wikidoc - User contributions [en]

TPM4

2018-03-16T05:21:24Z

81.104.142.198:

{{Underlinked|date=June 2016}}
{{Infobox_gene}}
'''[[Tropomyosin]] alpha-4 chain''' is a [[protein]] that in humans is encoded by the ''TPM4'' [[gene]].<ref name="pmid8641132">{{cite journal | vauthors = Wilton SD, Lim L, Dorosz SD, Gunn HC, Eyre HJ, Callen DF, Laing NG | title = Assignment of the human alpha-tropomyosin gene TPM4 to band 19p13.1 by fluorescence in situ hybridization | journal = Cytogenet Cell Genet | volume = 72 | issue = 4 | pages = 294–6 |date=Jul 1996 | pmid = 8641132 | pmc = | doi =10.1159/000134206 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TPM4 tropomyosin 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7171| accessdate = }}</ref>


{{PBB_Summary
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==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal |vauthors=Rasmussen HH, van Damme J, Puype M, etal |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960–9 |year= 1993 |pmid= 1286667 |doi=10.1002/elps.11501301199 }}
*{{cite journal | vauthors=MacLeod AR, Talbot K, Smillie LB, Houlker C |title=Characterization of a cDNA defining a gene family encoding TM30p1, a human fibroblast tropomyosin. |journal=J. Mol. Biol. |volume=194 |issue= 1 |pages= 1–10 |year= 1987 |pmid= 3612796 |doi=10.1016/0022-2836(87)90710-8 }}
*{{cite journal |vauthors=MacLeod AR, Houlker C, Reinach FC, etal |title=A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 23 |pages= 7835–9 |year= 1986 |pmid= 3865200 |doi=10.1073/pnas.82.23.7835 | pmc=390864 }}
*{{cite journal |vauthors=Lawrence B, Perez-Atayde A, Hibbard MK, etal |title=TPM3-ALK and TPM4-ALK oncogenes in inflammatory myofibroblastic tumors. |journal=Am. J. Pathol. |volume=157 |issue= 2 |pages= 377–84 |year= 2000 |pmid= 10934142 |doi= 10.1016/S0002-9440(10)64550-6| pmc=1850130 }}
*{{cite journal |vauthors=Meech SJ, McGavran L, Odom LF, etal |title=Unusual childhood extramedullary hematologic malignancy with natural killer cell properties that contains tropomyosin 4--anaplastic lymphoma kinase gene fusion |journal=Blood |volume=98 |issue= 4 |pages= 1209–16 |year= 2001 |pmid= 11493472 |doi=10.1182/blood.V98.4.1209 }}
*{{cite journal |vauthors=Yi J, Kloeker S, Jensen CC, etal |title=Members of the Zyxin family of LIM proteins interact with members of the p130Cas family of signal transducers |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9580–9 |year= 2002 |pmid= 11782456 |doi= 10.1074/jbc.M106922200 }}
*{{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 |vauthors=Gevaert K, Goethals M, Martens L, etal |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | vauthors=Lin KT, Lu RM, Tarn WY |title=The WW domain-containing proteins interact with the early spliceosome and participate in pre-mRNA splicing in vivo |journal=Mol. Cell. Biol. |volume=24 |issue= 20 |pages= 9176–85 |year= 2004 |pmid= 15456888 |doi= 10.1128/MCB.24.20.9176-9185.2004 | pmc=517884 }}
*{{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 |vauthors=Bruneel A, Labas V, Mailloux A, etal |title=Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis |journal=Proteomics |volume=5 |issue= 15 |pages= 3876–84 |year= 2006 |pmid= 16130169 |doi= 10.1002/pmic.200401239 }}
*{{cite journal |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
}}
{{refend}}


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{{Cytoskeletal Proteins}}

{{gene-19-stub}}

TKTL1

2018-03-15T02:46:53Z

81.104.142.198:

{{Infobox_gene}}
'''[[Transketolase]]-like protein 1''' is an [[enzyme]] with a catalytic function that in humans is encoded by the ''TKTL1'' [[gene]].<ref name="pmid8838793">{{cite journal |vauthors=Coy JF, Dubel S, Kioschis P, Thomas K, Micklem G, Delius H, Poustka A | title = Molecular cloning of tissue-specific transcripts of a transketolase-related gene: implications for the evolution of new vertebrate genes | journal = Genomics | volume = 32 | issue = 3 | pages = 309–16 |date=Feb 1997 | pmid = 8838793 | pmc = | doi = 10.1006/geno.1996.0124 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TKTL1 transketolase-like 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8277| accessdate = }}</ref>

{{PBB_Summary
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| summary_text =
}}

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA Cloning Using In Vitro Site-Specific Recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000 | pmc=310948 }}
*{{cite journal | author=Simpson JC |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 | pmc=1083732 |name-list-format=vanc| author2=Wellenreuther R | author3=Poustka A | display-authors=3 | last4=Pepperkok | first4=R | last5=Wiemann | first5=S }}
*{{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=Gerhard DS |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 |name-list-format=vanc| author2=Wagner L | author3=Feingold EA | display-authors=3 | last4=Shenmen | first4=CM | last5=Grouse | first5=LH | last6=Schuler | first6=G | last7=Klein | first7=SL | last8=Old | first8=S | last9=Rasooly | first9=R }}
*{{cite journal | author=Wiemann S |title=From ORFeome to Biology: A Functional Genomics Pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 |name-list-format=vanc| author2=Arlt D | author3=Huber W | display-authors=3 | last4=Wellenreuther | first4=R | last5=Schleeger | first5=S | last6=Mehrle | first6=A | last7=Bechtel | first7=S | last8=Sauermann | first8=M | last9=Korf | first9=U }}
*{{cite journal | author=Ross MT |title=The DNA sequence of the human X chromosome |journal=Nature |volume=434 |issue= 7031 |pages= 325–37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440 | pmc=2665286 |name-list-format=vanc| author2=Grafham DV | author3=Coffey AJ | display-authors=3 | last4=Scherer | first4=Steven | last5=McLay | first5=Kirsten | last6=Muzny | first6=Donna | last7=Platzer | first7=Matthias | last8=Howell | first8=Gareth R. | last9=Burrows | first9=Christine }}
*{{cite journal |vauthors=Coy JF, Dressler D, Wilde J, Schubert P |title=Mutations in the transketolase-like gene TKTL1: clinical implications for neurodegenerative diseases, diabetes and cancer |journal=[[Clinical Laboratory|Clin. Lab.]] |volume=51 |issue= 5–6 |pages= 257–73 |year= 2005 |pmid= 15991799 |doi= }}
*{{cite journal | author=Mehrle A |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 | pmc=1347501 |name-list-format=vanc| author2=Rosenfelder H | author3=Schupp I | display-authors=3 | last4=Del Val | first4=C | last5=Arlt | first5=D | last6=Hahne | first6=F | last7=Bechtel | first7=S | last8=Simpson | first8=J | last9=Hofmann | first9=O }}
*{{cite journal | author=Langbein S |title=Expression of transketolase TKTL1 predicts colon and urothelial cancer patient survival: Warburg effect reinterpreted |journal=Br. J. Cancer |volume=94 |issue= 4 |pages= 578–85 |year= 2006 |pmid= 16465194 |doi= 10.1038/sj.bjc.6602962 | pmc=2361175 |name-list-format=vanc| author2=Zerilli M | author3=Zur Hausen A | display-authors=3 | last4=Staiger | first4=W | last5=Rensch-Boschert | first5=K | last6=Lukan | first6=N | last7=Popa | first7=J | last8=Ternullo | first8=M P | last9=Steidler | first9=A }}
*{{cite journal | author=Staiger WI |title=Expression of the mutated transketolase TKTL1, a molecular marker in gastric cancer |journal=Oncol. Rep. |volume=16 |issue= 4 |pages= 657–61 |year= 2007 |pmid= 16969476 |doi= 10.3892/or.16.4.657|name-list-format=vanc| author2=Coy JF | author3=Grobholz R | display-authors=3 | last4=Hofheinz | first4=RD | last5=Lukan | first5=N | last6=Post | first6=S | last7=Schwarzbach | first7=MH | last8=Willeke | first8=F }}
*{{cite journal |vauthors=Zhang S, Yang JH, Guo CK, Cai PC |title=Gene silencing of TKTL1 by RNAi inhibits cell proliferation in human hepatoma cells |journal=Cancer Lett. |volume=253 |issue= 1 |pages= 108–14 |year= 2007 |pmid= 17321041 |doi= 10.1016/j.canlet.2007.01.010 }}
}}
{{refend}}


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{{gene-X-stub}}

UGT1A10

2018-03-15T02:21:34Z

81.104.142.198:

{{Infobox_gene}}
'''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>


{{PBB_Summary
| 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" />
}}

==Interactive pathway map==
{{IrinotecanPathway_WP229|highlight=UGT1A10}}

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{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 |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 |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 |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=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 |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 |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=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 |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 |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=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 |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=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=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 }}
}}
{{refend}}
{{Glycosyltransferases}}


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{{protein-stub}}

Carbohydrate-responsive element-binding protein

2018-03-07T21:56:18Z

81.104.142.198: /* Function */

{{Infobox_gene}}
'''Carbohydrate-responsive element-binding protein''' (ChREBP) also known as '''MLX-interacting protein-like''' (MLXIPL) is a [[protein]] that in humans is encoded by the ''MLXIPL'' [[gene]].<ref name="pmid9860302">{{cite journal | vauthors = Meng X, Lu X, Li Z, Green ED, Massa H, Trask BJ, Morris CA, Keating MT | title = Complete physical map of the common deletion region in Williams syndrome and identification and characterization of three novel genes | journal = Hum Genet | volume = 103 | issue = 5 | pages = 590–9 |date=Jan 1999 | pmid = 9860302 | pmc = | doi =10.1007/s004390050874 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MLXIPL MLX interacting protein-like| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51085| accessdate = }}</ref> The protein name derives from the protein's interaction with carbohydrate response element sequences of DNA.

== Function ==

This gene encodes a [[basic helix-loop-helix]] leucine zipper [[transcription factor]] of the [[Myc]] / [[MAX (gene)|Max]] / [[MXD1|Mad]] superfamily. This protein forms a heterodimeric complex and binds and activates, in a glucose-dependent manner, [[carbohydrate response element]] (ChoRE) motifs in the promoters of [[triglyceride]] synthesis genes.<ref name="entrez"/>

== Clinical significance ==

This gene is deleted in [[Williams syndrome|Williams-Beuren syndrome]], a multisystem developmental disorder caused by the deletion of contiguous genes at chromosome 7q11.23.<ref name="entrez"/>

== Interactions ==

MLXIPL has been shown to [[Protein-protein interaction|interact]] with [[MLX (gene)|MLX]].<ref name="pmid11230181">{{cite journal | vauthors = Cairo S, Merla G, Urbinati F, Ballabio A, Reymond A | title = WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network | journal = Hum. Mol. Genet. | volume = 10 | issue = 6 | pages = 617–27 |date=March 2001 | pmid = 11230181 | doi = 10.1093/hmg/10.6.617}}</ref>

== Role in glycolysis ==

ChREBP is translocated to the nucleus and binds to DNA after dephosphorylation of a p-Ser and a p-Thr residue by [[PP2A]], which itself is activated by [[Xylulose-5-phosphate]]. Xu5p is produced in the [[pentose phosphate pathway]] when levels of [[Glucose-6-phosphate]] are high (the cell has ample glucose). In the liver, ChREBP mediates activation of several regulatory enzymes of glycolysis and lipogenesis including L-type pyruvate kinase (L-PK), acetyl CoA carboxylase, and fatty acid synthase.

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
*{{cite journal | vauthors=de Luis O, Valero MC, Jurado LA |title=WBSCR14, a putative transcription factor gene deleted in Williams-Beuren syndrome: complete characterisation of the human gene and the mouse ortholog. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 3 |pages= 215–22 |year= 2000 |pmid= 10780788 |doi= 10.1038/sj.ejhg.5200435 }}
*{{cite journal | vauthors=Cairo S, Merla G, Urbinati F |title=WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network. |journal=Hum. Mol. Genet. |volume=10 |issue= 6 |pages= 617–27 |year= 2001 |pmid= 11230181 |doi=10.1093/hmg/10.6.617 |display-authors=etal}}
*{{cite journal | vauthors=Kawaguchi T, Takenoshita M, Kabashima T, Uyeda K |title=Glucose and cAMP regulate the L-type pyruvate kinase gene by phosphorylation/dephosphorylation of the carbohydrate response element binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 24 |pages= 13710–5 |year= 2002 |pmid= 11698644 |doi= 10.1073/pnas.231370798 | pmc=61106 }}
*{{cite journal | vauthors=Kawaguchi T, Osatomi K, Yamashita H |title=Mechanism for fatty acid "sparing" effect on glucose-induced transcription: regulation of carbohydrate-responsive element-binding protein by AMP-activated protein kinase. |journal=J. Biol. Chem. |volume=277 |issue= 6 |pages= 3829–35 |year= 2002 |pmid= 11724780 |doi= 10.1074/jbc.M107895200 |display-authors=etal}}
*{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal}}
*{{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}}
*{{cite journal | vauthors=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8 | pmc=395752 }}
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