Sequence information
Variant position: 438 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 587 The length of the canonical sequence.
Location on the sequence:
TNEWFFVAPMNTRRSSVGVG
V VEGKLYAVGGYDGASRQCLS
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 TNEWFFVAPMNTRRSSVGVGV VEGKLYAVGGYDGASRQCLS
Mouse TNEWFFVAPMNTRRSSVGVGV VEGKLYAVGGYDGASRQCLS
Rat TNEWFFVAPMNTRRSSVGVGV VEGKLYAVGGYDGASRQCLS
Bovine TNEWFFVAPMNTRRSSVGVGV VEGKLYAVGGYDGASRQCLS
Zebrafish ANEWMFVAPMNTRRSSVGVGV VDGKLYAVGGYDGASRQCLS
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
Chain
1 – 587
Kelch-like protein 3
Repeat
396 – 441
Kelch 3
Modified residue
433 – 433
Phosphoserine; by PKA
Mutagenesis
433 – 433
S -> ED. Phosphomimetic mutant that shows decreased interaction with WNK4.
Beta strand
435 – 439
Literature citations
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; THR-494; THR-501; HIS-528; CYS-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.