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Q24572

- CAF1_DROME

UniProt

Q24572 - CAF1_DROME

Protein

Probable histone-binding protein Caf1

Gene

Caf1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 nucleosome remodeling and deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the nucleosome remodeling factor (NURF) complex, which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin; and the polycomb group (PcG) repressor complex ESC-E(Z), which promotes repression of homeotic genes during development. Also required for transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2.5 Publications

    GO - Molecular functioni

    1. histone acetyltransferase binding Source: FlyBase
    2. histone binding Source: FlyBase
    3. histone deacetylase binding Source: FlyBase
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: FlyBase

    GO - Biological processi

    1. chromatin assembly Source: FlyBase
    2. chromatin silencing Source: FlyBase
    3. dendrite morphogenesis Source: FlyBase
    4. DNA repair Source: FlyBase
    5. eggshell chorion gene amplification Source: FlyBase
    6. histone acetylation Source: FlyBase
    7. histone H3-K27 methylation Source: GOC
    8. histone H3-K9 methylation Source: GOC
    9. histone methylation Source: FlyBase
    10. mitotic cytokinesis Source: FlyBase
    11. muscle organ development Source: FlyBase
    12. negative regulation of transcription from RNA polymerase II promoter Source: FlyBase
    13. neuron development Source: FlyBase
    14. neuron projection morphogenesis Source: FlyBase
    15. nucleosome assembly Source: FlyBase
    16. nucleosome mobilization Source: FlyBase
    17. nucleosome positioning Source: FlyBase
    18. positive regulation of cell proliferation Source: FlyBase
    19. regulation of mitotic cell cycle Source: FlyBase
    20. segment specification Source: FlyBase
    21. transcription, DNA-templated Source: FlyBase

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_180658. G0 and Early G1.
    SignaLinkiQ24572.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable histone-binding protein Caf1
    Alternative name(s):
    Chromatin assembly factor 1 p55 subunit
    Short name:
    CAF-1 p55 subunit
    Nucleosome-remodeling factor 55 kDa subunit
    Short name:
    NURF-55
    dCAF-1
    Gene namesi
    Name:Caf1
    ORF Names:CG4236
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0263979. Caf1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. CAF-1 complex Source: FlyBase
    2. ESC/E(Z) complex Source: FlyBase
    3. histone methyltransferase complex Source: FlyBase
    4. Myb complex Source: FlyBase
    5. nucleus Source: FlyBase
    6. NuRD complex Source: FlyBase
    7. NURF complex Source: FlyBase
    8. polytene chromosome Source: FlyBase
    9. Sin3-type complex Source: FlyBase
    10. transcription factor complex Source: FlyBase

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 430430Probable histone-binding protein Caf1PRO_0000050895Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine1 Publication
    Modified residuei100 – 1001Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ24572.
    PRIDEiQ24572.

    Expressioni

    Developmental stagei

    Highest level during early embryogenesis and then decreases in larvae, pupae and adults.1 Publication

    Gene expression databases

    BgeeiQ24572.

    Interactioni

    Subunit structurei

    Probably binds directly to helix 1 of the histone fold of histone H4, a region that is not accessible when H4 is in chromatin. Self associates. Associates with chromatin. Component of the CAF-1 complex, composed of Caf1, Caf1-105 and Caf1-180. Within the CAF-1 complex, Caf1-180 interacts directly with both Caf1 and Caf1-105. Component of the NuRD complex, composed of at least Caf1, Mi-2, MTA1-like and Rpd3. Within the NuRD complex, Caf1 may interact directly with Mi-2, MTA1-like and Rpd3. The NuRD complex may also associate with the methyl-DNA binding protein MBD-like via Caf1 and Mi-2. Component of the NURF complex, composed of Caf1, E(bx), Nurf-38 and Iswi. Component of the Esc/E(z) complex, composed of Caf1, esc, E(z), Su(z)1, and possibly Pho1. The Esc/E(z) complex may also associate with Pcl and Rpd3 during early embryogenesis. Interacts with Rbf and Rbf2. Component of the DREAM complex at least composed of Myb, Caf1, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52, Rpd3 and l3mbt.13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    E(z)P421247EBI-75924,EBI-112315
    escQ2433811EBI-75924,EBI-88911
    Rpd3Q945174EBI-75924,EBI-302197

    Protein-protein interaction databases

    BioGridi66900. 35 interactions.
    DIPiDIP-23697N.
    IntActiQ24572. 20 interactions.
    MINTiMINT-252601.
    STRINGi7227.FBpp0082511.

    Structurei

    Secondary structure

    1
    430
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 3524
    Beta strandi36 – 438
    Beta strandi51 – 533
    Beta strandi66 – 738
    Beta strandi77 – 793
    Beta strandi81 – 9010
    Beta strandi119 – 12911
    Beta strandi132 – 1376
    Beta strandi140 – 1478
    Beta strandi149 – 1513
    Beta strandi153 – 1575
    Helixi158 – 1603
    Beta strandi174 – 1785
    Beta strandi187 – 1893
    Beta strandi191 – 1933
    Beta strandi196 – 2005
    Beta strandi206 – 2105
    Helixi217 – 2193
    Beta strandi220 – 2223
    Beta strandi224 – 2274
    Beta strandi234 – 2396
    Beta strandi246 – 2516
    Beta strandi254 – 2607
    Beta strandi266 – 2683
    Beta strandi270 – 2745
    Beta strandi280 – 2856
    Beta strandi292 – 2976
    Beta strandi300 – 3067
    Helixi307 – 3093
    Beta strandi314 – 3185
    Beta strandi324 – 3296
    Beta strandi336 – 3416
    Beta strandi342 – 3443
    Beta strandi347 – 3504
    Helixi351 – 3533
    Helixi360 – 3656
    Beta strandi370 – 3734
    Beta strandi381 – 3866
    Beta strandi388 – 3903
    Beta strandi393 – 3986
    Beta strandi401 – 4088
    Helixi410 – 4134

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XYIX-ray1.75A1-430[»]
    2YB8X-ray2.30B1-418[»]
    2YBAX-ray2.55A/B1-418[»]
    3C99X-ray2.90A1-430[»]
    3C9CX-ray3.20A1-430[»]
    ProteinModelPortaliQ24572.
    SMRiQ24572. Positions 9-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ24572.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati126 – 15934WD 1Add
    BLAST
    Repeati179 – 21032WD 2Add
    BLAST
    Repeati229 – 26032WD 3Add
    BLAST
    Repeati275 – 30632WD 4Add
    BLAST
    Repeati319 – 35032WD 5Add
    BLAST
    Repeati376 – 40732WD 6Add
    BLAST

    Sequence similaritiesi

    Contains 6 WD repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG2319.
    GeneTreeiENSGT00570000079069.
    InParanoidiQ24572.
    KOiK10752.
    OMAiCQPDLRL.
    PhylomeDBiQ24572.

    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]

    Sequencei

    Sequence statusi: Complete.

    Q24572-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDRSDNAAE SFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT    50
    AQWLPDVTKQ DGKDYSVHRL ILGTHTSDEQ NHLLIASVQL PSEDAQFDGS 100
    HYDNEKGEFG GFGSVCGKIE IEIKINHEGE VNRARYMPQN ACVIATKTPS 150
    SDVLVFDYTK HPSKPEPSGE CQPDLRLRGH QKEGYGLSWN PNLNGYLLSA 200
    SDDHTICLWD INATPKEHRV IDAKNIFTGH TAVVEDVAWH LLHESLFGSV 250
    ADDQKLMIWD TRNNNTSKPS HTVDAHTAEV NCLSFNPYSE FILATGSADK 300
    TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLHVWD 350
    LSKIGEEQST EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWIICSVSED 400
    NIMQVWQMAE NVYNDEEPEI PASELETNTA 430
    Length:430
    Mass (Da):48,635
    Last modified:November 1, 1996 - v1
    Checksum:i90C5FB959F1660D5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62388 mRNA. Translation: AAB37257.1.
    AM294392 Genomic DNA. Translation: CAL26322.1.
    AM294393 Genomic DNA. Translation: CAL26323.1.
    AM294394 Genomic DNA. Translation: CAL26324.1.
    AM294395 Genomic DNA. Translation: CAL26325.1.
    AM294396 Genomic DNA. Translation: CAL26330.1.
    AM294397 Genomic DNA. Translation: CAL26335.1.
    AM294398 Genomic DNA. Translation: CAL26337.1.
    AM294399 Genomic DNA. Translation: CAL26338.1.
    AM294400 Genomic DNA. Translation: CAL26339.1.
    AM294401 Genomic DNA. Translation: CAL26340.1.
    AM294402 Genomic DNA. Translation: CAL26341.1.
    AM294403 Genomic DNA. Translation: CAL26342.1.
    AE014297 Genomic DNA. Translation: AAF55146.1.
    AY061408 mRNA. Translation: AAL28956.1.
    RefSeqiNP_524354.1. NM_079630.4.
    UniGeneiDm.1657.

    Genome annotation databases

    EnsemblMetazoaiFBtr0083052; FBpp0082511; FBgn0263979.
    GeneIDi41836.
    KEGGidme:Dmel_CG4236.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62388 mRNA. Translation: AAB37257.1 .
    AM294392 Genomic DNA. Translation: CAL26322.1 .
    AM294393 Genomic DNA. Translation: CAL26323.1 .
    AM294394 Genomic DNA. Translation: CAL26324.1 .
    AM294395 Genomic DNA. Translation: CAL26325.1 .
    AM294396 Genomic DNA. Translation: CAL26330.1 .
    AM294397 Genomic DNA. Translation: CAL26335.1 .
    AM294398 Genomic DNA. Translation: CAL26337.1 .
    AM294399 Genomic DNA. Translation: CAL26338.1 .
    AM294400 Genomic DNA. Translation: CAL26339.1 .
    AM294401 Genomic DNA. Translation: CAL26340.1 .
    AM294402 Genomic DNA. Translation: CAL26341.1 .
    AM294403 Genomic DNA. Translation: CAL26342.1 .
    AE014297 Genomic DNA. Translation: AAF55146.1 .
    AY061408 mRNA. Translation: AAL28956.1 .
    RefSeqi NP_524354.1. NM_079630.4.
    UniGenei Dm.1657.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XYI X-ray 1.75 A 1-430 [» ]
    2YB8 X-ray 2.30 B 1-418 [» ]
    2YBA X-ray 2.55 A/B 1-418 [» ]
    3C99 X-ray 2.90 A 1-430 [» ]
    3C9C X-ray 3.20 A 1-430 [» ]
    ProteinModelPortali Q24572.
    SMRi Q24572. Positions 9-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66900. 35 interactions.
    DIPi DIP-23697N.
    IntActi Q24572. 20 interactions.
    MINTi MINT-252601.
    STRINGi 7227.FBpp0082511.

    Proteomic databases

    PaxDbi Q24572.
    PRIDEi Q24572.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0083052 ; FBpp0082511 ; FBgn0263979 .
    GeneIDi 41836.
    KEGGi dme:Dmel_CG4236.

    Organism-specific databases

    CTDi 41836.
    FlyBasei FBgn0263979. Caf1.

    Phylogenomic databases

    eggNOGi COG2319.
    GeneTreei ENSGT00570000079069.
    InParanoidi Q24572.
    KOi K10752.
    OMAi CQPDLRL.
    PhylomeDBi Q24572.

    Enzyme and pathway databases

    Reactomei REACT_180658. G0 and Early G1.
    SignaLinki Q24572.

    Miscellaneous databases

    EvolutionaryTracei Q24572.
    GenomeRNAii 41836.
    NextBioi 825799.
    PROi Q24572.

    Gene expression databases

    Bgeei Q24572.

    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. "The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to a histone deacetylase-associated protein."
      Tyler J.K., Bulger M., Kamakaka R.T., Kobayashi R., Kadonaga J.T.
      Mol. Cell. Biol. 16:6149-6159(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 256-268; 301-313; 322-334 AND 354-376, FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
      Strain: Canton-S.
    2. "Widespread adaptive evolution of Drosophila genes with sex-biased expression."
      Proeschel M., Zhang Z., Parsch J.
      Genetics 174:893-900(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229, ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84 and ZBMEL95.
    3. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    4. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
    6. "Drosophila NURF-55, a WD repeat protein involved in histone metabolism."
      Martinez-Balbas M.A., Tsukiyama T., Gdula D., Wu C.
      Proc. Natl. Acad. Sci. U.S.A. 95:132-137(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 64-80; 256-269; 301-310; 314-339 AND 354-368, FUNCTION, IDENTIFICATION IN THE NURF COMPLEX, ASSOCIATION WITH CHROMATIN, SUBCELLULAR LOCATION.
    7. "Assembly of regularly spaced nucleosome arrays by Drosophila chromatin assembly factor 1 and a 56-kDa histone-binding protein."
      Bulger M., Ito T., Kamakaka R.T., Kadonaga J.T.
      Proc. Natl. Acad. Sci. U.S.A. 92:11726-11730(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE CAF-1 COMPLEX.
    8. "Postreplicative chromatin assembly by Drosophila and human chromatin assembly factor 1."
      Kamakaka R.T., Bulger M., Kaufman P.D., Stillman B., Kadonaga J.T.
      Mol. Cell. Biol. 16:810-817(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE CAF-1 COMPLEX.
    9. "Inorganic pyrophosphatase is a component of the Drosophila nucleosome remodeling factor complex."
      Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C.
      Genes Dev. 12:3206-3216(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ISWI AND NURF-38.
    10. "The Drosophila polycomb group proteins ESC and E(Z) are present in a complex containing the histone-binding protein p55 and the histone deacetylase RPD3."
      Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.
      Development 128:275-286(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND RPD3.
    11. "Interaction between the Drosophila CAF-1 and ASF1 chromatin assembly factors."
      Tyler J.K., Collins K.A., Prasad-Sinha J., Amiott E., Bulger M., Harte P.J., Kobayashi R., Kadonaga J.T.
      Mol. Cell. Biol. 21:6574-6584(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CAF1-105 AND CAF1-180.
    12. "Drosophila Enhancer of zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites."
      Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.
      Cell 111:185-196(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); RPD3 AND SU(Z)12.
    13. "Histone methyltransferase activity of a Drosophila Polycomb group repressor complex."
      Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B., Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.
      Cell 111:197-208(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND SU(Z)12.
    14. "Role for a Drosophila Myb-containing protein complex in site-specific DNA replication."
      Beall E.L., Manak J.R., Zhou S., Bell M., Lipsick J.S., Botchan M.R.
      Nature 420:833-837(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE DREAM COMPLEX.
    15. "Polycomb group proteins ESC and E(Z) are present in multiple distinct complexes that undergo dynamic changes during development."
      Furuyama T., Tie F., Harte P.J.
      Genesis 35:114-124(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND RPD3.
    16. "A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike and RPD3."
      Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.
      Mol. Cell. Biol. 23:3352-3362(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); PCL; RPD3 AND SU(Z)12.
    17. "The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD complex via p55 and MI-2."
      Marhold J., Brehm A., Kramer K.
      BMC Mol. Biol. 5:20-20(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE NURD COMPLEX, SELF-ASSOCIATION.
    18. "Native E2F/RBF complexes contain Myb-interacting proteins and repress transcription of developmentally controlled E2F target genes."
      Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O., Aasland R., White-Cooper H., Dyson N., Brehm A.
      Cell 119:181-193(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
    19. "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor complex."
      Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J., Botchan M.R.
      Genes Dev. 18:2929-2940(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE DREAM COMPLEX.
    20. "p55, the Drosophila ortholog of RbAp46/RbAp48, is required for the repression of dE2F2/RBF-regulated genes."
      Taylor-Harding B., Binne U.K., Korenjak M., Brehm A., Dyson N.J.
      Mol. Cell. Biol. 24:9124-9136(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RBF AND RBF2.
    21. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, IDENTIFICATION BY MASS SPECTROMETRY.
    22. "Phosphoproteome analysis of Drosophila melanogaster embryos."
      Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
      J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiCAF1_DROME
    AccessioniPrimary (citable) accession number: Q24572
    Secondary accession number(s): A0AP04, Q9VFB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3