564 and Ser-607 are greatly reduced during seizures, by 40% and 85% respectively.