4fo0
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fo0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fo0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fo0 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fo0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fo0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fo0 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/ARP8_HUMAN ARP8_HUMAN]] Plays an important role in the functional organization of mitotic chromosomes. Exhibits low basal ATPase activity, and unable to polymerize. Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA reoplication and probably DNA repair. Required for the recruitment of INO80 (and probably the INO80 complex) to sites of DNA damage. Strongly prefer nucleosomes and H3-H4 tetramers over H2A-H2B dimers, suggesting it may act as a nucleosome recognition module within the complex. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 04:50, 25 December 2014
Human actin-related protein Arp8 in its ATP-bound state
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