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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P22309: Variant p.Pro229Gln

UDP-glucuronosyltransferase 1A1
Gene: UGT1A1
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Variant information Variant position: help 229 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 Proline (P) to Glutamine (Q) at position 229 (P229Q, p.Pro229Gln). 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 hydrophobic (P) to medium size and polar (Q) 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 CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity; decreased SN-38 glucuronosyltransferase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 229 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 533 The length of the canonical sequence.
Location on the sequence: help RVKNMLIAFSQNFLCDVVYS P YATLASEFLQREVTVQDLLS 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                         RVKNMLIAFSQNFLCDVVYSPYATLASEFLQREVTVQDLLS

Mouse                         RVKNVLLAVSENFMCRVVYSPYGSLATEILQKEVTVQDLLS

Rat                           RVKNMIIALTENFLCRVVYSPYGSLATEILQKEVTVKDLLS
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 26 – 533 UDP-glucuronosyltransferase 1A1
Mutagenesis 233 – 233 L -> R. Decreased SN-38 glucuronosyltransferase activity.



Literature citations
Common human UGT1A polymorphisms and the altered metabolism of irinotecan active metabolite 7-ethyl-10-hydroxycamptothecin (SN-38).
Gagne J.F.; Montminy V.; Belanger P.; Journault K.; Gaucher G.; Guillemette C.;
Mol. Pharmacol. 62:608-617(2002)
Cited for: FUNCTION (ISOFORM 1); CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; SUBSTRATE SPECIFICITY; MUTAGENESIS OF LEU-233; CHARACTERIZATION OF VARIANTS ARG-71; GLN-229 AND ASP-486; Influence of mutations associated with Gilbert and Crigler-Najjar type II syndromes on the glucuronidation kinetics of bilirubin and other UDP-glucuronosyltransferase 1A substrates.
Udomuksorn W.; Elliot D.J.; Lewis B.C.; Mackenzie P.I.; Yoovathaworn K.; Miners J.O.;
Pharmacogenet. Genomics 17:1017-1029(2007)
Cited for: FUNCTION (ISOFORM 1); CATALYTIC ACTIVITY; KINETIC PARAMETERS; SUBSTRATE SPECIFICITY; CHARACTERIZATION OF VARIANTS CN2 ARG-71; LEU-83; GLN-229 AND ASP-486; Analysis of genes for bilirubin UDP-glucuronosyltransferase in Gilbert's syndrome.
Aono S.; Adachi Y.; Uyama E.; Yamada Y.; Keino H.; Nanno T.; Koiwai O.; Sato H.;
Lancet 345:958-959(1995)
Cited for: VARIANTS GILBS ARG-71; GLN-229 AND GLY-367; INVOLVEMENT IN GILBS; Analysis of bilirubin uridine 5'-diphosphate (UDP)-glucuronosyltransferase gene mutations in seven patients with Crigler-Najjar syndrome type II.
Yamamoto K.; Soeda Y.; Kamisako T.; Hosaka H.; Fukano M.; Sato H.; Fujiyama Y.; Dachi Y.; Satoh Y.; Bamba T.;
J. Hum. Genet. 43:111-114(1998)
Cited for: VARIANTS CN2 ARG-71; TRP-209; GLN-229 AND ASP-486; Genetic lesions of bilirubin uridine-diphosphoglucuronate glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert syndromes: correlation of genotype to phenotype.
Kadakol A.; Ghosh S.S.; Sappal B.S.; Sharma G.; Chowdhury J.R.; Chowdhury N.R.;
Hum. Mutat. 16:297-306(2000)
Cited for: VARIANTS CN1 ASP-39; PHE-170 DEL; ARG-177; ARG-276; VAL-291; GLU-308; TRP-336; ARG-357; THR-368; PHE-375; ARG-376; ARG-381; SER-387; PRO-401 AND GLU-428; VARIANTS CN2 ARG-15; GLN-175; TRP-209; GLY-225; ARG-331 AND ARG-376; VARIANTS GILBS ARG-71; GLN-229; THR-294; GLY-367 AND ASP-486;
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.