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Q16576

- RBBP7_HUMAN

UniProt

Q16576 - RBBP7_HUMAN

Protein

Histone-binding protein RBBP7

Gene

RBBP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Core histone-binding subunit that may target chromatin remodeling factors, histone acetyltransferases and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the type B histone acetyltransferase (HAT) complex, which is required for chromatin assembly following DNA replication; the core histone deacetylase (HDAC) complex, which promotes histone deacetylation and consequent transcriptional repression; the nucleosome remodeling and histone deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; and the PRC2/EED-EZH2 complex, which promotes repression of homeotic genes during development; and the NURF (nucleosome remodeling factor) complex.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. cellular heat acclimation Source: UniProtKB
    3. CENP-A containing nucleosome assembly Source: Reactome
    4. chromatin organization Source: Reactome
    5. DNA replication Source: UniProtKB-KW
    6. multicellular organismal development Source: ProtInc
    7. negative regulation of cell growth Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. nucleosome assembly Source: Reactome
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone, Chromatin regulator, Repressor

    Keywords - Biological processi

    DNA replication, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
    REACT_172610. HATs acetylate histones.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_953. RNA Polymerase I Transcription Initiation.
    SignaLinkiQ16576.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-binding protein RBBP7
    Alternative name(s):
    Histone acetyltransferase type B subunit 2
    Nucleosome-remodeling factor subunit RBAP46
    Retinoblastoma-binding protein 7
    Short name:
    RBBP-7
    Retinoblastoma-binding protein p46
    Gene namesi
    Name:RBBP7
    Synonyms:RBAP46
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:9890. RBBP7.

    Subcellular locationi

    GO - Cellular componenti

    1. ESC/E(Z) complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProt
    4. NuRD complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34254.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 425424Histone-binding protein RBBP7PRO_0000051195Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei3 – 31Phosphoserine1 Publication
    Modified residuei4 – 41N6-acetyllysine; alternate1 Publication
    Cross-linki4 – 4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
    Modified residuei119 – 1191N6-acetyllysineBy similarity
    Modified residuei159 – 1591N6-acetyllysineBy similarity
    Modified residuei354 – 3541Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ16576.
    PaxDbiQ16576.
    PeptideAtlasiQ16576.
    PRIDEiQ16576.

    PTM databases

    PhosphoSiteiQ16576.

    Miscellaneous databases

    PMAP-CutDBQ16576.

    Expressioni

    Gene expression databases

    ArrayExpressiQ16576.
    BgeeiQ16576.
    CleanExiHS_RBBP7.
    GenevestigatoriQ16576.

    Organism-specific databases

    HPAiCAB037084.

    Interactioni

    Subunit structurei

    Binds directly to helix 1 of the histone fold of histone H4, a region that is not accessible when H4 is in chromatin. Subunit of the type B histone acetyltransferase (HAT) complex, composed of RBBP7 and HAT1. Subunit of the core histone deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core HDAC complex associates with SIN3A, ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The core HDAC complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form the nucleosome remodeling and histone deacetylase complex (the NuRD complex). The NuRD complex may also interact with MBD3L1 and MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex, which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12. The PRC2/EED-EZH2 complex may also associate with HDAC1. Part of the nucleosome remodeling factor (NURF) complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein-binding domain of the retinoblastoma protein (RB1). Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Interacts with BRCA1, HDAC7 and SUV39H1.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DHX30Q7L2E34EBI-352227,EBI-1211456
    HDAC1Q135475EBI-352227,EBI-301834
    HIST2H4BP628054EBI-352227,EBI-302023
    NR2E3Q9Y5X42EBI-352227,EBI-7216962
    TBL3Q127882EBI-352227,EBI-715766

    Protein-protein interaction databases

    BioGridi111866. 104 interactions.
    DIPiDIP-436N.
    IntActiQ16576. 38 interactions.
    MINTiMINT-90512.
    STRINGi9606.ENSP00000369427.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 3021
    Beta strandi31 – 388
    Beta strandi46 – 538
    Beta strandi59 – 679
    Beta strandi72 – 743
    Beta strandi76 – 8611
    Beta strandi113 – 12412
    Beta strandi127 – 1315
    Beta strandi138 – 1425
    Beta strandi144 – 1463
    Beta strandi148 – 1525
    Helixi153 – 1553
    Beta strandi169 – 1735
    Beta strandi182 – 1843
    Beta strandi186 – 1883
    Beta strandi191 – 1955
    Beta strandi201 – 2055
    Beta strandi214 – 2174
    Beta strandi219 – 2224
    Beta strandi229 – 2346
    Beta strandi241 – 2466
    Beta strandi249 – 25911
    Beta strandi261 – 2633
    Beta strandi265 – 2695
    Beta strandi275 – 2806
    Beta strandi287 – 2926
    Beta strandi295 – 3017
    Beta strandi305 – 3073
    Beta strandi310 – 3134
    Beta strandi319 – 3246
    Beta strandi331 – 3366
    Beta strandi341 – 3455
    Helixi346 – 3483
    Helixi355 – 3584
    Beta strandi365 – 3695
    Beta strandi376 – 3816
    Beta strandi383 – 3853
    Beta strandi388 – 3936
    Beta strandi396 – 4038
    Helixi405 – 4084

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CFSX-ray2.40B1-411[»]
    3CFVX-ray2.60A/B1-411[»]
    ProteinModelPortaliQ16576.
    SMRiQ16576. Positions 1-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16576.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati47 – 12276WD 1Add
    BLAST
    Repeati128 – 17346WD 2Add
    BLAST
    Repeati181 – 21737WD 3Add
    BLAST
    Repeati228 – 26942WD 4Add
    BLAST
    Repeati275 – 31238WD 5Add
    BLAST
    Repeati318 – 36952WD 6Add
    BLAST
    Repeati376 – 40328WD 7Add
    BLAST

    Sequence similaritiesi

    Contains 7 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOGENOMiHOG000160330.
    HOVERGENiHBG053236.
    KOiK11659.
    OMAiHEDAVNC.
    PhylomeDBiQ16576.
    TreeFamiTF106485.

    Family and domain databases

    Gene3Di2.130.10.10. 1 hit.
    InterProiIPR020472. G-protein_beta_WD-40_rep.
    IPR022052. Histone-bd_RBBP4_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PfamiPF12265. CAF1C_H4-bd. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view]
    PRINTSiPR00320. GPROTEINBRPT.
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 1 hit.
    PROSITEiPS00678. WD_REPEATS_1. 3 hits.
    PS50082. WD_REPEATS_2. 5 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16576-1) [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

    MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP    50
    EVTKPEGKDY ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD 100
    KGEFGGFGSV TGKIECEIKI NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV 150
    FDYTKHPAKP DPSGECNPDL RLRGHQKEGY GLSWNSNLSG HLLSASDDHT 200
    VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES LFGSVADDQK 250
    LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW 300
    DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG 350
    EEQSAEDAED GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI 400
    WQMAENIYND EESDVTTSEL EGQGS 425
    Length:425
    Mass (Da):47,820
    Last modified:November 1, 1997 - v1
    Checksum:i1A4B4CD1A8E96815
    GO
    Isoform 2 (identifier: Q16576-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MASKEM → MAAEAGVVGAGASPDGDWRDQACGLLLHVHLSSRLGRAAPVRTGRHLRTV

    Note: No experimental confirmation available. Initiator Met-1 is removed. Contains a N-acetylalanine at position 2. Contains a phosphoserine at position 13.

    Show »
    Length:469
    Mass (Da):52,314
    Checksum:iD668D0B6D5715261
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MASKEM → MAAEAGVVGAGASPDGDWRD QACGLLLHVHLSSRLGRAAP VRTGRHLRTV in isoform 2. 1 PublicationVSP_043016

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35143 mRNA. Translation: AAC50231.1.
    X72841 mRNA. Translation: CAA51360.1.
    AK091911 mRNA. Translation: BAG52439.1.
    AL929302 Genomic DNA. Translation: CAI41283.1.
    CCDSiCCDS14179.1. [Q16576-1]
    CCDS56598.1. [Q16576-2]
    PIRiI39181.
    RefSeqiNP_001185648.1. NM_001198719.1. [Q16576-2]
    NP_002884.1. NM_002893.3. [Q16576-1]
    UniGeneiHs.495755.

    Genome annotation databases

    EnsembliENST00000380084; ENSP00000369424; ENSG00000102054. [Q16576-2]
    ENST00000380087; ENSP00000369427; ENSG00000102054. [Q16576-1]
    GeneIDi5931.
    KEGGihsa:5931.
    UCSCiuc004cxs.2. human. [Q16576-2]
    uc004cxt.3. human. [Q16576-1]

    Polymorphism databases

    DMDMi2494891.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U35143 mRNA. Translation: AAC50231.1 .
    X72841 mRNA. Translation: CAA51360.1 .
    AK091911 mRNA. Translation: BAG52439.1 .
    AL929302 Genomic DNA. Translation: CAI41283.1 .
    CCDSi CCDS14179.1. [Q16576-1 ]
    CCDS56598.1. [Q16576-2 ]
    PIRi I39181.
    RefSeqi NP_001185648.1. NM_001198719.1. [Q16576-2 ]
    NP_002884.1. NM_002893.3. [Q16576-1 ]
    UniGenei Hs.495755.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CFS X-ray 2.40 B 1-411 [» ]
    3CFV X-ray 2.60 A/B 1-411 [» ]
    ProteinModelPortali Q16576.
    SMRi Q16576. Positions 1-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111866. 104 interactions.
    DIPi DIP-436N.
    IntActi Q16576. 38 interactions.
    MINTi MINT-90512.
    STRINGi 9606.ENSP00000369427.

    PTM databases

    PhosphoSitei Q16576.

    Polymorphism databases

    DMDMi 2494891.

    Proteomic databases

    MaxQBi Q16576.
    PaxDbi Q16576.
    PeptideAtlasi Q16576.
    PRIDEi Q16576.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380084 ; ENSP00000369424 ; ENSG00000102054 . [Q16576-2 ]
    ENST00000380087 ; ENSP00000369427 ; ENSG00000102054 . [Q16576-1 ]
    GeneIDi 5931.
    KEGGi hsa:5931.
    UCSCi uc004cxs.2. human. [Q16576-2 ]
    uc004cxt.3. human. [Q16576-1 ]

    Organism-specific databases

    CTDi 5931.
    GeneCardsi GC0XM016772.
    HGNCi HGNC:9890. RBBP7.
    HPAi CAB037084.
    MIMi 300825. gene.
    neXtProti NX_Q16576.
    PharmGKBi PA34254.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOGENOMi HOG000160330.
    HOVERGENi HBG053236.
    KOi K11659.
    OMAi HEDAVNC.
    PhylomeDBi Q16576.
    TreeFami TF106485.

    Enzyme and pathway databases

    Reactomei REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172610. HATs acetylate histones.
    REACT_200808. PRC2 methylates histones and DNA.
    REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
    REACT_953. RNA Polymerase I Transcription Initiation.
    SignaLinki Q16576.

    Miscellaneous databases

    ChiTaRSi RBBP7. human.
    EvolutionaryTracei Q16576.
    GeneWikii RBBP7.
    GenomeRNAii 5931.
    NextBioi 23110.
    PMAP-CutDB Q16576.
    PROi Q16576.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16576.
    Bgeei Q16576.
    CleanExi HS_RBBP7.
    Genevestigatori Q16576.

    Family and domain databases

    Gene3Di 2.130.10.10. 1 hit.
    InterProi IPR020472. G-protein_beta_WD-40_rep.
    IPR022052. Histone-bd_RBBP4_N.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    Pfami PF12265. CAF1C_H4-bd. 1 hit.
    PF00400. WD40. 5 hits.
    [Graphical view ]
    PRINTSi PR00320. GPROTEINBRPT.
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 1 hit.
    PROSITEi PS00678. WD_REPEATS_1. 3 hits.
    PS50082. WD_REPEATS_2. 5 hits.
    PS50294. WD_REPEATS_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast."
      Qian Y.-W., Lee E.Y.-H.P.
      J. Biol. Chem. 270:25507-25513(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1.
    2. Nielsen M.S., Rasmussen H.H., Dejgaard K., Celis J.E., Leffers H.
      Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [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).
      Tissue: Kidney.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex."
      Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.
      Cell 89:357-364(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
    6. "The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities."
      Zhang Y., LeRoy G., Seelig H.-P., Lane W.S., Reinberg D.
      Cell 95:279-289(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NURD COMPLEX.
    7. "Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase."
      Verreault A., Kaufman P.D., Kobayashi R., Stillman B.
      Curr. Biol. 8:96-108(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HAT1 AND HISTONE H4.
    8. "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex."
      Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P., Hampsey M., Reinberg D.
      Mol. Cell 1:1021-1031(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
    9. "Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation."
      Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A., Reinberg D.
      Genes Dev. 13:1924-1935(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NURD COMPLEX.
    10. "BRCA1 interacts with components of the histone deacetylase complex."
      Yarden R.I., Brody L.C.
      Proc. Natl. Acad. Sci. U.S.A. 96:4983-4988(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRCA1 AND RB1.
    11. "Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB."
      Zhang Q., Vo N., Goodman R.H.
      Mol. Cell. Biol. 20:4970-4978(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CREBBP.
    12. "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1."
      Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.
      J. Biol. Chem. 276:6817-6824(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NURD COMPLEX.
    13. "Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex."
      Skowyra D., Zeremski M., Neznanov N., Li M., Choi Y., Uesugi M., Hauser C.A., Gu W., Gudkov A.V., Qin J.
      J. Biol. Chem. 276:8734-8739(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
    14. "Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein."
      Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.
      Genes Dev. 16:2893-2905(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP4 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
    15. "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)."
      Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.
      Mol. Cell. Biol. 22:835-848(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
    16. "Isolation of human NURF: a regulator of Engrailed gene expression."
      Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J., Shiekhattar R.
      EMBO J. 22:6089-6100(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NURF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity."
      Yao Y.-L., Yang W.-M.
      J. Biol. Chem. 278:42560-42568(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MTA1 HDAC COMPLEX.
    18. "MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex."
      Jiang C.-L., Jin S.-G., Pfeifer G.P.
      J. Biol. Chem. 279:52456-52464(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBD3L1.
    19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    22. "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 ALA-2 AND LYS-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-411 IN COMPLEX WITH HISTONE H4, DOMAINS WD REPEATS.

    Entry informationi

    Entry nameiRBBP7_HUMAN
    AccessioniPrimary (citable) accession number: Q16576
    Secondary accession number(s): Q5JP00
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 146 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3