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O88665

- BRD7_MOUSE

UniProt

O88665 - BRD7_MOUSE

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Protein

Bromodomain-containing protein 7

Gene
Brd7, Bp75
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. Transcriptional corepressor that down-regulates the expression of target genes. Binds to target promoters, leading to increased histone H3 acetylation at 'Lys-9' (H3K9ac). Binds to the ESR1 promoter. Recruits BRCA1 and 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', and thereby promotes efficient recruitment of TP53 to target promoters. Inhibits cell cycle progression from G1 to S phase By similarity. Activator of the Wnt signaling pathway in a DVL1-dependent manner by negatively regulating the GSK3B phosphotransferase activity. Induces dephosphorylation of GSK3B at 'Tyr-216'. Down-regulates TRIM24-mediated activation of transcriptional activation by AR.3 Publications

GO - Molecular functioni

  1. lysine-acetylated histone binding Source: UniProtKB
  2. p53 binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. transcription coactivator activity Source: UniProtKB
  5. transcription corepressor activity Source: UniProtKB
  6. transcription factor binding Source: MGI
  7. transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. negative regulation of cell proliferation Source: UniProtKB
  3. negative regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. positive regulation of histone acetylation Source: UniProtKB
  6. positive regulation of transcription, DNA-templated Source: UniProtKB
  7. regulation of transcription from RNA polymerase II promoter Source: Ensembl
  8. transcription, DNA-templated Source: UniProtKB-KW
  9. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Bromodomain-containing protein 7
Alternative name(s):
75 kDa bromodomain protein
Gene namesi
Name:Brd7
Synonyms:Bp75
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1349766. Brd7.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Bromodomain-containing protein 7PRO_0000227665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei279 – 2791Phosphoserine By similarity
Modified residuei328 – 3281N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiO88665.
PRIDEiO88665.

PTM databases

PhosphoSiteiO88665.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Developmental stagei

Expressed ubiquitously from 10.5 to 18.5 dpc.1 Publication

Gene expression databases

ArrayExpressiO88665.
BgeeiO88665.
CleanExiMM_BRD7.
GenevestigatoriO88665.

Interactioni

Subunit structurei

Interacts with IRF2 and HNRPUL1 By similarity. 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). Has low affinity for histone H3 acetylated at 'Lys-9' (H3K9ac). Has the highest affinity for histone H3 that is acetylated both at 'Lys-9' (H3K9ac) and 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) By similarity. Interacts with TRIM24, PTPN13 and DVL1. Identified in a complex with SMARCA4/BRG1, SMARCC1/BAF155, SMARCE1/BAF57, DPF2/BAF45D and ARID2, subunits of the SWI/SNF-B (PBAF) chromatin remodeling complex.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Pik3r1P2645011EBI-643930,EBI-641764
Pik3r2O089084EBI-643930,EBI-643570
Ptpn13Q645123EBI-643930,EBI-4284057

Protein-protein interaction databases

BioGridi205094. 4 interactions.
IntActiO88665. 4 interactions.
MINTiMINT-1704124.

Structurei

3D structure databases

ProteinModelPortaliO88665.
SMRiO88665. Positions 129-238, 338-393.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini148 – 21871BromoAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili536 – 56732 Reviewed predictionAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi65 – 9632Nuclear localization signal By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi57 – 9135Lys-richAdd
BLAST

Sequence similaritiesi

Contains 1 bromo domain.

Keywords - Domaini

Bromodomain, Coiled coil

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00530000063939.
HOGENOMiHOG000070022.
HOVERGENiHBG071934.
InParanoidiO88665.
KOiK11723.
OMAiGDIVSTY.
OrthoDBiEOG7D2FDM.
PhylomeDBiO88665.
TreeFamiTF106439.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
InterProiIPR001487. Bromodomain.
IPR021900. DUF3512.
[Graphical view]
PfamiPF00439. Bromodomain. 1 hit.
PF12024. DUF3512. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
PROSITEiPS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88665-1 [UniParc]FASTAAdd to Basket

« Hide

MGKKHKKHKS DRHFYEEYVE KPLKLVLKVG GSEVTELSTG SSGHDSSLFE    50
DRSDHDKHKD RKRKKRKKGE KQAPGEEKGR KRRRVKEDKK KRDRDRAENE 100
VDRDLQCHVP IRLDLPPEKP LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK 150
DPSAFFSFPV TDFIAPGYSM IIKHPMDFST MKEKIKNNDY QSIEELKDNF 200
KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL KQSIDFMSDL 250
QKTRKQKERT DACQSGEDSG CWQREREDSG DAETQAFRSP AKDNKRKDKD 300
VLEDKWRSSN SEREHEQIER VVQESGGKLT RRLANSQCEF ERRKPDGTTT 350
LGLLHPVDPI VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNRVTPVL 400
YLNYGPYSSY APHYDSTFAN ISKDDSDLIY STYGEDSDLP NNFSISEFLA 450
TCQDYPYVMA DSLLDVLTKG GHSRSLQDLD MSSPEDEGQT RALDTAKEAE 500
ITQIEPTGRL ESSSQDRLTA LQAVTTFGAP AEVFDSEEAE VFQRKLDETT 550
RLLRELQEAQ NERLSTRPPP NMICLLGPSY REMYLAEQVT NNLKELTQQV 600
TPGDVVSIHG VRKAMGISVP SPIVGNSFVD LTGECEEPKE TSTAECGPDA 650
S 651
Length:651
Mass (Da):74,000
Last modified:November 1, 1998 - v1
Checksum:i5D34B4F14FD51350
GO

Sequence cautioni

The sequence BAE23823.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021D → G in BAE23823. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF084259 mRNA. Translation: AAC33302.1.
AK004429 mRNA. Translation: BAB23299.1.
AK138934 mRNA. Translation: BAE23823.1. Different initiation.
AK142758 mRNA. Translation: BAE25187.1.
CCDSiCCDS22510.1.
RefSeqiNP_036177.1. NM_012047.2.
UniGeneiMm.5400.

Genome annotation databases

EnsembliENSMUST00000034085; ENSMUSP00000034085; ENSMUSG00000031660.
GeneIDi26992.
KEGGimmu:26992.
UCSCiuc009mrn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF084259 mRNA. Translation: AAC33302.1 .
AK004429 mRNA. Translation: BAB23299.1 .
AK138934 mRNA. Translation: BAE23823.1 . Different initiation.
AK142758 mRNA. Translation: BAE25187.1 .
CCDSi CCDS22510.1.
RefSeqi NP_036177.1. NM_012047.2.
UniGenei Mm.5400.

3D structure databases

ProteinModelPortali O88665.
SMRi O88665. Positions 129-238, 338-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205094. 4 interactions.
IntActi O88665. 4 interactions.
MINTi MINT-1704124.

PTM databases

PhosphoSitei O88665.

Proteomic databases

PaxDbi O88665.
PRIDEi O88665.

Protocols and materials databases

DNASUi 26992.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034085 ; ENSMUSP00000034085 ; ENSMUSG00000031660 .
GeneIDi 26992.
KEGGi mmu:26992.
UCSCi uc009mrn.2. mouse.

Organism-specific databases

CTDi 29117.
MGIi MGI:1349766. Brd7.

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00530000063939.
HOGENOMi HOG000070022.
HOVERGENi HBG071934.
InParanoidi O88665.
KOi K11723.
OMAi GDIVSTY.
OrthoDBi EOG7D2FDM.
PhylomeDBi O88665.
TreeFami TF106439.

Miscellaneous databases

NextBioi 304935.
PROi O88665.
SOURCEi Search...

Gene expression databases

ArrayExpressi O88665.
Bgeei O88665.
CleanExi MM_BRD7.
Genevestigatori O88665.

Family and domain databases

Gene3Di 1.20.920.10. 1 hit.
InterProi IPR001487. Bromodomain.
IPR021900. DUF3512.
[Graphical view ]
Pfami PF00439. Bromodomain. 1 hit.
PF12024. DUF3512. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00297. BROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF47370. SSF47370. 1 hit.
PROSITEi PS50014. BROMODOMAIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and molecular characterization of BP75, a novel bromodomain-containing protein."
    Cuppen E., van Ham M., Pepers B., Wieringa B., Hendriks W.
    FEBS Lett. 459:291-298(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PTPN13, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Strain: BALB/c.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-293 AND 478-651.
    Strain: C57BL/6J.
    Tissue: Aorta, Embryo, Fetal head and Vein.
  3. "BP75, bromodomain-containing M(r) 75,000 protein, binds dishevelled-1 and enhances Wnt signaling by inactivating glycogen synthase kinase-3 beta."
    Kim S., Lee J., Park J., Chung J.
    Cancer Res. 63:4792-4795(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DVL1.
  4. "BRD7, a novel PBAF-specific SWI/SNF subunit, is required for target gene activation and repression in embryonic stem cells."
    Kaeser M.D., Aslanian A., Dong M.Q., Yates J.R. III, Emerson B.M.
    J. Biol. Chem. 283:32254-32263(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH SMARCA4/BRG1; SMARCE1/BAF57; DPF2/BAF45D; SMARCC1/BAF155 AND ARID2.
  5. "TRIM24 mediates ligand-dependent activation of androgen receptor and is repressed by a bromodomain-containing protein, BRD7, in prostate cancer cells."
    Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N., Tanaka J., Imamura M., Hatakeyama S.
    Biochim. Biophys. Acta 1793:1828-1836(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM24, FUNCTION, SUBCELLULAR LOCATION.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiBRD7_MOUSE
AccessioniPrimary (citable) accession number: O88665
Secondary accession number(s): Q3UQ56, Q3UU06, Q9CT78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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