An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

PHD finger protein 1 (PHF1) is a novel reader for histone H4R3 symmetric dimethylation and coordinates with PRMT5-WDR77/CRL4B complex to promote tumorigenesis.

Liu R, Gao J, Yang Y, Qiu R, Zheng Y, Huang W, Zeng Y, Hou Y, Wang S, Leng S, Feng D, Yu W, Sun G, Shi H, Teng X, Wang Y

Histone post-translational modifications regulate chromatin structure and function largely through interactions with effector proteins that often contain multiple histone-binding domains. PHF1 [plant homeodomain (PHD) finger protein 1], which contains two kinds of histone reader modules, a Tudor domain and two PHD fingers, is an essential factor for epigenetic regulation and genome maintenance. While significant progress has been made in characterizing ... [more]

Nucleic Acids Res. Jul. 27, 2018; 46(13);6608-6626 [Pubmed: 29846670]

Throughput

High Throughput

Curated By

BioGRID

Interaction Summary

PHF1

Gene Ontology Biological Process

Gene Ontology Molecular Function

methylated histone binding [IDA]sequence-specific DNA binding transcription factor activity [TAS]

Gene Ontology Cellular Component

HSPA4