Variant position: 337 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 405 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 DLTPVVDAITDALLAARPRR RYYPGQGLGLMYFIHYYLPEG
Mouse DLSPVVDAIIDALLAAQPRS RYYPGRGLGLMYFIHHYLPEG
Rat DLSPVVDAIIDALLAAQPRS RYYTGRGLGLMYFIHHYLPGG
Bovine DLSPVVDAITDALLAAQPLR RYYPGHGLGLIYFIHYYLPEG
Rabbit DLSPVVDAITDALLAARPRP RYYPGRGLGLMYFIHYYLPEG
Sheep DLSPVVDAITDALLAAQPRR RYYPGHGLGLIYFIHYYLPEG
Zebrafish DLSPVIDTIVEALLSPQPQV RYYAGPGLILMYFICSYLPLS
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 – 405 11-beta-hydroxysteroid dehydrogenase type 2
335 – 339 Essential for protein stability
335 – 335 R -> AQ. Reduced enzyme activity.
335 – 335 R -> K. No effect on enzyme activity.
336 – 336 R -> AQ. Almost complete loss of enzyme activity.
336 – 336 R -> K. Reduced enzyme activity.
337 – 337 R -> AQ. Almost complete loss of enzyme activity.
337 – 337 R -> K. Reduced enzyme activity.
338 – 338 Y -> FA. Complete loss of enzyme activity.
339 – 339 Y -> AFH. Reduced enzyme activity.
A mutation in the HSD11B2 gene in a family with apparent mineralocorticoid excess.
Wilson R.C.; Krozowski Z.S.; Li K.; Obeyesekere V.R.; Razzaghy-Azar M.; Harbison M.D.; Wei J.-Q.; Shackleton C.H.L.; Funder J.W.; New M.I.;
J. Clin. Endocrinol. Metab. 80:2263-2266(1995)
Cited for: VARIANT AME CYS-337;
Examination of genotype and phenotype relationships in 14 patients with apparent mineralocorticoid excess.
Dave-Sharma S.; Wilson R.C.; Harbison M.D.; Newfield R.; Azar M.R.; Krozowski Z.S.; Funder J.W.; Shackleton C.H.L.; Bradlow H.L.; Wei J.-Q.; Hertecant J.; Moran A.; Neiberger R.E.; Balfe J.W.; Fattah A.; Daneman D.; Akkurt H.I.; De Santis C.; New M.I.;
J. Clin. Endocrinol. Metab. 83:2244-2254(1998)
Cited for: VARIANTS AME CYS-186; CYS-208; ASN-244; ARG-250; 250-PRO-SER-251; CYS-337 AND 337-ARG-TYR-338 DELINS HIS;
Impaired protein stability of 11beta-hydroxysteroid dehydrogenase type 2: a novel mechanism of apparent mineralocorticoid excess.
Atanasov A.G.; Ignatova I.D.; Nashev L.G.; Dick B.; Ferrari P.; Frey F.J.; Odermatt A.;
J. Am. Soc. Nephrol. 18:1262-1270(2007)
Cited for: VARIANTS AME CYS-337 AND HIS-338; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; BIOPHYSICOCHEMICAL PROPERTIES; MUTAGENESIS OF ARG-335; ARG-336; ARG-337; TYR-338 AND TYR-339;
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