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Literature summary for 2.3.1.48 extracted from

  • Badri, K.R.; Zhou, Y.; Dhru, U.; Aramgam, S.; Schuger, L.
    Tension Induced/inhibited Proteins (TIPs) are novel partners of the histone acetyltransferase p300: TIPs SANT domain in p300 activity and TIP-6-induced adipogenesis (2008), Mol. Cell. Biol., 28, 6358-6372.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.48

Application

Application Comment Organism
molecular biology the results demonstrate the importance of TIPs in the recruitment of p300 to specific promoters and in the regulation of p300 HAT activity through the involvement of the SANT domain Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information TIP (tension-induced/inhibited) proteins are identified as interacting partners of p300. TIPs do not have intrinsic catalytic activity but they recruit p300 HAT activity. TIP-6 binds directly and indirectly to p300 and histone H4 (H4). Deletion of the SANT domain does not abolish TIP-6 interaction with p300 and H4 but eliminates direct TIP-6 binding to p300. Chromatin immunoprecipitation assays show the recruitment of TIP-6, TIP-6DELTASANT, and p300 to the PPARgamma2 promoter, but H3/H4 acetylation occurres only when p300 is directly associated with TIP-6 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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Source Tissue

Source Tissue Comment Organism Textmining
3T3-L1 cell
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 Mus musculus
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adipose tissue
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 Mus musculus
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NIH-3T3 cell
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 Mus musculus
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Synonyms

Synonyms Comment Organism
histone acetyltransferase
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 Mus musculus
p300
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 Mus musculus