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O88665 (BRD7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bromodomain-containing protein 7
Alternative name(s):
75 kDa bromodomain protein
Gene names
Name:Brd7
Synonyms:Bp75
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length651 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.4 Ref.5

Subunit structure

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. Ref.1 Ref.3 Ref.4 Ref.5

Subcellular location

Nucleus Ref.1 Ref.5.

Tissue specificity

Ubiquitous. Ref.1

Developmental stage

Expressed ubiquitously from 10.5 to 18.5 dpc. Ref.1

Sequence similarities

Contains 1 bromo domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   DiseaseTumor suppressor
   DomainBromodomain
Coiled coil
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of G1/S transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of histone acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Inferred from physical interaction Ref.1. Source: MGI

   Molecular_functionlysine-acetylated histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

p53 binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.5. Source: UniProtKB

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.5. Source: UniProtKB

transcription factor binding

Inferred from sequence alignment PubMed 11025449. Source: MGI

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 651651Bromodomain-containing protein 7
PRO_0000227665

Regions

Domain148 – 21871Bromo
Coiled coil536 – 56732 Potential
Motif65 – 9632Nuclear localization signal By similarity
Compositional bias57 – 9135Lys-rich

Amino acid modifications

Modified residue2791Phosphoserine By similarity
Modified residue3281N6-acetyllysine Ref.6

Experimental info

Sequence conflict1021D → G in BAE23823. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88665 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 5D34B4F14FD51350

FASTA65174,000
        10         20         30         40         50         60 
MGKKHKKHKS DRHFYEEYVE KPLKLVLKVG GSEVTELSTG SSGHDSSLFE DRSDHDKHKD 

        70         80         90        100        110        120 
RKRKKRKKGE KQAPGEEKGR KRRRVKEDKK KRDRDRAENE VDRDLQCHVP IRLDLPPEKP 

       130        140        150        160        170        180 
LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK DPSAFFSFPV TDFIAPGYSM IIKHPMDFST 

       190        200        210        220        230        240 
MKEKIKNNDY QSIEELKDNF KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL 

       250        260        270        280        290        300 
KQSIDFMSDL QKTRKQKERT DACQSGEDSG CWQREREDSG DAETQAFRSP AKDNKRKDKD 

       310        320        330        340        350        360 
VLEDKWRSSN SEREHEQIER VVQESGGKLT RRLANSQCEF ERRKPDGTTT LGLLHPVDPI 

       370        380        390        400        410        420 
VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNRVTPVL YLNYGPYSSY APHYDSTFAN 

       430        440        450        460        470        480 
ISKDDSDLIY STYGEDSDLP NNFSISEFLA TCQDYPYVMA DSLLDVLTKG GHSRSLQDLD 

       490        500        510        520        530        540 
MSSPEDEGQT RALDTAKEAE ITQIEPTGRL ESSSQDRLTA LQAVTTFGAP AEVFDSEEAE 

       550        560        570        580        590        600 
VFQRKLDETT RLLRELQEAQ NERLSTRPPP NMICLLGPSY REMYLAEQVT NNLKELTQQV 

       610        620        630        640        650 
TPGDVVSIHG VRKAMGISVP SPIVGNSFVD LTGECEEPKE TSTAECGPDA S 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084259 mRNA. Translation: AAC33302.1.
AK004429 mRNA. Translation: BAB23299.1.
AK138934 mRNA. Translation: BAE23823.1. Different initiation.
AK142758 mRNA. Translation: BAE25187.1.
CCDSCCDS22510.1.
RefSeqNP_036177.1. NM_012047.2.
UniGeneMm.5400.

3D structure databases

ProteinModelPortalO88665.
SMRO88665. Positions 129-238, 338-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205094. 4 interactions.
IntActO88665. 4 interactions.
MINTMINT-1704124.

PTM databases

PhosphoSiteO88665.

Proteomic databases

PaxDbO88665.
PRIDEO88665.

Protocols and materials databases

DNASU26992.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034085; ENSMUSP00000034085; ENSMUSG00000031660.
GeneID26992.
KEGGmmu:26992.
UCSCuc009mrn.2. mouse.

Organism-specific databases

CTD29117.
MGIMGI:1349766. Brd7.

Phylogenomic databases

eggNOGCOG5076.
GeneTreeENSGT00530000063939.
HOGENOMHOG000070022.
HOVERGENHBG071934.
InParanoidO88665.
KOK11723.
OMAGDIVSTY.
OrthoDBEOG7D2FDM.
PhylomeDBO88665.
TreeFamTF106439.

Gene expression databases

ArrayExpressO88665.
BgeeO88665.
CleanExMM_BRD7.
GenevestigatorO88665.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
InterProIPR001487. Bromodomain.
IPR021900. DUF3512.
[Graphical view]
PfamPF00439. Bromodomain. 1 hit.
PF12024. DUF3512. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
PROSITEPS50014. BROMODOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio304935.
PROO88665.
SOURCESearch...

Entry information

Entry nameBRD7_MOUSE
AccessionPrimary (citable) accession number: O88665
Secondary accession number(s): Q3UQ56, Q3UU06, Q9CT78
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot