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O95696

- BRD1_HUMAN

UniProt

O95696 - BRD1_HUMAN

Protein

Bromodomain-containing protein 1

Gene

BRD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri214 – 26451PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. histone binding Source: UniProtKB
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H3 acetylation Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bromodomain-containing protein 1
    Alternative name(s):
    BR140-like protein
    Bromodomain and PHD finger-containing protein 2
    Gene namesi
    Name:BRD1
    Synonyms:BRL, BRPF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:1102. BRD1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25413.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10581058Bromodomain-containing protein 1PRO_0000211177Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei128 – 1281Phosphoserine1 Publication
    Modified residuei368 – 3681N6-acetyllysine1 Publication
    Modified residuei516 – 5161N6-acetyllysine1 Publication
    Modified residuei519 – 5191N6-acetyllysine1 Publication
    Modified residuei903 – 9031N6-acetyllysine1 Publication
    Modified residuei1052 – 10521Phosphoserine2 Publications
    Modified residuei1055 – 10551Phosphoserine4 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95696.
    PaxDbiO95696.
    PRIDEiO95696.

    2D gel databases

    OGPiO95696.

    PTM databases

    PhosphoSiteiO95696.

    Miscellaneous databases

    PMAP-CutDBO95696.

    Expressioni

    Tissue specificityi

    Highly expressed in testis.

    Gene expression databases

    ArrayExpressiO95696.
    BgeeiO95696.
    CleanExiHS_BRD1.
    GenevestigatoriO95696.

    Organism-specific databases

    HPAiHPA000807.
    HPA001063.

    Interactioni

    Subunit structurei

    Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3. Interacts (via PHD-type zinc finger domain) with unmodified histone H3. Interacts (via PWWP domain) with dimethylated and trimethylated 'Lys-79' on histone H3.4 Publications

    Protein-protein interaction databases

    BioGridi117273. 12 interactions.
    IntActiO95696. 3 interactions.
    MINTiMINT-1186761.
    STRINGi9606.ENSP00000216267.

    Structurei

    Secondary structure

    1
    1058
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni205 – 2084
    Beta strandi218 – 2203
    Beta strandi222 – 2254
    Beta strandi227 – 2293
    Beta strandi231 – 2333
    Beta strandi235 – 2373
    Beta strandi240 – 2423
    Helixi243 – 2464
    Helixi259 – 2668
    Turni328 – 3314
    Beta strandi338 – 3403
    Turni344 – 3463
    Beta strandi349 – 3513
    Helixi352 – 3587
    Beta strandi362 – 3698
    Turni371 – 3733
    Beta strandi376 – 3838
    Helixi386 – 3883
    Beta strandi389 – 3924
    Helixi566 – 58015
    Beta strandi586 – 5894
    Turni593 – 5953
    Helixi599 – 6024
    Helixi609 – 6179
    Helixi624 – 64118
    Helixi647 – 67630
    Beta strandi932 – 9354
    Beta strandi943 – 9475
    Helixi969 – 98012
    Beta strandi986 – 9916
    Beta strandi998 – 10025
    Helixi1003 – 10053
    Beta strandi1006 – 10116
    Helixi1013 – 10208
    Helixi1026 – 104520

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KU3NMR-A208-269[»]
    2L43NMR-A205-269[»]
    2LQ6NMR-A317-392[»]
    3LYIX-ray2.10A/B925-1049[»]
    3RCWX-ray2.21A/B/C/D/E/F/G/H556-688[»]
    ProteinModelPortaliO95696.
    SMRiO95696. Positions 208-269, 317-394, 563-680, 928-1047.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95696.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini579 – 64971BromoPROSITE-ProRule annotationAdd
    BLAST
    Domaini929 – 101284PWWPPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 PWWP domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri214 – 26451PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5141.
    HOGENOMiHOG000000705.
    HOVERGENiHBG004895.
    KOiK11349.
    OMAiSERPPVC.
    OrthoDBiEOG7FBRM7.
    PhylomeDBiO95696.
    TreeFamiTF316118.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR019542. Enhancer_polycomb-like_N.
    IPR000313. PWWP_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00439. Bromodomain. 1 hit.
    PF10513. EPL1. 1 hit.
    PF00855. PWWP. 1 hit.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 1 hit.
    SM00249. PHD. 2 hits.
    SM00293. PWWP. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50812. PWWP. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95696-1) [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

    MRRKGRCHRG SAARHPSSPC SVKHSPTRET LTYAQAQRMV EIEIEGRLHR     50
    ISIFDPLEII LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK 100
    NEALPSAHGT PASASALPEP KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL 150
    DNEVEYDMDE EDYAWLEIVN EKRKGDCVPA VSQSMFEFLM DRFEKESHCE 200
    NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA VHQECYGVPY 250
    IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE 300
    VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF 350
    HVTCAQKAGL YMKMEPVKEL TGGGTTFSVR KTAYCDVHTP PGCTRRPLNI 400
    YGDVEMKNGV CRKESSVKTV RSTSKVRKKA KKAKKALAEP CAVLPTVCAP 450
    YIPPQRLNRI ANQVAIQRKK QFVERAHSYW LLKRLSRNGA PLLRRLQSSL 500
    QSQRSSQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE LLRKREKLKR 550
    EQVKVEQVAM ELRLTPLTVL LRSVLDQLQD KDPARIFAQP VSLKEVPDYL 600
    DHIKHPMDFA TMRKRLEAQG YKNLHEFEED FDLIIDNCMK YNARDTVFYR 650
    AAVRLRDQGG VVLRQARREV DSIGLEEASG MHLPERPAAA PRRPFSWEDV 700
    DRLLDPANRA HLGLEEQLRE LLDMLDLTCA MKSSGSRSKR AKLLKKEIAL 750
    LRNKLSQQHS QPLPTGPGLE GFEEDGAALG PEAGEEVLPR LETLLQPRKR 800
    SRSTCGDSEV EEESPGKRLD AGLTNGFGGA RSEQEPGGGL GRKATPRRRC 850
    ASESSISSSN SPLCDSSFNA PKCGRGKPAL VRRHTLEDRS ELISCIENGN 900
    YAKAARIAAE VGQSSMWIST DAAASVLEPL KVVWAKCSGY PSYPALIIDP 950
    KMPRVPGHHN GVTIPAPPLD VLKIGEHMQT KSDEKLFLVL FFDNKRSWQW 1000
    LPKSKMVPLG IDETIDKLKM MEGRNSSIRK AVRIAFDRAM NHLSRVHGEP 1050
    TSDLSDID 1058
    Length:1,058
    Mass (Da):119,520
    Last modified:May 1, 1999 - v1
    Checksum:i6E7B07E8A030E104
    GO
    Isoform 2 (identifier: O95696-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         786-786: E → EGDKSPPKLE...QLGTKTFLSV

    Note: Contains a phosphoserine at position 906.

    Show »
    Length:1,189
    Mass (Da):133,243
    Checksum:i770DB2F610CB5052
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381R → G.
    Corresponds to variant rs11549978 [ dbSNP | Ensembl ].
    VAR_048424
    Natural varianti321 – 3211A → S.
    Corresponds to variant rs12157714 [ dbSNP | Ensembl ].
    VAR_048425
    Natural varianti730 – 7301A → T.
    Corresponds to variant rs35331092 [ dbSNP | Ensembl ].
    VAR_048426

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei786 – 7861E → EGDKSPPKLEPSDALPLPSN SETNSEPPTLKPVELNPEQS KLFKRVTFDNESHSACTQSA LVSGRPPEPTRASSGDVPAA AASAVAEPASDVNRRTSVLF CKSKSVSPPKSAKNTETQPT SPQLGTKTFLSV in isoform 2. 1 PublicationVSP_040262

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005067 mRNA. Translation: AAF34320.1.
    CR456408 mRNA. Translation: CAG30294.1.
    AK292428 mRNA. Translation: BAF85117.1.
    Z98885 Genomic DNA. Translation: CAB11574.1.
    Z98885 Genomic DNA. Translation: CAO72061.1.
    CH471138 Genomic DNA. Translation: EAW73473.1.
    CCDSiCCDS14080.1. [O95696-1]
    RefSeqiNP_055392.1. NM_014577.1. [O95696-1]
    XP_005261528.1. XM_005261471.1. [O95696-2]
    XP_006724273.1. XM_006724210.1. [O95696-2]
    XP_006724274.1. XM_006724211.1. [O95696-2]
    XP_006724276.1. XM_006724213.1. [O95696-1]
    UniGeneiHs.127950.

    Genome annotation databases

    EnsembliENST00000216267; ENSP00000216267; ENSG00000100425. [O95696-1]
    ENST00000404034; ENSP00000384076; ENSG00000100425. [O95696-1]
    ENST00000404760; ENSP00000385858; ENSG00000100425. [O95696-2]
    GeneIDi23774.
    KEGGihsa:23774.
    UCSCiuc003biu.4. human. [O95696-2]
    uc003biv.3. human. [O95696-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005067 mRNA. Translation: AAF34320.1 .
    CR456408 mRNA. Translation: CAG30294.1 .
    AK292428 mRNA. Translation: BAF85117.1 .
    Z98885 Genomic DNA. Translation: CAB11574.1 .
    Z98885 Genomic DNA. Translation: CAO72061.1 .
    CH471138 Genomic DNA. Translation: EAW73473.1 .
    CCDSi CCDS14080.1. [O95696-1 ]
    RefSeqi NP_055392.1. NM_014577.1. [O95696-1 ]
    XP_005261528.1. XM_005261471.1. [O95696-2 ]
    XP_006724273.1. XM_006724210.1. [O95696-2 ]
    XP_006724274.1. XM_006724211.1. [O95696-2 ]
    XP_006724276.1. XM_006724213.1. [O95696-1 ]
    UniGenei Hs.127950.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KU3 NMR - A 208-269 [» ]
    2L43 NMR - A 205-269 [» ]
    2LQ6 NMR - A 317-392 [» ]
    3LYI X-ray 2.10 A/B 925-1049 [» ]
    3RCW X-ray 2.21 A/B/C/D/E/F/G/H 556-688 [» ]
    ProteinModelPortali O95696.
    SMRi O95696. Positions 208-269, 317-394, 563-680, 928-1047.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117273. 12 interactions.
    IntActi O95696. 3 interactions.
    MINTi MINT-1186761.
    STRINGi 9606.ENSP00000216267.

    Chemistry

    ChEMBLi CHEMBL2176774.

    PTM databases

    PhosphoSitei O95696.

    2D gel databases

    OGPi O95696.

    Proteomic databases

    MaxQBi O95696.
    PaxDbi O95696.
    PRIDEi O95696.

    Protocols and materials databases

    DNASUi 23774.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216267 ; ENSP00000216267 ; ENSG00000100425 . [O95696-1 ]
    ENST00000404034 ; ENSP00000384076 ; ENSG00000100425 . [O95696-1 ]
    ENST00000404760 ; ENSP00000385858 ; ENSG00000100425 . [O95696-2 ]
    GeneIDi 23774.
    KEGGi hsa:23774.
    UCSCi uc003biu.4. human. [O95696-2 ]
    uc003biv.3. human. [O95696-1 ]

    Organism-specific databases

    CTDi 23774.
    GeneCardsi GC22M050166.
    HGNCi HGNC:1102. BRD1.
    HPAi HPA000807.
    HPA001063.
    MIMi 604589. gene.
    neXtProti NX_O95696.
    PharmGKBi PA25413.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5141.
    HOGENOMi HOG000000705.
    HOVERGENi HBG004895.
    KOi K11349.
    OMAi SERPPVC.
    OrthoDBi EOG7FBRM7.
    PhylomeDBi O95696.
    TreeFami TF316118.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    EvolutionaryTracei O95696.
    GenomeRNAii 23774.
    NextBioi 46753.
    PMAP-CutDB O95696.
    PROi O95696.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95696.
    Bgeei O95696.
    CleanExi HS_BRD1.
    Genevestigatori O95696.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR019542. Enhancer_polycomb-like_N.
    IPR000313. PWWP_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF10513. EPL1. 1 hit.
    PF00855. PWWP. 1 hit.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 1 hit.
    SM00249. PHD. 2 hits.
    SM00293. PWWP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50812. PWWP. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The cloning, mapping and expression of a novel gene, BRL, related to the AF10 leukaemia gene."
      McCullagh P., Chaplin T., Meerabux J., Grenzelias D., Lillington D., Poulsom R., Gregorini A., Saha V., Young B.D.
      Oncogene 18:7442-7452(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "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] (ISOFORM 2).
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
      Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
      Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
    8. Cited for: IDENTIFICATION IN THE MOZ/MORF COMPLEX.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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 SER-1055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-368; LYS-516; LYS-519 AND LYS-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-1052 AND SER-1055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-128; SER-1052 AND SER-1055, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-906 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Recognition of unmodified histone H3 by the first PHD finger of bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases monocytic leukemic zinc-finger protein (MOZ) and MOZ-related factor (MORF)."
      Qin S., Jin L., Zhang J., Liu L., Ji P., Wu M., Wu J., Shi Y.
      J. Biol. Chem. 286:36944-36955(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 208-269, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UNMODIFIED HISTONE H3.
    15. "Structural and histone binding ability characterizations of human PWWP domains."
      Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L., Qiu W., Wang Y., Min J.
      PLoS ONE 6:E18919-E18919(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 925-1049, INTERACTION WITH METHYLATED HISTONE H3.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 556-688.

    Entry informationi

    Entry nameiBRD1_HUMAN
    AccessioniPrimary (citable) accession number: O95696
    Secondary accession number(s): A6ZJA4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 119 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 22
      Human chromosome 22: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3