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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P16662: Variant p.Asn378Ser

UDP-glucuronosyltransferase 2B7
Gene: UGT2B7
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Variant information Variant position: help 378 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Asparagine (N) to Serine (S) at position 378 (N378S, p.Asn378Ser). 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 (N) to small size and polar (S) 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

Polymorphism: help 2 alleles have been identified: UGT2B7*1 (His-268) and UGT2B7*2 (Tyr-268). The sequence shown is that of allele UGT2B7*2. Additional information on the polymorphism described.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 378 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 529 The length of the canonical sequence.
Location on the sequence: help PQNDLLGHPKTRAFITHGGA N GIYEAIYHGIPMVGIPLFAD 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                         PQNDLLGHPKTRAFITHGGANGIYEAIYHGI-PMVGIPLFAD

Rat                           PQNDLLGHPKTKAFVTHGGANGIYESIHYGIPPMVGIPLFA

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 24 – 529 UDP-glucuronosyltransferase 2B7
Binding site 373 – 379
Binding site 398 – 398
Mutagenesis 373 – 373 T -> V. Reduced androsterone, hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.
Mutagenesis 374 – 374 H -> AE. Abolished androsterone glucuronosyltransferase activity; reduced hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.
Mutagenesis 378 – 378 N -> A. Abolished androsterone glucuronosyltransferase activity; reduced hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.
Mutagenesis 379 – 379 G -> D. Abolished androsterone glucuronosyltransferase activity; reduced hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.
Mutagenesis 379 – 379 G -> S. Abolished androsterone glucuronosyltransferase activity; no change in hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.
Mutagenesis 398 – 398 D -> AN. Reduced androsterone, hyodeoxycholic acid and tetrachlorocatechol glucuronosyltransferase activities.
Helix 377 – 386



Literature citations
No reference for the current variant in UniProtKB/Swiss-Prot.
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.