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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UH77: Variant p.Ala340Val

Kelch-like protein 3
Gene: KLHL3
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Variant information Variant position: help 340 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 Alanine (A) to Valine (V) at position 340 (A340V, p.Ala340Val). 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 small size and hydrophobic (A) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 PHA2D; does not affect interaction with WNK1 or CUL3. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 340 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 587 The length of the canonical sequence.
Location on the sequence: help YDFEEDRWDQIAELPSRRCR A GVVFMAGHVYAVGGFNGSLR 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                         YDFEEDRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLR

Mouse                         YDFEEGRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLR

Rat                           YDFEEGRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLR

Bovine                        YDFEEDRWDQIAELPSRRCRAGVVFMAGHVYAVGGFNGSLR

Zebrafish                     YDFQEDRWYQVADLPSRRCRAGVVYMAGKVYAVGGFNGSLR
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 – 587 Kelch-like protein 3
Repeat 302 – 347 Kelch 1



Literature citations
The CUL3-KLHL3 E3 ligase complex mutated in Gordon's hypertension syndrome interacts with and ubiquitylates WNK isoforms: disease-causing mutations in KLHL3 and WNK4 disrupt interaction.
Ohta A.; Schumacher F.R.; Mehellou Y.; Johnson C.; Knebel A.; Macartney T.J.; Wood N.T.; Alessi D.R.; Kurz T.;
Biochem. J. 451:111-122(2013)
Cited for: FUNCTION; INTERACTION WITH CUL3; CHARACTERIZATION OF VARIANTS PHA2D GLU-77; VAL-78; ALA-85; PHE-164; ARG-309; VAL-340; GLN-384; PRO-387; LEU-410; ASN-432; ASN-433; THR-494; HIS-528; CYS-528 AND LYS-529; Mutations in kelch-like 3 and cullin 3 cause hypertension and electrolyte abnormalities.
Boyden L.M.; Choi M.; Choate K.A.; Nelson-Williams C.J.; Farhi A.; Toka H.R.; Tikhonova I.R.; Bjornson R.; Mane S.M.; Colussi G.; Lebel M.; Gordon R.D.; Semmekrot B.A.; Poujol A.; Valimaki M.J.; De Ferrari M.E.; Sanjad S.A.; Gutkin M.; Karet F.E.; Tucci J.R.; Stockigt J.R.; Keppler-Noreuil K.M.; Porter C.C.; Anand S.K.; Whiteford M.L.; Davis I.D.; Dewar S.B.; Bettinelli A.; Fadrowski J.J.; Belsha C.W.; Hunley T.E.; Nelson R.D.; Trachtman H.; Cole T.R.; Pinsk M.; Bockenhauer D.; Shenoy M.; Vaidyanathan P.; Foreman J.W.; Rasoulpour M.; Thameem F.; Al-Shahrouri H.Z.; Radhakrishnan J.; Gharavi A.G.; Goilav B.; Lifton R.P.;
Nature 482:98-102(2012)
Cited for: VARIANTS PHA2D GLU-77; VAL-78; ALA-85; PHE-164; ARG-309; CYS-322; ILE-336; VAL-340; GLN-384; PRO-387; LEU-410; THR-427; GLN-431; ASN-432; ASN-433; 470-TRP--LEU-587 DEL; THR-494; THR-501; CYS-528; HIS-528; CYS-557 AND TRP-575; VARIANT ILE-438;
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.