Sandbox GGC1

From Proteopedia

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'''Histone H3.2'''
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'''Histone chaperone ASF1A'''
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<StructureSection load='6ATF' size='340' side='right' caption='Caption for this structure' scene=''>
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<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.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/Q71DI3 Core component of nucleosome]. 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.
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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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== Disease ==
== Disease ==

Revision as of 13:33, 16 September 2020

Histone chaperone ASF1A

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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