Sandbox GGC1

From Proteopedia

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'''Histone chaperone ASF1A'''
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'''Histone H3.3'''
<StructureSection load='ASF1A' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='ASF1A' size='340' side='right' caption='Caption for this structure' scene=''>
This is a default text for your page '''Sandbox GGC1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
This is a default text for your page '''Sandbox GGC1'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/Q9Y294]. Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit
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[https://www.uniprot.org/uniprot/P84243]. The Variant [https://www.uniprot.org/uniprot/P84243 histone H3] replaces H3 in a range of nucleosomes in active genes. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling
== Disease ==
== Disease ==

Revision as of 13:57, 16 September 2020

Histone H3.3

Caption for this structure

Drag the structure with the mouse to rotate

References

1. H3C15 - Histone H3.2 - Homo sapiens (Human) - H3C15 gene & protein https://www.uniprot.org/uniprot/Q71DI3 (accessed Sep 15, 2020)

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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