WDR5

WD repeat domain 5
PDB rendering based on 2cnx.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2CNX​, 2CO0​, 2G99​, 2G9A​, 2GNQ​, 2H13​, 2H14​, 2H68​, 2H6K​, 2H6N​, 2H6Q​, 2H9L​, 2H9M​, 2H9N​, 2H9P​, 2O9K​, 3EG6​, 3EMH​, 3MXX​, 3N0D​, 3N0E​, 3P4F​, 3PSL​, 3SMR​, 3UR4​, 3UVK​, 3UVL​, 3UVM​, 3UVN​, 3UVO​, 4A7J​, 4CY1​, 4CY2​, 4ERQ​, 4ERY​, 4ERZ​, 4ES0​, 4ESG​, 4EWR​, 4GM3​, 4GM8​, 4GM9​, 4GMB​, 4IA9​, 4O45​, 4QL1​, 4Y7R​
Identifiers
Symbols	WDR5 ; BIG-3; CFAP89; SWD3
External IDs	OMIM: 609012 MGI: 2155884 HomoloGene: 59931 IUPHAR: 2831 ChEMBL: 1075317 GeneCards: WDR5 Gene
Gene ontology Molecular function • protein binding • histone methyltransferase activity (H3-K4 specific) • histone acetyltransferase activity (H4-K5 specific) • histone acetyltransferase activity (H4-K8 specific) • histone acetyltransferase activity (H4-K16 specific) Cellular component • histone acetyltransferase complex • nucleus • nucleoplasm • Ada2/Gcn5/Ada3 transcription activator complex • histone methyltransferase complex • Set1C/COMPASS complex • MLL1 complex Biological process • skeletal system development • chromatin organization • transcription, DNA-templated • neuron projection development • positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter • histone H3 acetylation • histone H4-K5 acetylation • histone H4-K8 acetylation • histone H4-K16 acetylation • histone H3-K4 methylation Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	11091	140858
Ensembl	ENSG00000196363	ENSMUSG00000026917
UniProt	P61964	P61965
RefSeq (mRNA)	NM_017588	NM_080848
RefSeq (protein)	NP_060058	NP_543124
Location (UCSC)	Chr 9: 134.14 – 134.16 Mb	Chr 2: 27.52 – 27.54 Mb
PubMed search

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

1. 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. "Entrez Gene: WDR5 WD repeat domain 5".
3. 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.
4. 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.
5. 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.
6. 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.