ID   UDB28_HUMAN             Reviewed;         529 AA.
AC   Q9BY64; B5BUM0; Q9BY62; Q9BY63;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 179.
DE   RecName: Full=UDP-glucuronosyltransferase 2B28 {ECO:0000305|PubMed:11300766};
DE            Short=UDPGT 2B28;
DE            Short=UGT2B28;
DE            EC=2.4.1.17 {ECO:0000269|PubMed:11300766};
DE   Flags: Precursor;
GN   Name=UGT2B28 {ECO:0000312|HGNC:HGNC:13479};
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] (ISOFORMS 1 AND 2), FUNCTION (ISOFORMS 1 AND 2),
RP   CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11300766; DOI=10.1021/bi002607y;
RA   Levesque E., Turgeon D., Carrier J.-S., Montminy V., Beaulieu M.,
RA   Belanger A.;
RT   "Isolation and characterization of the UGT2B28 cDNA encoding a novel human
RT   steroid conjugating UDP-glucuronosyltransferase.";
RL   Biochemistry 40:3869-3881(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-365;
RP   ARG-447 AND ASP-458.
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA   Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA   Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA   Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA   Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA   Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA   Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in vitro-
RT   expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
CC   -!- FUNCTION: [Isoform 1]: UDP-glucuronosyltransferase (UGT) that catalyzes
CC       phase II 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:11300766). Essential for the elimination and
CC       detoxification of drugs, xenobiotics and endogenous compounds
CC       (PubMed:11300766). Catalyzes the glucuronidation of endogenous steroid
CC       hormones such as androgens (androsterone, 3alpha-androstanediol) and
CC       estrogens (estradiol, estrone) (PubMed:11300766). Catalyzes the
CC       glucuronidation of bile acid substrates, which are natural detergents
CC       for dietary lipids absorption (PubMed:11300766). Displays
CC       glucuronidation activity toward the phenolic compounds eugenol
CC       (PubMed:11300766). {ECO:0000269|PubMed:11300766}.
CC   -!- FUNCTION: [Isoform 2]: Lack UDP-glucuronosyltransferase (UGT) activity.
CC       {ECO:0000269|PubMed:11300766}.
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:11300766};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21033;
CC         Evidence={ECO:0000305|PubMed:11300766};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11300766}; Single-pass membrane protein
CC       {ECO:0000255}. Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:11300766}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=I;
CC         IsoId=Q9BY64-1; Sequence=Displayed;
CC       Name=2; Synonyms=II;
CC         IsoId=Q9BY64-2; Sequence=VSP_006710, VSP_006711;
CC   -!- TISSUE SPECIFICITY: Expressed in the liver, breast and kidney.
CC       {ECO:0000269|PubMed:11300766}.
CC   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK31809.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; AF177272; AAK31807.1; -; mRNA.
DR   EMBL; AF177273; AAK31808.1; -; mRNA.
DR   EMBL; AF177274; AAK31809.1; ALT_SEQ; mRNA.
DR   EMBL; AB451456; BAG70270.1; -; mRNA.
DR   CCDS; CCDS3528.1; -. [Q9BY64-1]
DR   CCDS; CCDS56330.1; -. [Q9BY64-2]
DR   RefSeq; NP_001193933.1; NM_001207004.1. [Q9BY64-2]
DR   RefSeq; NP_444267.1; NM_053039.1. [Q9BY64-1]
DR   AlphaFoldDB; Q9BY64; -.
DR   SMR; Q9BY64; -.
DR   BioGRID; 119987; 104.
DR   STRING; 9606.ENSP00000334276; -.
DR   ChEMBL; CHEMBL6189; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   GlyCosmos; Q9BY64; 1 site, No reported glycans.
DR   GlyGen; Q9BY64; 1 site.
DR   iPTMnet; Q9BY64; -.
DR   PhosphoSitePlus; Q9BY64; -.
DR   BioMuta; UGT2B28; -.
DR   DMDM; 20140759; -.
DR   jPOST; Q9BY64; -.
DR   MassIVE; Q9BY64; -.
DR   MaxQB; Q9BY64; -.
DR   PaxDb; 9606-ENSP00000334276; -.
DR   PeptideAtlas; Q9BY64; -.
DR   ProteomicsDB; 79588; -. [Q9BY64-1]
DR   ProteomicsDB; 79589; -. [Q9BY64-2]
DR   Antibodypedia; 66995; 50 antibodies from 13 providers.
DR   DNASU; 54490; -.
DR   Ensembl; ENST00000335568.10; ENSP00000334276.5; ENSG00000135226.18. [Q9BY64-1]
DR   Ensembl; ENST00000511240.1; ENSP00000427399.1; ENSG00000135226.18. [Q9BY64-2]
DR   GeneID; 54490; -.
DR   KEGG; hsa:54490; -.
DR   MANE-Select; ENST00000335568.10; ENSP00000334276.5; NM_053039.2; NP_444267.1.
DR   UCSC; uc003hej.3; human. [Q9BY64-1]
DR   AGR; HGNC:13479; -.
DR   CTD; 54490; -.
DR   DisGeNET; 54490; -.
DR   GeneCards; UGT2B28; -.
DR   HGNC; HGNC:13479; UGT2B28.
DR   HPA; ENSG00000135226; Tissue enriched (breast).
DR   MIM; 606497; gene.
DR   neXtProt; NX_Q9BY64; -.
DR   OpenTargets; ENSG00000135226; -.
DR   PharmGKB; PA37779; -.
DR   VEuPathDB; HostDB:ENSG00000135226; -.
DR   eggNOG; KOG1192; Eukaryota.
DR   GeneTree; ENSGT00940000165281; -.
DR   HOGENOM; CLU_012949_3_0_1; -.
DR   InParanoid; Q9BY64; -.
DR   OMA; CIKTTHI; -.
DR   PhylomeDB; Q9BY64; -.
DR   TreeFam; TF315472; -.
DR   BRENDA; 2.4.1.17; 2681.
DR   PathwayCommons; Q9BY64; -.
DR   Reactome; R-HSA-156588; Glucuronidation.
DR   Reactome; R-HSA-9749641; Aspirin ADME.
DR   BioGRID-ORCS; 54490; 11 hits in 1047 CRISPR screens.
DR   GenomeRNAi; 54490; -.
DR   Pharos; Q9BY64; Tbio.
DR   PRO; PR:Q9BY64; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9BY64; Protein.
DR   Bgee; ENSG00000135226; Expressed in gall bladder and 20 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005640; C:nuclear outer membrane; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0015020; F:glucuronosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0052695; P:cellular glucuronidation; IBA:GO_Central.
DR   GO; GO:0008210; P:estrogen metabolic process; IBA:GO_Central.
DR   GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB.
DR   GO; GO:0052697; P:xenobiotic glucuronidation; 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:SF86; UDP-GLUCURONOSYLTRANSFERASE 2B10-RELATED; 1.
DR   Pfam; PF00201; UDPGT; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   PROSITE; PS00375; UDPGT; 1.
DR   Genevisible; Q9BY64; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Endoplasmic reticulum; Glycoprotein;
KW   Glycosyltransferase; Membrane; Reference proteome; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..529
FT                   /note="UDP-glucuronosyltransferase 2B28"
FT                   /id="PRO_0000036046"
FT   TRANSMEM        495..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         135
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWQ1"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         335
FT                   /note="V -> I (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11300766"
FT                   /id="VSP_006710"
FT   VAR_SEQ         336..529
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11300766"
FT                   /id="VSP_006711"
FT   VARIANT         365
FT                   /note="L -> H (in dbSNP:rs4235127)"
FT                   /evidence="ECO:0000269|PubMed:19054851"
FT                   /id="VAR_059847"
FT   VARIANT         447
FT                   /note="I -> R (in dbSNP:rs6843900)"
FT                   /evidence="ECO:0000269|PubMed:19054851"
FT                   /id="VAR_060661"
FT   VARIANT         458
FT                   /note="H -> D (in dbSNP:rs6828191)"
FT                   /evidence="ECO:0000269|PubMed:19054851"
FT                   /id="VAR_060662"
FT   CONFLICT        173
FT                   /note="C -> R (in Ref. 2; BAG70270)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   529 AA;  60906 MW;  8C75277E964690C1 CRC64;
     MALKWTSVLL LIHLGCYFSS GSCGKVLVWT GEYSHWMNMK TILKELVQRG HEVTVLASSA
     SILFDPNDAF TLKLEVYPTS LTKTEFENII MQQVKRWSDI QKDSFWLYFS QEQEILWEFH
     DIFRNFCKDV VSNKKVMKKL QESRFDIIFA DAFFPCGELL AALLNIPFVY SLCFTPGYTI
     ERHSGGLIFP PSYIPVVMSK LSDQMTFMER VKNMIYVLYF DFWFQMCDMK KWDQFYSEVL
     GRPTTLFETM GKADIWLMRN SWSFQFPHPF LPNIDFVGGL HCKPAKPLPK EMEEFVQSSG
     ENGVVVFSLG SVISNMTAER ANVIATALAK IPQKVLWRFD GNKPDALGLN TRLYKWIPQN
     DLLGLPKTRA FITHGGANGI YEAIYHGIPM VGIPLFWDQP DNIAHMKAKG AAVRLDFHTM
     SSTDLLNALK TVINDPSYKE NVMKLSIIQH DQPVKPLHRA VFWIEFVMCH KGAKHLRVAA
     RDLTWFQYHS LDVIGFLLAC VATVIFVVTK FCLFCFWKFA RKGKKGKRD
//