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P22309

- UD11_HUMAN

UniProt

P22309 - UD11_HUMAN

Protein

UDP-glucuronosyltransferase 1-1

Gene

UGT1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX-alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate. Is also able to catalyze the glucuronidation of 17beta-estradiol, 17alpha-ethinylestradiol, 1-hydroxypyrene, 4-methylumbelliferone, 1-naphthol, paranitrophenol, scopoletin, and umbelliferone. Isoform 2 lacks transferase activity but acts as a negative regulator of isoform 1.3 Publications

    Catalytic activityi

    UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside.2 Publications

    Kineticsi

    1. KM=0.26 µM for bilirubin1 Publication

    Vmax=1080 pmol/min/mg enzyme with bilirubin as substrate1 Publication

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. enzyme inhibitor activity Source: BHF-UCL
    3. glucuronosyltransferase activity Source: BHF-UCL
    4. protein heterodimerization activity Source: UniProt
    5. protein homodimerization activity Source: UniProt
    6. retinoic acid binding Source: BHF-UCL
    7. steroid binding Source: BHF-UCL

    GO - Biological processi

    1. acute-phase response Source: Ensembl
    2. bilirubin conjugation Source: ProtInc
    3. biphenyl catabolic process Source: Ensembl
    4. cellular glucuronidation Source: UniProt
    5. cellular response to ethanol Source: Ensembl
    6. cellular response to glucocorticoid stimulus Source: Ensembl
    7. digestion Source: ProtInc
    8. drug metabolic process Source: BHF-UCL
    9. estrogen metabolic process Source: ProtInc
    10. flavone metabolic process Source: BHF-UCL
    11. flavonoid glucuronidation Source: BHF-UCL
    12. heme catabolic process Source: Reactome
    13. heterocycle metabolic process Source: BHF-UCL
    14. liver development Source: Ensembl
    15. negative regulation of catalytic activity Source: GOC
    16. negative regulation of cellular glucuronidation Source: UniProtKB
    17. negative regulation of steroid metabolic process Source: BHF-UCL
    18. organ regeneration Source: Ensembl
    19. porphyrin-containing compound metabolic process Source: Reactome
    20. response to drug Source: Ensembl
    21. response to lipopolysaccharide Source: Ensembl
    22. response to nutrient Source: Ensembl
    23. response to starvation Source: Ensembl
    24. retinoic acid metabolic process Source: BHF-UCL
    25. small molecule metabolic process Source: Reactome
    26. steroid metabolic process Source: BHF-UCL
    27. xenobiotic glucuronidation Source: BHF-UCL
    28. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_22297. Heme degradation.
    REACT_6784. Glucuronidation.
    SABIO-RKP22309.

    Protein family/group databases

    CAZyiGT1. Glycosyltransferase Family 1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-glucuronosyltransferase 1-1 (EC:2.4.1.17)
    Short name:
    UDPGT 1-1
    Short name:
    UGT1*1
    Short name:
    UGT1-01
    Short name:
    UGT1.1
    Alternative name(s):
    Bilirubin-specific UDPGT isozyme 1
    Short name:
    hUG-BR1
    UDP-glucuronosyltransferase 1-A
    Short name:
    UGT-1A
    Short name:
    UGT1A
    UDP-glucuronosyltransferase 1A1
    Gene namesi
    Name:UGT1A1
    Synonyms:GNT1, UGT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12530. UGT1A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytochrome complex Source: Ensembl
    2. endoplasmic reticulum Source: UniProt
    3. endoplasmic reticulum membrane Source: Reactome
    4. integral component of plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Involvement in diseasei

    Gilbert syndrome (GILBS) [MIM:143500]: Occurs as a consequence of reduced bilirubin transferase activity and is often detected in young adults with vague non-specific complaints.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711G → 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. 6 Publications
    Corresponds to variant rs4148323 [ dbSNP | Ensembl ].
    VAR_009504
    Natural varianti83 – 831F → L in GILBS; displays less than 10% of wild-type bilirubin glucuronidation activity. 1 Publication
    Corresponds to variant rs56059937 [ dbSNP | Ensembl ].
    VAR_026136
    Natural varianti229 – 2291P → Q in CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity. 3 Publications
    Corresponds to variant rs35350960 [ dbSNP | Ensembl ].
    VAR_009505
    Natural varianti294 – 2941I → T in GILBS and CN2; 40-55% normal activity; normal Km for bilirubin; when homozygous far less repressive and generates the mild Gilbert phenotype. 2 Publications
    VAR_026139
    Natural varianti367 – 3671R → G in GILBS. 2 Publications
    Corresponds to variant rs55750087 [ dbSNP | Ensembl ].
    VAR_012283
    Natural varianti486 – 4861Y → D in CN2, GILBS and HBLRTFN; displays less than 10% of wild-type bilirubin glucuronidation activity. 6 Publications
    VAR_007709
    Transient familial neonatal hyperbilirubinemia (HBLRTFN) [MIM:237900]: A 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.1 Publication
    Note: 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.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711G → 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. 6 Publications
    Corresponds to variant rs4148323 [ dbSNP | Ensembl ].
    VAR_009504
    Natural varianti486 – 4861Y → D in CN2, GILBS and HBLRTFN; displays less than 10% of wild-type bilirubin glucuronidation activity. 6 Publications
    VAR_007709
    Crigler-Najjar syndrome 1 (CN1) [MIM:218800]: Patients 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.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391H → D in CN1. 1 Publication
    VAR_026135
    Natural varianti170 – 1701Missing in CN1 and CN2; has nearly normal activity at pH 7.6 and is inactive at pH 6.4. 4 Publications
    VAR_007695
    Natural varianti177 – 1771C → R in CN1. 2 Publications
    VAR_007697
    Natural varianti276 – 2761G → R in CN1. 2 Publications
    VAR_007699
    Natural varianti291 – 2911E → V in CN1. 1 Publication
    VAR_026138
    Natural varianti292 – 2921A → V in CN1. 1 Publication
    VAR_007700
    Natural varianti308 – 3081G → E in CN1; no enzyme activity. 3 Publications
    VAR_007701
    Natural varianti336 – 3361R → L in CN1 and CN2. 1 Publication
    VAR_026140
    Natural varianti336 – 3361R → Q in CN1. 1 Publication
    VAR_026141
    Natural varianti357 – 3571Q → R in CN1. 3 Publications
    VAR_007703
    Natural varianti368 – 3681A → T in CN1. 2 Publications
    VAR_007704
    Natural varianti375 – 3751S → F in CN1; no enzyme activity. 5 Publications
    VAR_007705
    Natural varianti376 – 3761H → R in CN1 and CN2.
    VAR_026144
    Natural varianti377 – 3771G → V in CN1 and CN2. 1 Publication
    VAR_026145
    Natural varianti381 – 3811S → R in CN1. 2 Publications
    VAR_007706
    Natural varianti387 – 3871P → S in CN1. 2 Publications
    VAR_026146
    Natural varianti395 – 3951G → V in CN1; has no residual bilirubin glucuronidation activity. 2 Publications
    VAR_026147
    Natural varianti401 – 4011A → P in CN1. 2 Publications
    VAR_007707
    Natural varianti402 – 4021K → T in CN1; has no residual bilirubin glucuronidation activity; N-glycosylation does take place at this new additional site. 1 Publication
    VAR_064960
    Natural varianti428 – 4281K → E in CN1. 2 Publications
    VAR_007708
    Natural varianti461 – 4611W → R in CN1 and CN2. 2 Publications
    VAR_026149
    Crigler-Najjar syndrome 2 (CN2) [MIM:606785]: Patients 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.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151L → R in CN2; mutant protein rapidly degraded by the proteasome owing to its mislocalization in the cell. 3 Publications
    VAR_019410
    Natural varianti34 – 341P → Q in CN2. 1 Publication
    VAR_026134
    Natural varianti71 – 711G → 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. 6 Publications
    Corresponds to variant rs4148323 [ dbSNP | Ensembl ].
    VAR_009504
    Natural varianti170 – 1701Missing in CN1 and CN2; has nearly normal activity at pH 7.6 and is inactive at pH 6.4. 4 Publications
    VAR_007695
    Natural varianti171 – 1711Missing in CN2. 1 Publication
    VAR_064955
    Natural varianti175 – 1751L → Q in CN2; has low residual bilirubin glucuronidation activity of about 4.6% of that of the wild-type protein. 3 Publications
    VAR_019411
    Natural varianti191 – 1911S → F in CN2; has low residual bilirubin glucuronidation activity of about 5.3% of that of the wild-type protein. 1 Publication
    VAR_064956
    Natural varianti209 – 2091R → W in CN2; has low residual bilirubin glucuronidation activity of about 2.9% of that of the wild-type protein. 5 Publications
    VAR_007698
    Natural varianti225 – 2251V → G in CN2. 2 Publications
    Corresponds to variant rs35003977 [ dbSNP | Ensembl ].
    VAR_026137
    Natural varianti229 – 2291P → Q in CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity. 3 Publications
    Corresponds to variant rs35350960 [ dbSNP | Ensembl ].
    VAR_009505
    Natural varianti279 – 2791N → Y in CN2. 1 Publication
    VAR_064957
    Natural varianti294 – 2941I → T in GILBS and CN2; 40-55% normal activity; normal Km for bilirubin; when homozygous far less repressive and generates the mild Gilbert phenotype. 2 Publications
    VAR_026139
    Natural varianti331 – 3311Q → R in CN2; has no residual bilirubin glucuronidation activity. 2 Publications
    VAR_007702
    Natural varianti336 – 3361R → L in CN1 and CN2. 1 Publication
    VAR_026140
    Natural varianti336 – 3361R → W in CN2; has very low residual bilirubin glucuronidation activity of about 0.4% of that of the wild-type protein. 3 Publications
    VAR_026142
    Natural varianti354 – 3541W → R in CN2. 2 Publications
    VAR_026143
    Natural varianti370 – 3701I → V in CN2. 1 Publication
    VAR_064958
    Natural varianti376 – 3761H → R in CN1 and CN2.
    VAR_026144
    Natural varianti377 – 3771G → V in CN1 and CN2. 1 Publication
    VAR_026145
    Natural varianti387 – 3871P → H in CN2; has no residual bilirubin glucuronidation activity. 1 Publication
    VAR_064959
    Natural varianti400 – 4001N → D in CN2. 1 Publication
    Corresponds to variant rs28934877 [ dbSNP | Ensembl ].
    VAR_019412
    Natural varianti403 – 4031R → C in CN2. 1 Publication
    VAR_026148
    Natural varianti443 – 4431L → P in CN2; has no residual bilirubin glucuronidation activity. 2 Publications
    VAR_064961
    Natural varianti461 – 4611W → R in CN1 and CN2. 2 Publications
    VAR_026149
    Natural varianti478 – 4781A → D in CN2. 1 Publication
    VAR_026150
    Natural varianti486 – 4861Y → D in CN2, GILBS and HBLRTFN; displays less than 10% of wild-type bilirubin glucuronidation activity. 6 Publications
    VAR_007709

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi143500. phenotype.
    218800. phenotype.
    237900. phenotype.
    601816. phenotype.
    606785. phenotype.
    Orphaneti79234. Crigler-Najjar syndrome type 1.
    79235. Crigler-Najjar syndrome type 2.
    357. Gilbert syndrome.
    240885. Irinotecan toxicity.
    240905. Raltegravir toxicity.
    240973. Susceptibility to adverse reaction due to irinotecan treatment.
    241017. Susceptibility to icterus due to raltegravir treatment.
    2312. Transient familial neonatal hyperbilirubinemia.
    PharmGKBiPA420.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 533508UDP-glucuronosyltransferase 1-1PRO_0000036000Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi102 – 1021N-linked (GlcNAc...)1 Publication
    Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP22309.
    PeptideAtlasiP22309.
    PRIDEiP22309.

    PTM databases

    PhosphoSiteiP22309.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed in liver, colon and small intestine. Isoform 2 but not isoform 1 is expressed in kidney. Isoform 1 and isoform 2 are not expressed in esophagus. Not expressed in skin.3 Publications

    Gene expression databases

    BgeeiP22309.
    CleanExiHS_UGT1A1.
    GenevestigatoriP22309.

    Interactioni

    Subunit structurei

    Isoform 1 interacts with isoform 2/i2 suggesting that oligomerization is involved in negative regulation of transferase activity by isoform 2. Isoform 1 also interacts with respective i2 isoforms of UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8, UGT1A9 and UGT1A10. Part of a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX.2 Publications

    Protein-protein interaction databases

    BioGridi120087. 4 interactions.
    IntActiP22309. 9 interactions.
    STRINGi9606.ENSP00000304845.

    Structurei

    3D structure databases

    ProteinModelPortaliP22309.
    SMRiP22309. Positions 116-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei491 – 50717HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the UDP-glycosyltransferase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1819.
    HOGENOMiHOG000220832.
    HOVERGENiHBG004033.
    KOiK00699.
    OMAiESHFRRM.
    OrthoDBiEOG7GBFWS.
    PhylomeDBiP22309.
    TreeFamiTF315472.

    Family and domain databases

    InterProiIPR002213. UDP_glucos_trans.
    [Graphical view]
    PANTHERiPTHR11926. PTHR11926. 1 hit.
    PfamiPF00201. UDPGT. 1 hit.
    [Graphical view]
    PROSITEiPS00375. UDPGT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P22309-1) [UniParc]FASTAAdd to Basket

    Also known as: i1

    This isoform has been chosen as the 'canonical' 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

    MAVESQGGRP LVLGLLLCVL GPVVSHAGKI LLIPVDGSHW LSMLGAIQQL    50
    QQRGHEIVVL APDASLYIRD GAFYTLKTYP VPFQREDVKE SFVSLGHNVF 100
    ENDSFLQRVI KTYKKIKKDS AMLLSGCSHL LHNKELMASL AESSFDVMLT 150
    DPFLPCSPIV AQYLSLPTVF FLHALPCSLE FEATQCPNPF SYVPRPLSSH 200
    SDHMTFLQRV KNMLIAFSQN FLCDVVYSPY ATLASEFLQR EVTVQDLLSS 250
    ASVWLFRSDF VKDYPRPIMP NMVFVGGINC LHQNPLSQEF EAYINASGEH 300
    GIVVFSLGSM VSEIPEKKAM AIADALGKIP QTVLWRYTGT RPSNLANNTI 350
    LVKWLPQNDL LGHPMTRAFI THAGSHGVYE SICNGVPMVM MPLFGDQMDN 400
    AKRMETKGAG VTLNVLEMTS EDLENALKAV INDKSYKENI MRLSSLHKDR 450
    PVEPLDLAVF WVEFVMRHKG APHLRPAAHD LTWYQYHSLD VIGFLLAVVL 500
    TVAFITFKCC AYGYRKCLGK KGRVKKAHKS KTH 533
    Length:533
    Mass (Da):59,591
    Last modified:August 1, 1991 - v1
    Checksum:i19C90231AD0EB547
    GO
    Isoform 2 (identifier: P22309-2) [UniParc]FASTAAdd to Basket

    Also known as: i2, 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

    Sequence cautioni

    The sequence AAA61247.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAF03522.2 differs from that shown. Reason: Erroneous gene model prediction.

    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.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151L → R in CN2; mutant protein rapidly degraded by the proteasome owing to its mislocalization in the cell. 3 Publications
    VAR_019410
    Natural varianti34 – 341P → Q in CN2. 1 Publication
    VAR_026134
    Natural varianti39 – 391H → D in CN1. 1 Publication
    VAR_026135
    Natural varianti71 – 711G → 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. 6 Publications
    Corresponds to variant rs4148323 [ dbSNP | Ensembl ].
    VAR_009504
    Natural varianti83 – 831F → L in GILBS; displays less than 10% of wild-type bilirubin glucuronidation activity. 1 Publication
    Corresponds to variant rs56059937 [ dbSNP | Ensembl ].
    VAR_026136
    Natural varianti170 – 1701Missing in CN1 and CN2; has nearly normal activity at pH 7.6 and is inactive at pH 6.4. 4 Publications
    VAR_007695
    Natural varianti171 – 1711Missing in CN2. 1 Publication
    VAR_064955
    Natural varianti175 – 1751L → Q in CN2; has low residual bilirubin glucuronidation activity of about 4.6% of that of the wild-type protein. 3 Publications
    VAR_019411
    Natural varianti177 – 1771C → R in CN1. 2 Publications
    VAR_007697
    Natural varianti191 – 1911S → F in CN2; has low residual bilirubin glucuronidation activity of about 5.3% of that of the wild-type protein. 1 Publication
    VAR_064956
    Natural varianti209 – 2091R → W in CN2; has low residual bilirubin glucuronidation activity of about 2.9% of that of the wild-type protein. 5 Publications
    VAR_007698
    Natural varianti225 – 2251V → G in CN2. 2 Publications
    Corresponds to variant rs35003977 [ dbSNP | Ensembl ].
    VAR_026137
    Natural varianti229 – 2291P → Q in CN2 and GILBS; displays 2-fold decrease in biluribin affinity and 61% of wild-type bilirubin glucuronidation activity. 3 Publications
    Corresponds to variant rs35350960 [ dbSNP | Ensembl ].
    VAR_009505
    Natural varianti276 – 2761G → R in CN1. 2 Publications
    VAR_007699
    Natural varianti279 – 2791N → Y in CN2. 1 Publication
    VAR_064957
    Natural varianti291 – 2911E → V in CN1. 1 Publication
    VAR_026138
    Natural varianti292 – 2921A → V in CN1. 1 Publication
    VAR_007700
    Natural varianti294 – 2941I → T in GILBS and CN2; 40-55% normal activity; normal Km for bilirubin; when homozygous far less repressive and generates the mild Gilbert phenotype. 2 Publications
    VAR_026139
    Natural varianti308 – 3081G → E in CN1; no enzyme activity. 3 Publications
    VAR_007701
    Natural varianti331 – 3311Q → R in CN2; has no residual bilirubin glucuronidation activity. 2 Publications
    VAR_007702
    Natural varianti336 – 3361R → L in CN1 and CN2. 1 Publication
    VAR_026140
    Natural varianti336 – 3361R → Q in CN1. 1 Publication
    VAR_026141
    Natural varianti336 – 3361R → W in CN2; has very low residual bilirubin glucuronidation activity of about 0.4% of that of the wild-type protein. 3 Publications
    VAR_026142
    Natural varianti354 – 3541W → R in CN2. 2 Publications
    VAR_026143
    Natural varianti357 – 3571Q → R in CN1. 3 Publications
    VAR_007703
    Natural varianti367 – 3671R → G in GILBS. 2 Publications
    Corresponds to variant rs55750087 [ dbSNP | Ensembl ].
    VAR_012283
    Natural varianti368 – 3681A → T in CN1. 2 Publications
    VAR_007704
    Natural varianti370 – 3701I → V in CN2. 1 Publication
    VAR_064958
    Natural varianti375 – 3751S → F in CN1; no enzyme activity. 5 Publications
    VAR_007705
    Natural varianti376 – 3761H → R in CN1 and CN2.
    VAR_026144
    Natural varianti377 – 3771G → V in CN1 and CN2. 1 Publication
    VAR_026145
    Natural varianti381 – 3811S → R in CN1. 2 Publications
    VAR_007706
    Natural varianti387 – 3871P → H in CN2; has no residual bilirubin glucuronidation activity. 1 Publication
    VAR_064959
    Natural varianti387 – 3871P → S in CN1. 2 Publications
    VAR_026146
    Natural varianti395 – 3951G → V in CN1; has no residual bilirubin glucuronidation activity. 2 Publications
    VAR_026147
    Natural varianti400 – 4001N → D in CN2. 1 Publication
    Corresponds to variant rs28934877 [ dbSNP | Ensembl ].
    VAR_019412
    Natural varianti401 – 4011A → P in CN1. 2 Publications
    VAR_007707
    Natural varianti402 – 4021K → T in CN1; has no residual bilirubin glucuronidation activity; N-glycosylation does take place at this new additional site. 1 Publication
    VAR_064960
    Natural varianti403 – 4031R → C in CN2. 1 Publication
    VAR_026148
    Natural varianti428 – 4281K → E in CN1. 2 Publications
    VAR_007708
    Natural varianti443 – 4431L → P in CN2; has no residual bilirubin glucuronidation activity. 2 Publications
    VAR_064961
    Natural varianti461 – 4611W → R in CN1 and CN2. 2 Publications
    VAR_026149
    Natural varianti478 – 4781A → D in CN2. 1 Publication
    VAR_026150
    Natural varianti486 – 4861Y → D in CN2, GILBS and HBLRTFN; displays less than 10% of wild-type bilirubin glucuronidation activity. 6 Publications
    VAR_007709
    Natural varianti511 – 5111A → P.
    Corresponds to variant rs1042709 [ dbSNP | Ensembl ].
    VAR_025355

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei435 – 53399SYKEN…KSKTH → RKKQQSGRQM in isoform 2. 1 PublicationVSP_053958Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57899 mRNA. Translation: AAA63195.1.
    M84124, M84122, M84123 Genomic DNA. Translation: AAA61247.1. Sequence problems.
    M84125 Genomic DNA. Translation: AAA61248.1.
    DQ364247 mRNA. Translation: ABC96771.1.
    AF297093 Genomic DNA. Translation: AAG30424.1.
    AC006985 Genomic DNA. Translation: AAF03522.2. Sequence problems.
    D87674 Genomic DNA. Translation: BAA25600.1.
    CCDSiCCDS2510.1. [P22309-1]
    PIRiA39092.
    RefSeqiNP_000454.1. NM_000463.2. [P22309-1]
    UniGeneiHs.554822.

    Genome annotation databases

    GeneIDi54658.
    KEGGihsa:54658.
    UCSCiuc002vvb.3. human. [P22309-1]

    Polymorphism databases

    DMDMi136729.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Glucuronosyltransferase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57899 mRNA. Translation: AAA63195.1 .
    M84124 , M84122 , M84123 Genomic DNA. Translation: AAA61247.1 . Sequence problems.
    M84125 Genomic DNA. Translation: AAA61248.1 .
    DQ364247 mRNA. Translation: ABC96771.1 .
    AF297093 Genomic DNA. Translation: AAG30424.1 .
    AC006985 Genomic DNA. Translation: AAF03522.2 . Sequence problems.
    D87674 Genomic DNA. Translation: BAA25600.1 .
    CCDSi CCDS2510.1. [P22309-1 ]
    PIRi A39092.
    RefSeqi NP_000454.1. NM_000463.2. [P22309-1 ]
    UniGenei Hs.554822.

    3D structure databases

    ProteinModelPortali P22309.
    SMRi P22309. Positions 116-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120087. 4 interactions.
    IntActi P22309. 9 interactions.
    STRINGi 9606.ENSP00000304845.

    Chemistry

    BindingDBi P22309.
    ChEMBLi CHEMBL1287617.
    DrugBanki DB01048. Abacavir.
    DB00173. Adenine.
    DB00586. Diclofenac.
    DB00783. Estradiol.
    DB00973. Ezetimibe.
    DB00762. Irinotecan.
    DB00688. Mycophenolate mofetil.
    DB01024. Mycophenolic acid.
    DB00818. Propofol.
    DB01045. Rifampin.
    DB00197. Troglitazone.

    Protein family/group databases

    CAZyi GT1. Glycosyltransferase Family 1.

    PTM databases

    PhosphoSitei P22309.

    Polymorphism databases

    DMDMi 136729.

    Proteomic databases

    PaxDbi P22309.
    PeptideAtlasi P22309.
    PRIDEi P22309.

    Protocols and materials databases

    DNASUi 54658.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 54658.
    KEGGi hsa:54658.
    UCSCi uc002vvb.3. human. [P22309-1 ]

    Organism-specific databases

    CTDi 54658.
    GeneCardsi GC02P234668.
    HGNCi HGNC:12530. UGT1A1.
    MIMi 143500. phenotype.
    191740. gene.
    218800. phenotype.
    237900. phenotype.
    601816. phenotype.
    606785. phenotype.
    neXtProti NX_P22309.
    Orphaneti 79234. Crigler-Najjar syndrome type 1.
    79235. Crigler-Najjar syndrome type 2.
    357. Gilbert syndrome.
    240885. Irinotecan toxicity.
    240905. Raltegravir toxicity.
    240973. Susceptibility to adverse reaction due to irinotecan treatment.
    241017. Susceptibility to icterus due to raltegravir treatment.
    2312. Transient familial neonatal hyperbilirubinemia.
    PharmGKBi PA420.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1819.
    HOGENOMi HOG000220832.
    HOVERGENi HBG004033.
    KOi K00699.
    OMAi ESHFRRM.
    OrthoDBi EOG7GBFWS.
    PhylomeDBi P22309.
    TreeFami TF315472.

    Enzyme and pathway databases

    Reactomei REACT_22297. Heme degradation.
    REACT_6784. Glucuronidation.
    SABIO-RK P22309.

    Miscellaneous databases

    GenomeRNAii 54658.
    NextBioi 27033972.
    PROi P22309.
    SOURCEi Search...

    Gene expression databases

    Bgeei P22309.
    CleanExi HS_UGT1A1.
    Genevestigatori P22309.

    Family and domain databases

    InterProi IPR002213. UDP_glucos_trans.
    [Graphical view ]
    PANTHERi PTHR11926. PTHR11926. 1 hit.
    Pfami PF00201. UDPGT. 1 hit.
    [Graphical view ]
    PROSITEi PS00375. UDPGT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells."
      Ritter J.K., Crawford J.M., Owens I.S.
      J. Biol. Chem. 266:1043-1047(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini."
      Ritter J.K., Chen F., Sheen Y.Y., Tran H.M., Kimura S., Yeatman M.T., Owens I.S.
      J. Biol. Chem. 267:3257-3261(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    3. "Thirteen UDP-glucuronosyltransferase genes are encoded at the human UGT1 gene complex locus."
      Gong Q.H., Cho J.W., Huang T., Potter C., Gholami N., Basu N.K., Kubota S., Carvalho S., Pennington M.W., Owens I.S., Popescu N.C.
      Pharmacogenetics 11:357-368(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Guillemette C., Levesque E., Girard H., Bernard O.
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Analysis of the promoter of human bilirubin UDP-glucuronosyltransferase gene (UGT1*1) in relevance to Gilbert's syndrome."
      Ueyama H., Koiwai O., Soeda Y., Sato H., Satoh Y., Ohkubo I., Doida Y.
      Hepatol. Res. 9:152-163(1997)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
    7. "A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins."
      Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.
      Mol. Biol. Cell 13:4456-4469(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: COMPONENT OF A CHAPERONE COMPLEX.
    8. "Regulation of the UGT1A1 bilirubin-conjugating pathway: role of a new splicing event at the UGT1A locus."
      Levesque E., Girard H., Journault K., Lepine J., Guillemette C.
      Hepatology 45:128-138(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
    9. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBSTRATE SPECIFICITY, CHARACTERIZATION OF VARIANTS CN2 ARG-71; LEU-83; GLN-229 AND ASP-486.
    10. "Genetic diversity at the UGT1 locus is amplified by a novel 3' alternative splicing mechanism leading to nine additional UGT1A proteins that act as regulators of glucuronidation activity."
      Girard H., Levesque E., Bellemare J., Journault K., Caillier B., Guillemette C.
      Pharmacogenet. Genomics 17:1077-1089(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, CATALYTIC ACTIVITY, FUNCTION (ISOFORM 2), TISSUE SPECIFICITY.
    11. "Structure and concentration changes affect characterization of UGT isoform-specific metabolism of isoflavones."
      Tang L., Singh R., Liu Z., Hu M.
      Mol. Pharm. 6:1466-1482(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Crigler-Najjar syndrome in The Netherlands: identification of four novel UGT1A1 alleles, genotype-phenotype correlation, and functional analysis of 10 missense mutants."
      Sneitz N., Bakker C.T., de Knegt R.J., Halley D.J., Finel M., Bosma P.J.
      Hum. Mutat. 31:52-59(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBSTRATE SPECIFICITY, VARIANT CN1 THR-402, VARIANTS CN2 ARG-15; ARG-71; PHE-191; TRP-209; TRP-336; HIS-387; PRO-443 AND ASP-486, CHARACTERIZATION OF VARIANT CN1 THR-402, CHARACTERIZATION OF VARIANTS CN2 ARG-71; GLN-175; PHE-191; TRP-209; ARG-331; TRP-336; HIS-387; VAL-395 AND PRO-443.
    13. Cited for: INVOLVEMENT IN BILIQTL1.
    14. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102.
      Tissue: Liver.
    15. "Alternatively spliced products of the UGT1A gene interact with the enzymatically active proteins to inhibit glucuronosyltransferase activity in vitro."
      Bellemare J., Rouleau M., Girard H., Harvey M., Guillemette C.
      Drug Metab. Dispos. 38:1785-1789(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    16. "Mechanisms of inherited deficiencies of multiple UDP-glucuronosyltransferase isoforms in two patients with Crigler-Najjar syndrome, type I."
      Bosma P.J., Chowdhury J.R., Huang T.-J., Lahiri P., Elferink R.P.J.O., van Es H.H.G., Lederstein M., Whitington P.F., Jansen P.L.M., Chowdhury N.R.
      FASEB J. 6:2859-2863(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CN1 PHE-375.
    17. "Identification of defect in the genes for bilirubin UDP-glucuronosyl-transferase in a patient with Crigler-Najjar syndrome type II."
      Aono S., Yamada Y., Keino H., Hanada N., Nakagawa T., Sasaoka Y., Yazawa T., Sato H., Koiwai O.
      Biochem. Biophys. Res. Commun. 197:1239-1244(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CN2 ARG-71 AND ASP-486.
    18. "Identification of an A-to-G missense mutation in exon 2 of the UGT1 gene complex that causes Crigler-Najjar syndrome type 2."
      Moghrabi N., Clarke D.J., Boxer M., Burchell B.
      Genomics 18:171-173(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CN2 ARG-331.
    19. "A phenylalanine codon deletion at the UGT1 gene complex locus of a Crigler-Najjar type I patient generates a pH-sensitive bilirubin UDP-glucuronosyltransferase."
      Ritter J.K., Yeatman M.T., Kaiser C., Gridelli B., Owens I.S.
      J. Biol. Chem. 268:23573-23579(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CN1 PHE-170 DEL.
    20. Cited for: VARIANTS CN1 VAL-292; GLU-308; ARG-357; THR-368; ARG-381; PRO-401 AND GLU-428.
    21. "Identification of two single base substitutions in the UGT1 gene locus which abolish bilirubin uridine diphosphate glucuronosyltransferase activity in vitro."
      Erps L.T., Ritter J.K., Hersh J.H., Blossom D., Martin N.C., Owens I.S.
      J. Clin. Invest. 93:564-570(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CN1 GLU-308 AND PHE-375, CHARACTERIZATION OF VARIANTS CN1 GLU-308 AND PHE-375.
    22. "Discrimination between Crigler-Najjar type I and II by expression of mutant bilirubin uridine diphosphate-glucuronosyltransferase."
      Seppen J., Bosma P.J., Goldhoorn B.G., Bakker C.T.M., Roy Chowdhury J., Roy Chowdhury N., Jansen P.L.M., Oude Elferink R.P.J.
      J. Clin. Invest. 94:2385-2391(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CN1 PHE-170 DEL; ARG-177; ARG-276 AND PHE-375, VARIANTS CN2 GLN-175 AND TRP-209.
    23. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GILBS ARG-71; GLN-229 AND GLY-367.
      Tissue: Liver and Peripheral blood leukocyte.
    24. "A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type II."
      Seppen J., Steenken E., Lindhout D., Bosma P.J., Oude Elferink R.P.J.
      FEBS Lett. 390:294-298(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CN2 ARG-15, CHARACTERIZATION OF VARIANT CN2 ARG-15.
    25. "Coding defect and a TATA box mutation at the bilirubin UDP-glucuronosyltransferase gene cause Crigler-Najjar type I disease."
      Ciotti M., Chen F., Rubaltelli F.F., Owens I.S.
      Biochim. Biophys. Acta 1407:40-50(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CN2 THR-294, CHARACTERIZATION OF VARIANT CN2 THR-294.
    26. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CN2 ARG-71; TRP-209; GLN-229 AND ASP-486.
    27. "Gilbert syndrome caused by a homozygous missense mutation (Tyr486Asp) of bilirubin UDP-glucuronosyltransferase gene."
      Maruo Y., Sato H., Yamano T., Doida Y., Shimada M.
      J. Pediatr. 132:1045-1047(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GILBS ASP-486.
    28. "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) [PubMed] [Europe PMC] [Abstract]
      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-381; SER-387; PRO-401 AND GLU-428, VARIANTS CN2 ARG-15; GLN-175; TRP-209; GLY-225 AND ARG-331, VARIANTS GILBS ARG-71; GLN-229; THR-294; GLY-367 AND ASP-486.
    29. "Prolonged unconjugated hyperbilirubinemia associated with breast milk and mutations of the bilirubin uridine diphosphate-glucuronosyltransferase gene."
      Maruo Y., Nishizawa K., Sato H., Sawa H., Shimada M.
      Pediatrics 106:E59-E59(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HBLRTFN ARG-71 AND ASP-486.
    30. "Interaction of coding region mutations and the Gilbert-type promoter abnormality of the UGT1A1 gene causes moderate degrees of unconjugated hyperbilirubinaemia and may lead to neonatal kernicterus."
      Kadakol A., Sappal B.S., Ghosh S.S., Lowenheim M., Chowdhury A., Chowdhury S., Santra A., Arias I.M., Chowdhury J.R., Chowdhury N.R.
      J. Med. Genet. 38:244-249(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CN2 GLN-175.
    31. "Association of a homozygous (TA)8 promoter polymorphism and a N400D mutation of UGT1A1 in a child with Crigler-Najjar type II syndrome."
      Labrune P., Myara A., Chalas J., Le Bihan B., Capel L., Francoual J.
      Hum. Mutat. 20:399-401(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CN2 ASP-400.
    32. "Novel missense mutation of the UGT1A1 gene in Thai siblings with Gilbert's syndrome."
      Sutomo R., Laosombat V., Sadewa A.H., Yokoyama N., Nakamura H., Matsuo M., Nishio H.
      Pediatr. Int. 44:427-432(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GILBS LEU-83.
    33. "Rapid proteasomal degradation of translocation-deficient UDP-glucuronosyltransferase 1A1 proteins in patients with Crigler-Najjar type II."
      Ohnishi A., Emi Y.
      Biochem. Biophys. Res. Commun. 310:735-741(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT CN2 ARG-15.
    34. "Spectrum of UGT1A1 mutations in Crigler-Najjar (CN) syndrome patients: identification of twelve novel alleles and genotype-phenotype correlation."
      Servedio V., d'Apolito M., Maiorano N., Minuti B., Torricelli F., Ronchi F., Zancan L., Perrotta S., Vajro P., Boschetto L., Iolascon A.
      Hum. Mutat. 25:325-325(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CN1 GLN-336; ARG-357; PHE-375; SER-387 AND VAL-395, VARIANTS CN2 GLN-34; PHE-170 DEL; TRP-209; GLY-225; LEU-336; TRP-336; ARG-354; CYS-403 AND ASP-478, VARIANTS CN1/CN2 VAL-377 AND ARG-461.
    35. "Seven novel mutations of the UGT1A1 gene in patients with unconjugated hyperbilirubinemia."
      D'Apolito M., Marrone A., Servedio V., Vajro P., De Falco L., Iolascon A.
      Haematologica 92:133-134(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CN1 PHE-171 DEL, VARIANTS CN2 TYR-279; ARG-354; VAL-370; VAL-395; PRO-443 AND ARG-461.

    Entry informationi

    Entry nameiUD11_HUMAN
    AccessioniPrimary (citable) accession number: P22309
    Secondary accession number(s): A6NJC3, B8K286
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 163 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The gene 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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3