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'''UDP glucuronosyltransferase 2 family, polypeptide B4''', also known as '''UGT2B4''', is an [[enzyme]] that in humans is encoded by the ''UGT2B4'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UGT2B4 UDP glucuronosyltransferase 2 family, polypeptide B4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7363| accessdate = }}</ref><ref name="pmid3109396">{{cite journal | vauthors = Jackson MR, McCarthy LR, Harding D, Wilson S, Coughtrie MW, Burchell B | title = Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA | journal = Biochem. J. | volume = 242 | issue = 2 | pages = 581–8 |date=March 1987 | pmid = 3109396 | pmc = 1147744 | doi = | url =  }}</ref><ref name="pmid7835904">{{cite journal | vauthors = Monaghan G, Clarke DJ, Povey S, See CG, Boxer M, Burchell B | title = Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13 | journal = Genomics | volume = 23 | issue = 2 | pages = 496–9 |date=September 1994 | pmid = 7835904 | doi = 10.1006/geno.1994.1531 | url = }}</ref>
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UGT2B4 is mainly involved in the [[glucuronidation]] of [[hyodeoxycholic acid]], a [[bile acid]], and [[catechol]]-[[estrogen]]s, such as 17-[[epiestriol]] and 4-hydroxy-[[estrone]].<ref name="pmid17263731">{{cite journal |vauthors=Barre L, Fournel-Gigleux S, Finel M, Netter P, Magdalou J, Ouzzine M |title=Substrate specificity of the human UDP-glucuronosyltransferase UGT2B4 and UGT2B7. Identification of a critical aromatic amino acid residue at position 33 |journal=FEBS J. |volume=274 |issue=5 |pages=1256–64 |date=March 2007 |pmid=17263731 |doi=10.1111/j.1742-4658.2007.05670.x}}</ref>
{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = UDP glucuronosyltransferase 2 family, polypeptide B4
| HGNCid = 12553
| Symbol = UGT2B4
| AltSymbols =; UGT2B11
| OMIM = 600067
| ECnumber = 
| Homologene = 83187
| MGIid = 
| GeneAtlas_image1 = PBB_GE_UGT2B4_206505_at_tn.png
| Function = {{GNF_GO|id=GO:0015020 |text = glucuronosyltransferase activity}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006711 |text = estrogen catabolic process}} {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7363
    | Hs_Ensembl = ENSG00000156096
    | Hs_RefseqProtein = NP_066962
    | Hs_RefseqmRNA = NM_021139
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 70380474
    | Hs_GenLoc_end = 70396212
    | Hs_Uniprot = P06133
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
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'''UDP glucuronosyltransferase 2 family, polypeptide B4''', also known as '''UGT2B4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UGT2B4 UDP glucuronosyltransferase 2 family, polypeptide B4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7363| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
The expression of the UGT2B4 enzyme is upregulated by the [[farnesoid X receptor]] (FXR), a [[nuclear receptor]] which is activated by bile acids.<ref name="pmid12806625">{{cite journal | vauthors = Barbier O, Torra IP, Sirvent A, Claudel T, Blanquart C, Duran-Sandoval D, Kuipers F, Kosykh V, Fruchart JC, Staels B | title = FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of negative feedback control of FXR activity | journal = Gastroenterology | volume = 124 | issue = 7 | pages = 1926–40 |date=June 2003 | pmid = 12806625 | doi = 10.1016/S0016-5085(03)00388-3  | url =  }}</ref>  These same bile acids are substrates for the UGT2B4 enzyme.  Hence upregulation of UGT2B4 by activated FXR provides a mechanism for the detection, conjugation and subsequent elimination of toxic bile acids.
{{PBB_Summary
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| summary_text =  
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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Mackenzie PI, Owens IS, Burchell B, ''et al.'' |title=The UDP glycosyltransferase gene superfamily: recommended nomenclature update based on evolutionary divergence. |journal=Pharmacogenetics |volume=7 |issue= 4 |pages= 255-69 |year= 1997 |pmid= 9295054 |doi=  }}
*{{cite journal   |vauthors=Mackenzie PI, Owens IS, Burchell B, etal |title=The UDP glycosyltransferase gene superfamily: recommended nomenclature update based on evolutionary divergence |journal=Pharmacogenetics |volume=7 |issue= 4 |pages= 255–69 |year= 1997 |pmid= 9295054 |doi=10.1097/00008571-199708000-00001 }}
*{{cite journal  | author=Kadlubar FF, Miller JA, Miller EC |title=Hepatic microsomal N-glucuronidation and nucleic acid binding of N-hydroxy arylamines in relation to urinary bladder carcinogenesis. |journal=Cancer Res. |volume=37 |issue= 3 |pages= 805-14 |year= 1977 |pmid= 13929 |doi=  }}
*{{cite journal  | vauthors=Kadlubar FF, Miller JA, Miller EC |title=Hepatic microsomal N-glucuronidation and nucleic acid binding of N-hydroxy arylamines in relation to urinary bladder carcinogenesis |journal=Cancer Res. |volume=37 |issue= 3 |pages= 805–14 |year= 1977 |pmid= 13929 |doi=  }}
*{{cite journal | author=Ritter JK, Chen F, Sheen YY, ''et al.'' |title=Two human liver cDNAs encode UDP-glucuronosyltransferases with 2 log differences in activity toward parallel substrates including hyodeoxycholic acid and certain estrogen derivatives. |journal=Biochemistry |volume=31 |issue= 13 |pages= 3409-14 |year= 1992 |pmid= 1554722 |doi=  }}
*{{cite journal   |vauthors=Ritter JK, Chen F, Sheen YY, etal |title=Two human liver cDNAs encode UDP-glucuronosyltransferases with 2 log differences in activity toward parallel substrates including hyodeoxycholic acid and certain estrogen derivatives |journal=Biochemistry |volume=31 |issue= 13 |pages= 3409–14 |year= 1992 |pmid= 1554722 |doi=10.1021/bi00128a015 }}
*{{cite journal  | author=Fournel-Gigleux S, Jackson MR, Wooster R, Burchell B |title=Expression of a human liver cDNA encoding a UDP-glucuronosyltransferase catalysing the glucuronidation of hyodeoxycholic acid in cell culture. |journal=FEBS Lett. |volume=243 |issue= 2 |pages= 119-22 |year= 1989 |pmid= 2492950 |doi= }}
*{{cite journal  | vauthors=Fournel-Gigleux S, Jackson MR, Wooster R, Burchell B |title=Expression of a human liver cDNA encoding a UDP-glucuronosyltransferase catalysing the glucuronidation of hyodeoxycholic acid in cell culture |journal=FEBS Lett. |volume=243 |issue= 2 |pages= 119–22 |year= 1989 |pmid= 2492950 |doi=10.1016/0014-5793(89)80111-5  }}
*{{cite journal | author=Jackson MR, McCarthy LR, Harding D, ''et al.'' |title=Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA. |journal=Biochem. J. |volume=242 |issue= 2 |pages= 581-8 |year= 1987 |pmid= 3109396 |doi=  }}
*{{cite journal   |vauthors=Jackson MR, McCarthy LR, Harding D, etal |title=Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA |journal=Biochem. J. |volume=242 |issue= 2 |pages= 581–8 |year= 1987 |pmid= 3109396 |doi= | pmc=1147744 }}
*{{cite journal | author=Monaghan G, Clarke DJ, Povey S, ''et al.'' |title=Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13. |journal=Genomics |volume=23 |issue= 2 |pages= 496-9 |year= 1995 |pmid= 7835904 |doi= 10.1006/geno.1994.1531 }}
*{{cite journal   |vauthors=Monaghan G, Clarke DJ, Povey S, etal |title=Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13 |journal=Genomics |volume=23 |issue= 2 |pages= 496–9 |year= 1995 |pmid= 7835904 |doi= 10.1006/geno.1994.1531 }}
*{{cite journal  | author=Jin CJ, Miners JO, Lillywhite KJ, Mackenzie PI |title=cDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily. |journal=Biochem. Biophys. Res. Commun. |volume=194 |issue= 1 |pages= 496-503 |year= 1993 |pmid= 8333863 |doi= 10.1006/bbrc.1993.1847 }}
*{{cite journal  | vauthors=Jin CJ, Miners JO, Lillywhite KJ, Mackenzie PI |title=cDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily |journal=Biochem. Biophys. Res. Commun. |volume=194 |issue= 1 |pages= 496–503 |year= 1993 |pmid= 8333863 |doi= 10.1006/bbrc.1993.1847 }}
*{{cite journal | author=Babu SR, Lakshmi VM, Huang GP, ''et al.'' |title=Glucuronide conjugates of 4-aminobiphenyl and its N-hydroxy metabolites. pH stability and synthesis by human and dog liver. |journal=Biochem. Pharmacol. |volume=51 |issue= 12 |pages= 1679-85 |year= 1996 |pmid= 8687483 |doi=  }}
*{{cite journal   |vauthors=Babu SR, Lakshmi VM, Huang GP, etal |title=Glucuronide conjugates of 4-aminobiphenyl and its N-hydroxy metabolites. pH stability and synthesis by human and dog liver |journal=Biochem. Pharmacol. |volume=51 |issue= 12 |pages= 1679–85 |year= 1996 |pmid= 8687483 |doi=10.1016/0006-2952(96)00165-7 }}
*{{cite journal  | author=Monaghan G, Burchell B, Boxer M |title=Structure of the human UGT2B4 gene encoding a bile acid UDP-glucuronosyltransferase. |journal=Mamm. Genome |volume=8 |issue= 9 |pages= 692-4 |year= 1997 |pmid= 9271674 |doi=  }}
*{{cite journal  | vauthors=Monaghan G, Burchell B, Boxer M |title=Structure of the human UGT2B4 gene encoding a bile acid UDP-glucuronosyltransferase |journal=Mamm. Genome |volume=8 |issue= 9 |pages= 692–4 |year= 1997 |pmid= 9271674 |doi=10.1007/s003359900539 }}
*{{cite journal  | author=King CD, Rios GR, Assouline JA, Tephly TR |title=Expression of UDP-glucuronosyltransferases (UGTs) 2B7 and 1A6 in the human brain and identification of 5-hydroxytryptamine as a substrate. |journal=Arch. Biochem. Biophys. |volume=365 |issue= 1 |pages= 156-62 |year= 1999 |pmid= 10222050 |doi= 10.1006/abbi.1999.1155 }}
*{{cite journal  | vauthors=King CD, Rios GR, Assouline JA, Tephly TR |title=Expression of UDP-glucuronosyltransferases (UGTs) 2B7 and 1A6 in the human brain and identification of 5-hydroxytryptamine as a substrate |journal=Arch. Biochem. Biophys. |volume=365 |issue= 1 |pages= 156–62 |year= 1999 |pmid= 10222050 |doi= 10.1006/abbi.1999.1155 }}
*{{cite journal  | author=Lévesque E, Beaulieu M, Hum DW, Bélanger A |title=Characterization and substrate specificity of UGT2B4 (E458): a UDP-glucuronosyltransferase encoded by a polymorphic gene. |journal=Pharmacogenetics |volume=9 |issue= 2 |pages= 207-16 |year= 1999 |pmid= 10376768 |doi=  }}
*{{cite journal  | vauthors=Lévesque E, Beaulieu M, Hum DW, Bélanger A |title=Characterization and substrate specificity of UGT2B4 (E458): a UDP-glucuronosyltransferase encoded by a polymorphic gene |journal=Pharmacogenetics |volume=9 |issue= 2 |pages= 207–16 |year= 1999 |pmid= 10376768 |doi=  }}
*{{cite journal | author=Strassburg CP, Kneip S, Topp J, ''et al.'' |title=Polymorphic gene regulation and interindividual variation of UDP-glucuronosyltransferase activity in human small intestine. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36164-71 |year= 2000 |pmid= 10748067 |doi= 10.1074/jbc.M002180200 }}
*{{cite journal   |vauthors=Strassburg CP, Kneip S, Topp J, etal |title=Polymorphic gene regulation and interindividual variation of UDP-glucuronosyltransferase activity in human small intestine |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36164–71 |year= 2000 |pmid= 10748067 |doi= 10.1074/jbc.M002180200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Barbier O, Torra IP, Sirvent A, ''et al.'' |title=FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of negative feedback control of FXR activity. |journal=Gastroenterology |volume=124 |issue= 7 |pages= 1926-40 |year= 2003 |pmid= 12806625 |doi=  }}
*{{cite journal   |vauthors=Barbier O, Torra IP, Sirvent A, etal |title=FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of negative feedback control of FXR activity |journal=Gastroenterology |volume=124 |issue= 7 |pages= 1926–40 |year= 2003 |pmid= 12806625 |doi=10.1016/S0016-5085(03)00388-3 }}
*{{cite journal | author=Barbier O, Duran-Sandoval D, Pineda-Torra I, ''et al.'' |title=Peroxisome proliferator-activated receptor alpha induces hepatic expression of the human bile acid glucuronidating UDP-glucuronosyltransferase 2B4 enzyme. |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 32852-60 |year= 2003 |pmid= 12810707 |doi= 10.1074/jbc.M305361200 }}
*{{cite journal   |vauthors=Barbier O, Duran-Sandoval D, Pineda-Torra I, etal |title=Peroxisome proliferator-activated receptor alpha induces hepatic expression of the human bile acid glucuronidating UDP-glucuronosyltransferase 2B4 enzyme |journal=J. Biol. Chem. |volume=278 |issue= 35 |pages= 32852–60 |year= 2003 |pmid= 12810707 |doi= 10.1074/jbc.M305361200 }}
*{{cite journal | author=Saeki M, Saito Y, Jinno H, ''et al.'' |title=Single nucleotide polymorphisms and haplotype frequencies of UGT2B4 and UGT2B7 in a Japanese population. |journal=Drug Metab. Dispos. |volume=32 |issue= 9 |pages= 1048-54 |year= 2005 |pmid= 15319348 |doi=  }}
*{{cite journal   |vauthors=Saeki M, Saito Y, Jinno H, etal |title=Single nucleotide polymorphisms and haplotype frequencies of UGT2B4 and UGT2B7 in a Japanese population |journal=Drug Metab. Dispos. |volume=32 |issue= 9 |pages= 1048–54 |year= 2005 |pmid= 15319348 |doi=  }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Kimura K, Wakamatsu A, Suzuki Y, ''et al.'' |title=Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. |journal=Genome Res. |volume=16 |issue= 1 |pages= 55-65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 }}
*{{cite journal   |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406 | pmc=1356129 }}
*{{cite journal | author=Barre L, Fournel-Gigleux S, Finel M, ''et al.'' |title=Substrate specificity of the human UDP-glucuronosyltransferase UGT2B4 and UGT2B7. Identification of a critical aromatic amino acid residue at position 33. |journal=FEBS J. |volume=274 |issue= 5 |pages= 1256-64 |year= 2007 |pmid= 17263731 |doi= 10.1111/j.1742-4658.2007.05670.x }}
*{{cite journal   |vauthors=Barre L, Fournel-Gigleux S, Finel M, etal |title=Substrate specificity of the human UDP-glucuronosyltransferase UGT2B4 and UGT2B7. Identification of a critical aromatic amino acid residue at position 33 |journal=FEBS J. |volume=274 |issue= 5 |pages= 1256–64 |year= 2007 |pmid= 17263731 |doi= 10.1111/j.1742-4658.2007.05670.x }}
}}
}}
{{refend}}
{{refend}}
{{Glycosyltransferases}}
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Latest revision as of 09:43, 17 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

UDP glucuronosyltransferase 2 family, polypeptide B4, also known as UGT2B4, is an enzyme that in humans is encoded by the UGT2B4 gene.[1][2][3]

Function

UGT2B4 is mainly involved in the glucuronidation of hyodeoxycholic acid, a bile acid, and catechol-estrogens, such as 17-epiestriol and 4-hydroxy-estrone.[4]

The expression of the UGT2B4 enzyme is upregulated by the farnesoid X receptor (FXR), a nuclear receptor which is activated by bile acids.[5] These same bile acids are substrates for the UGT2B4 enzyme. Hence upregulation of UGT2B4 by activated FXR provides a mechanism for the detection, conjugation and subsequent elimination of toxic bile acids.

References

  1. ↑ "Entrez Gene: UGT2B4 UDP glucuronosyltransferase 2 family, polypeptide B4".
  2. ↑ Jackson MR, McCarthy LR, Harding D, Wilson S, Coughtrie MW, Burchell B (March 1987). "Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA". Biochem. J. 242 (2): 581–8. PMC 1147744. PMID 3109396.
  3. ↑ Monaghan G, Clarke DJ, Povey S, See CG, Boxer M, Burchell B (September 1994). "Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13". Genomics. 23 (2): 496–9. doi:10.1006/geno.1994.1531. PMID 7835904.
  4. ↑ Barre L, Fournel-Gigleux S, Finel M, Netter P, Magdalou J, Ouzzine M (March 2007). "Substrate specificity of the human UDP-glucuronosyltransferase UGT2B4 and UGT2B7. Identification of a critical aromatic amino acid residue at position 33". FEBS J. 274 (5): 1256–64. doi:10.1111/j.1742-4658.2007.05670.x. PMID 17263731.
  5. ↑ Barbier O, Torra IP, Sirvent A, Claudel T, Blanquart C, Duran-Sandoval D, Kuipers F, Kosykh V, Fruchart JC, Staels B (June 2003). "FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of negative feedback control of FXR activity". Gastroenterology. 124 (7): 1926–40. doi:10.1016/S0016-5085(03)00388-3. PMID 12806625.

Further reading



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