UD2B4_HUMAN
ID UD2B4_HUMAN Reviewed; 528 AA.
AC P06133; A6NCP7; B4DT75; G5E9X8; O60731; O60867; O75614; P36538; Q1HBF9;
AC Q6QQX7;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=UDP-glucuronosyltransferase 2B4 {ECO:0000303|PubMed:18719240};
DE Short=UDPGT 2B4;
DE Short=UGT2B4;
DE EC=2.4.1.17 {ECO:0000269|PubMed:18719240};
DE AltName: Full=HLUG25;
DE AltName: Full=Hyodeoxycholic acid-specific UDPGT;
DE AltName: Full=UDPGTh-1;
DE Flags: Precursor;
GN Name=UGT2B4 {ECO:0000312|HGNC:HGNC:12553}; Synonyms=UGT2B11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3109396; DOI=10.1042/bj2420581;
RA Jackson M.R., McCarthy L.R., Harding D., Wilson S., Coughtrie M.W.H.,
RA Burchell B.;
RT "Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA.";
RL Biochem. J. 242:581-588(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8333863; DOI=10.1006/bbrc.1993.1847;
RA Jin C.-J., Miners J.O., Lillywhite K.J., McKenzie P.I.;
RT "cDNA cloning and expression of two new members of the human liver UDP-
RT glucuronosyltransferase 2B subfamily.";
RL Biochem. Biophys. Res. Commun. 194:496-503(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-458, AND
RP CHARACTERIZATION.
RX PubMed=10376768;
RA Levesque E., Beaulieu M., Hum D.W., Belanger A.;
RT "Characterization and substrate specificity of UGT2B4 (E458): a UDP-
RT glucuronosyltransferase encoded by a polymorphic gene.";
RL Pharmacogenetics 9:207-216(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LEU-109 AND LEU-396.
RA McKenzie P.I.;
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Riedy M., Miller A.;
RT "Genomic organization and structure of the UGT2B gene complex at human
RT chromosome 4q13.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Shen C., Ke R., Wang C., Li H., Zhou G., Zhong G., Lin L., Yang S.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-40; THR-78; PRO-80;
RP ILE-277; GLU-458 AND ARG-511.
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver, and Pericardium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18177842; DOI=10.1016/j.bcp.2007.11.008;
RA Hashizume T., Xu Y., Mohutsky M.A., Alberts J., Hadden C., Kalhorn T.F.,
RA Isoherranen N., Shuhart M.C., Thummel K.E.;
RT "Identification of human UDP-glucuronosyltransferases catalyzing hepatic
RT 1alpha,25-dihydroxyvitamin D3 conjugation.";
RL Biochem. Pharmacol. 75:1240-1250(2008).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18719240; DOI=10.1124/dmd.108.022731;
RA Itaeaho K., Mackenzie P.I., Ikushiro S., Miners J.O., Finel M.;
RT "The configuration of the 17-hydroxy group variably influences the
RT glucuronidation of beta-estradiol and epiestradiol by human UDP-
RT glucuronosyltransferases.";
RL Drug Metab. Dispos. 36:2307-2315(2008).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-315.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23288867; DOI=10.1124/dmd.112.049072;
RA Sneitz N., Vahermo M., Mosorin J., Laakkonen L., Poirier D., Finel M.;
RT "Regiospecificity and stereospecificity of human UDP-
RT glucuronosyltransferases in the glucuronidation of estriol, 16-epiestriol,
RT 17-epiestriol, and 13-epiestradiol.";
RL Drug Metab. Dispos. 41:582-591(2013).
CC -!- FUNCTION: UDP-glucuronosyltransferase (UGT) that catalyzes phase II
CC biotransformation reactions in which lipophilic substrates are
CC conjugated with glucuronic acid to increase the metabolite's water
CC solubility, thereby facilitating excretion into either the urine or
CC bile (PubMed:18719240, PubMed:23288867). Essential for the elimination
CC and detoxification of drugs, xenobiotics and endogenous compounds
CC (PubMed:18719240, PubMed:23288867). Catalyzes the glucuronidation of
CC the endogenous estrogen hormones such as estradiol and estriol
CC (PubMed:18719240, PubMed:23288867). {ECO:0000269|PubMed:18719240,
CC ECO:0000269|PubMed:23288867}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor
CC beta-D-glucuronoside + H(+) + UDP; Xref=Rhea:RHEA:21032,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132367, ChEBI:CHEBI:132368; EC=2.4.1.17;
CC Evidence={ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC Evidence={ECO:0000305|PubMed:18719240, ECO:0000305|PubMed:23288867};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha-
CC estradiol 17-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:52872, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136642;
CC Evidence={ECO:0000269|PubMed:18719240};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52873;
CC Evidence={ECO:0000305|PubMed:18719240};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=16alpha,17alpha-estriol + UDP-alpha-D-glucuronate =
CC 16alpha,17alpha-estriol 17-O-(beta-D-glucuronate) + H(+) + UDP;
CC Xref=Rhea:RHEA:52916, ChEBI:CHEBI:15378, ChEBI:CHEBI:42156,
CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136883;
CC Evidence={ECO:0000269|PubMed:23288867};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52917;
CC Evidence={ECO:0000305|PubMed:23288867};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.77 uM for 17alpha-estradiol/epiestradiol (when assaying
CC glucuronidation at position 17) {ECO:0000269|PubMed:18719240};
CC KM=57.8 uM for calcitriol (when assaying glucuronidation at position
CC 25) {ECO:0000269|PubMed:18177842};
CC Vmax=135 pmol/min/mg enzyme for the formation of 17alpha-estradiol
CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240};
CC Vmax=17 pmol/min/mg enzyme for the formation of 17alpha-estradiol 17-
CC O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=3.8 pmol/min/mg enzyme for the formation of 16alpha,17beta-
CC estriol 16-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=9.2 pmol/min/mg enzyme for the formation of 16beta,17beta-
CC estriol 16-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=174 pmol/min/mg enzyme for the formation of 16alpha,17alpha-
CC estriol 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=4.3 pmol/min/mg enzyme for the formation of calcitriol 25-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:18177842};
CC Note=Some kinetic parameters were assessed using commercial enzymes,
CC which may represent a mix of both active and inactive protein forms,
CC and therefore modify the kinetic values.
CC {ECO:0000305|PubMed:18177842, ECO:0000305|PubMed:18719240};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:8333863}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P06133-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P06133-2; Sequence=VSP_056679, VSP_056680;
CC Name=3;
CC IsoId=P06133-3; Sequence=VSP_056869, VSP_056870;
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: UGT2B4 has been previously described as an enzyme named
CC UGT2B11. However the name UGT2B11 has now been reused for another human
CC protein (see AC O75310). {ECO:0000305, ECO:0000305|PubMed:8333863}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ugt2b4/";
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DR EMBL; Y00317; CAA68415.1; -; mRNA.
DR EMBL; AF064200; AAC95002.1; -; mRNA.
DR EMBL; AJ005162; CAA06396.1; -; mRNA.
DR EMBL; AF081793; AAC32272.1; -; mRNA.
DR EMBL; AF135416; AAF78145.1; -; Genomic_DNA.
DR EMBL; AY529122; AAS47487.1; -; mRNA.
DR EMBL; DQ520733; ABF47107.1; -; Genomic_DNA.
DR EMBL; AK292748; BAF85437.1; -; mRNA.
DR EMBL; AK300084; BAG61887.1; -; mRNA.
DR EMBL; AC093829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05591.1; -; Genomic_DNA.
DR EMBL; BC026264; AAH26264.1; -; mRNA.
DR CCDS; CCDS43234.1; -. [P06133-1]
DR CCDS; CCDS75137.1; -. [P06133-3]
DR PIR; JN0619; JN0619.
DR RefSeq; NP_001284544.1; NM_001297615.1. [P06133-3]
DR RefSeq; NP_001284545.1; NM_001297616.1. [P06133-2]
DR RefSeq; NP_066962.2; NM_021139.2. [P06133-1]
DR AlphaFoldDB; P06133; -.
DR SMR; P06133; -.
DR BioGRID; 113210; 1.
DR IntAct; P06133; 2.
DR STRING; 9606.ENSP00000305221; -.
DR ChEMBL; CHEMBL6196; -.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB08907; Canagliflozin.
DR DrugBank; DB01136; Carvedilol.
DR DrugBank; DB06119; Cenobamate.
DR DrugBank; DB00318; Codeine.
DR DrugBank; DB14635; Curcumin sulfate.
DR DrugBank; DB06292; Dapagliflozin.
DR DrugBank; DB09213; Dexibuprofen.
DR DrugBank; DB00514; Dextromethorphan.
DR DrugBank; DB00586; Diclofenac.
DR DrugBank; DB00783; Estradiol.
DR DrugBank; DB00712; Flurbiprofen.
DR DrugBank; DB11796; Fostemsavir.
DR DrugBank; DB06741; Gavestinel.
DR DrugBank; DB01241; Gemfibrozil.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB01050; Ibuprofen.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB00295; Morphine.
DR DrugBank; DB08804; Nandrolone decanoate.
DR DrugBank; DB00960; Pindolol.
DR DrugBank; DB00794; Primidone.
DR DrugBank; DB00503; Ritonavir.
DR DrugBank; DB00871; Terbutaline.
DR SwissLipids; SLP:000001708; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; P06133; 1 site.
DR iPTMnet; P06133; -.
DR PhosphoSitePlus; P06133; -.
DR BioMuta; UGT2B4; -.
DR DMDM; 6175083; -.
DR jPOST; P06133; -.
DR MassIVE; P06133; -.
DR MaxQB; P06133; -.
DR PaxDb; P06133; -.
DR PeptideAtlas; P06133; -.
DR PRIDE; P06133; -.
DR ProteomicsDB; 34076; -.
DR ProteomicsDB; 51871; -. [P06133-1]
DR ProteomicsDB; 850; -.
DR Antibodypedia; 24236; 205 antibodies from 27 providers.
DR DNASU; 7363; -.
DR Ensembl; ENST00000305107.7; ENSP00000305221.6; ENSG00000156096.14. [P06133-1]
DR Ensembl; ENST00000512583.5; ENSP00000421290.1; ENSG00000156096.14. [P06133-3]
DR GeneID; 7363; -.
DR KEGG; hsa:7363; -.
DR MANE-Select; ENST00000305107.7; ENSP00000305221.6; NM_021139.3; NP_066962.2.
DR UCSC; uc003hek.4; human. [P06133-1]
DR CTD; 7363; -.
DR DisGeNET; 7363; -.
DR GeneCards; UGT2B4; -.
DR HGNC; HGNC:12553; UGT2B4.
DR HPA; ENSG00000156096; Tissue enriched (liver).
DR MIM; 600067; gene.
DR neXtProt; NX_P06133; -.
DR OpenTargets; ENSG00000156096; -.
DR PharmGKB; PA360; -.
DR VEuPathDB; HostDB:ENSG00000156096; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000158332; -.
DR HOGENOM; CLU_012949_5_1_1; -.
DR InParanoid; P06133; -.
DR OMA; WKFARTA; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; P06133; -.
DR TreeFam; TF315472; -.
DR BRENDA; 2.4.1.17; 2681.
DR PathwayCommons; P06133; -.
DR Reactome; R-HSA-156588; Glucuronidation.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SignaLink; P06133; -.
DR BioGRID-ORCS; 7363; 8 hits in 1062 CRISPR screens.
DR ChiTaRS; UGT2B4; human.
DR GeneWiki; UGT2B4; -.
DR GenomeRNAi; 7363; -.
DR Pharos; P06133; Tbio.
DR PRO; PR:P06133; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P06133; protein.
DR Bgee; ENSG00000156096; Expressed in liver and 72 other tissues.
DR ExpressionAtlas; P06133; baseline and differential.
DR Genevisible; P06133; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0052695; P:cellular glucuronidation; IDA:UniProtKB.
DR GO; GO:0008210; P:estrogen metabolic process; IDA:UniProtKB.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Lipid metabolism; Membrane; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..528
FT /note="UDP-glucuronosyltransferase 2B4"
FT /id="PRO_0000036028"
FT TRANSMEM 493..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..14
FT /note="MSMKWTSALLLIQL -> MFFALLHVSSTNGL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056679"
FT VAR_SEQ 15..150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056680"
FT VAR_SEQ 364..369
FT /note="GHPKTR -> DIKRML (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_056869"
FT VAR_SEQ 370..528
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_056870"
FT VARIANT 40
FT /note="K -> N (in dbSNP:rs41299974)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_060713"
FT VARIANT 78
FT /note="P -> T (in dbSNP:rs41299976)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_060714"
FT VARIANT 80
FT /note="S -> P (in dbSNP:rs41299978)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_060715"
FT VARIANT 109
FT /note="F -> L"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_011328"
FT VARIANT 277
FT /note="V -> I (in dbSNP:rs41300004)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_060716"
FT VARIANT 396
FT /note="F -> L (in dbSNP:rs72552707)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_011329"
FT VARIANT 458
FT /note="D -> E (in dbSNP:rs13119049)"
FT /evidence="ECO:0000269|PubMed:10376768, ECO:0000269|Ref.7"
FT /id="VAR_007712"
FT VARIANT 511
FT /note="C -> R (in dbSNP:rs41298245)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_060717"
FT CONFLICT 171..172
FT /note="SL -> RP (in Ref. 1; CAA68415)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..293
FT /note="EME -> KWK (in Ref. 4; AAC32272)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="L -> V (in Ref. 6; AAS47487)"
FT /evidence="ECO:0000305|Ref.6"
FT CONFLICT 354
FT /note="Y -> H (in Ref. 6; AAS47487)"
FT /evidence="ECO:0000305|Ref.6"
FT CONFLICT 382..387
FT /note="EAIYHG -> KAISPR (in Ref. 1; CAA68415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 60513 MW; 6B45E6769971A078 CRC64;
MSMKWTSALL LIQLSCYFSS GSCGKVLVWP TEFSHWMNIK TILDELVQRG HEVTVLASSA
SISFDPNSPS TLKFEVYPVS LTKTEFEDII KQLVKRWAEL PKDTFWSYFS QVQEIMWTFN
DILRKFCKDI VSNKKLMKKL QESRFDVVLA DAVFPFGELL AELLKIPFVY SLRFSPGYAI
EKHSGGLLFP PSYVPVVMSE LSDQMTFIER VKNMIYVLYF EFWFQIFDMK KWDQFYSEVL
GRPTTLSETM AKADIWLIRN YWDFQFPHPL LPNVEFVGGL HCKPAKPLPK EMEEFVQSSG
ENGVVVFSLG SMVSNTSEER ANVIASALAK IPQKVLWRFD GNKPDTLGLN TRLYKWIPQN
DLLGHPKTRA FITHGGANGI YEAIYHGIPM VGVPLFADQP DNIAHMKAKG AAVSLDFHTM
SSTDLLNALK TVINDPLYKE NAMKLSRIHH DQPVKPLDRA VFWIEFVMRH KGAKHLRVAA
HDLTWFQYHS LDVTGFLLAC VATVIFIITK CLFCVWKFVR TGKKGKRD
