WDR5

WDR5
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, 5EAL, 5EAP, 5EAR, 4QQE, 5EAM
Identifiers
Aliases	WDR5 , BIG-3, CFAP89, SWD3, WD repeat-containing protein 5, WD repeat domain 5
External IDs	OMIM: 609012 MGI: 2155884 HomoloGene: 59931 GeneCards: WDR5
Gene location (Human) Chr. Chromosome 9 (human) [1] Band 9q34.2 Start 134,135,365 bp [1] End 134,159,968 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2|2 A3 Start 27,405,169 bp [2] End 27,426,547 bp [2]
RNA expression pattern Bgee Top expressed in sperm gastrocnemius muscle cerebellar hemisphere anterior pituitary secondary oocyte Right lobe of liver Ganglionic eminence Body of pancreas body of stomach left uterine tube More reference expression data BioGPS More reference expression data
Gene ontology Molecular function histone methyltransferase activity (H3-K4 specific) histone acetyltransferase activity (H4-K8 specific) histone acetyltransferase activity (H4-K5 specific) methylated histone binding GO:0001948 protein binding histone acetyltransferase activity (H4-K16 specific) histone-lysine N-methyltransferase activity histone binding Cellular component Set1C/COMPASS complex intracellular anatomical structure nucleoplasm MLL1 complex MLL3/4 complex histone acetyltransferase complex nucleus histone methyltransferase complex ciliary basal body Biological process skeletal system development regulation of transcription, DNA-templated transcription, DNA-templated histone H4-K5 acetylation histone H3-K4 methylation histone H3 acetylation histone H4-K16 acetylation neuron projection development histone H4-K8 acetylation cilium assembly post-translational protein modification regulation of megakaryocyte differentiation chromatin organization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11091	140858
Ensembl	ENSG00000196363	ENSMUSG00000026917
UniProt	P61964	P61965
RefSeq (mRNA)	NM_017588 NM_052821	NM_080848
RefSeq (protein)	NP_060058 NP_438172	NP_543124
Location (UCSC)	Chr 9: 134.14 – 134.16 Mb	Chr 2: 27.41 – 27.43 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

WD repeat-containing protein 5 is a protein that in humans is encoded by the WDR5 gene. ^{[5] [6]}

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. ^[6]

Interactions

WDR5 has been shown to interact with Host cell factor C1 ^{[7] [8]} and MLL. ^[7] It also interacts with the long non-coding RNA HOTTIP and to the lncRNA NeST. ^{[9] [10]} WDR5 is a key determinant for MYC recruitment to chromatin ^[11]

References

1. GRCh38: Ensembl release 89: ENSG00000196363 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026917 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: WDR5 WD repeat domain 5".
7. 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. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. ISSN   0270-7306. PMC   480881 . PMID   15199122.
8. 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. 17 (7): 896–911. doi:10.1101/gad.252103. ISSN   0890-9369. PMC   196026 . PMID   12670868.
9. Wells, Alexandria C.; Pobezinskaya, Elena L.; Pobezinsky, Leonid A. (April 2020). "Non-coding RNAs in CD8 T cell biology". Molecular Immunology. 120: 67–73. doi:10.1016/j.molimm.2020.01.023. ISSN   1872-9142. PMC   7093237 . PMID   32085976.
10. 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. Bibcode:2011Natur.472..120W. doi:10.1038/nature09819. PMC   3670758 . PMID   21423168.
11. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.
• 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. S2CID   17521631.
• 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. S2CID   14717470.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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. S2CID   13709685.
• 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. PMC   4698793 . 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. S2CID   26165068.
• 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. S2CID   12849159.
• 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.
• Bryan AF, Wang J, Howard GC, et al. (2020). "WDR5 is a conserved regulator of protein synthesis gene expression". Nucleic Acids Research. 48 (6): 2924–2941. doi: 10.1093/nar/gkaa051 . PMC   7102967 . PMID   31996893.