Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

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

Low Throughput

Additional Notes

assayed using ChIP/re-ChIP (i.e. sequential chromatin immunoprecipitation)

Curated By

BioGRID

Interaction Summary

PRMT5

Gene Ontology Biological Process

Gene Ontology Molecular Function

core promoter sequence-specific DNA binding [ISS]histone-arginine N-methyltransferase activity [IBA]methyltransferase activity [IDA]protein binding [IPI]protein-arginine omega-N symmetric methyltransferase activity [IMP]ribonucleoprotein complex binding [IPI]transcription corepressor activity [ISS]

Gene Ontology Cellular Component

DDB1