Sequence information
Variant position: 433 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:
AYSYKTNEWFFVAPMNTRRS
S VGVGVVEGKLYAVGGYDGAS
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 AYSYKTNEWFFVAPMNTRRSS VGVGVVEGKLYAVGGYDGAS
Mouse AYSYKTNEWFFVAPMNTRRSS VGVGVVEGKLYAVGGYDGAS
Rat AYSYKTNEWFFVAPMNTRRSS VGVGVVEGKLYAVGGYDGAS
Bovine AYSYKTNEWFFVAPMNTRRSS VGVGVVEGKLYAVGGYDGAS
Zebrafish AYNPKANEWMFVAPMNTRRSS VGVGVVDGKLYAVGGYDGAS
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.
Literature citations
Impaired degradation of WNK by Akt and PKA phosphorylation of KLHL3.
Yoshizaki Y.; Mori Y.; Tsuzaki Y.; Mori T.; Nomura N.; Wakabayashi M.; Takahashi D.; Zeniya M.; Kikuchi E.; Araki Y.; Ando F.; Isobe K.; Nishida H.; Ohta A.; Susa K.; Inoue Y.; Chiga M.; Rai T.; Sasaki S.; Uchida S.; Sohara E.;
Biochem. Biophys. Res. Commun. 467:229-234(2015)
Cited for: PHOSPHORYLATION AT SER-10; THR-295; THR-375; SER-376 AND SER-433; INTERACTION WITH WNK4; CHARACTERIZATION OF VARIANT PHA2D GLY-433; MUTAGENESIS OF SER-433;
KLHL3 mutations cause familial hyperkalemic hypertension by impairing ion transport in the distal nephron.
Louis-Dit-Picard H.; Barc J.; Trujillano D.; Miserey-Lenkei S.; Bouatia-Naji N.; Pylypenko O.; Beaurain G.; Bonnefond A.; Sand O.; Simian C.; Vidal-Petiot E.; Soukaseum C.; Mandet C.; Broux F.; Chabre O.; Delahousse M.; Esnault V.; Fiquet B.; Houillier P.; Bagnis C.I.; Koenig J.; Konrad M.; Landais P.; Mourani C.; Niaudet P.; Probst V.; Thauvin C.; Unwin R.J.; Soroka S.D.; Ehret G.; Ossowski S.; Caulfield M.; Bruneval P.; Estivill X.; Froguel P.; Hadchouel J.; Schott J.J.; Jeunemaitre X.;
Nat. Genet. 44:456-460(2012)
Cited for: VARIANTS PHA2D GLY-228; MET-361; TRP-362; TRP-384; VAL-398; LEU-410; LEU-426; ASN-432; GLY-433; VAL-500; HIS-528; CYS-528 AND LYS-529; FUNCTION; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; INTERACTION WITH SLC12A3;
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.