UDB28_HUMAN
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 03-AUG-2022, entry version 171.
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 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; Q9BY64; -.
DR PeptideAtlas; Q9BY64; -.
DR PRIDE; Q9BY64; -.
DR ProteomicsDB; 79588; -. [Q9BY64-1]
DR ProteomicsDB; 79589; -. [Q9BY64-2]
DR Antibodypedia; 66995; 48 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 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; RWIDLPK; -.
DR OrthoDB; 508327at2759; -.
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 989 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 19 other tissues.
DR Genevisible; Q9BY64; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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: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 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; 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
