Variant position: 565 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1243 The length of the canonical sequence.
Location on the sequence:
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 PMAPGPPSVFPPEPEEPEAD QHQPFLFRHASYSSTTSDCET
Mouse SLAPGPPSAFPPEPEEPEAD QHQSFLFRHASYSSTTSDCET
Rat SMTPGPPSAFPPEPEEPEAD QHQSFLFRHASYSSTTSDCET
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
1 – 1243 Serine/threonine-protein kinase WNK4
Human hypertension caused by mutations in WNK kinases.
Wilson F.H.; Disse-Nicodeme S.; Choate K.A.; Ishikawa K.; Nelson-Williams C.; Desitter I.; Gunel M.; Milford D.V.; Lipkin G.W.; Achard J.-M.; Feely M.P.; Dussol B.; Berland Y.; Unwin R.J.; Mayan H.; Simon D.B.; Farfel Z.; Jeunemaitre X.; Lifton R.P.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); DISEASE; VARIANTS PHA2B LYS-562; ALA-564; GLU-565 AND CYS-1185;
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: INTERACTION WITH KLHL3; CHARACTERIZATION OF VARIANTS PHA2B LYS-562 AND GLU-565;
Kelch-like 3 and Cullin 3 regulate electrolyte homeostasis via ubiquitination and degradation of WNK4.
Shibata S.; Zhang J.; Puthumana J.; Stone K.L.; Lifton R.P.;
Proc. Natl. Acad. Sci. U.S.A. 110:7838-7843(2013)
Cited for: UBIQUITINATION AT LYS-157; LYS-175; LYS-186; LYS-226; LYS-241; LYS-328; LYS-387; LYS-393; LYS-450; LYS-454; LYS-1010; LYS-1144; LYS-1157 AND LYS-1158; INTERACTION WITH KLHL3; CHARACTERIZATION OF VARIANTS PHA2B LYS-562 AND GLU-565;
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