WDR5: Difference between revisions
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{{ | '''WD repeat-containing protein 5''' is a [[protein]] that in humans is encoded by the ''WDR5'' [[gene]].<ref name="pmid11551928">{{cite journal |vauthors=Gori F, Divieti P, Demay MB | title = Cloning and characterization of a novel WD-40 repeat protein that dramatically accelerates osteoblastic differentiation | journal = J Biol Chem | volume = 276 | issue = 49 | pages = 46515–22 |date=Dec 2001 | pmid = 11551928 | pmc = | doi = 10.1074/jbc.M105757200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: WDR5 WD repeat domain 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11091| accessdate = }}</ref> | ||
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| summary_text = This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 7 WD repeats. Alternatively spliced transcript variants encoding the same protein have been identified.<ref name="entrez" | | summary_text = This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 7 WD repeats. Alternatively spliced transcript variants encoding the same protein have been identified.<ref name="entrez"/> | ||
}} | }} | ||
==Interactions== | |||
WDR5 has been shown to [[Protein-protein interaction|interact]] with [[Host cell factor C1]]<ref name=pmid15199122>{{cite journal |last=Yokoyama |first=Akihiko |authorlink= |author2=Wang Zhong |author3=Wysocka Joanna |author4=Sanyal Mrinmoy |author5=Aufiero Deborah J |author6=Kitabayashi Issay |author7=Herr Winship |author8=Cleary Michael L |date=Jul 2004 |title=Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression |journal=Mol. Cell. Biol. |volume=24 |issue=13 |pages=5639–49 |publisher= |location = United States| issn = 0270-7306| pmid = 15199122 |doi = 10.1128/MCB.24.13.5639-5649.2004 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=480881 }}</ref><ref name=pmid12670868>{{cite journal |last=Wysocka |first=Joanna |authorlink= |author2=Myers Michael P |author3=Laherty Carol D |author4=Eisenman Robert N |author5=Herr Winship |date=Apr 2003 |title=Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1 |journal=Genes Dev. |volume=17 |issue=7 |pages=896–911 |publisher= |location = United States| issn = 0890-9369| pmid = 12670868 |doi = 10.1101/gad.252103 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=196026 }}</ref> and [[MLL (gene)|MLL]].<ref name=pmid15199122/> It also interacts with the [[long non-coding RNA]] [[HOTTIP]].<ref name="pmid21423168">{{cite journal |vauthors=Wang KC, Yang YW, Liu B, Sanyal A, Corces-Zimmerman R, Chen Y, etal | title=A long noncoding RNA maintains active chromatin to coordinate homeotic gene expression. | journal=Nature | year= 2011 | volume= 472 | issue= 7341 | pages= 120–4 | pmid=21423168 | doi=10.1038/nature09819 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=21423168 }}</ref> | |||
WDR5 is a key determinant for [[MYC]] recruitment to [[chromatin]]<ref>{{cite journal | last1 = Thomas | first1 = L. R. | last2 = Tansey | first2 = W. P. | year = 2015 | title = Interaction with WDR5 Promotes Target Gene Recognition and Tumorigenesis by MYC | url = | journal = Molecular Cell | volume = 58 | issue = 3| pages = 1–13 | doi = 10.1016/j.molcel.2015.02.028 | pmid=25818646 | pmc=4427524}}</ref> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{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 |vauthors=Wysocka J, Myers MP, Laherty CD, etal |title=Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. |journal=Genes Dev. |volume=17 |issue= 7 |pages= 896–911 |year= 2003 |pmid= 12670868 |doi= 10.1101/gad.252103 | pmc=196026 }} | |||
*{{cite journal | *{{cite journal |vauthors=Gori F, Demay MB |title=BIG-3, a novel WD-40 repeat protein, is expressed in the developing growth plate and accelerates chondrocyte differentiation in vitro. |journal=Endocrinology |volume=145 |issue= 3 |pages= 1050–4 |year= 2004 |pmid= 14657013 |doi= 10.1210/en.2003-1314 }} | ||
*{{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=Yokoyama A, Wang Z, Wysocka J, etal |title=Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression. |journal=Mol. Cell. Biol. |volume=24 |issue= 13 |pages= 5639–49 |year= 2004 |pmid= 15199122 |doi= 10.1128/MCB.24.13.5639-5649.2004 | pmc=480881 }} | ||
*{{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=Andersen JS, Lam YW, Leung AK, etal |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 }} | ||
*{{cite journal | *{{cite journal |vauthors=Wysocka J, Swigut T, Milne TA, etal |title=WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. |journal=Cell |volume=121 |issue= 6 |pages= 859–72 |year= 2005 |pmid= 15960974 |doi= 10.1016/j.cell.2005.03.036 }} | ||
*{{cite journal | *{{cite journal |vauthors=Dou Y, Milne TA, Tackett AJ, etal |title=Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. |journal=Cell |volume=121 |issue= 6 |pages= 873–85 |year= 2005 |pmid= 15960975 |doi= 10.1016/j.cell.2005.04.031 }} | ||
*{{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=Gori F, Friedman L, Demay MB |title=Wdr5, a novel WD repeat protein, regulates osteoblast and chondrocyte differentiation in vivo. |journal=Journal of musculoskeletal & neuronal interactions |volume=5 |issue= 4 |pages= 338–9 |year= 2006 |pmid= 16340128 |doi= }} | ||
*{{cite journal | | *{{cite journal |vauthors=Lim J, Hao T, Shaw C, etal |title=A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration. |journal=Cell |volume=125 |issue= 4 |pages= 801–14 |year= 2006 |pmid= 16713569 |doi= 10.1016/j.cell.2006.03.032 }} | ||
*{{cite journal | *{{cite journal |vauthors=Ruthenburg AJ, Wang W, Graybosch DM, etal |title=Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 8 |pages= 704–12 |year= 2006 |pmid= 16829959 |doi= 10.1038/nsmb1119 }} | ||
*{{cite journal | *{{cite journal |vauthors=Couture JF, Collazo E, Trievel RC |title=Molecular recognition of histone H3 by the WD40 protein WDR5. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 8 |pages= 698–703 |year= 2006 |pmid= 16829960 |doi= 10.1038/nsmb1116 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Dou Y, Milne TA, Ruthenburg AJ, etal |title=Regulation of MLL1 H3K4 methyltransferase activity by its core components. |journal=Nat. Struct. Mol. Biol. |volume=13 |issue= 8 |pages= 713–9 |year= 2006 |pmid= 16878130 |doi= 10.1038/nsmb1128 }} | ||
*{{cite journal | *{{cite journal |vauthors=Schuetz A, Allali-Hassani A, Martín F, etal |title=Structural basis for molecular recognition and presentation of histone H3 by WDR5. |journal=EMBO J. |volume=25 |issue= 18 |pages= 4245–52 |year= 2006 |pmid= 16946699 |doi= 10.1038/sj.emboj.7601316 | pmc=1570438 }} | ||
*{{cite journal | *{{cite journal |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 }} | ||
*{{cite journal | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=11091}} | |||
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Revision as of 22:33, 17 September 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
Wikidata | |||||||
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WD repeat-containing protein 5 is a protein that in humans is encoded by the WDR5 gene.[1][2]
This gene encodes a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 7 WD repeats. Alternatively spliced transcript variants encoding the same protein have been identified.[2]
Interactions
WDR5 has been shown to interact with Host cell factor C1[3][4] and MLL.[3] It also interacts with the long non-coding RNA HOTTIP.[5] WDR5 is a key determinant for MYC recruitment to chromatin[6]
References
- ↑ Gori F, Divieti P, Demay MB (Dec 2001). "Cloning and characterization of a novel WD-40 repeat protein that dramatically accelerates osteoblastic differentiation". J Biol Chem. 276 (49): 46515–22. doi:10.1074/jbc.M105757200. PMID 11551928.
- ↑ 2.0 2.1 "Entrez Gene: WDR5 WD repeat domain 5".
- ↑ 3.0 3.1 Yokoyama, Akihiko; Wang Zhong; Wysocka Joanna; Sanyal Mrinmoy; Aufiero Deborah J; Kitabayashi Issay; Herr Winship; Cleary Michael L (Jul 2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Mol. Cell. Biol. United States. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. ISSN 0270-7306. PMC 480881. PMID 15199122.
- ↑ Wysocka, Joanna; Myers Michael P; Laherty Carol D; Eisenman Robert N; Herr Winship (Apr 2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. United States. 17 (7): 896–911. doi:10.1101/gad.252103. ISSN 0890-9369. PMC 196026. PMID 12670868.
- ↑ Wang KC, Yang YW, Liu B, Sanyal A, Corces-Zimmerman R, Chen Y, et al. (2011). "A long noncoding RNA maintains active chromatin to coordinate homeotic gene expression". Nature. 472 (7341): 120–4. doi:10.1038/nature09819. PMID 21423168.
- ↑ Thomas, L. R.; Tansey, W. P. (2015). "Interaction with WDR5 Promotes Target Gene Recognition and Tumorigenesis by MYC". Molecular Cell. 58 (3): 1–13. doi:10.1016/j.molcel.2015.02.028. PMC 4427524. PMID 25818646.
Further reading
- 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.
- Wysocka J, Myers MP, Laherty CD, et al. (2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
- Gori F, Demay MB (2004). "BIG-3, a novel WD-40 repeat protein, is expressed in the developing growth plate and accelerates chondrocyte differentiation in vitro". Endocrinology. 145 (3): 1050–4. doi:10.1210/en.2003-1314. PMID 14657013.
- 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.
- Yokoyama A, Wang Z, Wysocka J, et al. (2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Mol. Cell. Biol. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. PMC 480881. PMID 15199122.
- 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.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Wysocka J, Swigut T, Milne TA, et al. (2005). "WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development". Cell. 121 (6): 859–72. doi:10.1016/j.cell.2005.03.036. PMID 15960974.
- Dou Y, Milne TA, Tackett AJ, et al. (2005). "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF". Cell. 121 (6): 873–85. doi:10.1016/j.cell.2005.04.031. PMID 15960975.
- 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.
- Gori F, Friedman L, Demay MB (2006). "Wdr5, a novel WD repeat protein, regulates osteoblast and chondrocyte differentiation in vivo". Journal of musculoskeletal & neuronal interactions. 5 (4): 338–9. PMID 16340128.
- Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
- Ruthenburg AJ, Wang W, Graybosch DM, et al. (2006). "Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex". Nat. Struct. Mol. Biol. 13 (8): 704–12. doi:10.1038/nsmb1119. PMID 16829959.
- Couture JF, Collazo E, Trievel RC (2006). "Molecular recognition of histone H3 by the WD40 protein WDR5". Nat. Struct. Mol. Biol. 13 (8): 698–703. doi:10.1038/nsmb1116. PMID 16829960.
- Dou Y, Milne TA, Ruthenburg AJ, et al. (2006). "Regulation of MLL1 H3K4 methyltransferase activity by its core components". Nat. Struct. Mol. Biol. 13 (8): 713–9. doi:10.1038/nsmb1128. PMID 16878130.
- Schuetz A, Allali-Hassani A, Martín F, et al. (2006). "Structural basis for molecular recognition and presentation of histone H3 by WDR5". EMBO J. 25 (18): 4245–52. doi:10.1038/sj.emboj.7601316. PMC 1570438. PMID 16946699.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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