Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P48544: Variant p.Gly151Glu

G protein-activated inward rectifier potassium channel 4
Gene: KCNJ5
Feedback?
Variant information Variant position: help 151 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Glycine (G) to Glutamate (E) at position 151 (G151E, p.Gly151Glu). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from glycine (G) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description: help In HALD3; results in a profound alteration of channel function with loss of channel selectivity and membrane depolarization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 151 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 419 The length of the canonical sequence.
Location on the sequence: help ENLSGFVSAFLFSIETETTI G YGFRVITEKCPEGIILLLVQ 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         ENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQ

Mouse                         ENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQ

Rat                           ENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIILLLVQ

Pig                           ENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIVLLLVQ

Bovine                        ENLSGFVSAFLFSIETETTIGYGFRVITEKCPEGIVLLLVQ

Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 419 G protein-activated inward rectifier potassium channel 4
Intramembrane 148 – 154 Pore-forming
Motif 149 – 154 Selectivity filter



Literature citations
KCNJ5 mutations in European families with nonglucocorticoid remediable familial hyperaldosteronism.
Mulatero P.; Tauber P.; Zennaro M.C.; Monticone S.; Lang K.; Beuschlein F.; Fischer E.; Tizzani D.; Pallauf A.; Viola A.; Amar L.; Williams T.A.; Strom T.M.; Graf E.; Bandulik S.; Penton D.; Plouin P.F.; Warth R.; Allolio B.; Jeunemaitre X.; Veglio F.; Reincke M.;
Hypertension 59:235-240(2012)
Cited for: VARIANT ARG-168; VARIANTS HALD3 ARG-151; GLU-151 AND ALA-158; CHARACTERIZATION OF VARIANT HALD3 GLU-151; INVOLVEMENT IN ALDOSTERONISM ASSOCIATED WITH ADRENAL ADENOMAS; Hypertension with or without adrenal hyperplasia due to different inherited mutations in the potassium channel KCNJ5.
Scholl U.I.; Nelson-Williams C.; Yue P.; Grekin R.; Wyatt R.J.; Dillon M.J.; Couch R.; Hammer L.K.; Harley F.L.; Farhi A.; Wang W.H.; Lifton R.P.;
Proc. Natl. Acad. Sci. U.S.A. 109:2533-2538(2012)
Cited for: VARIANTS HALD3 ARG-151 AND GLU-151; a Novel Y152C KCNJ5 mutation responsible for familial hyperaldosteronism type III.
Monticone S.; Hattangady N.G.; Penton D.; Isales C.M.; Edwards M.A.; Williams T.A.; Sterner C.; Warth R.; Mulatero P.; Rainey W.E.;
J. Clin. Endocrinol. Metab. 98:E1861-E1865(2013)
Cited for: VARIANT HALD3 CYS-152; CHARACTERIZATION OF VARIANTS HALD3 GLU-151 AND CYS-152; FUNCTION; SUBCELLULAR LOCATION;
Disclaimer: 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.