E444V Summary

KCNH2 E444V was found in 0 papers (see below) with a total of 0 carriers: 0 had LQT2. E444V is not present in gnomAD. E444V has been functionally characterized in 0 papers. This residue is located in a Hotspot region for LQT2.

In silico predictions, functional data (if available), and location in structure are equivalent to observing 6 individuals unaffected with LQT2 and 4 individuals affected with LQT2.


E444V Reported Clinical Data

PMID Year Carriers Unaffected LQT2 Other disease
Summary totals might not agree with the literature table because of duplicate patients, which were excluded from the total counts.

E444V Predictions

PROVEAN scores less than -2 are considered deleterious. REVEL scores higher than 0.5 or 0.75 is considered likely pathogenic (higher sensitivity with the former cutoff, higher specificity with the latter cutoff). A PolyPhen-2 score of 0.85 or greater is considered likely pathogenic. PAM scores reflect the chemistry difference between WT and variant amino acid (more negative being greater difference between the two). BLAST-PSSM reflects the evolutionary conservation of residue substitutions, more negative numbers indicate fewer observations of the specific substitution than is expected.

PAM Score REVEL Score PROVEAN Score Polyphen2 Score BLAST-PSSM
NA 0.513 -2.989 0.005 -2

E444V has 30 neighbors (found in individuals) within 15 ångströms

A residue within a folded protein on average has nearest neighbors that fall roughly into two shells: a "nearest" neighbor around 5-6 angstroms and a second shell around 11 angstroms. NOTE: some residues appear multiple times at different distances. This results from the fact that the functional Kv11.1 channel is a homotetramer and occasionally the same residue from multiple subunits is present within the 15A window. All variants shown in the rightmost column have been observed in at least one individual in the literature or gnomAD.

ResidueNumber Distance(Å) Variants
429 14.7 A429P A429V
430 14.2
431 13.7 F431L
432 13.2
433 12.6
434 12
435 11.4 E435G E435X
436 10.7 T436M
437 10.1
438 9.3 E438K E438X
439 8.5
440 7.6 P440L
441 6.6 P441L P441R
442 5.4
443 3.8 T443fsX T443N
445 3.8
446 5.4
447 6.6 Y447X
448 7.6 A448S A448T
449 8.5
450 9.3
451 10.1 P451L
452 10.7
453 11.4
454 12
455 12.6
456 13.2 D456Y
457 13.7 L457P
458 14.2
459 14.7