Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

TRIM24 links a non-canonical histone signature to breast cancer.

Tsai WW, Wang Z, Yiu TT, Akdemir KC, Xia W, Winter S, Tsai CY, Shi X, Schwarzer D, Plunkett W, Aronow B, Gozani O, Fischle W, Hung MC, Patel DJ, Barton MC

Recognition of modified histone species by distinct structural domains within 'reader' proteins plays a critical role in the regulation of gene expression. Readers that simultaneously recognize histones with multiple marks allow transduction of complex chromatin modification patterns into specific biological outcomes. Here we report that chromatin regulator tripartite motif-containing 24 (TRIM24) functions in humans as a reader of dual histone ... [more]

Nature Dec. 16, 2010; 468(7326);927-32 [Pubmed: 21164480]

Throughput

Low Throughput

Additional Notes

Crystal Structure Of Trim24 Phd-Bromo Complexed With Histone H3 peptide.

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
TRIM24 HIST1H3H	Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.	Tsai WW (2010)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

TRIM24

Gene Ontology Biological Process

Gene Ontology Molecular Function

chromatin binding [IDA]estrogen response element binding [IDA]lysine-acetylated histone binding [IDA]methylated histone binding [IDA]p53 binding [IPI]protein binding [IPI]receptor binding [TAS]transcription coactivator activity [IDA]ubiquitin-protein transferase activity [IDA]zinc ion binding [IDA]

Gene Ontology Cellular Component

HIST1H3H