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{{ | '''Max-interacting transcriptional repressor MAD4''' is a [[protein]] that in humans is encoded by the ''MXD4'' [[gene]].<ref name="pmid8521822">{{cite journal |vauthors=Hurlin PJ, Queva C, Koskinen PJ, Steingrimsson E, Ayer DE, Copeland NG, Jenkins NA, Eisenman RN | title = Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation | journal = EMBO J | volume = 14 | issue = 22 | pages = 5646–59 |date=Jan 1996 | pmid = 8521822 | pmc = 394680 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MXD4 MAX dimerization protein 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10608| accessdate = }}</ref> | ||
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| summary_text = This gene is a member of the MAD gene family . The MAD genes encode basic helix-loop-helix-leucine zipper proteins that heterodimerize with MAX protein, forming a transcriptional repression complex. The MAD proteins compete for MAX binding with MYC, which heterodimerizes with MAX forming a transcriptional activation complex. Studies in rodents suggest that the MAD genes are tumor suppressors and contribute to the regulation of cell growth in differentiating tissues.<ref name="entrez">{{cite web | title = Entrez Gene: MXD4 MAX dimerization protein 4| url = | | summary_text = This gene is a member of the MAD gene family . The MAD genes encode basic helix-loop-helix-leucine zipper proteins that heterodimerize with MAX protein, forming a transcriptional repression complex. The MAD proteins compete for MAX binding with MYC, which heterodimerizes with MAX forming a transcriptional activation complex. Studies in rodents suggest that the MAD genes are tumor suppressors and contribute to the regulation of cell growth in differentiating tissues.<ref name="entrez">{{cite web | title = Entrez Gene: MXD4 MAX dimerization protein 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10608| accessdate = }}</ref> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
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| citations = | | citations = | ||
*{{cite journal | *{{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 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Marcotte R, Chen JM, Huard S, Wang E |title=c-Myc creates an activation loop by transcriptionally repressing its own functional inhibitor, hMad4, in young fibroblasts, a loop lost in replicatively senescent fibroblasts. |journal=J. Cell. Biochem. |volume=96 |issue= 5 |pages= 1071–85 |year= 2006 |pmid= 16167342 |doi= 10.1002/jcb.20503 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Pope SN, Lee IR |title=Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin. |journal=J. Steroid Biochem. Mol. Biol. |volume=94 |issue= 1-3 |pages= 203–8 |year= 2005 |pmid= 15862967 |doi= 10.1016/j.jsbmb.2005.01.007 }} | ||
*{{cite journal | *{{cite journal |vauthors=Hillier LW, Graves TA, Fulton RS, etal |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 }} | ||
*{{cite journal | *{{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 | *{{cite journal |vauthors=Jiang DJ, Yu HX, Hexige SY, etal |title=Human liver specific transcriptional factor [[TCP10L]] binds to MAD4. |journal=J. Biochem. Mol. Biol. |volume=37 |issue= 4 |pages= 402–7 |year= 2004 |pmid= 15469726 |doi= 10.5483/bmbrep.2004.37.4.402}} | ||
*{{cite journal | *{{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 | *{{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 | | *{{cite journal |vauthors=Kime L, Wright SC |title=Mad4 is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc. |journal=Biochem. J. |volume=370 |issue= Pt 1 |pages= 291–8 |year= 2003 |pmid= 12418961 |doi= 10.1042/BJ20021679 | pmc=1223147 }} | ||
*{{cite journal | *{{cite journal |vauthors=Cairo S, Merla G, Urbinati F, etal |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 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Billin AN, Eilers AL, Queva C, Ayer DE |title=Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36344–50 |year= 2000 |pmid= 10593926 |doi=10.1074/jbc.274.51.36344 }} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
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* {{MeshName|MXD4+protein,+human}} | * {{MeshName|MXD4+protein,+human}} | ||
{{NLM content}} | |||
{{Transcription factors|g1}} | |||
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[[Category:Transcription factors]] | [[Category:Transcription factors]] | ||
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{{gene-4-stub}} |
Revision as of 07:10, 4 September 2017
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Max-interacting transcriptional repressor MAD4 is a protein that in humans is encoded by the MXD4 gene.[1][2]
This gene is a member of the MAD gene family . The MAD genes encode basic helix-loop-helix-leucine zipper proteins that heterodimerize with MAX protein, forming a transcriptional repression complex. The MAD proteins compete for MAX binding with MYC, which heterodimerizes with MAX forming a transcriptional activation complex. Studies in rodents suggest that the MAD genes are tumor suppressors and contribute to the regulation of cell growth in differentiating tissues.[2]
References
- ↑ Hurlin PJ, Queva C, Koskinen PJ, Steingrimsson E, Ayer DE, Copeland NG, Jenkins NA, Eisenman RN (Jan 1996). "Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation". EMBO J. 14 (22): 5646–59. PMC 394680. PMID 8521822.
- ↑ 2.0 2.1 "Entrez Gene: MXD4 MAX dimerization protein 4".
Further reading
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Marcotte R, Chen JM, Huard S, Wang E (2006). "c-Myc creates an activation loop by transcriptionally repressing its own functional inhibitor, hMad4, in young fibroblasts, a loop lost in replicatively senescent fibroblasts". J. Cell. Biochem. 96 (5): 1071–85. doi:10.1002/jcb.20503. PMID 16167342.
- Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin". J. Steroid Biochem. Mol. Biol. 94 (1–3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967.
- Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Jiang DJ, Yu HX, Hexige SY, et al. (2004). "Human liver specific transcriptional factor TCP10L binds to MAD4". J. Biochem. Mol. Biol. 37 (4): 402–7. doi:10.5483/bmbrep.2004.37.4.402. PMID 15469726.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Kime L, Wright SC (2003). "Mad4 is regulated by a transcriptional repressor complex that contains Miz-1 and c-Myc". Biochem. J. 370 (Pt 1): 291–8. doi:10.1042/BJ20021679. PMC 1223147. PMID 12418961.
- Cairo S, Merla G, Urbinati F, et al. (2001). "WBSCR14, a gene mapping to the Williams--Beuren syndrome deleted region, is a new member of the Mlx transcription factor network". Hum. Mol. Genet. 10 (6): 617–27. doi:10.1093/hmg/10.6.617. PMID 11230181.
- Billin AN, Eilers AL, Queva C, Ayer DE (2000). "Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors". J. Biol. Chem. 274 (51): 36344–50. doi:10.1074/jbc.274.51.36344. PMID 10593926.
External links
- MXD4+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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