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 24-JAN-2024, entry version 152. 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, RC and 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}. Chromosome CC {ECO:0000250|UniProtKB:Q9NPI1}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000034085; -. DR PeptideAtlas; O88665; -. DR ProteomicsDB; 265378; -. DR Pumba; O88665; -. DR Antibodypedia; 14527; 261 antibodies from 32 providers. DR DNASU; 26992; -. DR Ensembl; ENSMUST00000034085.8; ENSMUSP00000034085.8; ENSMUSG00000031660.15. DR GeneID; 26992; -. DR KEGG; mmu:26992; -. DR UCSC; uc009mrn.2; mouse. DR AGR; MGI:1349766; -. 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; HQGHRER; -. DR OrthoDB; 1221506at2759; -. DR PhylomeDB; O88665; -. DR TreeFam; TF106439; -. DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation. DR BioGRID-ORCS; 26992; 5 hits in 86 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 285 other cell types or tissues. DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0000776; C:kinetochore; NAS:ComplexPortal. DR GO; GO:0016363; C:nuclear matrix; NAS: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; NAS: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; NAS:ComplexPortal. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; ISS:UniProtKB. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd05513; Bromo_brd7_like; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR021900; DUF3512. DR PANTHER; PTHR22881; BROMODOMAIN CONTAINING PROTEIN; 1. DR PANTHER; PTHR22881:SF12; BROMODOMAIN-CONTAINING PROTEIN 7; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF12024; DUF3512; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR Genevisible; O88665; MM. PE 1: Evidence at protein level; KW Acetylation; Bromodomain; Cell cycle; Chromosome; Coiled coil; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; 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 //