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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> | ||
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==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
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*{{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.
This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it. |