BRD7_MOUSE
ID BRD7_MOUSE Reviewed; 651 AA.
AC O88665; Q3UQ56; Q3UU06; Q9CT78;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Bromodomain-containing protein 7;
DE AltName: Full=75 kDa bromodomain protein;
GN Name=Brd7; Synonyms=Bp75;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PTPN13, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10526152; DOI=10.1016/s0014-5793(99)01191-6;
RA Cuppen E., van Ham M., Pepers B., Wieringa B., Hendriks W.;
RT "Identification and molecular characterization of BP75, a novel
RT bromodomain-containing protein.";
RL FEBS Lett. 459:291-298(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-293 AND 478-651.
RC STRAIN=C57BL/6J; TISSUE=Aorta, Embryo, Fetal head, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, AND INTERACTION WITH DVL1.
RX PubMed=12941796;
RA Kim S., Lee J., Park J., Chung J.;
RT "BP75, bromodomain-containing M(r) 75,000 protein, binds dishevelled-1 and
RT enhances Wnt signaling by inactivating glycogen synthase kinase-3 beta.";
RL Cancer Res. 63:4792-4795(2003).
RN [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A
RP COMPLEX WITH SMARCA4/BRG1; SMARCE1/BAF57; DPF2/BAF45D; SMARCC1/BAF155 AND
RP ARID2.
RX PubMed=18809673; DOI=10.1074/jbc.m806061200;
RA Kaeser M.D., Aslanian A., Dong M.Q., Yates J.R. III, Emerson B.M.;
RT "BRD7, a novel PBAF-specific SWI/SNF subunit, is required for target gene
RT activation and repression in embryonic stem cells.";
RL J. Biol. Chem. 283:32254-32263(2008).
RN [5]
RP INTERACTION WITH TRIM24, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
RA Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J.,
RA Imamura M., Hatakeyama S.;
RT "TRIM24 mediates ligand-dependent activation of androgen receptor and is
RT repressed by a bromodomain-containing protein, BRD7, in prostate cancer
RT cells.";
RL Biochim. Biophys. Acta 1793:1828-1836(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279; SER-475; SER-482 AND
RP SER-483, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-328, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Acts both as coactivator and as corepressor. May play a role
CC in chromatin remodeling. Transcriptional corepressor that down-
CC regulates the expression of target genes. Binds to target promoters,
CC leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds
CC to the ESR1 promoter. Recruits BRCA1 and POU2F1 to the ESR1 promoter.
CC Coactivator for TP53-mediated activation of transcription of a set of
CC target genes. Required for TP53-mediated cell-cycle arrest in response
CC to oncogene activation. Promotes acetylation of TP53 at 'Lys-382', and
CC thereby promotes efficient recruitment of TP53 to target promoters.
CC Inhibits cell cycle progression from G1 to S phase (By similarity).
CC Activator of the Wnt signaling pathway in a DVL1-dependent manner by
CC negatively regulating the GSK3B phosphotransferase activity. Induces
CC dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated
CC activation of transcriptional activation by AR. {ECO:0000250,
CC ECO:0000269|PubMed:12941796, ECO:0000269|PubMed:18809673,
CC ECO:0000269|PubMed:19909775}.
CC -!- SUBUNIT: Interacts with IRF2 and HNRPUL1 (By similarity). Interacts
CC (via N-terminus) with TP53. Interacts (via C-terminus) with EP300.
CC Interacts with BRCA1. Interacts (via bromo domain) with histone H3 (via
CC N-terminus) acetylated at 'Lys-14' (H3K14ac). Has low affinity for
CC histone H3 acetylated at 'Lys-9' (H3K9ac). Has the highest affinity for
CC histone H3 that is acetylated both at 'Lys-9' (H3K9ac) and at 'Lys-14'
CC (H3K14ac). Has very low affinity for non-acetylated histone H3.
CC Interacts (via bromo domain) with histone H4 (via N-terminus)
CC acetylated at 'Lys-8' (H3K8ac) (in vitro) (By similarity). Interacts
CC with TRIM24, PTPN13 and DVL1. Identified in a complex with
CC SMARCA4/BRG1, SMARCC1/BAF155, SMARCE1/BAF57, DPF2/BAF45D and ARID2,
CC subunits of the SWI/SNF-B (PBAF) chromatin remodeling complex.
CC {ECO:0000250, ECO:0000269|PubMed:10526152, ECO:0000269|PubMed:12941796,
CC ECO:0000269|PubMed:18809673, ECO:0000269|PubMed:19909775}.
CC -!- INTERACTION:
CC O88665; P26450: Pik3r1; NbExp=11; IntAct=EBI-643930, EBI-641764;
CC O88665; O08908: Pik3r2; NbExp=4; IntAct=EBI-643930, EBI-643570;
CC O88665; Q64512: Ptpn13; NbExp=3; IntAct=EBI-643930, EBI-4284057;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10526152,
CC ECO:0000269|PubMed:19909775}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10526152}.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously from 10.5 to 18.5 dpc.
CC {ECO:0000269|PubMed:10526152}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE23823.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF084259; AAC33302.1; -; mRNA.
DR EMBL; AK004429; BAB23299.1; -; mRNA.
DR EMBL; AK138934; BAE23823.1; ALT_INIT; mRNA.
DR EMBL; AK142758; BAE25187.1; -; mRNA.
DR CCDS; CCDS22510.1; -.
DR RefSeq; NP_036177.1; NM_012047.2.
DR RefSeq; XP_017168329.1; XM_017312840.1.
DR AlphaFoldDB; O88665; -.
DR BMRB; O88665; -.
DR SMR; O88665; -.
DR BioGRID; 205094; 7.
DR ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR IntAct; O88665; 4.
DR MINT; O88665; -.
DR STRING; 10090.ENSMUSP00000034085; -.
DR ChEMBL; CHEMBL3822348; -.
DR iPTMnet; O88665; -.
DR PhosphoSitePlus; O88665; -.
DR EPD; O88665; -.
DR jPOST; O88665; -.
DR MaxQB; O88665; -.
DR PaxDb; O88665; -.
DR PeptideAtlas; O88665; -.
DR PRIDE; O88665; -.
DR ProteomicsDB; 265378; -.
DR Antibodypedia; 14527; 231 antibodies from 32 providers.
DR DNASU; 26992; -.
DR Ensembl; ENSMUST00000034085; ENSMUSP00000034085; ENSMUSG00000031660.
DR GeneID; 26992; -.
DR KEGG; mmu:26992; -.
DR UCSC; uc009mrn.2; mouse.
DR CTD; 29117; -.
DR MGI; MGI:1349766; Brd7.
DR VEuPathDB; HostDB:ENSMUSG00000031660; -.
DR eggNOG; KOG1828; Eukaryota.
DR GeneTree; ENSGT00950000183170; -.
DR HOGENOM; CLU_020704_0_1_1; -.
DR InParanoid; O88665; -.
DR OMA; PADDNSI; -.
DR OrthoDB; 439339at2759; -.
DR PhylomeDB; O88665; -.
DR TreeFam; TF106439; -.
DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR BioGRID-ORCS; 26992; 5 hits in 80 CRISPR screens.
DR ChiTaRS; Brd7; mouse.
DR PRO; PR:O88665; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O88665; protein.
DR Bgee; ENSMUSG00000031660; Expressed in undifferentiated genital tubercle and 281 other tissues.
DR Genevisible; O88665; MM.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IPI:MGI.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
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:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0035066; P:positive regulation of histone acetylation; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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 1: Evidence at protein 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_0000227665"
FT DOMAIN 148..218
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 34..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..316
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 MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT MOD_RES 328
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPI1"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 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 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"
FT CONFLICT 102
FT /note="D -> G (in Ref. 2; BAE23823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 651 AA; 74000 MW; 5D34B4F14FD51350 CRC64;
MGKKHKKHKS DRHFYEEYVE KPLKLVLKVG GSEVTELSTG SSGHDSSLFE DRSDHDKHKD
RKRKKRKKGE KQAPGEEKGR KRRRVKEDKK KRDRDRAENE VDRDLQCHVP IRLDLPPEKP
LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK DPSAFFSFPV TDFIAPGYSM IIKHPMDFST
MKEKIKNNDY QSIEELKDNF KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL
KQSIDFMSDL QKTRKQKERT DACQSGEDSG CWQREREDSG DAETQAFRSP AKDNKRKDKD
VLEDKWRSSN SEREHEQIER VVQESGGKLT RRLANSQCEF ERRKPDGTTT LGLLHPVDPI
VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNRVTPVL YLNYGPYSSY APHYDSTFAN
ISKDDSDLIY STYGEDSDLP NNFSISEFLA TCQDYPYVMA DSLLDVLTKG GHSRSLQDLD
MSSPEDEGQT RALDTAKEAE ITQIEPTGRL ESSSQDRLTA LQAVTTFGAP AEVFDSEEAE
VFQRKLDETT RLLRELQEAQ NERLSTRPPP NMICLLGPSY REMYLAEQVT NNLKELTQQV
TPGDVVSIHG VRKAMGISVP SPIVGNSFVD LTGECEEPKE TSTAECGPDA S
