Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00918: Variant p.Gln92Pro

Carbonic anhydrase 2
Gene: CA2
Feedback?
Variant information Variant position: help 92 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Glutamine (Q) to Proline (P) at position 92 (Q92P, p.Gln92Pro). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and polar (Q) to medium size and hydrophobic (P) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In OPTB3; in Czechoslovakia. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 92 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 260 The length of the canonical sequence.
Location on the sequence: help DSQDKAVLKGGPLDGTYRLI Q FHFHWGSLDGQGSEHTVDKK 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         DSQDKAVLK--GGP-LDGTYRLIQFHFHWGSLD--GQGSEHTVDKK

Mouse                         DSQDNAVLK--GGP-LSDSYRLIQFHFHWGSSD--GQGSEH

Rat                           DSQDFAVLK--EGP-LSGSYRLIQFHFHWGSSD--GQGSEH

Bovine                        DSQDKAVLK--DGP-LTGTYRLVQFHFHWGSSD--DQGSEH

Rabbit                        DSHDKTVLK--EGP-LEGTYRLIQFHFHWGSSD--GQGSEH

Sheep                         DSQDKAVLK--DGP-LTGTYRLVQFHFHWGSSD--DQGSEH

Chicken                       DSSDKSVLQ--GGA-LDGVYRLVQFHIHWGSCE--GQGSEH

Caenorhabditis elegans        DLPNRPTINITGGPTMPYRYKLHQISVHFGRADEGEKGSEH
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 2 – 260 Carbonic anhydrase 2
Domain 3 – 259 Alpha-carbonic anhydrase
Binding site 94 – 94
Binding site 96 – 96
Site 92 – 92 Involved in the binding of some activators, including histamine and L-histidine
Mutagenesis 94 – 94 H -> CDENQ. Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding.
Mutagenesis 106 – 106 E -> AQ. Strongly reduced CO(2) hydrase activity.
Mutagenesis 106 – 106 E -> D. Normal CO(2) hydrase activity.
Beta strand 88 – 97



Literature citations
Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis.
Hu P.Y.; Lim E.J.; Ciccolella J.; Strisciuglio P.; Sly W.S.;
Hum. Mutat. 9:383-387(1997)
Cited for: VARIANT OPTB3 PRO-92; Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation.
Shah G.N.; Bonapace G.; Hu P.Y.; Strisciuglio P.; Sly W.S.;
Hum. Mutat. 24:272-272(2004)
Cited for: VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144; FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144;
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.