2lo3

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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=2lo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lo3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lo3 RCSB], [http://www.ebi.ac.uk/pdbsum/2lo3 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=2lo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lo3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lo3 RCSB], [http://www.ebi.ac.uk/pdbsum/2lo3 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/SGF73_YEAST SGF73_YEAST]] Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs).
==See Also==
==See Also==

Revision as of 15:29, 24 December 2014

Solution structure of Sgf73(59-102) zinc finger domain

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