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UDP-glucuronosyltransferase 1-1 (UDPGT 1-1) (UGT1*1) (UGT1-01) (UGT1.1) (EC 2.4.1.17) (Bilirubin-specific UDPGT isozyme 1) (hUG-BR1) (UDP-glucuronosyltransferase 1-A) (UGT-1A) (UGT1A) (UDP-glucuronosyltransferase 1A1)

 UD11_HUMAN              Reviewed;         533 AA.
P22309; A6NJC3; B8K286;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
30-AUG-2017, entry version 190.
RecName: Full=UDP-glucuronosyltransferase 1-1;
Short=UDPGT 1-1;
Short=UGT1*1;
Short=UGT1-01;
Short=UGT1.1;
EC=2.4.1.17;
AltName: Full=Bilirubin-specific UDPGT isozyme 1;
Short=hUG-BR1;
AltName: Full=UDP-glucuronosyltransferase 1-A;
Short=UGT-1A;
Short=UGT1A;
AltName: Full=UDP-glucuronosyltransferase 1A1;
Flags: Precursor;
Name=UGT1A1; Synonyms=GNT1, UGT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=1898728;
Ritter J.K., Crawford J.M., Owens I.S.;
"Cloning of two human liver bilirubin UDP-glucuronosyltransferase
cDNAs with expression in COS-1 cells.";
J. Biol. Chem. 266:1043-1047(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=1339448;
Ritter J.K., Chen F., Sheen Y.Y., Tran H.M., Kimura S., Yeatman M.T.,
Owens I.S.;
"A novel complex locus UGT1 encodes human bilirubin, phenol, and other
UDP-glucuronosyltransferase isozymes with identical carboxyl
termini.";
J. Biol. Chem. 267:3257-3261(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11434514; DOI=10.1097/00008571-200106000-00011;
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.;
"Thirteen UDP-glucuronosyltransferase genes are encoded at the human
UGT1 gene complex locus.";
Pharmacogenetics 11:357-368(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Guillemette C., Levesque E., Girard H., Bernard O.;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
Ueyama H., Koiwai O., Soeda Y., Sato H., Satoh Y., Ohkubo I.,
Doida Y.;
"Analysis of the promoter of human bilirubin UDP-
glucuronosyltransferase gene (UGT1*1) in relevance to Gilbert's
syndrome.";
Hepatol. Res. 9:152-163(1997).
[7]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[8]
ALTERNATIVE SPLICING, FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION,
SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=17187418; DOI=10.1002/hep.21464;
Levesque E., Girard H., Journault K., Lepine J., Guillemette C.;
"Regulation of the UGT1A1 bilirubin-conjugating pathway: role of a new
splicing event at the UGT1A locus.";
Hepatology 45:128-138(2007).
[9]
FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBSTRATE
SPECIFICITY, AND CHARACTERIZATION OF VARIANTS CN2 ARG-71; LEU-83;
GLN-229 AND ASP-486.
PubMed=18004206; DOI=10.1097/FPC.0b013e328256b1b6;
Udomuksorn W., Elliot D.J., Lewis B.C., Mackenzie P.I.,
Yoovathaworn K., Miners J.O.;
"Influence of mutations associated with Gilbert and Crigler-Najjar
type II syndromes on the glucuronidation kinetics of bilirubin and
other UDP-glucuronosyltransferase 1A substrates.";
Pharmacogenet. Genomics 17:1017-1029(2007).
[10]
ALTERNATIVE SPLICING, CATALYTIC ACTIVITY, FUNCTION (ISOFORM 2), AND
TISSUE SPECIFICITY.
PubMed=18004212; DOI=10.1097/FPC.0b013e3282f1f118;
Girard H., Levesque E., Bellemare J., Journault K., Caillier B.,
Guillemette C.;
"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.";
Pharmacogenet. Genomics 17:1077-1089(2007).
[11]
FUNCTION.
PubMed=19545173; DOI=10.1021/mp8002557;
Tang L., Singh R., Liu Z., Hu M.;
"Structure and concentration changes affect characterization of UGT
isoform-specific metabolism of isoflavones.";
Mol. Pharm. 6:1466-1482(2009).
[12]
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, AND CHARACTERIZATION
OF VARIANTS CN2 ARG-71; GLN-175; PHE-191; TRP-209; ARG-331; TRP-336;
HIS-387; VAL-395 AND PRO-443.
PubMed=19830808; DOI=10.1002/humu.21133;
Sneitz N., Bakker C.T., de Knegt R.J., Halley D.J., Finel M.,
Bosma P.J.;
"Crigler-Najjar syndrome in The Netherlands: identification of four
novel UGT1A1 alleles, genotype-phenotype correlation, and functional
analysis of 10 missense mutants.";
Hum. Mutat. 31:52-59(2010).
[13]
INVOLVEMENT IN BILIQTL1.
PubMed=19414484; DOI=10.1093/hmg/ddp202;
Johnson A.D., Kavousi M., Smith A.V., Chen M.H., Dehghan A.,
Aspelund T., Lin J.P., van Duijn C.M., Harris T.B., Cupples L.A.,
Uitterlinden A.G., Launer L., Hofman A., Rivadeneira F., Stricker B.,
Yang Q., O'Donnell C.J., Gudnason V., Witteman J.C.;
"Genome-wide association meta-analysis for total serum bilirubin
levels.";
Hum. Mol. Genet. 18:2700-2710(2009).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
SUBUNIT.
PubMed=20610558; DOI=10.1124/dmd.110.034835;
Bellemare J., Rouleau M., Girard H., Harvey M., Guillemette C.;
"Alternatively spliced products of the UGT1A gene interact with the
enzymatically active proteins to inhibit glucuronosyltransferase
activity in vitro.";
Drug Metab. Dispos. 38:1785-1789(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
VARIANT CN1 PHE-375.
PubMed=1634050;
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.;
"Mechanisms of inherited deficiencies of multiple UDP-
glucuronosyltransferase isoforms in two patients with Crigler-Najjar
syndrome, type I.";
FASEB J. 6:2859-2863(1992).
[18]
VARIANTS CN2 ARG-71 AND ASP-486.
PubMed=8280139; DOI=10.1006/bbrc.1993.2610;
Aono S., Yamada Y., Keino H., Hanada N., Nakagawa T., Sasaoka Y.,
Yazawa T., Sato H., Koiwai O.;
"Identification of defect in the genes for bilirubin UDP-glucuronosyl-
transferase in a patient with Crigler-Najjar syndrome type II.";
Biochem. Biophys. Res. Commun. 197:1239-1244(1993).
[19]
VARIANT CN2 ARG-331.
PubMed=8276413; DOI=10.1006/geno.1993.1451;
Moghrabi N., Clarke D.J., Boxer M., Burchell B.;
"Identification of an A-to-G missense mutation in exon 2 of the UGT1
gene complex that causes Crigler-Najjar syndrome type 2.";
Genomics 18:171-173(1993).
[20]
VARIANT CN1 PHE-170 DEL.
PubMed=8226884;
Ritter J.K., Yeatman M.T., Kaiser C., Gridelli B., Owens I.S.;
"A phenylalanine codon deletion at the UGT1 gene complex locus of a
Crigler-Najjar type I patient generates a pH-sensitive bilirubin UDP-
glucuronosyltransferase.";
J. Biol. Chem. 268:23573-23579(1993).
[21]
VARIANTS CN1 VAL-292; GLU-308; ARG-357; THR-368; ARG-381; PRO-401 AND
GLU-428.
PubMed=7989045; DOI=10.1007/BF00206965;
Labrune P., Myara A., Hadchouel M., Ronchi F., Bernard O., Trivin F.,
Roy Chowdhury N., Roy Chowdhury J., Munnich A., Odievre M.;
"Genetic heterogeneity of Crigler-Najjar syndrome type I: a study of
14 cases.";
Hum. Genet. 94:693-697(1994).
[22]
VARIANTS CN1 GLU-308 AND PHE-375, AND CHARACTERIZATION OF VARIANTS CN1
GLU-308 AND PHE-375.
PubMed=7906695; DOI=10.1172/JCI117008;
Erps L.T., Ritter J.K., Hersh J.H., Blossom D., Martin N.C.,
Owens I.S.;
"Identification of two single base substitutions in the UGT1 gene
locus which abolish bilirubin uridine diphosphate
glucuronosyltransferase activity in vitro.";
J. Clin. Invest. 93:564-570(1994).
[23]
VARIANTS CN1 PHE-170 DEL; ARG-177; ARG-276 AND PHE-375, AND VARIANTS
CN2 GLN-175 AND TRP-209.
PubMed=7989595; DOI=10.1172/JCI117604;
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.;
"Discrimination between Crigler-Najjar type I and II by expression of
mutant bilirubin uridine diphosphate-glucuronosyltransferase.";
J. Clin. Invest. 94:2385-2391(1994).
[24]
VARIANTS GILBS ARG-71; GLN-229 AND GLY-367.
TISSUE=Liver, and Peripheral blood leukocyte;
PubMed=7715297; DOI=10.1016/S0140-6736(95)90702-5;
Aono S., Adachi Y., Uyama E., Yamada Y., Keino H., Nanno T.,
Koiwai O., Sato H.;
"Analysis of genes for bilirubin UDP-glucuronosyltransferase in
Gilbert's syndrome.";
Lancet 345:958-959(1995).
[25]
VARIANT CN2 ARG-15, AND CHARACTERIZATION OF VARIANT CN2 ARG-15.
PubMed=8706880; DOI=10.1016/0014-5793(96)00677-1;
Seppen J., Steenken E., Lindhout D., Bosma P.J., Oude Elferink R.P.J.;
"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.";
FEBS Lett. 390:294-298(1996).
[26]
VARIANT CN2 THR-294, AND CHARACTERIZATION OF VARIANT CN2 THR-294.
PubMed=9639672; DOI=10.1016/S0925-4439(98)00030-1;
Ciotti M., Chen F., Rubaltelli F.F., Owens I.S.;
"Coding defect and a TATA box mutation at the bilirubin UDP-
glucuronosyltransferase gene cause Crigler-Najjar type I disease.";
Biochim. Biophys. Acta 1407:40-50(1998).
[27]
VARIANTS CN2 ARG-71; TRP-209; GLN-229 AND ASP-486.
PubMed=9621515; DOI=10.1007/s100380050050;
Yamamoto K., Soeda Y., Kamisako T., Hosaka H., Fukano M., Sato H.,
Fujiyama Y., Dachi Y., Satoh Y., Bamba T.;
"Analysis of bilirubin uridine 5'-diphosphate (UDP)-
glucuronosyltransferase gene mutations in seven patients with Crigler-
Najjar syndrome type II.";
J. Hum. Genet. 43:111-114(1998).
[28]
VARIANT GILBS ASP-486.
PubMed=9627603; DOI=10.1016/S0022-3476(98)70408-1;
Maruo Y., Sato H., Yamano T., Doida Y., Shimada M.;
"Gilbert syndrome caused by a homozygous missense mutation (Tyr486Asp)
of bilirubin UDP-glucuronosyltransferase gene.";
J. Pediatr. 132:1045-1047(1998).
[29]
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,
AND VARIANTS GILBS ARG-71; GLN-229; THR-294; GLY-367 AND ASP-486.
PubMed=11013440;
DOI=10.1002/1098-1004(200010)16:4<297::AID-HUMU2>3.0.CO;2-Z;
Kadakol A., Ghosh S.S., Sappal B.S., Sharma G., Chowdhury J.R.,
Chowdhury N.R.;
"Genetic lesions of bilirubin uridine-diphosphoglucuronate
glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert
syndromes: correlation of genotype to phenotype.";
Hum. Mutat. 16:297-306(2000).
[30]
VARIANTS HBLRTFN ARG-71 AND ASP-486.
PubMed=11061796; DOI=10.1542/peds.106.5.e59;
Maruo Y., Nishizawa K., Sato H., Sawa H., Shimada M.;
"Prolonged unconjugated hyperbilirubinemia associated with breast milk
and mutations of the bilirubin uridine diphosphate-
glucuronosyltransferase gene.";
Pediatrics 106:E59-E59(2000).
[31]
VARIANT CN2 GLN-175.
PubMed=11370628; DOI=10.1136/jmg.38.4.244;
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.;
"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.";
J. Med. Genet. 38:244-249(2001).
[32]
VARIANT CN2 ASP-400.
PubMed=12402338; DOI=10.1002/humu.10122;
Labrune P., Myara A., Chalas J., Le Bihan B., Capel L., Francoual J.;
"Association of a homozygous (TA)8 promoter polymorphism and a N400D
mutation of UGT1A1 in a child with Crigler-Najjar type II syndrome.";
Hum. Mutat. 20:399-401(2002).
[33]
VARIANT GILBS LEU-83.
PubMed=12139570; DOI=10.1046/j.1442-200X.2002.t01-1-01577.x;
Sutomo R., Laosombat V., Sadewa A.H., Yokoyama N., Nakamura H.,
Matsuo M., Nishio H.;
"Novel missense mutation of the UGT1A1 gene in Thai siblings with
Gilbert's syndrome.";
Pediatr. Int. 44:427-432(2002).
[34]
CHARACTERIZATION OF VARIANT CN2 ARG-15.
PubMed=14550264; DOI=10.1016/j.bbrc.2003.09.072;
Ohnishi A., Emi Y.;
"Rapid proteasomal degradation of translocation-deficient UDP-
glucuronosyltransferase 1A1 proteins in patients with Crigler-Najjar
type II.";
Biochem. Biophys. Res. Commun. 310:735-741(2003).
[35]
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, AND VARIANTS CN1/CN2 VAL-377 AND ARG-461.
PubMed=15712364; DOI=10.1002/humu.9322;
Servedio V., d'Apolito M., Maiorano N., Minuti B., Torricelli F.,
Ronchi F., Zancan L., Perrotta S., Vajro P., Boschetto L.,
Iolascon A.;
"Spectrum of UGT1A1 mutations in Crigler-Najjar (CN) syndrome
patients: identification of twelve novel alleles and genotype-
phenotype correlation.";
Hum. Mutat. 25:325-325(2005).
[36]
VARIANT CN1 PHE-171 DEL, AND VARIANTS CN2 TYR-279; ARG-354; VAL-370;
VAL-395; PRO-443 AND ARG-461.
PubMed=17229650; DOI=10.3324/haematol.10585;
D'Apolito M., Marrone A., Servedio V., Vajro P., De Falco L.,
Iolascon A.;
"Seven novel mutations of the UGT1A1 gene in patients with
unconjugated hyperbilirubinemia.";
Haematologica 92:133-134(2007).
[37]
VARIANT CN1 ASN-36, AND VARIANT CN2 CYS-230.
PubMed=23992562; DOI=10.1111/ahg.12039;
Khan S., Irfan M., Sher G., Zubaida B., Alvi M.A., Yasinzai M.,
Naeem M.;
"UGT1A1 gene mutations in Pakistani children suffering from inherited
nonhemolytic unconjugated hyperbilirubinemias.";
Ann. Hum. Genet. 77:482-487(2013).
[38]
VARIANTS CN2 PHE-170 DEL AND CYS-367.
PubMed=23099197; DOI=10.1016/j.clinbiochem.2012.10.007;
Minucci A., Canu G., Gentile L., Cimino V., Giardina B., Zuppi C.,
Capoluongo E.;
"Identification of a novel mutation in UDP-glucuronosyltransferase
(UGT1A1) gene in a child with neonatal unconjugated
hyperbilirubinemia.";
Clin. Biochem. 46:170-172(2013).
-!- FUNCTION: 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. {ECO:0000269|PubMed:18004206,
ECO:0000269|PubMed:19545173, ECO:0000269|PubMed:19830808}.
-!- CATALYTIC ACTIVITY: UDP-glucuronate + acceptor = UDP + acceptor
beta-D-glucuronoside. {ECO:0000269|PubMed:18004206,
ECO:0000269|PubMed:18004212}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.26 uM for bilirubin {ECO:0000269|PubMed:18004206};
Vmax=1080 pmol/min/mg enzyme with bilirubin as substrate
{ECO:0000269|PubMed:18004206};
-!- SUBUNIT: 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. {ECO:0000269|PubMed:17187418,
ECO:0000269|PubMed:20610558}.
-!- SUBCELLULAR LOCATION: Isoform 1: Microsome
{ECO:0000269|PubMed:17187418}. Endoplasmic reticulum membrane
{ECO:0000305|PubMed:17187418}; Single-pass membrane protein
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 2: Microsome
{ECO:0000269|PubMed:17187418}. Endoplasmic reticulum
{ECO:0000305|PubMed:17187418}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=i1;
IsoId=P22309-1; Sequence=Displayed;
Name=2; Synonyms=i2, UGT1A1s;
IsoId=P22309-2; Sequence=VSP_053958;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:1339448,
ECO:0000269|PubMed:17187418, ECO:0000269|PubMed:18004212}.
-!- POLYMORPHISM: Genetic variation in UGT1A1 defines the bilirubin
serum levels quantitative trait locus 1 (BILIQTL1) [MIM:601816].
Variation in serum bilirubin is associated with altered
cardiovascular disease risk and drug metabolism.
{ECO:0000269|PubMed:19414484}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:11013440, ECO:0000269|PubMed:12139570,
ECO:0000269|PubMed:7715297, ECO:0000269|PubMed:9627603}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:11061796}. 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.
-!- DISEASE: 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. {ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:15712364, ECO:0000269|PubMed:1634050,
ECO:0000269|PubMed:17229650, ECO:0000269|PubMed:19830808,
ECO:0000269|PubMed:23992562, ECO:0000269|PubMed:7906695,
ECO:0000269|PubMed:7989045, ECO:0000269|PubMed:7989595,
ECO:0000269|PubMed:8226884}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: 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.
{ECO:0000269|PubMed:11013440, ECO:0000269|PubMed:11370628,
ECO:0000269|PubMed:12402338, ECO:0000269|PubMed:14550264,
ECO:0000269|PubMed:15712364, ECO:0000269|PubMed:17229650,
ECO:0000269|PubMed:18004206, ECO:0000269|PubMed:19830808,
ECO:0000269|PubMed:23099197, ECO:0000269|PubMed:23992562,
ECO:0000269|PubMed:7989595, ECO:0000269|PubMed:8276413,
ECO:0000269|PubMed:8280139, ECO:0000269|PubMed:8706880,
ECO:0000269|PubMed:9621515, ECO:0000269|PubMed:9639672}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- 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.
-!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA61247.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAF03522.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Glucuronosyltransferase entry;
URL="https://en.wikipedia.org/wiki/Glucuronosyltransferase";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M57899; AAA63195.1; -; mRNA.
EMBL; M84124; AAA61247.1; ALT_SEQ; Genomic_DNA.
EMBL; M84122; AAA61247.1; JOINED; Genomic_DNA.
EMBL; M84123; AAA61247.1; JOINED; Genomic_DNA.
EMBL; M84125; AAA61248.1; -; Genomic_DNA.
EMBL; DQ364247; ABC96771.1; -; mRNA.
EMBL; AF297093; AAG30424.1; -; Genomic_DNA.
EMBL; AC006985; AAF03522.2; ALT_SEQ; Genomic_DNA.
EMBL; D87674; BAA25600.1; -; Genomic_DNA.
CCDS; CCDS2510.1; -. [P22309-1]
PIR; A39092; A39092.
RefSeq; NP_000454.1; NM_000463.2. [P22309-1]
UniGene; Hs.554822; -.
ProteinModelPortal; P22309; -.
BioGrid; 120087; 4.
ELM; P22309; -.
IntAct; P22309; 9.
STRING; 9606.ENSP00000304845; -.
BindingDB; P22309; -.
ChEMBL; CHEMBL1287617; -.
DrugBank; DB01048; Abacavir.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB00173; Adenine.
DrugBank; DB01076; Atorvastatin.
DrugBank; DB06626; Axitinib.
DrugBank; DB00586; Diclofenac.
DrugBank; DB08930; Dolutegravir.
DrugBank; DB06210; Eltrombopag.
DrugBank; DB00530; Erlotinib.
DrugBank; DB00783; Estradiol.
DrugBank; DB00773; Etoposide.
DrugBank; DB00973; Ezetimibe.
DrugBank; DB04953; Ezogabine.
DrugBank; DB01544; Flunitrazepam.
DrugBank; DB00712; Flurbiprofen.
DrugBank; DB01095; Fluvastatin.
DrugBank; DB06741; Gavestinel.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB05039; Indacaterol.
DrugBank; DB00328; Indomethacin.
DrugBank; DB00762; Irinotecan.
DrugBank; DB00678; Losartan.
DrugBank; DB00227; Lovastatin.
DrugBank; DB00295; Morphine.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB01024; Mycophenolic acid.
DrugBank; DB00704; Naltrexone.
DrugBank; DB00788; Naproxen.
DrugBank; DB04868; Nilotinib.
DrugBank; DB06589; Pazopanib.
DrugBank; DB00818; Propofol.
DrugBank; DB06817; Raltegravir.
DrugBank; DB08896; Regorafenib.
DrugBank; DB01045; Rifampicin.
DrugBank; DB00641; Simvastatin.
DrugBank; DB00398; Sorafenib.
DrugBank; DB00870; Suprofen.
DrugBank; DB01420; Testosterone Propionate.
DrugBank; DB00197; Troglitazone.
SwissLipids; SLP:000001697; -.
CAZy; GT1; Glycosyltransferase Family 1.
iPTMnet; P22309; -.
PhosphoSitePlus; P22309; -.
BioMuta; UGT1A1; -.
DMDM; 136729; -.
PaxDb; P22309; -.
PeptideAtlas; P22309; -.
PRIDE; P22309; -.
DNASU; 54658; -.
Ensembl; ENST00000305208; ENSP00000304845; ENSG00000241635. [P22309-1]
Ensembl; ENST00000360418; ENSP00000353593; ENSG00000241635. [P22309-2]
GeneID; 54658; -.
KEGG; hsa:54658; -.
CTD; 54658; -.
DisGeNET; 54658; -.
GeneCards; UGT1A1; -.
HGNC; HGNC:12530; UGT1A1.
MalaCards; UGT1A1; -.
MIM; 143500; phenotype.
MIM; 191740; gene.
MIM; 218800; phenotype.
MIM; 237900; phenotype.
MIM; 601816; phenotype.
MIM; 606785; phenotype.
neXtProt; NX_P22309; -.
OpenTargets; ENSG00000241635; -.
Orphanet; 79234; Crigler-Najjar syndrome type 1.
Orphanet; 79235; Crigler-Najjar syndrome type 2.
Orphanet; 357; Gilbert syndrome.
Orphanet; 240885; Irinotecan toxicity.
Orphanet; 240905; Raltegravir toxicity.
Orphanet; 2312; Transient familial neonatal hyperbilirubinemia.
PharmGKB; PA37181; -.
PharmGKB; PA420; -.
eggNOG; KOG1192; Eukaryota.
eggNOG; COG1819; LUCA.
GeneTree; ENSGT00760000118949; -.
HOGENOM; HOG000220832; -.
HOVERGEN; HBG004033; -.
InParanoid; P22309; -.
KO; K00699; -.
OMA; ESHFRRM; -.
OrthoDB; EOG091G06JC; -.
PhylomeDB; P22309; -.
TreeFam; TF315472; -.
BRENDA; 2.4.1.17; 2681.
BRENDA; 2.4.1.95; 2681.
Reactome; R-HSA-156588; Glucuronidation.
Reactome; R-HSA-189483; Heme degradation.
SABIO-RK; P22309; -.
GenomeRNAi; 54658; -.
PRO; PR:P22309; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000241635; -.
CleanEx; HS_UGT1A1; -.
ExpressionAtlas; P22309; baseline and differential.
Genevisible; P22309; HS.
GO; GO:0070069; C:cytochrome complex; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0004857; F:enzyme inhibitor activity; IDA:BHF-UCL.
GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0001972; F:retinoic acid binding; IDA:BHF-UCL.
GO; GO:0005496; F:steroid binding; IDA:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0006789; P:bilirubin conjugation; TAS:Reactome.
GO; GO:0070980; P:biphenyl catabolic process; IEA:Ensembl.
GO; GO:0052695; P:cellular glucuronidation; IDA:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
GO; GO:0007586; P:digestion; NAS:ProtInc.
GO; GO:0017144; P:drug metabolic process; IC:BHF-UCL.
GO; GO:0008210; P:estrogen metabolic process; TAS:ProtInc.
GO; GO:0051552; P:flavone metabolic process; IDA:BHF-UCL.
GO; GO:0052696; P:flavonoid glucuronidation; IDA:BHF-UCL.
GO; GO:0042167; P:heme catabolic process; TAS:Reactome.
GO; GO:0046483; P:heterocycle metabolic process; IC:BHF-UCL.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:2001030; P:negative regulation of cellular glucuronidation; IDA:UniProtKB.
GO; GO:0045922; P:negative regulation of fatty acid metabolic process; ISS:BHF-UCL.
GO; GO:1904224; P:negative regulation of glucuronosyltransferase activity; ISS:BHF-UCL.
GO; GO:0045939; P:negative regulation of steroid metabolic process; IC:BHF-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0042594; P:response to starvation; IEA:Ensembl.
GO; GO:0042573; P:retinoic acid metabolic process; IC:BHF-UCL.
GO; GO:0008202; P:steroid metabolic process; IC:BHF-UCL.
GO; GO:0052697; P:xenobiotic glucuronidation; IDA:BHF-UCL.
InterPro; IPR002213; UDP_glucos_trans.
InterPro; IPR035595; UDP_glycos_trans_CS.
PANTHER; PTHR11926; PTHR11926; 1.
Pfam; PF00201; UDPGT; 1.
PROSITE; PS00375; UDPGT; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
Microsome; Reference proteome; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 533 UDP-glucuronosyltransferase 1-1.
/FTId=PRO_0000036000.
TRANSMEM 491 507 Helical. {ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 435 533 SYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLR
PAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRK
CLGKKGRVKKAHKSKTH -> RKKQQSGRQM (in
isoform 2). {ECO:0000303|Ref.4}.
/FTId=VSP_053958.
VARIANT 15 15 L -> R (in CN2; mutant protein rapidly
degraded by the proteasome owing to its
mislocalization in the cell;
dbSNP:rs111033541).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:14550264,
ECO:0000269|PubMed:19830808,
ECO:0000269|PubMed:8706880}.
/FTId=VAR_019410.
VARIANT 34 34 P -> Q (in CN2).
{ECO:0000269|PubMed:15712364}.
/FTId=VAR_026134.
VARIANT 36 36 D -> N (in CN1).
{ECO:0000269|PubMed:23992562}.
/FTId=VAR_071402.
VARIANT 39 39 H -> D (in CN1; dbSNP:rs72551339).
{ECO:0000269|PubMed:11013440}.
/FTId=VAR_026135.
VARIANT 71 71 G -> 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;
dbSNP:rs4148323).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:11061796,
ECO:0000269|PubMed:18004206,
ECO:0000269|PubMed:19830808,
ECO:0000269|PubMed:7715297,
ECO:0000269|PubMed:8280139,
ECO:0000269|PubMed:9621515}.
/FTId=VAR_009504.
VARIANT 83 83 F -> L (in GILBS; displays less than 10%
of wild-type bilirubin glucuronidation
activity; dbSNP:rs56059937).
{ECO:0000269|PubMed:12139570,
ECO:0000269|PubMed:18004206}.
/FTId=VAR_026136.
VARIANT 170 170 Missing (in CN1 and CN2; has nearly
normal activity at pH 7.6 and is inactive
at pH 6.4). {ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:15712364,
ECO:0000269|PubMed:23099197,
ECO:0000269|PubMed:7989595,
ECO:0000269|PubMed:8226884}.
/FTId=VAR_007695.
VARIANT 171 171 Missing (in CN2).
{ECO:0000269|PubMed:17229650}.
/FTId=VAR_064955.
VARIANT 175 175 L -> Q (in CN2; has low residual
bilirubin glucuronidation activity of
about 4.6% of that of the wild-type
protein; dbSNP:rs72551341).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:11370628,
ECO:0000269|PubMed:19830808,
ECO:0000269|PubMed:7989595}.
/FTId=VAR_019411.
VARIANT 177 177 C -> R (in CN1; dbSNP:rs72551342).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:7989595}.
/FTId=VAR_007697.
VARIANT 191 191 S -> F (in CN2; has low residual
bilirubin glucuronidation activity of
about 5.3% of that of the wild-type
protein). {ECO:0000269|PubMed:19830808}.
/FTId=VAR_064956.
VARIANT 209 209 R -> W (in CN2; has low residual
bilirubin glucuronidation activity of
about 2.9% of that of the wild-type
protein; dbSNP:rs72551343).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:15712364,
ECO:0000269|PubMed:19830808,
ECO:0000269|PubMed:7989595,
ECO:0000269|PubMed:9621515}.
/FTId=VAR_007698.
VARIANT 225 225 V -> G (in CN2; dbSNP:rs35003977).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:15712364}.
/FTId=VAR_026137.
VARIANT 229 229 P -> Q (in CN2 and GILBS; displays 2-fold
decrease in biluribin affinity and 61% of
wild-type bilirubin glucuronidation
activity; dbSNP:rs35350960).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:18004206,
ECO:0000269|PubMed:7715297,
ECO:0000269|PubMed:9621515}.
/FTId=VAR_009505.
VARIANT 230 230 Y -> C (in CN2; dbSNP:rs754922685).
{ECO:0000269|PubMed:23992562}.
/FTId=VAR_071403.
VARIANT 276 276 G -> R (in CN1; dbSNP:rs72551345).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:7989595}.
/FTId=VAR_007699.
VARIANT 279 279 N -> Y (in CN2; dbSNP:rs397978903).
{ECO:0000269|PubMed:17229650}.
/FTId=VAR_064957.
VARIANT 291 291 E -> V (in CN1).
{ECO:0000269|PubMed:11013440}.
/FTId=VAR_026138.
VARIANT 292 292 A -> V (in CN1).
{ECO:0000269|PubMed:7989045}.
/FTId=VAR_007700.
VARIANT 294 294 I -> T (in GILBS and CN2; 40-55% normal
activity; normal Km for bilirubin; when
homozygous far less repressive and
generates the mild Gilbert phenotype;
dbSNP:rs72551347).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:9639672}.
/FTId=VAR_026139.
VARIANT 308 308 G -> E (in CN1; no enzyme activity;
dbSNP:rs62625011).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:7906695,
ECO:0000269|PubMed:7989045}.
/FTId=VAR_007701.
VARIANT 331 331 Q -> R (in CN2; has no residual bilirubin
glucuronidation activity;
dbSNP:rs72551348).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:19830808,
ECO:0000269|PubMed:8276413}.
/FTId=VAR_007702.
VARIANT 336 336 R -> L (in CN1 and CN2).
{ECO:0000269|PubMed:15712364}.
/FTId=VAR_026140.
VARIANT 336 336 R -> Q (in CN1; dbSNP:rs750453538).
{ECO:0000269|PubMed:15712364}.
/FTId=VAR_026141.
VARIANT 336 336 R -> W (in CN2; has very low residual
bilirubin glucuronidation activity of
about 0.4% of that of the wild-type
protein; dbSNP:rs139607673).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:15712364,
ECO:0000269|PubMed:19830808}.
/FTId=VAR_026142.
VARIANT 354 354 W -> R (in CN2).
{ECO:0000269|PubMed:15712364,
ECO:0000269|PubMed:17229650}.
/FTId=VAR_026143.
VARIANT 357 357 Q -> R (in CN1; dbSNP:rs72551351).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:15712364,
ECO:0000269|PubMed:7989045}.
/FTId=VAR_007703.
VARIANT 367 367 R -> C (in CN2; dbSNP:rs55750087).
{ECO:0000269|PubMed:23099197}.
/FTId=VAR_071404.
VARIANT 367 367 R -> G (in GILBS; dbSNP:rs55750087).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:7715297}.
/FTId=VAR_012283.
VARIANT 368 368 A -> T (in CN1; dbSNP:rs72551352).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:7989045}.
/FTId=VAR_007704.
VARIANT 370 370 I -> V (in CN2; dbSNP:rs748989741).
{ECO:0000269|PubMed:17229650}.
/FTId=VAR_064958.
VARIANT 375 375 S -> F (in CN1; no enzyme activity;
dbSNP:rs72551353).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:15712364,
ECO:0000269|PubMed:1634050,
ECO:0000269|PubMed:7906695,
ECO:0000269|PubMed:7989595}.
/FTId=VAR_007705.
VARIANT 376 376 H -> R (in CN1 and CN2).
/FTId=VAR_026144.
VARIANT 377 377 G -> V (in CN1 and CN2).
{ECO:0000269|PubMed:15712364}.
/FTId=VAR_026145.
VARIANT 381 381 S -> R (in CN1; dbSNP:rs72551354).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:7989045}.
/FTId=VAR_007706.
VARIANT 387 387 P -> H (in CN2; has no residual bilirubin
glucuronidation activity).
{ECO:0000269|PubMed:19830808}.
/FTId=VAR_064959.
VARIANT 387 387 P -> S (in CN1).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:15712364}.
/FTId=VAR_026146.
VARIANT 395 395 G -> V (in CN1; has no residual bilirubin
glucuronidation activity;
dbSNP:rs367897068).
{ECO:0000269|PubMed:15712364,
ECO:0000269|PubMed:17229650,
ECO:0000269|PubMed:19830808}.
/FTId=VAR_026147.
VARIANT 400 400 N -> D (in CN2; dbSNP:rs28934877).
{ECO:0000269|PubMed:12402338}.
/FTId=VAR_019412.
VARIANT 401 401 A -> P (in CN1; dbSNP:rs72551355).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:7989045}.
/FTId=VAR_007707.
VARIANT 402 402 K -> T (in CN1; has no residual bilirubin
glucuronidation activity; N-glycosylation
does take place at this new additional
site). {ECO:0000269|PubMed:19830808}.
/FTId=VAR_064960.
VARIANT 403 403 R -> C (in CN2; dbSNP:rs778766461).
{ECO:0000269|PubMed:15712364}.
/FTId=VAR_026148.
VARIANT 428 428 K -> E (in CN1; dbSNP:rs72551356).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:7989045}.
/FTId=VAR_007708.
VARIANT 443 443 L -> P (in CN2; has no residual bilirubin
glucuronidation activity;
dbSNP:rs758411577).
{ECO:0000269|PubMed:17229650,
ECO:0000269|PubMed:19830808}.
/FTId=VAR_064961.
VARIANT 461 461 W -> R (in CN1 and CN2).
{ECO:0000269|PubMed:15712364,
ECO:0000269|PubMed:17229650}.
/FTId=VAR_026149.
VARIANT 478 478 A -> D (in CN2).
{ECO:0000269|PubMed:15712364}.
/FTId=VAR_026150.
VARIANT 486 486 Y -> D (in CN2, GILBS and HBLRTFN;
displays less than 10% of wild-type
bilirubin glucuronidation activity;
dbSNP:rs34993780).
{ECO:0000269|PubMed:11013440,
ECO:0000269|PubMed:11061796,
ECO:0000269|PubMed:18004206,
ECO:0000269|PubMed:19830808,
ECO:0000269|PubMed:8280139,
ECO:0000269|PubMed:9621515,
ECO:0000269|PubMed:9627603}.
/FTId=VAR_007709.
VARIANT 511 511 A -> P (in dbSNP:rs1042709).
/FTId=VAR_025355.
SEQUENCE 533 AA; 59591 MW; 19C90231AD0EB547 CRC64;
MAVESQGGRP LVLGLLLCVL GPVVSHAGKI LLIPVDGSHW LSMLGAIQQL QQRGHEIVVL
APDASLYIRD GAFYTLKTYP VPFQREDVKE SFVSLGHNVF ENDSFLQRVI KTYKKIKKDS
AMLLSGCSHL LHNKELMASL AESSFDVMLT DPFLPCSPIV AQYLSLPTVF FLHALPCSLE
FEATQCPNPF SYVPRPLSSH SDHMTFLQRV KNMLIAFSQN FLCDVVYSPY ATLASEFLQR
EVTVQDLLSS ASVWLFRSDF VKDYPRPIMP NMVFVGGINC LHQNPLSQEF EAYINASGEH
GIVVFSLGSM VSEIPEKKAM AIADALGKIP QTVLWRYTGT RPSNLANNTI LVKWLPQNDL
LGHPMTRAFI THAGSHGVYE SICNGVPMVM MPLFGDQMDN AKRMETKGAG VTLNVLEMTS
EDLENALKAV INDKSYKENI MRLSSLHKDR PVEPLDLAVF WVEFVMRHKG APHLRPAAHD
LTWYQYHSLD VIGFLLAVVL TVAFITFKCC AYGYRKCLGK KGRVKKAHKS KTH


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EIAAB45196 Bilirubin-specific UDPGT isozyme 1,GNT1,Homo sapiens,hUG-BR1,Human,UDP-glucuronosyltransferase 1-1,UDP-glucuronosyltransferase 1-A,UDP-glucuronosyltransferase 1A1,UDPGT 1-1,UGT1,UGT1*1,UGT1.1,UGT1-01,
EIAAB45204 Bilirubin-specific UDPGT isozyme 2,GNT1,Homo sapiens,hUG-BR2,Human,UDP-glucuronosyltransferase 1-4,UDP-glucuronosyltransferase 1A4,UDP-glucuronosyltransferase 1-D,UDPGT 1-4,UGT1,UGT1*4,UGT1.4,UGT1-04,
EIAAB45201 B2,Bilirubin-specific UDPGT,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-2,UDPGT 1-2,Ugt1,UGT1*2,UGT1.2,UGT1-02,UGT1A2
EIAAB45200 Bilirubin-specific UDPGT,Mouse,Mus musculus,UDP-glucuronosyltransferase 1-2,UDPGT 1-2,Ugt1,UGT1*2,UGT1.2,UGT1-02,UGT1A2
EIAAB45199 GNT1,Homo sapiens,Human,UDP-glucuronosyltransferase 1-10,UDP-glucuronosyltransferase 1A10,UDP-glucuronosyltransferase 1-J,UDPGT 1-10,UGT1,UGT1*10,UGT1.10,UGT1-10,UGT1A10,UGT1J,UGT-1J
EIAAB45218 GNT1,Homo sapiens,Human,lugP4,UDP-glucuronosyltransferase 1-9,UDP-glucuronosyltransferase 1A9,UDP-glucuronosyltransferase 1-I,UDPGT 1-9,UGT1,UGT1*9,UGT1.9,UGT1-09,UGT1A9,UGT1I,UGT-1I
EIAAB45215 GNT1,Homo sapiens,Human,UDP-glucuronosyltransferase 1-8,UDP-glucuronosyltransferase 1A8,UDP-glucuronosyltransferase 1-H,UDPGT 1-8,UGT1,UGT1*8,UGT1.8,UGT1-08,UGT1A8,UGT1H,UGT-1H
EIAAB45207 GNT1,Homo sapiens,Human,UDP-glucuronosyltransferase 1-5,UDP-glucuronosyltransferase 1A5,UDP-glucuronosyltransferase 1-E,UDPGT 1-5,UGT1,UGT1*5,UGT1.5,UGT1-05,UGT1A5,UGT1E,UGT-1E
EIAAB45203 GNT1,Homo sapiens,Human,UDP-glucuronosyltransferase 1-3,UDP-glucuronosyltransferase 1A3,UDP-glucuronosyltransferase 1-C,UDPGT 1-3,UGT1,UGT1*3,UGT1.3,UGT1-03,UGT1A3,UGT1C,UGT-1C
EIAAB45212 GNT1,Homo sapiens,Human,UDP-glucuronosyltransferase 1-7,UDP-glucuronosyltransferase 1A7,UDP-glucuronosyltransferase 1-G,UDPGT 1-7,UGT1,UGT1*7,UGT1.7,UGT1-07,UGT1A7,UGT1G,UGT-1G
EIAAB45210 GNT1,Homo sapiens,Human,Phenol-metabolizing UDP-glucuronosyltransferase,UDP-glucuronosyltransferase 1-6,UDP-glucuronosyltransferase 1A6,UDP-glucuronosyltransferase 1-F,UDPGT 1-6,UGT1,UGT1*6,UGT1.6,UGT
EIAAB45211 A1,P-nitrophenol-specific UDPGT,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-6,UDPGT 1-6,Ugt1,UGT1*6,UGT1.6,UGT1-06,UGT1A6
EIAAB45197 Mouse,Mus musculus,UDP-glucuronosyltransferase 1-1,UDP-glucuronosyltransferase 1A1,UDPGT 1-1,Ugt1,UGT1*1,UGT1.1,UGT1-01,Ugt1a1,UGTBR1
EIAAB45217 Mouse,Mus musculus,UDP-glucuronosyltransferase 1-7,UDP-glucuronosyltransferase 1-9,UDPGT,UDPGT 1-9,Ugt1,UGT1*9,UGT1.9,UGT1-09,UGT1A12,Ugt1a12,Ugt1a9,UGTP4
EIAAB45198 B1,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-1,UDP-glucuronosyltransferase 1A1,UDPGT 1-1,Ugt1,UGT1*1,UGT1.1,UGT1-01,Ugt1a1
EIAAB45208 Mouse,Mus musculus,Phenol UDP-glucuronosyltransferase,UDP-glucuronosyltransferase 1-6,UDPGT 1-6,UGP1A1,Ugt1,UGT1*6,UGT1.6,UGT1-06,UGT1A6,Ugt1a6,Ugt1a6a
EIAAB45205 Oryctolagus cuniculus,Rabbit,UDP-glucuronosyltransferase 1-4,UDPGT 1-4,UGT1,UGT1*4,UGT1.4,UGT1-04,UGT1A4
EIAAB45209 Oryctolagus cuniculus,Rabbit,UDP-glucuronosyltransferase 1-6,UDPGT 1-6,UGT1,UGT1*6,UGT1.6,UGT1-06,UGT1A6
EIAAB45206 B5,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-5,UDPGT 1-5,Ugt1,UGT1*5,UGT1.5,UGT1-05,UGT1A5
EIAAB45213 A2,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-7,UDPGT 1-7,Ugt1,UGT1*7,UGT1.7,UGT1-07,UGT1A7
EIAAB45202 B3,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-3,UDPGT 1-3,Ugt1,UGT1*3,UGT1.3,UGT1-03,UGT1A3
EIAAB45216 A3,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-8,UDPGT 1-8,Ugt1,UGT1*8,UGT1.8,UGT1-08,UGT1A8
EIAAB45214 Mouse,Mus musculus,UDP-glucuronosyltransferase 1-7C,UDPGT 1-7C,UGT1*7C,UGT1.7C,UGT1-07C,UGT1A10,Ugt1a10,Ugt1a7c
EIAAB45229 3,4-catechol estrogen-specific UDPGT,Homo sapiens,Human,UDP-glucuronosyltransferase 2B7,UDP-glucuronosyltransferase 2B9,UDPGT 2B7,UDPGT 2B9,UDPGTh-2,UGT2B7,UGTB2B9
EIAAB45243 17-beta-hydroxysteroid-specific UDPGT,Rat,Rattus norvegicus,RLUG38,Testosterone, dihydrotestosterone, and beta-estradiol-specific UDPGT,UDP-glucuronosyltransferase 2B17,UDP-glucuronosyltransferase 2B5


 

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