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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q02094: Variant p.Phe65Ser

Ammonium transporter Rh type A
Gene: RHAG
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Variant information Variant position: help 65 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 Phenylalanine (F) to Serine (S) at position 65 (F65S, p.Phe65Ser). 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 large size and aromatic (F) to small size and polar (S) 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 OHST; enhances monovalent cation leak; decreases ammonium fluxes; highly decreases STOM expression; decreases membrane expression; no effect on water permeability. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 65 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 409 The length of the canonical sequence.
Location on the sequence: help GIFFELYPLFQDVHVMIFVG F GFLMTFLKKYGFSSVGINLL 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                         G--IFFELYPLFQDVHVMIFVGFGFLMTFLKKYGFSSVGINLL

                              D--RSLELYPLFQDVHVMIFVGFGFLMTFLKKYGFSSVGIN

Mouse                         D--QFFQLYPLFQDVHVMIFVGFGFLMTFLKKYGFSGVGFN

Rat                           D--QFFQLYPLFQHVHVMIFVGFGFLMTFLKKYGFSGVGFN

Bovine                        DVEKTMESYPFFQDVHIMVFAGFGFLMTFLWKYGFSGVGIN
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 – 409 Ammonium transporter Rh type A
Transmembrane 52 – 72 Helical
Helix 64 – 68



Literature citations
The monovalent cation leak in overhydrated stomatocytic red blood cells results from amino acid substitutions in the Rh-associated glycoprotein.
Bruce L.J.; Guizouarn H.; Burton N.M.; Gabillat N.; Poole J.; Flatt J.F.; Brady R.L.; Borgese F.; Delaunay J.; Stewart G.W.;
Blood 113:1350-1357(2009)
Cited for: INVOLVEMENT IN OHST; VARIANTS OHST ARG-61 AND SER-65; CHARACTERIZATION OF VARIANTS OHST ARG-61 AND SER-65; FUNCTION; TISSUE SPECIFICITY; SUBCELLULAR LOCATION; GLYCOSYLATION; Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S.
Stewart A.K.; Shmukler B.E.; Vandorpe D.H.; Rivera A.; Heneghan J.F.; Li X.; Hsu A.; Karpatkin M.; O'Neill A.F.; Bauer D.E.; Heeney M.M.; John K.; Kuypers F.A.; Gallagher P.G.; Lux S.E.; Brugnara C.; Westhoff C.M.; Alper S.L.;
Am. J. Physiol. 301:C1325-C1343(2011)
Cited for: VARIANT OHST SER-65; CHARACTERIZATION OF VARIANT OHST SER-65; FUNCTION; TRANSPORTER ACTIVITY; Human RhAG ammonia channel is impaired by the Phe65Ser mutation in overhydrated stomatocytic red cells.
Genetet S.; Ripoche P.; Picot J.; Bigot S.; Delaunay J.; Armari-Alla C.; Colin Y.; Mouro-Chanteloup I.;
Am. J. Physiol. 302:C419-C428(2012)
Cited for: CHARACTERIZATION OF VARIANT OHST SER-65; FUNCTION; SUBCELLULAR LOCATION; GLYCOSYLATION; TISSUE SPECIFICITY;
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.