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Q09028

- RBBP4_HUMAN

UniProt

Q09028 - RBBP4_HUMAN

Protein

Histone-binding protein RBBP4

Gene

RBBP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors 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 chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; 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; 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. histone binding Source: BHF-UCL
    2. histone deacetylase binding Source: BHF-UCL
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. ATP-dependent chromatin remodeling Source: UniProt
    3. CENP-A containing nucleosome assembly Source: Reactome
    4. chromatin assembly Source: UniProtKB
    5. chromatin remodeling Source: HGNC
    6. DNA replication Source: UniProtKB-KW
    7. DNA replication-dependent nucleosome assembly Source: UniProt
    8. DNA replication-independent nucleosome assembly Source: UniProt
    9. G2/M transition of mitotic cell cycle Source: Reactome
    10. mitotic cell cycle Source: Reactome
    11. negative regulation of cell proliferation Source: ProtInc
    12. nucleosome assembly Source: Reactome
    13. regulation of cell cycle Source: Reactome
    14. regulation of transcription, DNA-templated Source: UniProtKB-KW
    15. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Cell cycle, DNA replication, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_1006. Polo-like kinase mediated events.
    REACT_111214. G0 and Early G1.
    REACT_169436. Oxidative Stress Induced Senescence.
    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.
    SignaLinkiQ09028.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-binding protein RBBP4
    Alternative name(s):
    Chromatin assembly factor 1 subunit C
    Short name:
    CAF-1 subunit C
    Chromatin assembly factor I p48 subunit
    Short name:
    CAF-I 48 kDa subunit
    Short name:
    CAF-I p48
    Nucleosome-remodeling factor subunit RBAP48
    Retinoblastoma-binding protein 4
    Short name:
    RBBP-4
    Retinoblastoma-binding protein p48
    Gene namesi
    Name:RBBP4
    Synonyms:RBAP48
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9887. RBBP4.

    Subcellular locationi

    GO - Cellular componenti

    1. CAF-1 complex Source: UniProtKB
    2. ESC/E(Z) complex Source: UniProtKB
    3. nuclear chromatin Source: UniProt
    4. nucleoplasm Source: UniProt
    5. nucleus Source: HGNC
    6. NuRD complex Source: UniProtKB
    7. NURF complex Source: UniProtKB
    8. protein complex Source: UniProt
    9. Sin3 complex Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 425424Histone-binding protein RBBP4PRO_0000051186Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 Publications
    Modified residuei4 – 41N6-acetyllysine; alternate1 Publication
    Cross-linki4 – 4Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
    Modified residuei110 – 1101Phosphoserine1 Publication
    Modified residuei160 – 1601N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ09028.
    PaxDbiQ09028.
    PRIDEiQ09028.

    PTM databases

    PhosphoSiteiQ09028.

    Expressioni

    Gene expression databases

    ArrayExpressiQ09028.
    BgeeiQ09028.
    CleanExiHS_RBBP4.
    GenevestigatoriQ09028.

    Organism-specific databases

    HPAiCAB006264.

    Interactioni

    Subunit structurei

    Interacts with SUV39H1 and HDAC7 By similarity. 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 chromatin assembly factor 1 (CAF-1) complex, which is composed of RBBP4, CHAF1B and CHAF1A. 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. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. 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 SPEN/MINT. Interacts with BRCA1. Interacts with CREBBP, and this interaction may be enhanced by the binding of phosphorylated CREB1 to CREBBP. Component of the DREAM complex (also named LINC complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent cells where it represses cell cycle-dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to MYBL2. Interacts with PHF6.By similarity25 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DHX30Q7L2E33EBI-620823,EBI-1211456
    HDAC1Q135476EBI-620823,EBI-301834
    NR2E3Q9Y5X42EBI-620823,EBI-7216962
    ZFPM1Q8IX074EBI-620823,EBI-3942619

    Protein-protein interaction databases

    BioGridi111863. 146 interactions.
    DIPiDIP-33495N.
    IntActiQ09028. 55 interactions.
    MINTiMINT-90543.
    STRINGi9606.ENSP00000362592.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi17 – 3115
    Beta strandi32 – 398
    Beta strandi48 – 547
    Beta strandi62 – 698
    Beta strandi73 – 753
    Beta strandi78 – 869
    Beta strandi115 – 1228
    Beta strandi128 – 1336
    Beta strandi136 – 1438
    Beta strandi145 – 1473
    Beta strandi149 – 1535
    Helixi154 – 1563
    Beta strandi170 – 1745
    Beta strandi180 – 1856
    Beta strandi187 – 1893
    Beta strandi192 – 1976
    Beta strandi202 – 2065
    Helixi207 – 2093
    Beta strandi213 – 2186
    Beta strandi220 – 2234
    Beta strandi230 – 2356
    Beta strandi242 – 2476
    Beta strandi250 – 2567
    Beta strandi262 – 2643
    Beta strandi266 – 2705
    Beta strandi276 – 2816
    Beta strandi288 – 2936
    Beta strandi296 – 3027
    Beta strandi310 – 3145
    Beta strandi320 – 3256
    Beta strandi332 – 3376
    Beta strandi342 – 3465
    Helixi347 – 3493
    Beta strandi366 – 3705
    Beta strandi377 – 3826
    Beta strandi384 – 3863
    Beta strandi389 – 3946
    Beta strandi397 – 4048
    Helixi406 – 4094

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XU7X-ray1.90A/B1-425[»]
    3GFCX-ray2.30A1-425[»]
    4PBYX-ray2.50A/B1-425[»]
    4PBZX-ray2.15A1-425[»]
    4PC0X-ray2.50A/B1-425[»]
    ProteinModelPortaliQ09028.
    SMRiQ09028. Positions 11-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ09028.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati122 – 15534WD 1Add
    BLAST
    Repeati175 – 20632WD 2Add
    BLAST
    Repeati225 – 25632WD 3Add
    BLAST
    Repeati271 – 30232WD 4Add
    BLAST
    Repeati315 – 34632WD 5Add
    BLAST
    Repeati372 – 40332WD 6Add
    BLAST

    Sequence similaritiesi

    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    HOVERGENiHBG053236.
    InParanoidiQ09028.
    KOiK10752.
    OMAiCQPDLRL.
    OrthoDBiEOG70PBXB.
    PhylomeDBiQ09028.
    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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q09028-1) [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

    MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL    50
    PDVTRPEGKD FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS 100
    EKGEFGGFGS VSGKIEIEIK INHEGEVNRA RYMPQNPCII ATKTPSSDVL 150
    VFDYTKHPSK PDPSGECNPD LRLRGHQKEG YGLSWNPNLS GHLLSASDDH 200
    TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE SLFGSVADDQ 250
    KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL 300
    WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI 350
    GEEQSPEDAE DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ 400
    VWQMAENIYN DEDPEGSVDP EGQGS 425
    Length:425
    Mass (Da):47,656
    Last modified:January 23, 2007 - v3
    Checksum:iB71E2D55A444C360
    GO
    Isoform 2 (identifier: Q09028-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         7-7: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:424
    Mass (Da):47,585
    Checksum:i52055B5C74BCF3D8
    GO
    Isoform 3 (identifier: Q09028-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         405-425: AENIYNDEDPEGSVDPEGQGS → ELVLDH

    Note: No experimental confirmation available.

    Show »
    Length:410
    Mass (Da):46,158
    Checksum:i59B630D6055A70B2
    GO
    Isoform 4 (identifier: Q09028-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-35: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:390
    Mass (Da):43,482
    Checksum:iA61A43F6AC30C8CE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti61 – 611F → G in AAH15123. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3535Missing in isoform 4. 1 PublicationVSP_040087Add
    BLAST
    Alternative sequencei7 – 71Missing in isoform 2. 1 PublicationVSP_040088
    Alternative sequencei405 – 42521AENIY…EGQGS → ELVLDH in isoform 3. 1 PublicationVSP_040089Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74262 mRNA. Translation: CAA52321.1.
    X71810 mRNA. Translation: CAA50685.1.
    BT007309 mRNA. Translation: AAP35973.1.
    AK299251 mRNA. Translation: BAG61282.1.
    AK312571 mRNA. Translation: BAG35466.1.
    AK222779 mRNA. Translation: BAD96499.1.
    AC114489 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX07513.1.
    CH471059 Genomic DNA. Translation: EAX07514.1.
    BC003092 mRNA. Translation: AAH03092.1.
    BC015123 mRNA. Translation: AAH15123.1.
    BC053904 mRNA. Translation: AAH53904.1.
    BC075836 mRNA. Translation: AAH75836.1.
    CCDSiCCDS366.1. [Q09028-1]
    CCDS44105.1. [Q09028-2]
    CCDS44106.1. [Q09028-4]
    PIRiS36112.
    RefSeqiNP_001128727.1. NM_001135255.1. [Q09028-2]
    NP_001128728.1. NM_001135256.1. [Q09028-4]
    NP_005601.1. NM_005610.2. [Q09028-1]
    UniGeneiHs.16003.

    Genome annotation databases

    EnsembliENST00000373485; ENSP00000362584; ENSG00000162521. [Q09028-3]
    ENST00000373493; ENSP00000362592; ENSG00000162521. [Q09028-1]
    ENST00000414241; ENSP00000398242; ENSG00000162521. [Q09028-2]
    ENST00000458695; ENSP00000396057; ENSG00000162521. [Q09028-4]
    GeneIDi5928.
    KEGGihsa:5928.
    UCSCiuc001bvr.3. human. [Q09028-1]
    uc001bvs.3. human. [Q09028-2]

    Polymorphism databases

    DMDMi1172846.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74262 mRNA. Translation: CAA52321.1 .
    X71810 mRNA. Translation: CAA50685.1 .
    BT007309 mRNA. Translation: AAP35973.1 .
    AK299251 mRNA. Translation: BAG61282.1 .
    AK312571 mRNA. Translation: BAG35466.1 .
    AK222779 mRNA. Translation: BAD96499.1 .
    AC114489 Genomic DNA. No translation available.
    CH471059 Genomic DNA. Translation: EAX07513.1 .
    CH471059 Genomic DNA. Translation: EAX07514.1 .
    BC003092 mRNA. Translation: AAH03092.1 .
    BC015123 mRNA. Translation: AAH15123.1 .
    BC053904 mRNA. Translation: AAH53904.1 .
    BC075836 mRNA. Translation: AAH75836.1 .
    CCDSi CCDS366.1. [Q09028-1 ]
    CCDS44105.1. [Q09028-2 ]
    CCDS44106.1. [Q09028-4 ]
    PIRi S36112.
    RefSeqi NP_001128727.1. NM_001135255.1. [Q09028-2 ]
    NP_001128728.1. NM_001135256.1. [Q09028-4 ]
    NP_005601.1. NM_005610.2. [Q09028-1 ]
    UniGenei Hs.16003.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XU7 X-ray 1.90 A/B 1-425 [» ]
    3GFC X-ray 2.30 A 1-425 [» ]
    4PBY X-ray 2.50 A/B 1-425 [» ]
    4PBZ X-ray 2.15 A 1-425 [» ]
    4PC0 X-ray 2.50 A/B 1-425 [» ]
    ProteinModelPortali Q09028.
    SMRi Q09028. Positions 11-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111863. 146 interactions.
    DIPi DIP-33495N.
    IntActi Q09028. 55 interactions.
    MINTi MINT-90543.
    STRINGi 9606.ENSP00000362592.

    PTM databases

    PhosphoSitei Q09028.

    Polymorphism databases

    DMDMi 1172846.

    Proteomic databases

    MaxQBi Q09028.
    PaxDbi Q09028.
    PRIDEi Q09028.

    Protocols and materials databases

    DNASUi 5928.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373485 ; ENSP00000362584 ; ENSG00000162521 . [Q09028-3 ]
    ENST00000373493 ; ENSP00000362592 ; ENSG00000162521 . [Q09028-1 ]
    ENST00000414241 ; ENSP00000398242 ; ENSG00000162521 . [Q09028-2 ]
    ENST00000458695 ; ENSP00000396057 ; ENSG00000162521 . [Q09028-4 ]
    GeneIDi 5928.
    KEGGi hsa:5928.
    UCSCi uc001bvr.3. human. [Q09028-1 ]
    uc001bvs.3. human. [Q09028-2 ]

    Organism-specific databases

    CTDi 5928.
    GeneCardsi GC01P033116.
    HGNCi HGNC:9887. RBBP4.
    HPAi CAB006264.
    MIMi 602923. gene.
    neXtProti NX_Q09028.
    PharmGKBi PA34251.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2319.
    HOVERGENi HBG053236.
    InParanoidi Q09028.
    KOi K10752.
    OMAi CQPDLRL.
    OrthoDBi EOG70PBXB.
    PhylomeDBi Q09028.
    TreeFami TF106485.

    Enzyme and pathway databases

    Reactomei REACT_1006. Polo-like kinase mediated events.
    REACT_111214. G0 and Early G1.
    REACT_169436. Oxidative Stress Induced Senescence.
    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 Q09028.

    Miscellaneous databases

    ChiTaRSi RBBP4. human.
    EvolutionaryTracei Q09028.
    GeneWikii RBBP4.
    GenomeRNAii 5928.
    NextBioi 23094.
    PROi Q09028.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q09028.
    Bgeei Q09028.
    CleanExi HS_RBBP4.
    Genevestigatori Q09028.

    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. "A retinoblastoma-binding protein related to a negative regulator of Ras in yeast."
      Qian Y.-W., Wang Y.-C.J., Hollingsworth R.E. Jr., Jones D., Ling N., Lee E.Y.-H.P.
      Nature 364:648-652(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 134-158 AND 254-271.
    2. "Molecular cloning and expression of two novel human cDNAs encoding proteins containing WD-40 repeats and sharing similarity to yeast MSI1 a negative regulation of the RAS-cAMP pathway."
      Nielsen M.S., Rasmussen H.H., Celis J.E., Leffers H.
      Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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] (ISOFORMS 1 AND 4).
      Tissue: Brain.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Liver.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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).
      Tissue: Bone marrow, Brain, Eye and Uterus.
    9. Bienvenut W.V.
      Submitted (FEB-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15 AND 297-304, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    10. "Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes."
      Bauw G., Rasmussen H.H., van den Bulcke M., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 11:528-536(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
      Tissue: Keratinocyte.
    11. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
      Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
      Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 60-65; 144-160 AND 221-240.
      Tissue: Keratinocyte.
    12. "Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4."
      Verreault A., Kaufman P.D., Kobayashi R., Stillman B.
      Cell 87:95-104(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN THE CAF-1 COMPLEX, INTERACTION WITH HISTONE H4.
    13. "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.
    14. "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: INTERACTION WITH RB1.
    15. "A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p."
      Taunton J., Hassig C.A., Schreiber S.L.
      Science 272:408-411(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC1.
    16. "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.
    17. "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 HISTONE H4.
    18. "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.
    19. "A role for histone deacetylase activity in HDAC1-mediated transcriptional repression."
      Hassig C.A., Tong J.K., Fleischer T.C., Owa T., Grable P.G., Ayer D.E., Schreiber S.L.
      Proc. Natl. Acad. Sci. U.S.A. 95:3519-3524(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC1.
    20. "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.
    21. "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.
    22. "RbAp48 belongs to the histone deacetylase complex that associates with the retinoblastoma protein."
      Nicolas E., Morales V., Magnaghi-Jaulin L., Harel-Bellan A., Richard-Foy H., Trouche D.
      J. Biol. Chem. 275:9797-9804(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC1 AND RB1.
    23. "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.
    24. "Sharp, an inducible cofactor that integrates nuclear receptor repression and activation."
      Shi Y., Downes M., Xie W., Kao H.-Y., Ordentlich P., Tsai C.-C., Hon M., Evans R.M.
      Genes Dev. 15:1140-1151(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPEN.
    25. "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.
    26. "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 A SIN3 HDAC COMPLEX.
    27. "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; RBBP7 AND SUZ12, TRANSIENT INTERACTION WITH HDAC1, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
    28. "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 MULTIPLE SIN3 HDAC COMPLEXES.
    29. "Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
      Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
      Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH AEBP2; EED; EZH2 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
    30. "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.
    31. "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: INTERACTION WITH MTA1.
    32. "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.
    33. "MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing."
      Jin S.-G., Jiang C.-L., Rauch T., Li H., Pfeifer G.P.
      J. Biol. Chem. 280:12700-12709(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBD3L2.
    34. "LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes."
      Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.
      Cell Cycle 6:1903-1913(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
    35. "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence."
      Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.
      Mol. Cell 26:539-551(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
    36. "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].
    37. "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-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    38. "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].
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    42. "Structural and functional insights into the human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6."
      Liu Z., Li F., Ruan K., Zhang J., Mei Y., Wu J., Shi Y.
      J. Biol. Chem. 289:10069-10083(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PHF6.

    Entry informationi

    Entry nameiRBBP4_HUMAN
    AccessioniPrimary (citable) accession number: Q09028
    Secondary accession number(s): B2R6G9
    , B4DRH0, D3DPQ3, P31149, Q53H02, Q96BV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 160 of the entry and version 3 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 1
      Human chromosome 1: 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