BRD7_PONAB
ID BRD7_PONAB Reviewed; 651 AA.
AC Q5R8B0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Bromodomain-containing protein 7;
GN Name=BRD7;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts both as coactivator and as corepressor. May play a role
CC in chromatin remodeling. Activator of the Wnt signaling pathway in a
CC DVL1-dependent manner by negatively regulating the GSK3B
CC phosphotransferase activity. Induces dephosphorylation of GSK3B at
CC 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional
CC activation by AR. Transcriptional corepressor that down-regulates the
CC expression of target genes. Binds to target promoters, leading to
CC increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1
CC promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter. Coactivator
CC for TP53-mediated activation of transcription of a set of target genes.
CC Required for TP53-mediated cell-cycle arrest in response to oncogene
CC activation. Promotes acetylation of TP53 at 'Lys-382', and thereby
CC promotes efficient recruitment of TP53 to target promoters. Inhibits
CC cell cycle progression from G1 to S phase (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TRIM24, PTPN13 and DVL1. Identified in a
CC complex with SMARCA4/BRG1, SMARCC1/BAF155, SMARCE1/BAF57, DPF2/BAF45D
CC and ARID2, subunits of the SWI/SNF-B (PBAF) chromatin remodeling
CC complex. Interacts with IRF2 and HNRPUL1. Interacts (via N-terminus)
CC with TP53. Interacts (via C-terminus) with EP300. Interacts with BRCA1.
CC Interacts (via bromo domain) with histone H3 (via N-terminus)
CC acetylated at 'Lys-14' (H3K14ac). Has low affinity for histone H3
CC acetylated at 'Lys-9' (H3K9ac). Has the highest affinity for histone H3
CC that is acetylated both at 'Lys-9' (H3K9ac) and at 'Lys-14' (H3K14ac).
CC Has very low affinity for non-acetylated histone H3. Interacts (via
CC bromo domain) with histone H4 (via N-terminus) acetylated at 'Lys-8'
CC (H3K8ac) (in vitro) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; CR859843; CAH92000.1; -; mRNA.
DR AlphaFoldDB; Q5R8B0; -.
DR BMRB; Q5R8B0; -.
DR SMR; Q5R8B0; -.
DR STRING; 9601.ENSPPYP00000008289; -.
DR eggNOG; KOG1828; Eukaryota.
DR InParanoid; Q5R8B0; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.20.920.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR021900; DUF3512.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12024; DUF3512; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Bromodomain; Cell cycle; Coiled coil; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..651
FT /note="Bromodomain-containing protein 7"
FT /id="PRO_0000227666"
FT DOMAIN 148..218
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 35..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 536..567
FT /evidence="ECO:0000255"
FT MOTIF 65..96
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 90..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT MOD_RES 328
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88665"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88665"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 241
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 305
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 344
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT CROSSLNK 389
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
SQ SEQUENCE 651 AA; 74064 MW; 0C2850EA991F5643 CRC64;
MGKKHKKHKS DKHLYEEYVE KPLKLVLKVG GNEVTELSTG SSGHDSSLFE DKNDHDKHKD
RKRKKRKKGE KQIPGEEKGR KRRRVKEDKK KRDRDRVENE AEKDLQCHAP VRLDLPPEKP
LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK DPSAFFSFPV TDFIAPGYSM IIKHPMDFST
MKEKIKNNDY QSIEELKDNF KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL
KQSIDFMADL QKTRKQKDGT DTSQSGEDGG CWQREREDSG DAEAHASKSP SKENKKKDND
MLEDKFKSNN LEREQEQLDR IVKESGGKLT RRLVNSQCEF ERRKPDGTTT LGLLHPVDPI
VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNKVTPVL YLNYGPYSSY APHYDSTFAN
ISKDDSDLIY STYGEDSDLP SDFSIHEFLA TCQDYPYVMA DSLLDVLTKG GHSRTLQEME
MSLPEDEGHT RTLDTAKEME ITEVEPPGRL DSSTQDRLIA LKAVTNFGVP VEVFDSEEAE
IFQKKLDETT RLLRELQEAQ NERLSTRPPP NMICLLGPSY REMHLAEQVT NNLKELAQQV
TPGDIVSTYG VRKAMGISIP SPVMENNFVD LTEDTEEPKK TDVAECGPGG S
