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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16394: Variant p.Asp164His

Exostosin-1
Gene: EXT1
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Variant information Variant position: help 164 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 Aspartate (D) to Histidine (H) at position 164 (D164H, p.Asp164His). 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 (D) to medium size and polar (H) 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 EXT1; loss of heparan sulfate proteoglycan biosynthetic process. Any additional useful information about the variant.


Sequence information Variant position: help 164 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 746 The length of the canonical sequence.
Location on the sequence: help YTSDPSQACLFVLSLDTLDR D QLSPQYVHNLRSKVQSLHLW 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                         YTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQSL--HLW

Mouse                         YTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQSL--H

Bovine                        YTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQSL--H

Caenorhabditis elegans        YTNDPNEACIFLLGIDTTDRDVRSQNYVKNVNDYIESLDPS

Drosophila                    YTSDPTAACLFVLGIDTLDRDSLSEDYVRNVPSRLARL--P
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 – 746 Exostosin-1
Topological domain 29 – 746 Lumenal
Binding site 166 – 166
Mutagenesis 162 – 162 D -> N. Loss of N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity; when associated with N-164.
Mutagenesis 164 – 164 D -> E. Loss of heparan sulfate proteoglycan biosynthetic process.
Mutagenesis 164 – 164 D -> N. Loss of N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity; when associated with N-162.
Mutagenesis 164 – 164 Missing. Loss of heparan sulfate proteoglycan biosynthetic process.



Literature citations
EXT-mutation analysis and loss of heterozygosity in sporadic and hereditary osteochondromas and secondary chondrosarcomas.
Bovee J.V.M.G.; Cleton-Jansen A.-M.; Wuyts W.; Caethoven G.; Taminiau A.H.M.; Bakker E.; van Hul W.; Cornelisse C.J.; Hogendoorn P.C.W.;
Am. J. Hum. Genet. 65:689-698(1999)
Cited for: VARIANT EXT1 HIS-164; VARIANTS 235-PRO--LYS-239 DEL AND SER-316; Etiological point mutations in the hereditary multiple exostoses gene EXT1: a functional analysis of heparan sulfate polymerase activity.
Cheung P.K.; McCormick C.; Crawford B.E.; Esko J.D.; Tufaro F.; Duncan G.;
Am. J. Hum. Genet. 69:55-66(2001)
Cited for: CHARACTERIZATION OF VARIANTS EXT1 LYS-27; HIS-164; GLY-280; SER-340; SER-316; VAL-486 AND LEU-496; MUTAGENESIS OF GLN-27; ASP-164; ASN-316; ALA-486 AND PRO-496; FUNCTION; PATHWAY;
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.