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Q9NPI1

- BRD7_HUMAN

UniProt

Q9NPI1 - BRD7_HUMAN

Protein

Bromodomain-containing protein 7

Gene

BRD7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Acts both as coactivator and as corepressor. May play a role in chromatin remodeling. 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 By similarity. 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 similarity5 Publications

    GO - Molecular functioni

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

    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: MGI
    8. transcription, DNA-templated Source: UniProtKB-KW
    9. Wnt signaling pathway Source: UniProtKB-KW

    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
    Protein CELTIX-1
    Gene namesi
    Name:BRD7
    Synonyms:BP75, CELTIX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:14310. BRD7.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA25417.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 651651Bromodomain-containing protein 7PRO_0000227664Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei279 – 2791Phosphoserine3 Publications
    Modified residuei328 – 3281N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NPI1.
    PaxDbiQ9NPI1.
    PRIDEiQ9NPI1.

    PTM databases

    PhosphoSiteiQ9NPI1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NPI1.
    BgeeiQ9NPI1.
    CleanExiHS_BRD7.
    GenevestigatoriQ9NPI1.

    Organism-specific databases

    HPAiCAB046458.

    Interactioni

    Subunit structurei

    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 By similarity. Interacts with IRF2 and HNRPUL1. 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 similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EP300Q094723EBI-711221,EBI-447295
    HNRNPUL1Q9BUJ25EBI-711221,EBI-1018153
    TP53P046378EBI-711221,EBI-366083

    Protein-protein interaction databases

    BioGridi118883. 36 interactions.
    DIPiDIP-32509N.
    IntActiQ9NPI1. 26 interactions.
    MINTiMINT-1383082.
    STRINGi9606.ENSP00000378180.

    Structurei

    Secondary structure

    1
    651
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi133 – 14816
    Helixi152 – 1543
    Beta strandi156 – 1583
    Turni162 – 1643
    Beta strandi165 – 1673
    Helixi168 – 1714
    Helixi178 – 1858
    Turni186 – 1883
    Helixi193 – 20917
    Beta strandi213 – 2164
    Helixi217 – 23519

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I7KNMR-A129-236[»]
    ProteinModelPortaliQ9NPI1.
    SMRiQ9NPI1. Positions 129-238, 338-393.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NPI1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini148 – 21871BromoPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili536 – 56732Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi65 – 9632Nuclear localization signal1 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 9189Lys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 bromo domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Bromodomain, Coiled coil

    Phylogenomic databases

    eggNOGiCOG5076.
    HOGENOMiHOG000070022.
    HOVERGENiHBG071934.
    KOiK11723.
    OMAiGDIVSTY.
    OrthoDBiEOG7D2FDM.
    PhylomeDBiQ9NPI1.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NPI1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGKKHKKHKS DKHLYEEYVE KPLKLVLKVG GNEVTELSTG SSGHDSSLFE    50
    DKNDHDKHKD RKRKKRKKGE KQIPGEEKGR KRRRVKEDKK KRDRDRVENE 100
    AEKDLQCHAP VRLDLPPEKP LTSSLAKQEE VEQTPLQEAL NQLMRQLQRK 150
    DPSAFFSFPV TDFIAPGYSM IIKHPMDFST MKEKIKNNDY QSIEELKDNF 200
    KLMCTNAMIY NKPETIYYKA AKKLLHSGMK ILSQERIQSL KQSIDFMADL 250
    QKTRKQKDGT DTSQSGEDGG CWQREREDSG DAEAHAFKSP SKENKKKDKD 300
    MLEDKFKSNN LEREQEQLDR IVKESGGKLT RRLVNSQCEF ERRKPDGTTT 350
    LGLLHPVDPI VGEPGYCPVR LGMTTGRLQS GVNTLQGFKE DKRNKVTPVL 400
    YLNYGPYSSY APHYDSTFAN ISKDDSDLIY STYGEDSDLP SDFSIHEFLA 450
    TCQDYPYVMA DSLLDVLTKG GHSRTLQEME MSLPEDEGHT RTLDTAKEME 500
    ITEVEPPGRL DSSTQDRLIA LKAVTNFGVP VEVFDSEEAE IFQKKLDETT 550
    RLLRELQEAQ NERLSTRPPP NMICLLGPSY REMHLAEQVT NNLKELAQQV 600
    TPGDIVSTYG VRKAMGISIP SPVMENNFVD LTEDTEEPKK TDVAECGPGG 650
    S 651
    Length:651
    Mass (Da):74,139
    Last modified:October 1, 2000 - v1
    Checksum:i29B7947644C215E7
    GO
    Isoform 2 (identifier: Q9NPI1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         500-500: E → EQ

    Show »
    Length:652
    Mass (Da):74,267
    Checksum:iAE7A8BB828D0B538
    GO

    Sequence cautioni

    The sequence AAH01611.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB55031.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC11089.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661R → G in AAF19526. (PubMed:11025449)Curated
    Sequence conflicti83 – 831R → T in AAF19526. (PubMed:11025449)Curated
    Sequence conflicti96 – 961R → Q in AAF19526. (PubMed:11025449)Curated
    Sequence conflicti170 – 1701M → I in AAH94706. (PubMed:15489334)Curated
    Sequence conflicti485 – 4851E → G in BAB55031. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei500 – 5001E → EQ in isoform 2. 2 PublicationsVSP_017564

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF213969 mRNA. Translation: AAF19526.1.
    AJ271881 mRNA. Translation: CAB72445.1.
    AF152604 mRNA. Translation: AAF75126.1.
    BC001611 mRNA. Translation: AAH01611.1. Different initiation.
    AC007493 Genomic DNA. No translation available.
    AC007597 Genomic DNA. No translation available.
    AC023826 Genomic DNA. No translation available.
    BC050728 mRNA. Translation: AAH50728.1.
    BC094706 mRNA. Translation: AAH94706.1.
    AK027308 mRNA. Translation: BAB55031.1. Different initiation.
    AK074613 mRNA. Translation: BAC11089.1. Different initiation.
    CCDSiCCDS10742.1. [Q9NPI1-1]
    CCDS54007.1. [Q9NPI1-2]
    RefSeqiNP_001167455.1. NM_001173984.2. [Q9NPI1-2]
    NP_037395.2. NM_013263.4. [Q9NPI1-1]
    UniGeneiHs.437894.

    Genome annotation databases

    EnsembliENST00000394688; ENSP00000378180; ENSG00000166164. [Q9NPI1-1]
    ENST00000394689; ENSP00000378181; ENSG00000166164. [Q9NPI1-2]
    GeneIDi29117.
    KEGGihsa:29117.
    UCSCiuc002ege.2. human. [Q9NPI1-2]
    uc021thx.1. human. [Q9NPI1-1]

    Polymorphism databases

    DMDMi74734307.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF213969 mRNA. Translation: AAF19526.1 .
    AJ271881 mRNA. Translation: CAB72445.1 .
    AF152604 mRNA. Translation: AAF75126.1 .
    BC001611 mRNA. Translation: AAH01611.1 . Different initiation.
    AC007493 Genomic DNA. No translation available.
    AC007597 Genomic DNA. No translation available.
    AC023826 Genomic DNA. No translation available.
    BC050728 mRNA. Translation: AAH50728.1 .
    BC094706 mRNA. Translation: AAH94706.1 .
    AK027308 mRNA. Translation: BAB55031.1 . Different initiation.
    AK074613 mRNA. Translation: BAC11089.1 . Different initiation.
    CCDSi CCDS10742.1. [Q9NPI1-1 ]
    CCDS54007.1. [Q9NPI1-2 ]
    RefSeqi NP_001167455.1. NM_001173984.2. [Q9NPI1-2 ]
    NP_037395.2. NM_013263.4. [Q9NPI1-1 ]
    UniGenei Hs.437894.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I7K NMR - A 129-236 [» ]
    ProteinModelPortali Q9NPI1.
    SMRi Q9NPI1. Positions 129-238, 338-393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118883. 36 interactions.
    DIPi DIP-32509N.
    IntActi Q9NPI1. 26 interactions.
    MINTi MINT-1383082.
    STRINGi 9606.ENSP00000378180.

    PTM databases

    PhosphoSitei Q9NPI1.

    Polymorphism databases

    DMDMi 74734307.

    Proteomic databases

    MaxQBi Q9NPI1.
    PaxDbi Q9NPI1.
    PRIDEi Q9NPI1.

    Protocols and materials databases

    DNASUi 29117.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394688 ; ENSP00000378180 ; ENSG00000166164 . [Q9NPI1-1 ]
    ENST00000394689 ; ENSP00000378181 ; ENSG00000166164 . [Q9NPI1-2 ]
    GeneIDi 29117.
    KEGGi hsa:29117.
    UCSCi uc002ege.2. human. [Q9NPI1-2 ]
    uc021thx.1. human. [Q9NPI1-1 ]

    Organism-specific databases

    CTDi 29117.
    GeneCardsi GC16M050352.
    HGNCi HGNC:14310. BRD7.
    HPAi CAB046458.
    neXtProti NX_Q9NPI1.
    PharmGKBi PA25417.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000070022.
    HOVERGENi HBG071934.
    KOi K11723.
    OMAi GDIVSTY.
    OrthoDBi EOG7D2FDM.
    PhylomeDBi Q9NPI1.
    TreeFami TF106439.

    Miscellaneous databases

    EvolutionaryTracei Q9NPI1.
    GeneWikii BRD7.
    GenomeRNAii 29117.
    NextBioi 52203.
    PROi Q9NPI1.

    Gene expression databases

    ArrayExpressi Q9NPI1.
    Bgeei Q9NPI1.
    CleanExi HS_BRD7.
    Genevestigatori Q9NPI1.

    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

    1. "Molecular characterization of celtix-1, a bromodomain protein interacting with the transcription factor interferon regulatory factor 2."
      Staal A., Enserink J.M., Stein J.L., Stein G.S., van Wijnen A.J.
      J. Cell. Physiol. 185:269-279(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH IRF2, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    2. "Regulation of transcription by the heterogeneous nuclear ribonucleoprotein E1B-AP5 is mediated by complex formation with the novel bromodomain-containing protein BRD7."
      Kzhyshkowska J.G., Rusch A., Wolf H., Dobner T.
      Biochem. J. 371:385-393(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH HNRPUL1, ASSOCIATION WITH HISTONES AND HNRPUL1.
      Tissue: Fetal brain.
    3. Yu Y., Li G.Y.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-651 (ISOFORM 2).
      Tissue: Brain and Skin.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-651 (ISOFORM 1).
      Tissue: Embryo.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "The transcriptional regulation role of BRD7 by binding to acetylated histone through bromodomain."
      Peng C., Zhou J., Liu H.Y., Zhou M., Wang L.L., Zhang Q.H., Yang Y.X., Xiong W., Shen S.R., Li X.L., Li G.Y.
      J. Cell. Biochem. 97:882-892(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ACETYLATED HISTONE H3.
    9. "Identification of nuclear localization signal that governs nuclear import of BRD7 and its essential roles in inhibiting cell cycle progression."
      Zhou M., Liu H., Xu X., Zhou H., Li X., Peng C., Shen S., Xiong W., Ma J., Zeng Z., Fang S., Nie X., Yang Y., Zhou J., Xiang J., Cao L., Peng S., Li S., Li G.
      J. Cell. Biochem. 98:920-930(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. "BRD7, a subunit of SWI/SNF complexes, binds directly to BRCA1 and regulates BRCA1-dependent transcription."
      Harte M.T., O'Brien G.J., Ryan N.M., Gorski J.J., Savage K.I., Crawford N.T., Mullan P.B., Harkin D.P.
      Cancer Res. 70:2538-2547(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROMOTER BINDING, INTERACTION WITH BRCA1.
    12. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TP53 AND EP300.
    13. "Polybromo-associated BRG1-associated factor components BRD7 and BAF180 are critical regulators of p53 required for induction of replicative senescence."
      Burrows A.E., Smogorzewska A., Elledge S.J.
      Proc. Natl. Acad. Sci. U.S.A. 107:14280-14285(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4."
      Sun H., Liu J., Zhang J., Shen W., Huang H., Xu C., Dai H., Wu J., Shi Y.
      Biochem. Biophys. Res. Commun. 358:435-441(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 129-236, INTERACTION WITH ACETYLATED HISTONE PEPTIDES.

    Entry informationi

    Entry nameiBRD7_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPI1
    Secondary accession number(s): Q4VC09
    , Q8N2L9, Q96KA4, Q9BV48, Q9UH59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 21, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3