The domain within your query sequence starts at position 331 and ends at position 626; the E-value for the Noc2 domain shown below is 1.8e-128.
AFLGPILKQMYIMYVRNCKFTSPSTLPLISFMQRTLTEMLALDPSVSYQHAFLYIRQLAV HLRNAMTAGKKETHQSVYNWQYVHCLYLWCRVLSTLGSSEILQPLLYPLSQIIIGCIKLL PTARFYPLRMHCVRALTLLSQTIGTFIPVLPFILEIFQQVDFNRRPGRMSSKPINFSVIL KLSSTNLQEKAYRDGLLEQLCDLTLEYLHSQAHSIAFPELVLPTVLQLKSFLRECKVANY CRQVRQLLEKVQENAQHIQSLRQSATFSVSDQMAVDAWEKQVREEGTPLTRYYGHW
Noc2 |
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PFAM accession number: | PF03715 |
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Interpro abstract (IPR005343): | In Saccharomyces cerevisiae, Noc2 forms a nucleolar complex with Mak21 that binds to 90S and 66S pre-ribosomes. It also forms a nuclear complex with Noc3 that binds to 66S pre-ribosomes [ (PUBMED:11371346) ]. Both complexes mediate intranuclear transport of ribosomal precursors [ (PUBMED:11371346) ]. In humans, Noc2 (also known as NIR) acts as an inhibitor of histone acetyltransferase activity; prevents acetylation of all core histones by the EP300/p300 histone acetyltransferase at p53/TP53-regulated target promoters in a histone deacetylases (HDAC)-independent manner. It also acts as a transcription corepressor of p53/TP53- and TP63-mediated transactivation of the p21/CDKN1A promoter. It is involved in the regulation of p53/TP53-dependent apoptosis [ (PUBMED:16322561) (PUBMED:20123734) (PUBMED:20959462) ]. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Noc2