Contents

Search


Bromodomain-containing protein 7 (75 kDa bromodomain protein, protein CELTIX-1, BRD7, BP75, CELTIX1)

Function: - acts both as coactivator & as corepressor - may play a role in chromatin remodeling - activates Wnt signaling pathway - negatively regulates GSK3B (DVL1-dependent) - induces dephosphorylation of GSK3B at Y216 - down-regulates TRIM24-mediated activation of transcriptional activation by AR (putative) - increases histone H3 acetylation at Lys-9 (H3K9ac) - binds to the ESR1 promoter - recruits BRCA1 & POU2F1 to the ESR1 promoter - coactivator for TP53-mediated activation of transcription of a set of target genes - required for TP53-mediated cell-cycle arrest in response to oncogene activation - promotes acetylation of TP53 at Lys-382, & thus promotes efficient recruitment of TP53 to target promoters - inhibits cell cycle progression from G1 phase to S phase - identified in a complex with SMARCA4/BRG1, SMARCC1/BAF155, SMARCE1/BAF57, DPF2/BAF45D & ARID2, subunits of the SWI/SNF-B (PBAF) chromatin remodeling complex (putative) - interacts with TRIM24, PTPN13 & DVL1 - interacts with PTPN13, DVL, IRF2, HNRPUL1 - interacts with IRF2 & HNRPUL1 - interacts (via N-terminus) with TP53. interacts (via C-terminus) with EP300. interacts with BRCA1 - interacts (via bromo domain) with histone H3 (via N-terminus) acetylated at Lys-14 (H3K14ac) - low affinity for histone H3 acetylated at Lys-9 (H3K9ac) - has highest affinity for histone H3 that is acetylated both at Lys-9 (H3K9ac) & at Lys-14 (H3K14ac) has very low affinity for non-acetylated histone H3 - interacts (via bromo domain) with histone H4 (via N-terminus) acetylated at Lys-8 (H3K8ac) (in vitro) Structure: contains 1 bromo domain Compartment: nucleus (isoform 2) Alternative splicing: named isoforms=2

General

Bromodomain-containing protein

Properties

SIZE: MW = 74 kD entity length = 651 aa COMPARTMENT: cell nucleus MOTIF: lysine-rich region {3-91} MOTIF: lysine residue (SEVERAL) bromodomain {148-218} coiled coil {536-567}

Database Correlations

UniProt Q9NPI1 Pfam PF00439

References

UniProt :accession Q9NPI1