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UDP-glucuronosyltransferase 1-9 (UDPGT 1-9) (UGT1*9) (UGT1-09) (UGT1.9) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1-I) (UGT-1I) (UGT1I) (UDP-glucuronosyltransferase 1A9) (lugP4)

 UD19_HUMAN              Reviewed;         530 AA.
O60656; B8K285; P36509; Q9HAX0;
11-APR-2003, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
20-DEC-2017, entry version 155.
RecName: Full=UDP-glucuronosyltransferase 1-9;
Short=UDPGT 1-9;
Short=UGT1*9;
Short=UGT1-09;
Short=UGT1.9;
EC=2.4.1.17;
AltName: Full=UDP-glucuronosyltransferase 1-I;
Short=UGT-1I;
Short=UGT1I;
AltName: Full=UDP-glucuronosyltransferase 1A9;
AltName: Full=lugP4;
Flags: Precursor;
Name=UGT1A9; 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].
TISSUE=Liver;
PubMed=1910331; DOI=10.1042/bj2780465;
Wooster R., Sutherland L., Ebner T., Clarke D., da Cruz e Silva O.,
Burchell B.;
"Cloning and stable expression of a new member of the human liver
phenol/bilirubin: UDP-glucuronosyltransferase cDNA family.";
Biochem. J. 278:465-469(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Ciotti M., Potter C., Owens I.S.;
"Human phenol metabolizing UDP-glucuronosyltransferase.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[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 [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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-285.
Owens I.S., Gong Q., Cho J.W., Potter C., Gholami N.;
"Human phenol UDP-glucuronosyltransferase (UGT1A9) gene isozyme exon
1.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[7]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
Guillemette C., Levesque E., Girard H., Bernard O.;
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[8]
CATALYTIC ACTIVITY, FUNCTION (ISOFORM 2), ALTERNATIVE SPLICING, 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).
[9]
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).
[10]
CATALYTIC ACTIVITY, FUNCTION (ISOFORM 2), AND 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).
[11]
GLYCOSYLATION AT ASN-71; ASN-292 AND ASN-344.
PubMed=19951703; DOI=10.1016/j.bcp.2009.11.020;
Nakajima M., Koga T., Sakai H., Yamanaka H., Fujiwara R., Yokoi T.;
"N-Glycosylation plays a role in protein folding of human UGT1A9.";
Biochem. Pharmacol. 79:1165-1172(2010).
[12]
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).
[13]
VARIANT [LARGE SCALE ANALYSIS] ILE-442.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[14]
VARIANT THR-33.
PubMed=19204906; DOI=10.1002/humu.20946;
Menard V., Girard H., Harvey M., Perusse L., Guillemette C.;
"Analysis of inherited genetic variations at the UGT1 locus in the
French-Canadian population.";
Hum. Mutat. 30:677-687(2009).
-!- FUNCTION: UDPGT is of major importance in the conjugation and
subsequent elimination of potentially toxic xenobiotics and
endogenous compounds. This isoform has specificity for phenols.
Isoform 2 lacks transferase activity but acts as a negative
regulator of isoform 1. {ECO:0000269|PubMed:19545173}.
-!- CATALYTIC ACTIVITY: UDP-glucuronate + acceptor = UDP + acceptor
beta-D-glucuronoside. {ECO:0000269|PubMed:18004212,
ECO:0000269|PubMed:20610558}.
-!- 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 UGT1A1, UGT1A3, UGT1A4, UGT1A6, UGT1A7, UGT1A8 and
UGT1A10. {ECO:0000269|PubMed:20610558}.
-!- SUBCELLULAR LOCATION: Microsome. Endoplasmic reticulum membrane
{ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=i1;
IsoId=O60656-1; Sequence=Displayed;
Name=2; Synonyms=i2, UGT1A9s;
IsoId=O60656-2; Sequence=VSP_053965;
-!- TISSUE SPECIFICITY: Liver. Isoform 1 and isoform 2 are expressed
in liver, kidney, colon, esophagus and small intestine.
{ECO:0000269|PubMed:18004212}.
-!- 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=AAB19791.2; Type=Frameshift; Positions=59, 82; Evidence={ECO:0000305};
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EMBL; S55985; AAB19791.2; ALT_FRAME; mRNA.
EMBL; AF056188; AAC31425.1; -; mRNA.
EMBL; AF297093; AAG30418.1; -; Genomic_DNA.
EMBL; AC006985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC019072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC058844; AAH58844.1; -; mRNA.
EMBL; AF297091; AAG29816.1; -; Genomic_DNA.
EMBL; DQ364246; ABC96770.1; -; mRNA.
CCDS; CCDS2505.1; -. [O60656-1]
PIR; S17512; S17512.
RefSeq; NP_066307.1; NM_021027.2. [O60656-1]
UniGene; Hs.554822; -.
ProteinModelPortal; O60656; -.
BioGrid; 120073; 6.
IntAct; O60656; 7.
STRING; 9606.ENSP00000346768; -.
BindingDB; O60656; -.
ChEMBL; CHEMBL1743319; -.
DrugBank; DB00316; Acetaminophen.
DrugBank; DB06403; Ambrisentan.
DrugBank; DB00921; Buprenorphine.
DrugBank; DB08907; Canagliflozin.
DrugBank; DB06695; Dabigatran etexilate.
DrugBank; DB06292; Dapagliflozin.
DrugBank; DB00494; Entacapone.
DrugBank; DB00749; Etodolac.
DrugBank; DB04953; Ezogabine.
DrugBank; DB00712; Flurbiprofen.
DrugBank; DB06741; Gavestinel.
DrugBank; DB00502; Haloperidol.
DrugBank; DB00062; Human Serum Albumin.
DrugBank; DB00327; Hydromorphone.
DrugBank; DB01050; Ibuprofen.
DrugBank; DB00328; Indomethacin.
DrugBank; DB00762; Irinotecan.
DrugBank; DB06738; Ketobemidone.
DrugBank; DB01283; Lumiracoxib.
DrugBank; DB00688; Mycophenolate mofetil.
DrugBank; DB01024; Mycophenolic acid.
DrugBank; DB00731; Nateglinide.
DrugBank; DB04552; Niflumic Acid.
DrugBank; DB00842; Oxazepam.
DrugBank; DB04824; Phenolphthalein.
DrugBank; DB00818; Propofol.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB01015; Sulfamethoxazole.
DrugBank; DB06204; Tapentadol.
DrugBank; DB00197; Troglitazone.
DrugBank; DB00580; Valdecoxib.
DrugBank; DB00313; Valproic Acid.
DrugBank; DB00744; Zileuton.
SwissLipids; SLP:000001713; -. [O60656-1]
CAZy; GT1; Glycosyltransferase Family 1.
iPTMnet; O60656; -.
PhosphoSitePlus; O60656; -.
BioMuta; UGT1A9; -.
PaxDb; O60656; -.
PeptideAtlas; O60656; -.
PRIDE; O60656; -.
DNASU; 54600; -.
Ensembl; ENST00000354728; ENSP00000346768; ENSG00000241119. [O60656-1]
GeneID; 54600; -.
KEGG; hsa:54600; -.
CTD; 54600; -.
DisGeNET; 54600; -.
EuPathDB; HostDB:ENSG00000241119.1; -.
GeneCards; UGT1A9; -.
HGNC; HGNC:12541; UGT1A9.
MIM; 191740; gene.
MIM; 606434; gene.
neXtProt; NX_O60656; -.
OpenTargets; ENSG00000241119; -.
PharmGKB; PA419; -.
eggNOG; KOG1192; Eukaryota.
eggNOG; COG1819; LUCA.
GeneTree; ENSGT00760000118949; -.
HOGENOM; HOG000220832; -.
HOVERGEN; HBG004033; -.
InParanoid; O60656; -.
KO; K00699; -.
OMA; MPEVSWH; -.
OrthoDB; EOG091G06JC; -.
PhylomeDB; O60656; -.
TreeFam; TF315472; -.
BRENDA; 2.4.1.17; 2681.
Reactome; R-HSA-156588; Glucuronidation.
Reactome; R-HSA-1989781; PPARA activates gene expression.
SABIO-RK; O60656; -.
SIGNOR; O60656; -.
GeneWiki; UGT1A9; -.
GenomeRNAi; 54600; -.
PRO; PR:O60656; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000241119; -.
ExpressionAtlas; O60656; baseline and differential.
Genevisible; O60656; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0004857; F:enzyme inhibitor activity; IGI: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:0052695; P:cellular glucuronidation; IDA:UniProtKB.
GO; GO:0051552; P:flavone metabolic process; IDA:BHF-UCL.
GO; GO:0052696; P:flavonoid glucuronidation; IDA:BHF-UCL.
GO; GO:0008152; P:metabolic process; TAS:ProtInc.
GO; GO:2001030; P:negative regulation of cellular glucuronidation; IDA:UniProtKB.
GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IDA:BHF-UCL.
GO; GO:1904224; P:negative regulation of glucuronosyltransferase activity; IDA:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0042573; P:retinoic acid metabolic process; IC:BHF-UCL.
GO; GO:0052697; P:xenobiotic glucuronidation; IDA:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
InterPro; IPR002213; UDP_glucos_trans.
InterPro; IPR035595; UDP_glycos_trans_CS.
Pfam; PF00201; UDPGT; 1.
PROSITE; PS00375; UDPGT; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Endoplasmic reticulum;
Glycoprotein; Glycosyltransferase; Membrane; Microsome; Polymorphism;
Reference proteome; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 530 UDP-glucuronosyltransferase 1-9.
/FTId=PRO_0000036008.
TRANSMEM 488 504 Helical. {ECO:0000255}.
MOD_RES 99 99 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q62452}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19951703}.
CARBOHYD 292 292 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19951703}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19951703}.
VAR_SEQ 432 530 SYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLR
PAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRK
CLGKKGRVKKAHKSKTH -> RKKQQSGRQM (in
isoform 2). {ECO:0000305}.
/FTId=VSP_053965.
VARIANT 33 33 M -> T (in dbSNP:rs72551330).
{ECO:0000269|PubMed:19204906}.
/FTId=VAR_058587.
VARIANT 442 442 S -> I (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036035.
CONFLICT 29 29 L -> V (in Ref. 1; AAB19791).
{ECO:0000305}.
CONFLICT 200 200 A -> D (in Ref. 1; AAB19791).
{ECO:0000305}.
CONFLICT 279 282 QGKP -> ERKA (in Ref. 1; AAB19791).
{ECO:0000305}.
SEQUENCE 530 AA; 59941 MW; C417B9E86B403078 CRC64;
MACTGWTSPL PLCVCLLLTC GFAEAGKLLV VPMDGSHWFT MRSVVEKLIL RGHEVVVVMP
EVSWQLGRSL NCTVKTYSTS YTLEDLDREF KAFAHAQWKA QVRSIYSLLM GSYNDIFDLF
FSNCRSLFKD KKLVEYLKES SFDAVFLDPF DNCGLIVAKY FSLPSVVFAR GILCHYLEEG
AQCPAPLSYV PRILLGFSDA MTFKERVRNH IMHLEEHLLC HRFFKNALEI ASEILQTPVT
EYDLYSHTSI WLLRTDFVLD YPKPVMPNMI FIGGINCHQG KPLPMEFEAY INASGEHGIV
VFSLGSMVSE IPEKKAMAIA DALGKIPQTV LWRYTGTRPS NLANNTILVK WLPQNDLLGH
PMTRAFITHA GSHGVYESIC NGVPMVMMPL FGDQMDNAKR METKGAGVTL NVLEMTSEDL
ENALKAVIND KSYKENIMRL SSLHKDRPVE PLDLAVFWVE FVMRHKGAPH LRPAAHDLTW
YQYHSLDVIG FLLAVVLTVA FITFKCCAYG YRKCLGKKGR VKKAHKSKTH


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EIAAB45209 Oryctolagus cuniculus,Rabbit,UDP-glucuronosyltransferase 1-6,UDPGT 1-6,UGT1,UGT1*6,UGT1.6,UGT1-06,UGT1A6
EIAAB45205 Oryctolagus cuniculus,Rabbit,UDP-glucuronosyltransferase 1-4,UDPGT 1-4,UGT1,UGT1*4,UGT1.4,UGT1-04,UGT1A4
EIAAB45216 A3,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-8,UDPGT 1-8,Ugt1,UGT1*8,UGT1.8,UGT1-08,UGT1A8
EIAAB45202 B3,Rat,Rattus norvegicus,UDP-glucuronosyltransferase 1-3,UDPGT 1-3,Ugt1,UGT1*3,UGT1.3,UGT1-03,UGT1A3
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
EIAAB45214 Mouse,Mus musculus,UDP-glucuronosyltransferase 1-7C,UDPGT 1-7C,UGT1*7C,UGT1.7C,UGT1-07C,UGT1A10,Ugt1a10,Ugt1a7c
UD12_RAT ELISA Kit FOR UDP-glucuronosyltransferase 1-2; organism: Rat; gene name: Ugt1 96T
UD13_RAT ELISA Kit FOR UDP-glucuronosyltransferase 1-3; organism: Rat; gene name: Ugt1 96T


 

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