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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9GZX3: Variant p.Glu274Lys

Carbohydrate sulfotransferase 6
Gene: CHST6
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Variant information Variant position: help 274 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 Glutamate (E) to Lysine (K) at position 274 (E274K, p.Glu274Lys). 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 acidic (E) to large size and basic (K) 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 MCD; abolishes the ability to sulfate keratan. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 274 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 395 The length of the canonical sequence.
Location on the sequence: help EAATLKPPPFLRGRYRLVRF E DLAREPLAEIRALYAFTGLS 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.
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 1 – 395 Carbohydrate sulfotransferase 6
Topological domain 27 – 395 Lumenal



Literature citations
Macular corneal dystrophy type I and type II are caused by distinct mutations in a new sulphotransferase gene.
Akama T.O.; Nishida K.; Nakayama J.; Watanabe H.; Ozaki K.; Nakamura T.; Dota A.; Kawasaki S.; Inoue Y.; Maeda N.; Yamamoto S.; Fujiwara T.; Thonar E.J.-M.A.; Shimomura Y.; Kinoshita S.; Tanigami A.; Fukuda M.N.;
Nat. Genet. 26:237-241(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; TISSUE SPECIFICITY; VARIANTS MCD CYS-50; ARG-174; GLU-203; TRP-211 AND LYS-274; Human corneal GlcNAc 6-O-sulfotransferase and mouse intestinal GlcNAc 6-O-sulfotransferase both produce keratan sulfate.
Akama T.O.; Nakayama J.; Nishida K.; Hiraoka N.; Suzuki M.; McAuliffe J.; Hindsgaul O.; Fukuda M.; Fukuda M.N.;
J. Biol. Chem. 276:16271-16278(2001)
Cited for: FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANTS MCD CYS-50; ARG-174; GLU-203; TRP-211; THR-217 AND LYS-274; Enzymatic synthesis in vitro of the disulfated disaccharide unit of corneal keratan sulfate.
Akama T.O.; Misra A.K.; Hindsgaul O.; Fukuda M.N.;
J. Biol. Chem. 277:42505-42513(2002)
Cited for: FUNCTION; SUBSTRATE SPECIFICITY; VARIANTS MCD CYS-50; ARG-174; GLU-203; TRP-211; THR-217 AND LYS-274; Novel mutations in the CHST6 gene associated with macular corneal dystrophy in southern India.
Warren J.F.; Aldave A.J.; Srinivasan M.; Thonar E.J.; Kumar A.B.; Cevallos V.; Whitcher J.P.; Margolis T.P.;
Arch. Ophthalmol. 121:1608-1612(2003)
Cited for: VARIANTS MCD ARG-22; TYR-42; LEU-53; HIS-93; PRO-97; TYR-102; CYS-127; GLN-205; THR-206; PRO-249 AND LYS-274; Molecular analysis of the CHST6 gene in Korean patients with macular corneal dystrophy: Identification of three novel mutations.
Park S.H.; Ahn Y.J.; Chae H.; Kim Y.; Kim M.S.; Kim M.;
Mol. Vis. 21:1201-1209(2015)
Cited for: VARIANTS MCD PHE-118; ARG-174; ARG-186; TRP-205; LYS-274; TYR-308 AND HIS-358;
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.