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Entry version 212 (17 Jun 2020)
Sequence version 1 (01 Aug 1991)
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Protein

UDP-glucuronosyltransferase 1A1

Gene

UGT1A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:15472229, PubMed:18004206, PubMed:18004212, PubMed:18719240, PubMed:19830808, PubMed:23288867). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:18004206, PubMed:18004212, PubMed:20610558). Catalyzes the glucironidation of endogenous estrogens hormones such as estradiol and estrone, and xenoestrogens such as epiestradiol (PubMed:15472229, PubMed:18719240, PubMed:23288867). Involved in the glucuronidation of bilirubin, a degradation product occurring in the normal catabolic pathway that breaks down heme in vertebrates (PubMed:17187418, PubMed:18004206, PubMed:19830808). Also catalyzes the glucuronidation the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (PubMed:19545173). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, a drug which can inhibit the effect of angiotensin II (PubMed:18674515).10 Publications
Lacks UGT glucuronidation activity but acts as a negative regulator of isoform 1.2 Publications

Miscellaneous

UGT1A1 isoform is part of the UGT1A complex locus which displays alternative use of promoters, first exons and terminal exons. The locus is defined by 13 first exons, which are alternatively spliced to 3 other common exons and 2 alternative terminal exons 5. From the 27 possible mRNA isoforms, 9 produce functionally active polypeptides (UGT1A1, 1A3, 1A4, 1A5, 1A6, 1A7, 1A8, 1A9 and 1A10) called isoforms 1 (i1). Use of an alternative exon 5 (5b) as terminal exon is leading to 9 additional alternatively spliced products termed isoforms i2 and which lack transferase activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.26 µM for bilirubin1 Publication
  2. KM=70 µM for 4-methylumbelliferone1 Publication
  3. KM=23 µM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 3)1 Publication
  4. KM=60.6 µM for 17beta-estradiol/estradiol (when assaying glucuronidation at position 3)1 Publication
  5. KM=11.2 µM for 17alpha-estradiol/epiestradiol (when assaying glucuronidation at position 3)1 Publication
  6. KM=38 µM for estrone (when assaying glucuronidation at position 3)1 Publication
  7. KM=165 µM for the formation of 2-hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate)1 Publication
  8. KM=15 µM for 2-hydroxy-17beta-estradiol (when assaying glucuronidation at position 2)1 Publication
  9. KM=19 µM for 2-hydroxy-estrone (when assaying glucuronidation at position 3)1 Publication
  10. KM=38 µM for 4-hydroxy-17beta-estradiol (when assaying glucuronidation at position 3)1 Publication
  11. KM=74 µM for 4-hydroxy-17beta-estradiol (when assaying glucuronidation at position 4)1 Publication
  12. KM=21 µM for 4-hydroxy-estrone (when assaying glucuronidation at position 3)1 Publication
  13. KM=19 µM for 4-hydroxy-estrone (when assaying glucuronidation at position 4)1 Publication
  14. KM=49 µM for 2-methoxy-17beta-estradiol (when assaying glucuronidation at position 3)1 Publication
  15. KM=49 µM for 2-methoxyestrone (when assaying glucuronidation at position 3)1 Publication
  16. KM=14 µM for 4-methoxy-17beta-estradiol (when assaying glucuronidation at position 3)1 Publication
  17. KM=103 µM for 4-methoxyestrone (when assaying glucuronidation at position 3)1 Publication
  18. KM=21.5 µM for losartan (when assaying glucuronidation at position N2 of the tetrazole ring)1 Publication
  1. Vmax=1080 pmol/min/mg enzyme with bilirubin as substrate1 Publication
  2. Vmax=255 pmol/min/mg enzyme with 4-methylumbelliferone as substrate1 Publication
  3. Vmax=274 pmol/min/mg enzyme with 1-naphthol as substrate1 Publication
  4. Vmax=767 pmol/min/mg enzyme with 17beta-estradiol as substrate1 Publication
  5. Vmax=704 pmol/min/mg enzyme for the formation of 17beta-estradiol 3-O-(beta-D-glucuronate)1 Publication
  6. Vmax=93 pmol/min/mg enzyme for the formation of 17beta-estradiol 3-O-(beta-D-glucuronate)1 Publication
  7. Vmax=115 pmol/min/mg enzyme for the formation of 17alpha-estradiol 3-O-(beta-D-glucuronate)1 Publication
  8. Vmax=3 pmol/min/mg enzyme for the formation of estrone 3-O-(beta-D-glucuronate)1 Publication
  9. Vmax=1037 pmol/min/mg enzyme for the formation of 2-hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate)1 Publication
  10. Vmax=36 pmol/min/mg enzyme for the formation of 2-hydroxy-17beta-estradiol 2-O-(beta-D-glucuronate)1 Publication
  11. Vmax=326 pmol/min/mg enzyme for the formation of 2-hydroxy-estrone 3-O-(beta-D-glucuronate)1 Publication
  12. Vmax=19 pmol/min/mg enzyme for the formation of 4-hydroxy-17beta-estradiol 3-O-(beta-D-glucuronate)1 Publication
  13. Vmax=42 pmol/min/mg enzyme for the formation of 4-hydroxy-17beta-estradiol 4-O-(beta-D-glucuronate)1 Publication
  14. Vmax=34 pmol/min/mg enzyme for the formation of 4-hydroxy-estrone 3-O-(beta-D-glucuronate)1 Publication
  15. Vmax=11 pmol/min/mg enzyme for the formation of 4-hydroxy-estrone 4-O-(beta-D-glucuronate)1 Publication
  16. Vmax=222 pmol/min/mg enzyme for the formation of 2-methoxy-17beta-estradiol 3-O-(beta-D-glucuronate)1 Publication
  17. Vmax=39 pmol/min/mg enzyme for the formation of 2-methoxyestrone 3-O-(beta-D-glucuronate)1 Publication
  18. Vmax=19 pmol/min/mg enzyme for the formation of 4-methoxy-17beta-estradiol 3-O-(beta-D-glucuronate)1 Publication
  19. Vmax=4 pmol/min/mg enzyme for the formation of 4-methoxyestrone 3-O-(beta-D-glucuronate)1 Publication
  20. Vmax=32.2 pmol/min/mg enzyme for the formation of losartan N2-(beta-D-glucuronate)1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosyltransferase, Transferase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.4.1.17 2681
2.4.1.95 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-156588 Glucuronidation
R-HSA-5579002 Defective UGT1A1 causes hyperbilirubinemia

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P22309

SIGNOR Signaling Network Open Resource

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SIGNORi
P22309

Protein family/group databases

Carbohydrate-Active enZymes

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CAZyi
GT1 Glycosyltransferase Family 1

Chemistry databases

SwissLipids knowledge resource for lipid biology

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SwissLipidsi
SLP:000001697

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
UDP-glucuronosyltransferase 1A12 Publications (EC:2.4.1.177 Publications)
Short name:
UGT1A1
Alternative name(s):
Bilirubin-specific UDPGT isozyme 1
Short name:
hUG-BR1
UDP-glucuronosyltransferase 1-1
Short name:
UDPGT 1-1
Short name:
UGT1*1
Short name:
UGT1-01
Short name:
UGT1.1
UDP-glucuronosyltransferase 1A isoform 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:UGT1A1Imported
Synonyms:GNT1, UGT1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000241635.7

Human Gene Nomenclature Database

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HGNCi
HGNC:12530 UGT1A1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
191740 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P22309

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei491 – 507HelicalSequence analysisAdd BLAST17

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Gilbert syndrome (GILBS)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionOccurs as a consequence of reduced bilirubin transferase activity and is often detected in young adults with vague non-specific complaints.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_02613683F → L in GILBS; displays less than 10% of wild-type bilirubin glucuronidation activity. 2 PublicationsCorresponds to variant dbSNP:rs56059937Ensembl.1
Natural variantiVAR_009505229P → Q in CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity. 4 PublicationsCorresponds to variant dbSNP:rs35350960Ensembl.1
Natural variantiVAR_026139294I → T in GILBS and CN2; 40-55% normal bilirubin glucuronidation activity; normal Km for bilirubin; when homozygous far less repressive and generates the mild Gilbert phenotype. 2 PublicationsCorresponds to variant dbSNP:rs72551347Ensembl.1
Natural variantiVAR_012283367R → G in GILBS. 2 PublicationsCorresponds to variant dbSNP:rs55750087Ensembl.1
Transient familial neonatal hyperbilirubinemia (HBLRTFN)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry. The defect has been ascribed to various breast milk substances, but the component or combination of components that is responsible remains unclear. Defects of UGT1A1 are an underlying cause of the prolonged unconjugated hyperbilirubinemia associated with breast milk. One or more components in the milk may trigger the jaundice in infants who have such mutations. Mutations are identical to those detected in patients with Gilbert syndrome, a risk factor of neonatal non-physiologic hyperbilirubinemia and a genetic factor in fasting hyperbilirubinemia.
Disease descriptionA condition characterized by excessive concentration of bilirubin in the blood, which may lead to jaundice. Breast milk jaundice is a common problem in nursing infants.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00950471G → R in CN2, GILBS and HBLRTFN; has significant residual bilirubin glucuronidation activity of about 25% to 50% of that of the wild-type protein; displays no change in biluribin affinity. 7 PublicationsCorresponds to variant dbSNP:rs4148323Ensembl.1
Natural variantiVAR_007709486Y → D in CN2, GILBS and HBLRTFN; displays less than 10% of wild-type bilirubin glucuronidation activity. 7 PublicationsCorresponds to variant dbSNP:rs34993780Ensembl.1
Crigler-Najjar syndrome 1 (CN1)10 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionPatients have severe hyperbilirubinemia and usually die of kernicterus (bilirubin accumulation in the basal ganglia and brainstem nuclei) within the first year of life. CN1 inheritance is autosomal recessive.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07140236D → N in CN1. 1 Publication1
Natural variantiVAR_02613539H → D in CN1. 1 PublicationCorresponds to variant dbSNP:rs72551339Ensembl.1
Natural variantiVAR_007695170Missing in CN1 and CN2; has nearly normal activity at pH 7.6 and is inactive at pH 6.4. 5 Publications1
Natural variantiVAR_007697177C → R in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551342Ensembl.1
Natural variantiVAR_007699276G → R in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551345Ensembl.1
Natural variantiVAR_026138291E → V in CN1. 1 Publication1
Natural variantiVAR_007700292A → V in CN1. 1 PublicationCorresponds to variant dbSNP:rs758873309Ensembl.1
Natural variantiVAR_007701308G → E in CN1; no bilirubin glucuronidation activity. 3 PublicationsCorresponds to variant dbSNP:rs62625011Ensembl.1
Natural variantiVAR_026140336R → L in CN1 and CN2. 1 Publication1
Natural variantiVAR_026141336R → Q in CN1. 1 PublicationCorresponds to variant dbSNP:rs750453538Ensembl.1
Natural variantiVAR_007703357Q → R in CN1. 3 PublicationsCorresponds to variant dbSNP:rs72551351Ensembl.1
Natural variantiVAR_007704368A → T in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551352Ensembl.1
Natural variantiVAR_007705375S → F in CN1; no bilirubin glucuronidation activity. 5 PublicationsCorresponds to variant dbSNP:rs72551353Ensembl.1
Natural variantiVAR_026144376H → R in CN1 and CN2. Corresponds to variant dbSNP:rs1349037761Ensembl.1
Natural variantiVAR_026145377G → V in CN1 and CN2. 1 PublicationCorresponds to variant dbSNP:rs1283652721Ensembl.1
Natural variantiVAR_007706381S → R in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551354Ensembl.1
Natural variantiVAR_026146387P → S in CN1. 2 PublicationsCorresponds to variant dbSNP:rs901936528Ensembl.1
Natural variantiVAR_026147395G → V in CN1; has no residual bilirubin glucuronidation activity. 3 PublicationsCorresponds to variant dbSNP:rs367897068Ensembl.1
Natural variantiVAR_007707401A → P in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551355Ensembl.1
Natural variantiVAR_064960402K → T in CN1; has no residual bilirubin glucuronidation activity; N-glycosylation does take place at this new additional site. 1 Publication1
Natural variantiVAR_007708428K → E in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551356Ensembl.1
Natural variantiVAR_026149461W → R in CN1 and CN2. 2 PublicationsCorresponds to variant dbSNP:rs1476500325Ensembl.1
Crigler-Najjar syndrome 2 (CN2)16 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionPatients have less severe hyperbilirubinemia and usually survive into adulthood without neurologic damage. Phenobarbital, which induces the partially deficient glucuronyl transferase, can diminish the jaundice. CN2 inheritance is autosomal dominant.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01941015L → R in CN2; mutant protein rapidly degraded by the proteasome owing to its mislocalization in the cell. 4 PublicationsCorresponds to variant dbSNP:rs111033541Ensembl.1
Natural variantiVAR_02613434P → Q in CN2. 1 Publication1
Natural variantiVAR_00950471G → R in CN2, GILBS and HBLRTFN; has significant residual bilirubin glucuronidation activity of about 25% to 50% of that of the wild-type protein; displays no change in biluribin affinity. 7 PublicationsCorresponds to variant dbSNP:rs4148323Ensembl.1
Natural variantiVAR_007695170Missing in CN1 and CN2; has nearly normal activity at pH 7.6 and is inactive at pH 6.4. 5 Publications1
Natural variantiVAR_064955171Missing in CN2. 1 Publication1
Natural variantiVAR_019411175L → Q in CN2; has low residual bilirubin glucuronidation activity of about 4.6% of that of the wild-type protein. 4 PublicationsCorresponds to variant dbSNP:rs72551341Ensembl.1
Natural variantiVAR_064956191S → F in CN2; has low residual bilirubin glucuronidation activity of about 5.3% of that of the wild-type protein. 1 Publication1
Natural variantiVAR_007698209R → W in CN2; has low residual bilirubin glucuronidation activity of about 2.9% of that of the wild-type protein. 5 PublicationsCorresponds to variant dbSNP:rs72551343Ensembl.1
Natural variantiVAR_026137225V → G in CN2. 2 PublicationsCorresponds to variant dbSNP:rs35003977Ensembl.1
Natural variantiVAR_009505229P → Q in CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity. 4 PublicationsCorresponds to variant dbSNP:rs35350960Ensembl.1
Natural variantiVAR_071403230Y → C in CN2. 1 PublicationCorresponds to variant dbSNP:rs754922685Ensembl.1
Natural variantiVAR_064957279N → Y in CN2. 1 PublicationCorresponds to variant dbSNP:rs397978903Ensembl.1
Natural variantiVAR_026139294I → T in GILBS and CN2; 40-55% normal bilirubin glucuronidation activity; normal Km for bilirubin; when homozygous far less repressive and generates the mild Gilbert phenotype. 2 PublicationsCorresponds to variant dbSNP:rs72551347Ensembl.1
Natural variantiVAR_007702331Q → R in CN2; has no residual bilirubin glucuronidation activity. 3 PublicationsCorresponds to variant dbSNP:rs72551348Ensembl.1
Natural variantiVAR_026140336R → L in CN1 and CN2. 1 Publication1
Natural variantiVAR_026142336R → W in CN2; has very low residual bilirubin glucuronidation activity of about 0.4% of that of the wild-type protein. 3 PublicationsCorresponds to variant dbSNP:rs139607673Ensembl.1
Natural variantiVAR_026143354W → R in CN2. 2 Publications1
Natural variantiVAR_071404367R → C in CN2. 1 PublicationCorresponds to variant dbSNP:rs55750087Ensembl.1
Natural variantiVAR_064958370I → V in CN2. 1 PublicationCorresponds to variant dbSNP:rs748989741Ensembl.1
Natural variantiVAR_026144376H → R in CN1 and CN2. Corresponds to variant dbSNP:rs1349037761Ensembl.1
Natural variantiVAR_026145377G → V in CN1 and CN2. 1 PublicationCorresponds to variant dbSNP:rs1283652721Ensembl.1
Natural variantiVAR_064959387P → H in CN2; has no residual bilirubin glucuronidation activity. 1 Publication1
Natural variantiVAR_019412400N → D in CN2. 1 PublicationCorresponds to variant dbSNP:rs28934877Ensembl.1
Natural variantiVAR_026148403R → C in CN2. 1 PublicationCorresponds to variant dbSNP:rs778766461Ensembl.1
Natural variantiVAR_064961443L → P in CN2; has no residual bilirubin glucuronidation activity. 2 PublicationsCorresponds to variant dbSNP:rs758411577Ensembl.1
Natural variantiVAR_026149461W → R in CN1 and CN2. 2 PublicationsCorresponds to variant dbSNP:rs1476500325Ensembl.1
Natural variantiVAR_026150478A → D in CN2. 1 Publication1
Natural variantiVAR_007709486Y → D in CN2, GILBS and HBLRTFN; displays less than 10% of wild-type bilirubin glucuronidation activity. 7 PublicationsCorresponds to variant dbSNP:rs34993780Ensembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
54658

MalaCards human disease database

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MalaCardsi
UGT1A1
MIMi143500 phenotype
218800 phenotype
237900 phenotype
601816 phenotype
606785 phenotype

Open Targets

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OpenTargetsi
ENSG00000241635

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
79234 Crigler-Najjar syndrome type 1
79235 Crigler-Najjar syndrome type 2
240885 Irinotecan toxicity
357 NON RARE IN EUROPE: Gilbert syndrome
240905 Raltegravir toxicity
2312 Transient familial neonatal hyperbilirubinemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37181
PA420

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P22309 Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1287617

Drug and drug target database

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DrugBanki
DB01048 Abacavir
DB00316 Acetaminophen
DB00173 Adenine
DB03496 Alvocidib
DB01072 Atazanavir
DB01076 Atorvastatin
DB06626 Axitinib
DB11799 Bictegravir
DB11967 Binimetinib
DB00564 Carbamazepine
DB01136 Carvedilol
DB00439 Cerivastatin
DB14635 Curcumin sulfate
DB11963 Dacomitinib
DB01609 Deferasirox
DB11943 Delafloxacin
DB00304 Desogestrel
DB09213 Dexibuprofen
DB08930 Dolutegravir
DB00625 Efavirenz
DB06210 Eltrombopag
DB13874 Enasidenib
DB00530 Erlotinib
DB11827 Ertugliflozin
DB14575 Eslicarbazepine
DB09119 Eslicarbazepine acetate
DB00783 Estradiol
DB13952 Estradiol acetate
DB13953 Estradiol benzoate
DB13954 Estradiol cypionate
DB13955 Estradiol dienanthate
DB13956 Estradiol valerate
DB00977 Ethinylestradiol
DB00773 Etoposide
DB00973 Ezetimibe
DB04953 Ezogabine
DB01544 Flunitrazepam
DB00712 Flurbiprofen
DB01095 Fluvastatin
DB12010 Fostamatinib
DB00947 Fulvestrant
DB00695 Furosemide
DB02703 Fusidic acid
DB06741 Gavestinel
DB01241 Gemfibrozil
DB13879 Glecaprevir
DB01067 Glipizide
DB05039 Indacaterol
DB00224 Indinavir
DB00328 Indomethacin
DB00762 Irinotecan
DB01026 Ketoconazole
DB01009 Ketoprofen
DB00598 Labetalol
DB00555 Lamotrigine
DB12070 Letermovir
DB00451 Levothyroxine
DB00279 Liothyronine
DB00455 Loratadine
DB00678 Losartan
DB00227 Lovastatin
DB06077 Lumateperone
DB00916 Metronidazole
DB05018 Migalastat
DB00350 Minoxidil
DB00295 Morphine
DB06510 Muraglitazar
DB00688 Mycophenolate mofetil
DB01024 Mycophenolic acid
DB01183 Naloxone
DB00704 Naltrexone
DB00220 Nelfinavir
DB04868 Nilotinib
DB09079 Nintedanib
DB09297 Paritaprevir
DB06589 Pazopanib
DB12978 Pexidartinib
DB01174 Phenobarbital
DB00252 Phenytoin
DB13878 Pibrentasvir
DB00794 Primidone
DB01032 Probenecid
DB09288 Propacetamol
DB00818 Propofol
DB00481 Raloxifene
DB06817 Raltegravir
DB08896 Regorafenib
DB01045 Rifampicin
DB00503 Ritonavir
DB12332 Rucaparib
DB09298 Silibinin
DB00641 Simvastatin
DB09276 Sodium aurothiomalate
DB00398 Sorafenib
DB00870 Suprofen
DB12020 Tecovirimat
DB01420 Testosterone propionate
DB00906 Tiagabine
DB00932 Tipranavir
DB00193 Tramadol
DB00197 Troglitazone
DB15328 Ubrogepant
DB00313 Valproic acid
DB00495 Zidovudine
DB00909 Zonisamide

DrugCentral

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DrugCentrali
P22309

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2990

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
UGT1A1

Domain mapping of disease mutations (DMDM)

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DMDMi
136729

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003600026 – 533UDP-glucuronosyltransferase 1A1Add BLAST508

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi102N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi295N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi347N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P22309

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P22309

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P22309

PeptideAtlas

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PeptideAtlasi
P22309

PRoteomics IDEntifications database

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PRIDEi
P22309

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
1325
53981 [P22309-1]

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1873

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P22309

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P22309

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in liver, colon and small intestine. Not expressed in kidney, esophagus and skin.3 Publications
Expressed in liver, colon, small intestine and kidney. Not expressed in esophagus and skin.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000241635 Expressed in liver and 44 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P22309 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P22309 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000241635 Group enriched (intestine, liver)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:17179145). Homooligomer (Probable).

Interacts with UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9 and UGT1A10 to form heterodimers (PubMed:17179145).

Isoform 1 interacts with isoform 2/i2 suggesting that oligomerization is involved in negative regulation of transferase activity by isoform 2 (PubMed:17187418, PubMed:20610558). Isoform 1 also interacts with respective i2 isoforms of UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9 and UGT1A10 (PubMed:20610558).

1 Publication3 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
120087, 4 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P22309

Protein interaction database and analysis system

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IntActi
P22309, 9 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000304845

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P22309

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P22309 protein

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the UDP-glycosyltransferase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1192 Eukaryota
COG1819 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000159677

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_012949_3_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P22309

KEGG Orthology (KO)

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KOi
K00699

Identification of Orthologs from Complete Genome Data

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OMAi
WLSMHGV

Database for complete collections of gene phylogenies

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PhylomeDBi
P22309

TreeFam database of animal gene trees

More...
TreeFami
TF315472

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002213 UDP_glucos_trans
IPR035595 UDP_glycos_trans_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00201 UDPGT, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00375 UDPGT, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P22309-1) [UniParc]FASTAAdd to basket
Also known as: i11 Publication

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAVESQGGRP LVLGLLLCVL GPVVSHAGKI LLIPVDGSHW LSMLGAIQQL
60 70 80 90 100
QQRGHEIVVL APDASLYIRD GAFYTLKTYP VPFQREDVKE SFVSLGHNVF
110 120 130 140 150
ENDSFLQRVI KTYKKIKKDS AMLLSGCSHL LHNKELMASL AESSFDVMLT
160 170 180 190 200
DPFLPCSPIV AQYLSLPTVF FLHALPCSLE FEATQCPNPF SYVPRPLSSH
210 220 230 240 250
SDHMTFLQRV KNMLIAFSQN FLCDVVYSPY ATLASEFLQR EVTVQDLLSS
260 270 280 290 300
ASVWLFRSDF VKDYPRPIMP NMVFVGGINC LHQNPLSQEF EAYINASGEH
310 320 330 340 350
GIVVFSLGSM VSEIPEKKAM AIADALGKIP QTVLWRYTGT RPSNLANNTI
360 370 380 390 400
LVKWLPQNDL LGHPMTRAFI THAGSHGVYE SICNGVPMVM MPLFGDQMDN
410 420 430 440 450
AKRMETKGAG VTLNVLEMTS EDLENALKAV INDKSYKENI MRLSSLHKDR
460 470 480 490 500
PVEPLDLAVF WVEFVMRHKG APHLRPAAHD LTWYQYHSLD VIGFLLAVVL
510 520 530
TVAFITFKCC AYGYRKCLGK KGRVKKAHKS KTH
Length:533
Mass (Da):59,591
Last modified:August 1, 1991 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i19C90231AD0EB547
GO
Isoform 2 (identifier: P22309-2) [UniParc]FASTAAdd to basket
Also known as: i21 Publication, UGT1A1s

The sequence of this isoform differs from the canonical sequence as follows:
     435-533: SYKENIMRLS...VKKAHKSKTH → RKKQQSGRQM

Show »
Length:444
Mass (Da):49,368
Checksum:i71E6711DDEFED403
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA61247 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAF03522 differs from that shown. Reason: Erroneous gene model prediction.Curated

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Genetic variation in UGT1A1 defines the bilirubin serum levels quantitative trait locus 1 (BILIQTL1) [MIMi:601816]. Variation in serum bilirubin is associated with altered cardiovascular disease risk and drug metabolism.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01941015L → R in CN2; mutant protein rapidly degraded by the proteasome owing to its mislocalization in the cell. 4 PublicationsCorresponds to variant dbSNP:rs111033541Ensembl.1
Natural variantiVAR_02613434P → Q in CN2. 1 Publication1
Natural variantiVAR_07140236D → N in CN1. 1 Publication1
Natural variantiVAR_02613539H → D in CN1. 1 PublicationCorresponds to variant dbSNP:rs72551339Ensembl.1
Natural variantiVAR_00950471G → R in CN2, GILBS and HBLRTFN; has significant residual bilirubin glucuronidation activity of about 25% to 50% of that of the wild-type protein; displays no change in biluribin affinity. 7 PublicationsCorresponds to variant dbSNP:rs4148323Ensembl.1
Natural variantiVAR_02613683F → L in GILBS; displays less than 10% of wild-type bilirubin glucuronidation activity. 2 PublicationsCorresponds to variant dbSNP:rs56059937Ensembl.1
Natural variantiVAR_007695170Missing in CN1 and CN2; has nearly normal activity at pH 7.6 and is inactive at pH 6.4. 5 Publications1
Natural variantiVAR_064955171Missing in CN2. 1 Publication1
Natural variantiVAR_019411175L → Q in CN2; has low residual bilirubin glucuronidation activity of about 4.6% of that of the wild-type protein. 4 PublicationsCorresponds to variant dbSNP:rs72551341Ensembl.1
Natural variantiVAR_007697177C → R in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551342Ensembl.1
Natural variantiVAR_064956191S → F in CN2; has low residual bilirubin glucuronidation activity of about 5.3% of that of the wild-type protein. 1 Publication1
Natural variantiVAR_007698209R → W in CN2; has low residual bilirubin glucuronidation activity of about 2.9% of that of the wild-type protein. 5 PublicationsCorresponds to variant dbSNP:rs72551343Ensembl.1
Natural variantiVAR_026137225V → G in CN2. 2 PublicationsCorresponds to variant dbSNP:rs35003977Ensembl.1
Natural variantiVAR_009505229P → Q in CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity. 4 PublicationsCorresponds to variant dbSNP:rs35350960Ensembl.1
Natural variantiVAR_071403230Y → C in CN2. 1 PublicationCorresponds to variant dbSNP:rs754922685Ensembl.1
Natural variantiVAR_007699276G → R in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551345Ensembl.1
Natural variantiVAR_064957279N → Y in CN2. 1 PublicationCorresponds to variant dbSNP:rs397978903Ensembl.1
Natural variantiVAR_026138291E → V in CN1. 1 Publication1
Natural variantiVAR_007700292A → V in CN1. 1 PublicationCorresponds to variant dbSNP:rs758873309Ensembl.1
Natural variantiVAR_026139294I → T in GILBS and CN2; 40-55% normal bilirubin glucuronidation activity; normal Km for bilirubin; when homozygous far less repressive and generates the mild Gilbert phenotype. 2 PublicationsCorresponds to variant dbSNP:rs72551347Ensembl.1
Natural variantiVAR_007701308G → E in CN1; no bilirubin glucuronidation activity. 3 PublicationsCorresponds to variant dbSNP:rs62625011Ensembl.1
Natural variantiVAR_007702331Q → R in CN2; has no residual bilirubin glucuronidation activity. 3 PublicationsCorresponds to variant dbSNP:rs72551348Ensembl.1
Natural variantiVAR_026140336R → L in CN1 and CN2. 1 Publication1
Natural variantiVAR_026141336R → Q in CN1. 1 PublicationCorresponds to variant dbSNP:rs750453538Ensembl.1
Natural variantiVAR_026142336R → W in CN2; has very low residual bilirubin glucuronidation activity of about 0.4% of that of the wild-type protein. 3 PublicationsCorresponds to variant dbSNP:rs139607673Ensembl.1
Natural variantiVAR_026143354W → R in CN2. 2 Publications1
Natural variantiVAR_007703357Q → R in CN1. 3 PublicationsCorresponds to variant dbSNP:rs72551351Ensembl.1
Natural variantiVAR_071404367R → C in CN2. 1 PublicationCorresponds to variant dbSNP:rs55750087Ensembl.1
Natural variantiVAR_012283367R → G in GILBS. 2 PublicationsCorresponds to variant dbSNP:rs55750087Ensembl.1
Natural variantiVAR_007704368A → T in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551352Ensembl.1
Natural variantiVAR_064958370I → V in CN2. 1 PublicationCorresponds to variant dbSNP:rs748989741Ensembl.1
Natural variantiVAR_007705375S → F in CN1; no bilirubin glucuronidation activity. 5 PublicationsCorresponds to variant dbSNP:rs72551353Ensembl.1
Natural variantiVAR_026144376H → R in CN1 and CN2. Corresponds to variant dbSNP:rs1349037761Ensembl.1
Natural variantiVAR_026145377G → V in CN1 and CN2. 1 PublicationCorresponds to variant dbSNP:rs1283652721Ensembl.1
Natural variantiVAR_007706381S → R in CN1. 2 PublicationsCorresponds to variant dbSNP:rs72551354Ensembl.1
Natural variantiVAR_064959387P → H in CN2; has no residual bilirubin glucuronidation activity. 1 Publication1
Natural variantiVAR_026146387P → S in CN1. 2 PublicationsCorresponds to variant dbSNP:rs901936528Ensembl.1
Natural variantiVAR_026147395G → V in CN1; has no residual bilirubin glucuronidation activity. 3 Publications