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4twi
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=4twi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4twi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4twi RCSB], [http://www.ebi.ac.uk/pdbsum/4twi 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=4twi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4twi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4twi RCSB], [http://www.ebi.ac.uk/pdbsum/4twi PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NPD1_ARCFU NPD1_ARCFU]] NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affinity, thereby repressing transcription (By similarity).<ref>PMID:10841563</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 10:40, 25 December 2014
The structure of Sir2Af1 bound to a succinylated histone peptide
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