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Q9H0E9

- BRD8_HUMAN

UniProt

Q9H0E9 - BRD8_HUMAN

Protein

Bromodomain-containing protein 8

Gene

BRD8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Isoform 2 stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. At least isoform 1 and isoform 2 are components of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.3 Publications

    GO - Molecular functioni

    1. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    2. thyroid hormone receptor activity Source: ProtInc

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. chromatin organization Source: Reactome
    3. histone H2A acetylation Source: UniProtKB
    4. histone H4 acetylation Source: UniProtKB
    5. intracellular receptor signaling pathway Source: GOC
    6. regulation of growth Source: UniProtKB-KW
    7. regulation of transcription, DNA-templated Source: UniProtKB
    8. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    9. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Growth regulation, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bromodomain-containing protein 8
    Alternative name(s):
    Skeletal muscle abundant protein
    Skeletal muscle abundant protein 2
    Thyroid hormone receptor coactivating protein of 120 kDa
    Short name:
    TrCP120
    p120
    Gene namesi
    Name:BRD8
    Synonyms:SMAP, SMAP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:19874. BRD8.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: HPA
    2. NuA4 histone acetyltransferase complex Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. Swr1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134923194.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12351235Bromodomain-containing protein 8PRO_0000211185Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei85 – 851N6-acetyllysineBy similarity
    Modified residuei387 – 3871Phosphoserine1 Publication
    Modified residuei481 – 4811N6-acetyllysine1 Publication
    Modified residuei621 – 6211Phosphoserine1 Publication
    Modified residuei637 – 6371Phosphoserine1 Publication
    Modified residuei641 – 6411Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H0E9.
    PaxDbiQ9H0E9.
    PRIDEiQ9H0E9.

    Miscellaneous databases

    PMAP-CutDBQ9H0E9.

    Expressioni

    Tissue specificityi

    Expressed in adipose tissue, brain, heart, kidney, liver, lung, pancreas, placenta and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ9H0E9.
    BgeeiQ9H0E9.
    CleanExiHS_BRD8.
    HS_SMAP2.
    GenevestigatoriQ9H0E9.

    Organism-specific databases

    HPAiHPA001841.

    Interactioni

    Subunit structurei

    Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. BRD8 isoform 2 interacts with RXRA/NR2B1 and THRB/ERBA2 By similarity. Component of a SWR1-like complex.By similarity4 Publications

    Protein-protein interaction databases

    BioGridi116108. 18 interactions.
    DIPiDIP-31762N.
    IntActiQ9H0E9. 13 interactions.
    MINTiMINT-3065717.
    STRINGi9606.ENSP00000254900.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H0E9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini724 – 79471Bromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1120 – 119071Bromo 2PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili97 – 17175Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 2 bromo domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Bromodomain, Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5076.
    HOGENOMiHOG000074125.
    HOVERGENiHBG050732.
    InParanoidiQ9H0E9.
    KOiK11321.
    PhylomeDBiQ9H0E9.
    TreeFamiTF106422.

    Family and domain databases

    Gene3Di1.20.920.10. 2 hits.
    InterProiIPR001487. Bromodomain.
    [Graphical view]
    PfamiPF00439. Bromodomain. 2 hits.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 2 hits.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 2 hits.
    PROSITEiPS50014. BROMODOMAIN_2. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H0E9-1) [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

    MATGTGKHKL LSTGPTEPWS IREKLCLASS VMRSGDQNWV SVSRAIKPFA     50
    EPGRPPDWFS QKHCASQYSE LLETTETPKR KRGEKGEVVE TVEDVIVRKL 100
    TAERVEELKK VIKETQERYR RLKRDAELIQ AGHMDSRLDE LCNDIATKKK 150
    LEEEEAEVKR KATDAAYQAR QAVKTPPRRL PTVMVRSPID SASPGGDYPL 200
    GDLTPTTMEE ATSGVNESEM AVASGHLNST GVLLEVGGVL PMIHGGEIQQ 250
    TPNTVAASPA ASGAPTLSRL LEAGPTQFTT PLASFTTVAS EPPVKLVPPP 300
    VESVSQATIV MMPALPAPSS APAVSTTESV APVSQPDNCV PMEAVGDPHT 350
    VTVSMDSSEI SMIINSIKEE CFRSGVAEAP VGSKAPSIDG KEELDLAEKM 400
    DIAVSYTGEE LDFETVGDII AIIEDKVDDH PEVLDVAAVE AALSFCEEND 450
    DPQSLPGPWE HPIQQERDKP VPLPAPEMTV KQERLDFEET ENKGIHELVD 500
    IREPSAEIKV EPAEPEPVIS GAEIVAGVVP ATSMEPPELR SQDLDEELGS 550
    TAAGEIVEAD VAIGKGDETP LTNVKTEASP ESMLSPSHGS NPIEDPLEAE 600
    TQHKFEMSDS LKEESGTIFG SQIKDAPGED EEEDGVSEAA SLEEPKEEDQ 650
    GEGYLSEMDN EPPVSESDDG FSIHNATLQS HTLADSIPSS PASSQFSVCS 700
    EDQEAIQAQK IWKKAIMLVW RAAANHRYAN VFLQPVTDDI APGYHSIVQR 750
    PMDLSTIKKN IENGLIRSTA EFQRDIMLMF QNAVMYNSSD HDVYHMAVEM 800
    QRDVLEQIQQ FLATQLIMQT SESGISAKSL RGRDSTRKQD ASEKDSVPMG 850
    SPAFLLSLFM GHEWVWLDSE QDHPNDSELS NDCRSLFSSW DSSLDLDVGN 900
    WRETEDPEAE ELEESSPERE PSELLVGDGG SEESQEAARK ASHQNLLHFL 950
    SEVAYLMEPL CISSNESSEG CCPPSGTRQE GREIKASEGE RELCRETEEL 1000
    SAKGDPLVAE KPLGENGKPE VASAPSVICT VQGLLTESEE GEAQQESKGE 1050
    DQGEVYVSEM EDQPPSGECD DAFNIKETPL VDTLFSHATS SKLTDLSQDD 1100
    PVQDHLLFKK TLLPVWKMIA SHRFSSPFLK PVSERQAPGY KDVVKRPMDL 1150
    TSLKRNLSKG RIRTMAQFLR DLMLMFQNAV MYNDSDHHVY HMAVEMRQEV 1200
    LEQIQVLNIW LDKRKGSSSL EGEPANPVDD GKPVF 1235
    Length:1,235
    Mass (Da):135,336
    Last modified:November 30, 2010 - v2
    Checksum:i3738078C77FC17D1
    GO
    Isoform 2 (identifier: Q9H0E9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         215-215: V → VTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLV
         860-878: MGHEWVWLDSEQDHPNDSE → DGGTRGRRCAIEADMKMKK
         879-1235: Missing.

    Note: Contains a phosphothreonine at position 264. Contains a phosphoserine at position 268. Contains a phosphoserine at position 284. Contains a phosphoserine at position 924.

    Show »
    Length:951
    Mass (Da):102,839
    Checksum:i80C0A7A6ACB4E8ED
    GO
    Isoform 3 (identifier: Q9H0E9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-147: MATGTGKHKL...LDELCNDIAT → MSFAMTL
         215-215: V → VTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLV
         263-301: Missing.
         845-859: Missing.
         860-878: MGHEWVWLDSEQDHPNDSE → DGGTRGRRCAIEADMKMKK
         879-1235: Missing.

    Note: Contains a phosphothreonine at position 124. Contains a phosphoserine at position 128. Contains a phosphoserine at position 144.

    Show »
    Length:757
    Mass (Da):81,354
    Checksum:iC1D728727505F85D
    GO
    Isoform 4 (identifier: Q9H0E9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         215-215: V → VTPGTLPSTPVTSFPGIPDTLPPGSAPLEAPMTPVTDDSPQKKMLGQKATPPPSPLLSELLKKGSLLPTSPRLV
         263-332: Missing.
         846-846: S → G
         847-975: Missing.
         979-992: QEGREIKASEGERE → GRRCAIEADMKMKK
         993-1235: Missing.

    Note: Contains a phosphothreonine at position 264. Contains a phosphoserine at position 268. Contains a phosphoserine at position 284.

    Show »
    Length:866
    Mass (Da):94,297
    Checksum:i3400AEB14E9412FC
    GO

    Sequence cautioni

    The sequence AAB87858.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH08039.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH08076.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA63925.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti306 – 3061Q → H in AAB87858. (PubMed:9368056)Curated
    Sequence conflicti557 – 5571V → L in CAA60949. (PubMed:8611617)Curated
    Sequence conflicti557 – 5571V → L in CAA63925. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti490 – 4901T → M.1 Publication
    Corresponds to variant rs11750814 [ dbSNP | Ensembl ].
    VAR_030695
    Natural varianti896 – 8961L → P.
    Corresponds to variant rs6883021 [ dbSNP | Ensembl ].
    VAR_048428
    Natural varianti1198 – 11981Q → R.6 Publications
    Corresponds to variant rs412051 [ dbSNP | Ensembl ].
    VAR_048429

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 147147MATGT…NDIAT → MSFAMTL in isoform 3. 1 PublicationVSP_012879Add
    BLAST
    Alternative sequencei215 – 2151V → VTPGTLPSTPVTSFPGIPDT LPPGSAPLEAPMTPVTDDSP QKKMLGQKATPPPSPLLSEL LKKGSLLPTSPRLV in isoform 2, isoform 3 and isoform 4. 5 PublicationsVSP_012880
    Alternative sequencei263 – 33270Missing in isoform 4. 1 PublicationVSP_023187Add
    BLAST
    Alternative sequencei263 – 30139Missing in isoform 3. 1 PublicationVSP_012881Add
    BLAST
    Alternative sequencei845 – 85915Missing in isoform 3. 1 PublicationVSP_012882Add
    BLAST
    Alternative sequencei846 – 8461S → G in isoform 4. 1 PublicationVSP_023188
    Alternative sequencei847 – 975129Missing in isoform 4. 1 PublicationVSP_023189Add
    BLAST
    Alternative sequencei860 – 87819MGHEW…PNDSE → DGGTRGRRCAIEADMKMKK in isoform 2 and isoform 3. 4 PublicationsVSP_012883Add
    BLAST
    Alternative sequencei879 – 1235357Missing in isoform 2 and isoform 3. 4 PublicationsVSP_012884Add
    BLAST
    Alternative sequencei979 – 99214QEGRE…EGERE → GRRCAIEADMKMKK in isoform 4. 1 PublicationVSP_023190Add
    BLAST
    Alternative sequencei993 – 1235243Missing in isoform 4. 1 PublicationVSP_023191Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87613 mRNA. Translation: CAA60949.1.
    AL136823 mRNA. Translation: CAB66757.1.
    AB209079 mRNA. Translation: BAD92316.1.
    AC109442 Genomic DNA. No translation available.
    AC113382 Genomic DNA. No translation available.
    BC008039 mRNA. Translation: AAH08039.1. Different initiation.
    BC008076 mRNA. Translation: AAH08076.1. Different initiation.
    AF016270 mRNA. Translation: AAB87858.1. Different initiation.
    X94234 mRNA. Translation: CAA63925.1. Different initiation.
    CCDSiCCDS34241.1. [Q9H0E9-2]
    CCDS4198.1. [Q9H0E9-1]
    CCDS54907.1. [Q9H0E9-4]
    PIRiS58225.
    S68142.
    RefSeqiNP_001157798.1. NM_001164326.1. [Q9H0E9-4]
    NP_006687.3. NM_006696.3. [Q9H0E9-2]
    NP_631938.1. NM_139199.1.
    UniGeneiHs.519337.

    Genome annotation databases

    EnsembliENST00000230901; ENSP00000230901; ENSG00000112983. [Q9H0E9-2]
    ENST00000254900; ENSP00000254900; ENSG00000112983. [Q9H0E9-1]
    ENST00000411594; ENSP00000394330; ENSG00000112983. [Q9H0E9-4]
    GeneIDi10902.
    KEGGihsa:10902.
    UCSCiuc003lcf.1. human. [Q9H0E9-1]
    uc003lcg.3. human. [Q9H0E9-2]
    uc003lci.3. human. [Q9H0E9-4]
    uc021yea.1. human. [Q9H0E9-3]

    Polymorphism databases

    DMDMi313104080.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87613 mRNA. Translation: CAA60949.1 .
    AL136823 mRNA. Translation: CAB66757.1 .
    AB209079 mRNA. Translation: BAD92316.1 .
    AC109442 Genomic DNA. No translation available.
    AC113382 Genomic DNA. No translation available.
    BC008039 mRNA. Translation: AAH08039.1 . Different initiation.
    BC008076 mRNA. Translation: AAH08076.1 . Different initiation.
    AF016270 mRNA. Translation: AAB87858.1 . Different initiation.
    X94234 mRNA. Translation: CAA63925.1 . Different initiation.
    CCDSi CCDS34241.1. [Q9H0E9-2 ]
    CCDS4198.1. [Q9H0E9-1 ]
    CCDS54907.1. [Q9H0E9-4 ]
    PIRi S58225.
    S68142.
    RefSeqi NP_001157798.1. NM_001164326.1. [Q9H0E9-4 ]
    NP_006687.3. NM_006696.3. [Q9H0E9-2 ]
    NP_631938.1. NM_139199.1.
    UniGenei Hs.519337.

    3D structure databases

    ProteinModelPortali Q9H0E9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116108. 18 interactions.
    DIPi DIP-31762N.
    IntActi Q9H0E9. 13 interactions.
    MINTi MINT-3065717.
    STRINGi 9606.ENSP00000254900.

    Polymorphism databases

    DMDMi 313104080.

    Proteomic databases

    MaxQBi Q9H0E9.
    PaxDbi Q9H0E9.
    PRIDEi Q9H0E9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230901 ; ENSP00000230901 ; ENSG00000112983 . [Q9H0E9-2 ]
    ENST00000254900 ; ENSP00000254900 ; ENSG00000112983 . [Q9H0E9-1 ]
    ENST00000411594 ; ENSP00000394330 ; ENSG00000112983 . [Q9H0E9-4 ]
    GeneIDi 10902.
    KEGGi hsa:10902.
    UCSCi uc003lcf.1. human. [Q9H0E9-1 ]
    uc003lcg.3. human. [Q9H0E9-2 ]
    uc003lci.3. human. [Q9H0E9-4 ]
    uc021yea.1. human. [Q9H0E9-3 ]

    Organism-specific databases

    CTDi 10902.
    GeneCardsi GC05M137475.
    HGNCi HGNC:19874. BRD8.
    HPAi HPA001841.
    MIMi 602848. gene.
    neXtProti NX_Q9H0E9.
    PharmGKBi PA134923194.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000074125.
    HOVERGENi HBG050732.
    InParanoidi Q9H0E9.
    KOi K11321.
    PhylomeDBi Q9H0E9.
    TreeFami TF106422.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi BRD8. human.
    GeneWikii BRD8.
    GenomeRNAii 10902.
    NextBioi 41403.
    PMAP-CutDB Q9H0E9.
    PROi Q9H0E9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0E9.
    Bgeei Q9H0E9.
    CleanExi HS_BRD8.
    HS_SMAP2.
    Genevestigatori Q9H0E9.

    Family and domain databases

    Gene3Di 1.20.920.10. 2 hits.
    InterProi IPR001487. Bromodomain.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 2 hits.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 2 hits.
    PROSITEi PS50014. BROMODOMAIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a human cDNA encoding a putative transcription factor containing a bromodomain."
      Nielsen M.S., Petersen C.M., Gliemann J., Madsen P.
      Biochim. Biophys. Acta 1306:14-16(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, VARIANT ARG-1198.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-1198.
      Tissue: Testis.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS MET-490 AND ARG-1198.
      Tissue: Brain.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(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] OF 2-1235 (ISOFORM 2), VARIANT ARG-1198.
      Tissue: Muscle.
    6. "Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein."
      Monden T., Wondisford F.E., Hollenberg A.N.
      J. Biol. Chem. 272:29834-29841(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-1235 (ISOFORM 2), INTERACTION WITH THRB, VARIANT ARG-1198.
      Tissue: Brain.
    7. Nielsen M.S.
      Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-1235 (ISOFORM 4), VARIANT ARG-1198.
      Tissue: Skin.
    8. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
      Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
      J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-44; 63-79; 83-98; 125-137; 138-148; 150-159; 270-295; 385-399; 485-493; 541-565; 576-604 AND 625-646, IDENTIFICATION IN NUA4 COMPLEX (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY.
    9. "p120 acts as a specific coactivator for 9-cis-retinoic acid receptor (RXR) on peroxisome proliferator-activated receptor-gamma/RXR heterodimers."
      Monden T., Kishi M., Hosoya T., Satoh T., Wondisford F.E., Hollenberg A.N., Yamada M., Mori M.
      Mol. Endocrinol. 13:1695-1703(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RXRA.
    10. "The highly conserved and multifunctional NuA4 HAT complex."
      Doyon Y., Cote J.
      Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON NUA4 COMPLEX.
    11. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
      Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
      Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX (ISOFORMS 1 AND 2), IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
    12. "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-637 AND SER-641, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264; SER-268 AND SER-284 (ISOFORMS 2 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124; SER-128 AND SER-144 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264 AND SER-268 (ISOFORMS 2 AND 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124 AND SER-128 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-621 AND SER-641, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-924 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.

    Entry informationi

    Entry nameiBRD8_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0E9
    Secondary accession number(s): O43178
    , Q15355, Q58AB0, Q59GN0, Q969M9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3