3ur4
From Proteopedia
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref> | [[http://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref> | ||
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- | ==See Also== | ||
- | *[[WD-repeat protein 5|WD-repeat protein 5]] | ||
== References == | == References == | ||
<references/> | <references/> |
Revision as of 10:08, 8 November 2017
Crystal structure of human WD repeat domain 5 with compound
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Categories: Human | Al-Awar, R | Arrowsmith, C H | Bolshan, Y | Bountra, C | Brown, P | Chau, I | Dombrovski, L | Dong, A | Edwards, A M | Hajian, T | Hassani, A Allali | Nguyen, K T | Poda, G | Structural genomic | Schapira, M | Senisterra, G | Smil, D | Vedadi, M | Wasney, G A | Weigelt, J | Wernimont, A | Wu, H | Sgc | Transcription | Transcription-inhibitor complex | Wd repeat domain 5 | Wdr5