Variant position: 404 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 630 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human KIFGSICSLSGVLVIALPVP VIVSNFSRIYHQNQRADKRRA
Mouse KIFGSICSLSGVLVIALPVP VIVSNFSRIYHQNQRADKRRA
Rat KIFGSICSLSGVLVIALPVP VIVSNFSRIYHQNQRADKRRA
Rabbit KIFGSICSLSGVLVIALPVP VIVSNFSRIYHQNQRADKRRA
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 630 Potassium voltage-gated channel subfamily D member 2
385 – 413 Helical; Name=Segment S6
397 – 397 V -> A. May impair protein folding.
398 – 398 I -> A. Loss of channel activity.
399 – 399 A -> V. May impair protein folding.
401 – 401 P -> A. May impair protein folding.
402 – 404 VPV -> IPI. Increases pak current amplitude and causes a positive shift in the voltage-dependence of activation and steady-state inactivation. May increase the affinity for the closed-inactivated state of the channel.
403 – 403 P -> A. Loss of channel activity.
405 – 405 I -> A. Loss of channel activity.
406 – 406 V -> A. Loss of channel activity.
407 – 407 S -> A. Increases peak current amplitude but has no effect on the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel.
408 – 408 N -> A. Decreases peak current amplitude and causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel.
409 – 409 F -> A. May impair protein folding.
Exome sequencing identifies de novo gain of function missense mutation in KCND2 in identical twins with autism and seizures that slows potassium channel inactivation.
Lee H.; Lin M.C.; Kornblum H.I.; Papazian D.M.; Nelson S.F.;
Hum. Mol. Genet. 23:3481-3489(2014)
Cited for: VARIANT MET-404; CHARACTERIZATION OF VARIANT MET-404; FUNCTION; SUBCELLULAR LOCATION;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.