UDB15_HUMAN
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 03-AUG-2022, entry version 187.
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 3-
CC O-(beta-D-glucuronate) {ECO:0000269|PubMed:18719240};
CC Vmax=5 pmol/min/mg enzyme for the formation of 17beta-estradiol 3-O-
CC (beta-D-glucuronate) {ECO:0000269|PubMed:18719240};
CC Vmax=10.1 pmol/min/mg enzyme for the formation of 16beta,17beta-
CC estriol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=88.1 pmol/min/mg enzyme for the formation of 16alpha,17alpha-
CC estriol 3-O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=9.4 pmol/min/mg enzyme for the formation of 17beta-estradiol 3-
CC O-(beta-D-glucuronate) {ECO:0000269|PubMed:23288867};
CC Vmax=349 pmol/min/mg enzyme for the formation of 17alpha-estradiol 3-
CC 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 5alpha-
CC 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 5alpha-androstane-
CC 3alpha,17beta-diol glucuronide {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; 3.
DR IntAct; P54855; 1.
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 SwissLipids; SLP:000001709; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyConnect; 2087; 2 N-Linked glycans (1 site).
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; P54855; -.
DR PeptideAtlas; P54855; -.
DR PRIDE; P54855; -.
DR ProteomicsDB; 56742; -.
DR Antibodypedia; 24200; 92 antibodies from 19 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 CTD; 7366; -.
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; 508327at2759; -.
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; 28 hits in 992 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 48 other tissues.
DR Genevisible; P54855; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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 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 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 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
