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 24-JAN-2024, entry version 210. 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 CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; CC Vmax=3.8 pmol/min/mg enzyme for the formation of CC 16alpha,17beta-estriol 16-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=9.2 pmol/min/mg enzyme for the formation of CC 16beta,17beta-estriol 16-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=174 pmol/min/mg enzyme for the formation of CC 16alpha,17alpha-estriol 17-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=4.3 pmol/min/mg enzyme for the formation of calcitriol CC 25-O-(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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; DB00647; Dextropropoxyphene. 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; DB00333; Methadone. DR DrugBank; DB00295; Morphine. DR DrugBank; DB08804; Nandrolone decanoate. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB00794; Primidone. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB12095; Telotristat ethyl. DR DrugBank; DB00871; Terbutaline. DR SwissLipids; SLP:000001708; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR GlyCosmos; P06133; 1 site, No reported glycans. DR GlyGen; P06133; 1 site. DR iPTMnet; P06133; -. DR PhosphoSitePlus; P06133; -. DR SwissPalm; P06133; -. DR BioMuta; UGT2B4; -. DR DMDM; 6175083; -. DR jPOST; P06133; -. DR MassIVE; P06133; -. DR MaxQB; P06133; -. DR PaxDb; 9606-ENSP00000305221; -. DR PeptideAtlas; P06133; -. DR ProteomicsDB; 34076; -. DR ProteomicsDB; 51871; -. [P06133-1] DR ProteomicsDB; 850; -. DR Antibodypedia; 24236; 224 antibodies from 27 providers. DR DNASU; 7363; -. DR Ensembl; ENST00000305107.7; ENSP00000305221.6; ENSG00000156096.15. [P06133-1] DR Ensembl; ENST00000512583.5; ENSP00000421290.1; ENSG00000156096.15. [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 AGR; HGNC:12553; -. 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; 382054at2759; -. 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 1142 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 cell types or tissues. DR ExpressionAtlas; P06133; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR002213; UDP_glucos_trans. DR InterPro; IPR035595; UDP_glycos_trans_CS. DR PANTHER; PTHR48043; EG:EG0003.4 PROTEIN-RELATED; 1. DR PANTHER; PTHR48043:SF12; UDP-GLUCURONOSYLTRANSFERASE 2B17-RELATED; 1. DR Pfam; PF00201; UDPGT; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00375; UDPGT; 1. DR Genevisible; P06133; HS. 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 //