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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q86Y38: Variant p.Arg481Trp

Xylosyltransferase 1
Gene: XYLT1
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Variant information Variant position: help 481 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 Arginine (R) to Tryptophan (W) at position 481 (R481W, p.Arg481Trp). 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 large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 DBQD2; causes retention in the endoplasmic reticulum; impairs dermatan sulfate proteoglycan synthesis. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 481 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 959 The length of the canonical sequence.
Location on the sequence: help KQGLDRLFLECDAHMWRLGD R RIPEGIAVDGGSDWFLLNRR 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                         KQGLDRLFLECDAHMWRLGDRRIPEGIAVDGGSDWFLLNRR

                              KQGLDRLFLECDAHMWRLGDRRIPEGIAVDGGSDWFLLNRK

Chimpanzee                    KQGLDRLFLECDAHMWRLGDRRIPEGIAVDGGSDWFLLNRR

Mouse                         KQGLDRLFLECDTHMWRLGDRRIPEGIAVDGGSDWFLLNRK
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 – 959 Xylosyltransferase 1
Topological domain 39 – 959 Lumenal
Disulfide bond 301 – 542
Mutagenesis 462 – 462 Q -> AW. No effect on enzyme activity.
Mutagenesis 462 – 462 Q -> R. Decreased enzyme activity.
Mutagenesis 471 – 471 C -> A. Strongly reduced enzyme activity.
Mutagenesis 494 – 494 D -> A. Decreased enzyme activity.
Mutagenesis 494 – 494 D -> N. Loss of enzyme activity.



Literature citations
The missing 'link': an autosomal recessive short stature syndrome caused by a hypofunctional XYLT1 mutation.
Schreml J.; Durmaz B.; Cogulu O.; Keupp K.; Beleggia F.; Pohl E.; Milz E.; Coker M.; Ucar S.K.; Nurnberg G.; Nurnberg P.; Kuhn J.; Ozkinay F.;
Hum. Genet. 133:29-39(2014)
Cited for: VARIANT DBQD2 TRP-481; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; PATHWAY; Endoplasmic reticulum retention of xylosyltransferase 1 (XYLT1) mutants underlying Desbuquois dysplasia type II.
Al-Jezawi N.K.; Ali B.R.; Al-Gazali L.;
Am. J. Med. Genet. A 173:1773-1781(2017)
Cited for: INVOLVEMENT IN DBQD2; CHARACTERIZATION OF VARIANTS DBQD2 TRP-481 AND CYS-598; SUBCELLULAR LOCATION;
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.