Sequence information
Variant position: 143 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 354 The length of the canonical sequence.
Location on the sequence:
GNPNDPHGSEHTVSGQHFAA
E LHIVHYNSDLYPDASTASNK
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 GNPNDPHGSEHTVSGQHFAAE LHIVHYNSDLYPDASTASNK
Mouse GNRNDPHGSEHTVSGKHFAAE LHIVHYNSDLYPDFSTASDK
Rabbit GNRNDPYGSEHTVGGKQFAAE LHIVHYNSDSYPDISTASNK
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.
Literature citations
Loss of carbonic anhydrase XII function in individuals with elevated sweat chloride concentration and pulmonary airway disease.
Lee M.; Vecchio-Pagan B.; Sharma N.; Waheed A.; Li X.; Raraigh K.S.; Robbins S.; Han S.T.; Franca A.L.; Pellicore M.J.; Evans T.A.; Arcara K.M.; Nguyen H.; Luan S.; Belchis D.; Hertecant J.; Zabner J.; Sly W.S.; Cutting G.R.;
Hum. Mol. Genet. 25:1923-1933(2016)
Cited for: FUNCTION; CATALYTIC ACTIVITY; TISSUE SPECIFICITY; SUBCELLULAR LOCATION; VARIANT HYCHL GLN-121; CHARACTERIZATION OF VARIANTS HYCHL GLN-121 AND LYS-143;
Hyperchlorhidrosis caused by homozygous mutation in CA12, encoding carbonic anhydrase XII.
Feldshtein M.; Elkrinawi S.; Yerushalmi B.; Marcus B.; Vullo D.; Romi H.; Ofir R.; Landau D.; Sivan S.; Supuran C.T.; Birk O.S.;
Am. J. Hum. Genet. 87:713-720(2010)
Cited for: VARIANT HYCHL LYS-143; INVOLVEMENT IN HYCHL; BIOPHYSICOCHEMICAL PROPERTIES;
Autosomal recessive hyponatremia due to isolated salt wasting in sweat associated with a mutation in the active site of carbonic cnhydrase 12.
Muhammad E.; Leventhal N.; Parvari G.; Hanukoglu A.; Hanukoglu I.; Chalifa-Caspi V.; Feinstein Y.; Weinbrand J.; Jacoby H.; Manor E.; Nagar T.; Beck J.C.; Sheffield V.C.; Hershkovitz E.; Parvari R.;
Hum. Genet. 129:397-405(2011)
Cited for: VARIANT HYCHL LYS-143;
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.