ID UDB15_HUMAN Reviewed; 530 AA. AC P54855; A6NDX0; A6NNJ4; A8K054; P23765; Q9UK63; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 3. DT 27-MAR-2024, entry version 196. DE RecName: Full=UDP-glucuronosyltransferase 2B15 {ECO:0000303|PubMed:18719240}; DE Short=UDPGT 2B15; DE Short=UGT2B15; DE EC=2.4.1.17 {ECO:0000269|PubMed:16595710, ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:7835232, ECO:0000269|PubMed:9295060}; DE AltName: Full=HLUG4; DE AltName: Full=UDP-glucuronosyltransferase 2B8; DE Short=UDPGT 2B8; DE AltName: Full=UDPGTh-3; DE Flags: Precursor; GN Name=UGT2B15 {ECO:0000312|HGNC:HGNC:12546}; GN Synonyms=UGT2B8 {ECO:0000305|PubMed:2116769}; 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], CHARACTERIZATION, TISSUE SPECIFICITY, AND RP VARIANTS ASP-85 AND THR-523. RC TISSUE=Liver; RX PubMed=8399210; DOI=10.1021/bi00091a015; RA Chen F., Ritter J.K., Wang M.G., McBride O.W., Lubet R.A., Owens I.S.; RT "Characterization of a cloned human dihydrotestosterone/androstanediol UDP- RT glucuronosyltransferase and its comparison to other steroid isoforms."; RL Biochemistry 32:10648-10657(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANTS ASP-85 AND THR-523. RC TISSUE=Liver; RX PubMed=7835232; RA Green M.D., Oturu E.M., Tephly T.R.; RT "Stable expression of a human liver UDP-glucuronosyltransferase (UGT2B15) RT with activity toward steroid and xenobiotic substrates."; RL Drug Metab. Dispos. 22:799-805(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND VARIANT RP THR-523. RX PubMed=9295060; DOI=10.1097/00008571-199708000-00007; RA Levesque E., Beaulieu M., Green M.D., Tephly T.R., Belanger A., Hum D.W.; RT "Isolation and characterization of UGT2B15(Y85): a UDP- RT glucuronosyltransferase encoded by a polymorphic gene."; RL Pharmacogenetics 7:317-325(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-523. RC TISSUE=Mammary gland; 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 [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-530, AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Liver; RX PubMed=2116769; DOI=10.1016/0003-9861(90)90428-2; RA Coffman B.L., Tephly T.R., Irshaid Y.M., Green M.D., Smith C., RA Jackson M.R., Wooster R., Burchell B.; RT "Characterization and primary sequence of a human hepatic microsomal RT estriol UDPglucuronosyltransferase."; RL Arch. Biochem. Biophys. 281:170-175(1990). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE RP SPECIFICITY. RX PubMed=16595710; DOI=10.1124/dmd.106.009621; RA Murai T., Samata N., Iwabuchi H., Ikeda T.; RT "Human UDP-glucuronosyltransferase, UGT1A8, glucuronidates RT dihydrotestosterone to a monoglucuronide and further to a structurally RT novel diglucuronide."; RL Drug Metab. Dispos. 34:1102-1108(2006). RN [9] 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 [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65. 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 [11] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE RP SPECIFICITY. 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). RN [12] 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 [13] RP VARIANT THR-523. RX PubMed=15618667; DOI=10.2133/dmpk.17.164; RA Toide K., Umeda S., Yamazaki H., Takahashi Y., Terauchi Y., Fujii T., RA Kamataki T.; RT "A major genotype in UDP-glucuronosyltransferase 2B15."; RL Drug Metab. Pharmacokinet. 17:164-166(2002). 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:7835232, PubMed:9295060, PubMed:16595710, PubMed:18719240, CC PubMed:23288867). Essential for the elimination and detoxification of CC drugs, xenobiotics and endogenous compounds (PubMed:7835232). Catalyzes CC the glucuronidation of endogenous steroid hormones such as androgens CC (testosterone, androsterone) and estrogens (estradiol, epiestradiol, CC estriol, catechol estrogens) (PubMed:7835232, PubMed:9295060, CC PubMed:16595710, PubMed:18719240, PubMed:23288867). Displays CC glucuronidation activity toward several classes of xenobiotic CC substrates, including phenolic compounds (eugenol, 4-nitrophenol, 4- CC hydroxybiphenyl) and phenylpropanoids (naringenin, coumarins) CC (PubMed:7835232). Catalyzes the glucuronidation of monoterpenoid CC alcohols such as borneol, menthol and isomenthol, a class of natural CC compounds used in essential oils (By similarity). CC {ECO:0000250|UniProtKB:P36511, ECO:0000269|PubMed:16595710, CC ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867, CC ECO:0000269|PubMed:7835232, ECO:0000269|PubMed:9295060}. 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:16595710, ECO:0000269|PubMed:18719240, CC ECO:0000269|PubMed:23288867, ECO:0000269|PubMed:7835232, CC ECO:0000269|PubMed:9295060}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033; CC Evidence={ECO:0000305|PubMed:16595710, ECO:0000305|PubMed:18719240, CC ECO:0000305|PubMed:23288867, ECO:0000305|PubMed:7835232, CC ECO:0000305|PubMed:9295060}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17alpha-estradiol + UDP-alpha-D-glucuronate = 17alpha- CC estradiol 3-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:52868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17160, CC ChEBI:CHEBI:57529, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223; CC Evidence={ECO:0000269|PubMed:18719240, ECO:0000269|PubMed:23288867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52869; CC Evidence={ECO:0000305|PubMed:18719240, ECO:0000305|PubMed:23288867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=16alpha,17alpha-estriol + UDP-alpha-D-glucuronate = CC 16alpha,17alpha-estriol 3-O-(beta-D-glucuronate) + H(+) + UDP; CC Xref=Rhea:RHEA:52924, ChEBI:CHEBI:15378, ChEBI:CHEBI:42156, CC ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:136882; CC Evidence={ECO:0000269|PubMed:23288867}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52925; CC Evidence={ECO:0000305|PubMed:23288867}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-hydroxy-5alpha-androstan-3-one + UDP-alpha-D- CC glucuronate = 5alpha-dihydrotestosterone 17-O-(beta-D-glucuronate) + CC H(+) + UDP; Xref=Rhea:RHEA:53000, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16330, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, CC ChEBI:CHEBI:136914; Evidence={ECO:0000269|PubMed:16595710}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53001; CC Evidence={ECO:0000305|PubMed:16595710}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=26.1 uM for 17alpha-estradiol/epiestradiol (when assaying CC glucuronidation at position 3) {ECO:0000269|PubMed:18719240}; CC KM=90 uM for UDP-alpha-D-glucuronate (when assaying glucuronidation CC with eugenol and 4-methylumbelliferone as substrates) CC {ECO:0000269|PubMed:7835232}; CC KM=15 uM for 4-hydroxy-estrone {ECO:0000269|PubMed:7835232}; CC KM=15 uM for 5alpha-androstane-3alpha,17beta-diol CC {ECO:0000269|PubMed:7835232}; CC KM=28 uM for naringenin {ECO:0000269|PubMed:7835232}; CC KM=78 uM for 4-methylumbelliferone {ECO:0000269|PubMed:7835232}; CC KM=8 uM for eugenol {ECO:0000269|PubMed:7835232}; CC KM=180 uM for 4-nitrophenol {ECO:0000269|PubMed:7835232}; CC KM=30 uM for 4-hydroxybiphenyl {ECO:0000269|PubMed:7835232}; CC Vmax=350 pmol/min/mg enzyme for the formation of 17alpha-estradiol CC 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240}; CC Vmax=5 pmol/min/mg enzyme for the formation of 17beta-estradiol CC 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240}; CC Vmax=10.1 pmol/min/mg enzyme for the formation of CC 16beta,17beta-estriol 3-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=88.1 pmol/min/mg enzyme for the formation of CC 16alpha,17alpha-estriol 3-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:23288867}; CC Vmax=9.4 pmol/min/mg enzyme for the formation of 17beta-estradiol CC 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; CC Vmax=349 pmol/min/mg enzyme for the formation of 17alpha-estradiol CC 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; CC Vmax=12.3 pmol/min/mg enzyme for the formation of 17alpha-estradiol CC 17-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867}; CC Vmax=388 pmol/min/mg enzyme for the formation of CC 5alpha-dihydrotestosterone 17-O-(beta-D-glucuronate) CC {ECO:0000269|PubMed:16595710}; CC Vmax=14 pmol/min/mg enzyme for the formation of 4-hydroxy-estrone CC glucuronide {ECO:0000269|PubMed:7835232}; CC Vmax=49 pmol/min/mg enzyme for the formation of CC 5alpha-androstane-3alpha,17beta-diol glucuronide CC {ECO:0000269|PubMed:7835232}; CC Vmax=72 pmol/min/mg enzyme for the formation of naringenin CC glucuronide {ECO:0000269|PubMed:7835232}; CC Vmax=5 pmol/min/mg enzyme for the formation of 4-methylumbelliferone CC glucuronide {ECO:0000269|PubMed:7835232}; CC Vmax=100 pmol/min/mg enzyme for the formation of eugenol glucuronide CC {ECO:0000269|PubMed:7835232}; CC Vmax=23 pmol/min/mg enzyme for the formation of 4-nitrophenol CC glucuronide {ECO:0000269|PubMed:7835232}; CC Vmax=55 pmol/min/mg enzyme for the formation of 4-hydroxybiphenyl CC glucuronide {ECO:0000269|PubMed:7835232}; 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:16595710, ECO:0000305|PubMed:18719240, CC ECO:0000305|PubMed:23288867}; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000305|PubMed:23288867}; Single-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in many tissues. Present in liver, CC prostate and testis. {ECO:0000269|PubMed:8399210}. CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family. CC {ECO:0000305}. 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; AF548389; AAN40695.1; -; mRNA. DR EMBL; U08854; AAC50077.1; -; mRNA. DR EMBL; AF180322; AAD55093.1; -; mRNA. DR EMBL; AK289419; BAF82108.1; -; mRNA. DR EMBL; AC019173; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC147055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX05574.1; -; Genomic_DNA. DR EMBL; U06641; AAA83406.1; -; mRNA. DR CCDS; CCDS3524.1; -. DR PIR; A48633; A48633. DR PIR; S11309; S11309. DR RefSeq; NP_001067.2; NM_001076.3. DR PDB; 6IPB; X-ray; 1.78 A; A/B/C/D=284-451. DR PDB; 7CJX; X-ray; 1.99 A; A/B/C/D=284-447. DR PDBsum; 6IPB; -. DR PDBsum; 7CJX; -. DR AlphaFoldDB; P54855; -. DR SMR; P54855; -. DR BioGRID; 113213; 4. DR IntAct; P54855; 2. DR STRING; 9606.ENSP00000341045; -. DR BindingDB; P54855; -. DR ChEMBL; CHEMBL6161; -. DR DrugBank; DB00316; Acetaminophen. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB14635; Curcumin sulfate. DR DrugBank; DB06695; Dabigatran etexilate. DR DrugBank; DB11943; Delafloxacin. DR DrugBank; DB00514; Dextromethorphan. DR DrugBank; DB13874; Enasidenib. DR DrugBank; DB00783; Estradiol. DR DrugBank; DB00973; Ezetimibe. DR DrugBank; DB00983; Formoterol. DR DrugBank; DB11796; Fostemsavir. DR DrugBank; DB12471; Ibrexafungerp. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB00455; Loratadine. DR DrugBank; DB00186; Lorazepam. DR DrugBank; DB06077; Lumateperone. DR DrugBank; DB00295; Morphine. DR DrugBank; DB00842; Oxazepam. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB00794; Primidone. DR DrugBank; DB09288; Propacetamol. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB00871; Terbutaline. DR DrugBank; DB00197; Troglitazone. DR DrugBank; DB00313; Valproic acid. DR DrugBank; DB09185; Viloxazine. DR SwissLipids; SLP:000001709; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR GlyConnect; 2087; 2 N-Linked glycans (1 site). DR GlyCosmos; P54855; 3 sites, 4 glycans. DR GlyGen; P54855; 3 sites, 4 N-linked glycans (1 site). DR iPTMnet; P54855; -. DR PhosphoSitePlus; P54855; -. DR BioMuta; UGT2B15; -. DR DMDM; 332278237; -. DR jPOST; P54855; -. DR MassIVE; P54855; -. DR MaxQB; P54855; -. DR PaxDb; 9606-ENSP00000341045; -. DR PeptideAtlas; P54855; -. DR ProteomicsDB; 56742; -. DR Antibodypedia; 24200; 109 antibodies from 21 providers. DR DNASU; 7366; -. DR Ensembl; ENST00000338206.6; ENSP00000341045.5; ENSG00000196620.10. DR GeneID; 7366; -. DR KEGG; hsa:7366; -. DR MANE-Select; ENST00000338206.6; ENSP00000341045.5; NM_001076.4; NP_001067.2. DR UCSC; uc021xow.2; human. DR AGR; HGNC:12546; -. DR DisGeNET; 7366; -. DR GeneCards; UGT2B15; -. DR HGNC; HGNC:12546; UGT2B15. DR HPA; ENSG00000196620; Group enriched (gallbladder, liver). DR MIM; 600069; gene. DR neXtProt; NX_P54855; -. DR OpenTargets; ENSG00000196620; -. DR PharmGKB; PA37188; -. DR VEuPathDB; HostDB:ENSG00000196620; -. DR eggNOG; KOG1192; Eukaryota. DR GeneTree; ENSGT00940000163930; -. DR HOGENOM; CLU_012949_3_0_1; -. DR InParanoid; P54855; -. DR OMA; ILDRWIY; -. DR OrthoDB; 382054at2759; -. DR PhylomeDB; P54855; -. DR TreeFam; TF315472; -. DR BRENDA; 2.4.1.17; 2681. DR PathwayCommons; P54855; -. DR Reactome; R-HSA-156588; Glucuronidation. DR Reactome; R-HSA-9749641; Aspirin ADME. DR Reactome; R-HSA-9753281; Paracetamol ADME. DR SABIO-RK; P54855; -. DR SignaLink; P54855; -. DR BioGRID-ORCS; 7366; 30 hits in 1048 CRISPR screens. DR GeneWiki; UGT2B15; -. DR GenomeRNAi; 7366; -. DR Pharos; P54855; Tbio. DR PRO; PR:P54855; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P54855; Protein. DR Bgee; ENSG00000196620; Expressed in gall bladder and 49 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. 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 GO; GO:0008202; P:steroid metabolic process; TAS:ProtInc. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 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:SF58; UDP-GLUCURONOSYLTRANSFERASE 2B15; 1. DR Pfam; PF00201; UDPGT; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PROSITE; PS00375; UDPGT; 1. DR Genevisible; P54855; HS. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum; KW Glycoprotein; Glycosyltransferase; Lipid metabolism; Membrane; KW Reference proteome; Signal; Steroid metabolism; Transferase; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..530 FT /note="UDP-glucuronosyltransferase 2B15" FT /id="PRO_0000036039" FT TRANSMEM 495..515 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 136 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BWQ1" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 316 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 483 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 85 FT /note="Y -> D (in dbSNP:rs1902023)" FT /evidence="ECO:0000269|PubMed:7835232, FT ECO:0000269|PubMed:8399210" FT /id="VAR_007713" FT VARIANT 523 FT /note="K -> T (in dbSNP:rs4148269)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15618667, ECO:0000269|PubMed:7835232, FT ECO:0000269|PubMed:8399210, ECO:0000269|PubMed:9295060" FT /id="VAR_018348" FT CONFLICT 119 FT /note="E -> A (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 145 FT /note="K -> R (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 150..155 FT /note="LADALN -> PGDPVF (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 162 FT /note="A -> S (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="F -> L (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 170..177 FT /note="LYSLRFSV -> VYRSRISR (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 181 FT /note="F -> I (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="S -> I (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="M -> L (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="H -> D (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 443 FT /note="V -> A (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT CONFLICT 501 FT /note="C -> W (in Ref. 7; AAA83406)" FT /evidence="ECO:0000305" FT HELIX 291..298 FT /evidence="ECO:0007829|PDB:6IPB" FT HELIX 299..303 FT /evidence="ECO:0007829|PDB:6IPB" FT STRAND 305..308 FT /evidence="ECO:0007829|PDB:6IPB" FT HELIX 314..316 FT /evidence="ECO:0007829|PDB:6IPB" FT HELIX 319..329 FT /evidence="ECO:0007829|PDB:6IPB" FT STRAND 332..339 FT /evidence="ECO:0007829|PDB:6IPB" FT STRAND 352..357 FT /evidence="ECO:0007829|PDB:6IPB" FT HELIX 360..364 FT /evidence="ECO:0007829|PDB:6IPB" FT STRAND 369..374 FT /evidence="ECO:0007829|PDB:6IPB" FT HELIX 378..387 FT /evidence="ECO:0007829|PDB:6IPB" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:6IPB" FT HELIX 398..409 FT /evidence="ECO:0007829|PDB:6IPB" FT STRAND 412..415 FT /evidence="ECO:0007829|PDB:6IPB" FT TURN 418..420 FT /evidence="ECO:0007829|PDB:6IPB" FT HELIX 423..435 FT /evidence="ECO:0007829|PDB:6IPB" FT HELIX 437..450 FT /evidence="ECO:0007829|PDB:6IPB" SQ SEQUENCE 530 AA; 61036 MW; EB2DAE838769C955 CRC64; MSLKWTSVFL LIQLSCYFSS GSCGKVLVWP TEYSHWINMK TILEELVQRG HEVTVLTSSA STLVNASKSS AIKLEVYPTS LTKNYLEDSL LKILDRWIYG VSKNTFWSYF SQLQELCWEY YDYSNKLCKD AVLNKKLMMK LQESKFDVIL ADALNPCGEL LAELFNIPFL YSLRFSVGYT FEKNGGGFLF PPSYVPVVMS ELSDQMIFME RIKNMIHMLY FDFWFQIYDL KKWDQFYSEV LGRPTTLFET MGKAEMWLIR TYWDFEFPRP FLPNVDFVGG LHCKPAKPLP KEMEEFVQSS GENGIVVFSL GSMISNMSEE SANMIASALA QIPQKVLWRF DGKKPNTLGS NTRLYKWLPQ NDLLGHPKTK AFITHGGTNG IYEAIYHGIP MVGIPLFADQ HDNIAHMKAK GAALSVDIRT MSSRDLLNAL KSVINDPVYK ENVMKLSRIH HDQPMKPLDR AVFWIEFVMR HKGAKHLRVA AHNLTWIQYH SLDVIAFLLA CVATVIFIIT KFCLFCFRKL AKKGKKKKRD //