Sequence information
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:
DLTPVVDAITDALLAARPRR
R YYPGQGLGLMYFIHYYLPEG
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 DLTPVVDAITDALLAARPRRR YYPGQGLGLMYFIHYYLPEG
Mouse DLSPVVDAIIDALLAAQPRSR YYPGRGLGLMYFIHHYLPEG
Rat DLSPVVDAIIDALLAAQPRSR YYTGRGLGLMYFIHHYLPGG
Bovine DLSPVVDAITDALLAAQPLRR YYPGHGLGLIYFIHYYLPEG
Rabbit DLSPVVDAITDALLAARPRPR YYPGRGLGLMYFIHYYLPEG
Sheep DLSPVVDAITDALLAAQPRRR YYPGHGLGLIYFIHYYLPEG
Zebrafish DLSPVIDTIVEALLSPQPQVR YYAGPGLILMYFICSYLPLS
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 – 405
11-beta-hydroxysteroid dehydrogenase type 2
Region
335 – 339
Essential for protein stability
Mutagenesis
335 – 335
R -> AQ. Reduced enzyme activity.
Mutagenesis
335 – 335
R -> K. No effect on enzyme activity.
Mutagenesis
336 – 336
R -> AQ. Almost complete loss of enzyme activity.
Mutagenesis
336 – 336
R -> K. Reduced enzyme activity.
Mutagenesis
337 – 337
R -> AQ. Almost complete loss of enzyme activity.
Mutagenesis
337 – 337
R -> K. Reduced enzyme activity.
Mutagenesis
338 – 338
Y -> FA. Complete loss of enzyme activity.
Mutagenesis
339 – 339
Y -> AFH. Reduced enzyme activity.
Literature citations
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;
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.