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{{Infobox_gene}}
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'''UDP-glucuronosyltransferase 1-10''' is an [[enzyme]] that in humans is encoded by the ''UGT1A10'' [[gene]].<ref name="pmid9295054">{{cite journal |vauthors=Mackenzie PI, Owens IS, Burchell B, Bock KW, Bairoch A, Belanger A, Fournel-Gigleux S, Green M, Hum DW, Iyanagi T, Lancet D, Louisot P, Magdalou J, Chowdhury JR, Ritter JK, Schachter H, Tephly TR, Tipton KF, Nebert DW | title = The UDP glycosyltransferase gene superfamily: recommended nomenclature update based on evolutionary divergence | journal = Pharmacogenetics | volume = 7 | issue = 4 | pages = 255–69 |date=Oct 1997 | pmid = 9295054 | pmc = | doi =10.1097/00008571-199708000-00001 }}</ref><ref name="pmid9325166">{{cite journal |vauthors=Mojarrabi B, Mackenzie PI | title = The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid | journal = Biochem Biophys Res Commun | volume = 238 | issue = 3 | pages = 775–8 |date=Oct 1997 | pmid = 9325166 | pmc =  | doi = 10.1006/bbrc.1997.7388 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UGT1A10 UDP glucuronosyltransferase 1 family, polypeptide A10| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54575| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source = 
| PDB =
| Name = UDP glucuronosyltransferase 1 family, polypeptide A10
| HGNCid = 12531
| Symbol = UGT1A10
| AltSymbols =; UDPGT; UGT1J; UGT1H; UGT1*7; UGT1G; HLUGP4; LUGP4; UGT1AI
| OMIM = 606435
| ECnumber = 
| Homologene = 80236
| MGIid = 3580642
| Function = {{GNF_GO|id=GO:0015020 |text = glucuronosyltransferase activity}} {{GNF_GO|id=GO:0016758 |text = transferase activity, transferring hexosyl groups}} {{GNF_GO|id=GO:0008194 |text = UDP-glycosyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_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:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 54575
    | Hs_Ensembl =
    | Hs_RefseqProtein = NP_061948
    | Hs_RefseqmRNA = NM_019075
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr =
    | Hs_GenLoc_start =
    | Hs_GenLoc_end =
    | Hs_Uniprot =   
    | Mm_EntrezGene = 394430
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_001004717
    | Mm_RefseqProtein = XP_001004717
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''UDP glucuronosyltransferase 1 family, polypeptide A10''', also known as '''UGT1A10''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UGT1A10 UDP glucuronosyltransferase 1 family, polypeptide A10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54575| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The enzyme encoded by this gene has glucuronidase activity on mycophenolic acid, coumarins, and quinolines.<ref name="entrez">{{cite web | title = Entrez Gene: UGT1A10 UDP glucuronosyltransferase 1 family, polypeptide A10| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54575| accessdate = }}</ref>
| summary_text = This gene encodes a UDP-glucuronosyltransferase, an enzyme of the [[glucuronidation pathway]] that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The enzyme encoded by this gene has glucuronidase activity on [[mycophenolic acid]], [[coumarins]], and [[quinolines]].<ref name="entrez" />
}}
}}
==Interactive pathway map==
{{IrinotecanPathway_WP229|highlight=UGT1A10}}


==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=Tukey RH, Strassburg CP |title=Human UDP-glucuronosyltransferases: metabolism, expression, and disease |journal=Annu. Rev. Pharmacol. Toxicol. |volume=40 |issue=  |pages= 581–616 |year= 2000 |pmid= 10836148 |doi= 10.1146/annurev.pharmtox.40.1.581 }}
*{{cite journal  | author=Tukey RH, Strassburg CP |title=Human UDP-glucuronosyltransferases: metabolism, expression, and disease. |journal=Annu. Rev. Pharmacol. Toxicol. |volume=40 |issue=  |pages= 581-616 |year= 2000 |pmid= 10836148 |doi= 10.1146/annurev.pharmtox.40.1.581 }}
*{{cite journal  |vauthors=Tukey RH, Strassburg CP |title=Genetic multiplicity of the human UDP-glucuronosyltransferases and regulation in the gastrointestinal tract |journal=Mol. Pharmacol. |volume=59 |issue= 3 |pages= 405–14 |year= 2001 |pmid= 11179432 |doi=  }}
*{{cite journal  | author=Tukey RH, Strassburg CP |title=Genetic multiplicity of the human UDP-glucuronosyltransferases and regulation in the gastrointestinal tract. |journal=Mol. Pharmacol. |volume=59 |issue= 3 |pages= 405-14 |year= 2001 |pmid= 11179432 |doi=  }}
*{{cite journal  |vauthors=King CD, Rios GR, Green MD, Tephly TR |title=UDP-glucuronosyltransferases |journal=Curr. Drug Metab. |volume=1 |issue= 2 |pages= 143–61 |year= 2001 |pmid= 11465080 |doi=10.2174/1389200003339171 }}
*{{cite journal  | author=King CD, Rios GR, Green MD, Tephly TR |title=UDP-glucuronosyltransferases. |journal=Curr. Drug Metab. |volume=1 |issue= 2 |pages= 143-61 |year= 2001 |pmid= 11465080 |doi=  }}
*{{cite journal  |vauthors=Harding D, Jeremiah SJ, Povey S, Burchell B |title=Chromosomal mapping of a human phenol UDP-glucuronosyltransferase, GNT1 |journal=Ann. Hum. Genet. |volume=54 |issue= Pt 1 |pages= 17–21 |year= 1990 |pmid= 2108603 |doi=10.1111/j.1469-1809.1990.tb00356.x }}
*{{cite journal  | author=Harding D, Jeremiah SJ, Povey S, Burchell B |title=Chromosomal mapping of a human phenol UDP-glucuronosyltransferase, GNT1. |journal=Ann. Hum. Genet. |volume=54 |issue= Pt 1 |pages= 17-21 |year= 1990 |pmid= 2108603 |doi=  }}
*{{cite journal  | author=van Es HH |title=Assignment of the human UDP glucuronosyltransferase gene (UGT1A1) to chromosome region 2q37 |journal=Cytogenet. Cell Genet. |volume=63 |issue= 2 |pages= 114–6 |year= 1993 |pmid= 8467709 |doi=10.1159/000133513  |name-list-format=vanc| author2=Bout A  | author3=Liu J  | display-authors=3  | last4=Anderson  | first4=L.  | last5=Duncan  | first5=A.M.V.  | last6=Bosma  | first6=P.  | last7=Elferink  | first7=Oude  | last8=Jansen  | first8=P.L.M.  | last9=Chowdhury  | first9=Roy }}
*{{cite journal  | author=van Es HH, Bout A, Liu J, ''et al.'' |title=Assignment of the human UDP glucuronosyltransferase gene (UGT1A1) to chromosome region 2q37. |journal=Cytogenet. Cell Genet. |volume=63 |issue= 2 |pages= 114-6 |year= 1993 |pmid= 8467709 |doi=  }}
*{{cite journal  |vauthors=Strassburg CP, Oldhafer K, Manns MP, Tukey RH |title=Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue |journal=Mol. Pharmacol. |volume=52 |issue= 2 |pages= 212–20 |year= 1997 |pmid= 9271343 |doi=  }}
*{{cite journal  | author=Strassburg CP, Oldhafer K, Manns MP, Tukey RH |title=Differential expression of the UGT1A locus in human liver, biliary, and gastric tissue: identification of UGT1A7 and UGT1A10 transcripts in extrahepatic tissue. |journal=Mol. Pharmacol. |volume=52 |issue= 2 |pages= 212-20 |year= 1997 |pmid= 9271343 |doi=  }}
*{{cite journal  |vauthors=Mojarrabi B, Mackenzie PI |title=Characterization of two UDP glucuronosyltransferases that are predominantly expressed in human colon |journal=Biochem. Biophys. Res. Commun. |volume=247 |issue= 3 |pages= 704–9 |year= 1998 |pmid= 9647757 |doi= 10.1006/bbrc.1998.8843 }}
*{{cite journal  | author=Mojarrabi B, Mackenzie PI |title=The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid. |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 3 |pages= 775-8 |year= 1997 |pmid= 9325166 |doi= 10.1006/bbrc.1997.7388 }}
*{{cite journal  | author=Strassburg CP |title=Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus |journal=Biochem. J. |volume=338 |issue=  2|pages= 489–98 |year= 1999 |pmid= 10024527 |doi=10.1042/0264-6021:3380489  | pmc=1220077  |name-list-format=vanc| author2=Strassburg A  | author3=Nguyen N  | display-authors=3  | last4=Li  | first4=Qing  | last5=Manns  | first5=Michael P.  | last6=Tukey  | first6=Robert H. }}
*{{cite journal  | author=Mojarrabi B, Mackenzie PI |title=Characterization of two UDP glucuronosyltransferases that are predominantly expressed in human colon. |journal=Biochem. Biophys. Res. Commun. |volume=247 |issue= 3 |pages= 704-9 |year= 1998 |pmid= 9647757 |doi= 10.1006/bbrc.1998.8843 }}
*{{cite journal  |vauthors=Cheng Z, Radominska-Pandya A, Tephly TR |title=Studies on the substrate specificity of human intestinal UDP- lucuronosyltransferases 1A8 and 1A10 |journal=Drug Metab. Dispos. |volume=27 |issue= 10 |pages= 1165–70 |year= 1999 |pmid= 10497143 |doi=  }}
*{{cite journal  | author=Strassburg CP, Strassburg A, Nguyen N, ''et al.'' |title=Regulation and function of family 1 and family 2 UDP-glucuronosyltransferase genes (UGT1A, UGT2B) in human oesophagus. |journal=Biochem. J. |volume=338 ( Pt 2) |issue=  |pages= 489-98 |year= 1999 |pmid= 10024527 |doi=  }}
*{{cite journal  | author=Strassburg CP |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 |name-list-format=vanc| author2=Kneip S  | author3=Topp J  | display-authors=3  | last4=Obermayer-Straub  | first4=P  | last5=Barut  | first5=A  | last6=Tukey  | first6=RH  | last7=Manns  | first7=MP }}
*{{cite journal  | author=Cheng Z, Radominska-Pandya A, Tephly TR |title=Studies on the substrate specificity of human intestinal UDP- lucuronosyltransferases 1A8 and 1A10. |journal=Drug Metab. Dispos. |volume=27 |issue= 10 |pages= 1165-70 |year= 1999 |pmid= 10497143 |doi=  }}
*{{cite journal  | author=Gong QH |title=Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus |journal=Pharmacogenetics |volume=11 |issue= 4 |pages= 357–68 |year= 2001 |pmid= 11434514 |doi=10.1097/00008571-200106000-00011  |name-list-format=vanc| author2=Cho JW  | author3=Huang T  | display-authors=3  | last4=Potter  | first4=Christine  | last5=Gholami  | first5=Nahid  | last6=Basu  | first6=Nikhil K.  | last7=Kubota  | first7=Shigeki  | last8=Carvalho  | first8=Sheryl  | last9=Pennington  | first9=Matthew W. }}
*{{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=Zheng Z, Fang JL, Lazarus P |title=Glucuronidation: an important mechanism for detoxification of benzo[a]pyrene metabolites in aerodigestive tract tissues |journal=Drug Metab. Dispos. |volume=30 |issue= 4 |pages= 397–403 |year= 2002 |pmid= 11901093 |doi=10.1124/dmd.30.4.397 }}
*{{cite journal  | author=Gong QH, Cho JW, Huang T, ''et al.'' |title=Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. |journal=Pharmacogenetics |volume=11 |issue= 4 |pages= 357-68 |year= 2001 |pmid= 11434514 |doi=  }}
*{{cite journal  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Zheng Z, Fang JL, Lazarus P |title=Glucuronidation: an important mechanism for detoxification of benzo[a]pyrene metabolites in aerodigestive tract tissues. |journal=Drug Metab. Dispos. |volume=30 |issue= 4 |pages= 397-403 |year= 2002 |pmid= 11901093 |doi=  }}
*{{cite journal  | author=Jinno H |title=Functional characterization of wild-type and variant (T202I and M59I) human UDP-glucuronosyltransferase 1A10 |journal=Drug Metab. Dispos. |volume=31 |issue= 5 |pages= 528–32 |year= 2003 |pmid= 12695339 |doi=10.1124/dmd.31.5.528  |name-list-format=vanc| author2=Saeki M  | author3=Tanaka-Kagawa T  | display-authors=3  | last4=Hanioka  | first4=N  | last5=Saito  | first5=Y  | last6=Ozawa  | first6=S  | last7=Ando  | first7=M  | last8=Shirao  | first8=K  | last9=Minami  | first9=H }}
*{{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  | author=Jinno H, Saeki M, Tanaka-Kagawa T, ''et al.'' |title=Functional characterization of wild-type and variant (T202I and M59I) human UDP-glucuronosyltransferase 1A10. |journal=Drug Metab. Dispos. |volume=31 |issue= 5 |pages= 528-32 |year= 2003 |pmid= 12695339 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{Glycosyltransferases}}
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Latest revision as of 02:21, 15 March 2018

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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 1-10 is an enzyme that in humans is encoded by the UGT1A10 gene.[1][2][3]

This gene encodes a UDP-glucuronosyltransferase, an enzyme of the glucuronidation pathway that transforms small lipophilic molecules, such as steroids, bilirubin, hormones, and drugs, into water-soluble, excretable metabolites. This gene is part of a complex locus that encodes several UDP-glucuronosyltransferases. The locus includes thirteen unique alternate first exons followed by four common exons. Four of the alternate first exons are considered pseudogenes. Each of the remaining nine 5' exons may be spliced to the four common exons, resulting in nine proteins with different N-termini and identical C-termini. Each first exon encodes the substrate binding site, and is regulated by its own promoter. The enzyme encoded by this gene has glucuronidase activity on mycophenolic acid, coumarins, and quinolines.[3]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]

[[File:
<imagemap> Image:IrinotecanPathway_WP229.png
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Irinotecan Pathway edit
  1. ↑ The interactive pathway map can be edited at WikiPathways: "IrinotecanPathway_WP46359".

References

  1. ↑ Mackenzie PI, Owens IS, Burchell B, Bock KW, Bairoch A, Belanger A, Fournel-Gigleux S, Green M, Hum DW, Iyanagi T, Lancet D, Louisot P, Magdalou J, Chowdhury JR, Ritter JK, Schachter H, Tephly TR, Tipton KF, Nebert DW (Oct 1997). "The UDP glycosyltransferase gene superfamily: recommended nomenclature update based on evolutionary divergence". Pharmacogenetics. 7 (4): 255–69. doi:10.1097/00008571-199708000-00001. PMID 9295054.
  2. ↑ Mojarrabi B, Mackenzie PI (Oct 1997). "The human UDP glucuronosyltransferase, UGT1A10, glucuronidates mycophenolic acid". Biochem Biophys Res Commun. 238 (3): 775–8. doi:10.1006/bbrc.1997.7388. PMID 9325166.
  3. ↑ 3.0 3.1 "Entrez Gene: UGT1A10 UDP glucuronosyltransferase 1 family, polypeptide A10".

Further reading



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