CAF1_DROME
ID CAF1_DROME Reviewed; 430 AA.
AC Q24572; A0AP04; Q9VFB4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Chromatin assembly factor 1 p55 subunit {ECO:0000303|PubMed:8887645, ECO:0000312|FlyBase:FBgn0263979};
DE Short=CAF-1 p55 subunit {ECO:0000303|PubMed:8887645};
DE AltName: Full=CAF-1 {ECO:0000303|PubMed:8887645};
DE AltName: Full=Nucleosome-remodeling factor 55 kDa subunit {ECO:0000303|PubMed:9419341};
DE Short=NURF-55 {ECO:0000303|PubMed:9419341};
GN Name=Caf1-55 {ECO:0000312|FlyBase:FBgn0263979};
GN Synonyms=Caf1 {ECO:0000312|FlyBase:FBgn0263979};
GN ORFNames=CG4236 {ECO:0000312|FlyBase:FBgn0263979};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 256-268; 301-313; 322-334
RP AND 354-376, FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=8887645; DOI=10.1128/mcb.16.11.6149;
RA Tyler J.K., Bulger M., Kamakaka R.T., Kobayashi R., Kadonaga J.T.;
RT "The p55 subunit of Drosophila chromatin assembly factor 1 is homologous to
RT a histone deacetylase-associated protein.";
RL Mol. Cell. Biol. 16:6149-6159(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL229,
RC ZBMEL377, ZBMEL384, ZBMEL398, ZBMEL82, ZBMEL84, and ZBMEL95;
RX PubMed=16951084; DOI=10.1534/genetics.106.058008;
RA Proeschel M., Zhang Z., Parsch J.;
RT "Widespread adaptive evolution of Drosophila genes with sex-biased
RT expression.";
RL Genetics 174:893-900(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP PROTEIN SEQUENCE OF 64-80; 256-269; 301-310; 314-339 AND 354-368, FUNCTION,
RP IDENTIFICATION IN THE NURF COMPLEX, ASSOCIATION WITH CHROMATIN, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9419341; DOI=10.1073/pnas.95.1.132;
RA Martinez-Balbas M.A., Tsukiyama T., Gdula D., Wu C.;
RT "Drosophila NURF-55, a WD repeat protein involved in histone metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:132-137(1998).
RN [7]
RP CHARACTERIZATION OF THE CAF-1 COMPLEX.
RX PubMed=8524837; DOI=10.1073/pnas.92.25.11726;
RA Bulger M., Ito T., Kamakaka R.T., Kadonaga J.T.;
RT "Assembly of regularly spaced nucleosome arrays by Drosophila chromatin
RT assembly factor 1 and a 56-kDa histone-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11726-11730(1995).
RN [8]
RP CHARACTERIZATION OF THE CAF-1 COMPLEX.
RX PubMed=8622682; DOI=10.1128/mcb.16.3.810;
RA Kamakaka R.T., Bulger M., Kaufman P.D., Stillman B., Kadonaga J.T.;
RT "Postreplicative chromatin assembly by Drosophila and human chromatin
RT assembly factor 1.";
RL Mol. Cell. Biol. 16:810-817(1996).
RN [9]
RP FUNCTION, AND INTERACTION WITH ISWI AND NURF-38.
RX PubMed=9784495; DOI=10.1101/gad.12.20.3206;
RA Gdula D.A., Sandaltzopoulos R., Tsukiyama T., Ossipow V., Wu C.;
RT "Inorganic pyrophosphatase is a component of the Drosophila nucleosome
RT remodeling factor complex.";
RL Genes Dev. 12:3206-3216(1998).
RN [10]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND HDAC1.
RX PubMed=11124122; DOI=10.1242/dev.128.2.275;
RA Tie F., Furuyama T., Prasad-Sinha J., Jane E., Harte P.J.;
RT "The Drosophila polycomb group proteins ESC and E(Z) are present in a
RT complex containing the histone-binding protein p55 and the histone
RT deacetylase RPD3.";
RL Development 128:275-286(2001).
RN [11]
RP INTERACTION WITH CAF1-105 AND CAF1-180.
RX PubMed=11533245; DOI=10.1128/mcb.21.19.6574-6584.2001;
RA Tyler J.K., Collins K.A., Prasad-Sinha J., Amiott E., Bulger M.,
RA Harte P.J., Kobayashi R., Kadonaga J.T.;
RT "Interaction between the Drosophila CAF-1 and ASF1 chromatin assembly
RT factors.";
RL Mol. Cell. Biol. 21:6574-6584(2001).
RN [12]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); HDAC1 AND SU(Z)12.
RX PubMed=12408863; DOI=10.1016/s0092-8674(02)00975-3;
RA Czermin B., Melfi R., McCabe D., Seitz V., Imhof A., Pirrotta V.;
RT "Drosophila Enhancer of zeste/ESC complexes have a histone H3
RT methyltransferase activity that marks chromosomal Polycomb sites.";
RL Cell 111:185-196(2002).
RN [13]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND SU(Z)12.
RX PubMed=12408864; DOI=10.1016/s0092-8674(02)00976-5;
RA Mueller J., Hart C.M., Francis N.J., Vargas M.L., Sengupta A., Wild B.,
RA Miller E.L., O'Connor M.B., Kingston R.E., Simon J.A.;
RT "Histone methyltransferase activity of a Drosophila Polycomb group
RT repressor complex.";
RL Cell 111:197-208(2002).
RN [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP DREAM COMPLEX.
RX PubMed=12490953; DOI=10.1038/nature01228;
RA Beall E.L., Manak J.R., Zhou S., Bell M., Lipsick J.S., Botchan M.R.;
RT "Role for a Drosophila Myb-containing protein complex in site-specific DNA
RT replication.";
RL Nature 420:833-837(2002).
RN [15]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z) AND HDAC1.
RX PubMed=12533794; DOI=10.1002/gene.10173;
RA Furuyama T., Tie F., Harte P.J.;
RT "Polycomb group proteins ESC and E(Z) are present in multiple distinct
RT complexes that undergo dynamic changes during development.";
RL Genesis 35:114-124(2003).
RN [16]
RP IDENTIFICATION IN AN ESC/E(Z) COMPLEX WITH ESC; E(Z); PCL; HDAC1 AND
RP SU(Z)12.
RX PubMed=12697833; DOI=10.1128/mcb.23.9.3352-3362.2003;
RA Tie F., Prasad-Sinha J., Birve A., Rasmuson-Lestander A., Harte P.J.;
RT "A 1-megadalton ESC/E(Z) complex from Drosophila that contains polycomblike
RT and RPD3.";
RL Mol. Cell. Biol. 23:3352-3362(2003).
RN [17]
RP IDENTIFICATION IN THE NURD COMPLEX, AND SELF-ASSOCIATION.
RX PubMed=15516265; DOI=10.1186/1471-2199-5-20;
RA Marhold J., Brehm A., Kramer K.;
RT "The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD
RT complex via p55 and MI-2.";
RL BMC Mol. Biol. 5:20-20(2004).
RN [18]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15479636; DOI=10.1016/j.cell.2004.09.034;
RA Korenjak M., Taylor-Harding B., Binne U.K., Satterlee J.S., Stevaux O.,
RA Aasland R., White-Cooper H., Dyson N., Brehm A.;
RT "Native E2F/RBF complexes contain Myb-interacting proteins and repress
RT transcription of developmentally controlled E2F target genes.";
RL Cell 119:181-193(2004).
RN [19]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=15545624; DOI=10.1101/gad.1255204;
RA Lewis P.W., Beall E.L., Fleischer T.C., Georlette D., Link A.J.,
RA Botchan M.R.;
RT "Identification of a Drosophila Myb-E2F2/RBF transcriptional repressor
RT complex.";
RL Genes Dev. 18:2929-2940(2004).
RN [20]
RP FUNCTION, AND INTERACTION WITH RBF AND RBF2.
RX PubMed=15456884; DOI=10.1128/mcb.24.20.9124-9136.2004;
RA Taylor-Harding B., Binne U.K., Korenjak M., Brehm A., Dyson N.J.;
RT "p55, the Drosophila ortholog of RbAp46/RbAp48, is required for the
RT repression of dE2F2/RBF-regulated genes.";
RL Mol. Cell. Biol. 24:9124-9136(2004).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC assembly factors, chromatin remodeling factors and histone deacetylases
CC to their histone substrates in a manner that is regulated by
CC nucleosomal DNA. Component of several complexes which regulate
CC chromatin metabolism. These include the chromatin assembly factor 1
CC (CAF-1) complex, which is required for chromatin assembly following DNA
CC replication and DNA repair; the nucleosome remodeling and deacetylase
CC complex (the NuRD complex), which promotes transcriptional repression
CC by histone deacetylation and nucleosome remodeling; the nucleosome
CC remodeling factor (NURF) complex, which catalyzes ATP-dependent
CC nucleosome sliding and facilitates transcription of chromatin; and the
CC polycomb group (PcG) repressor complex ESC-E(Z), which promotes
CC repression of homeotic genes during development. Also required for
CC transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2.
CC {ECO:0000269|PubMed:12490953, ECO:0000269|PubMed:15456884,
CC ECO:0000269|PubMed:8887645, ECO:0000269|PubMed:9419341,
CC ECO:0000269|PubMed:9784495}.
CC -!- SUBUNIT: Probably binds directly to helix 1 of the histone fold of
CC histone H4, a region that is not accessible when H4 is in chromatin.
CC Self associates. Associates with chromatin. Component of the CAF-1
CC complex, composed of Caf1-55, Caf1-105 and Caf1-180. Within the CAF-1
CC complex, Caf1-180 interacts directly with both Caf1-55 and Caf1-105.
CC Component of the NuRD complex, composed of at least Caf1-55, Mi-2,
CC MTA1-like and HDAC1/Rpd3. Within the NuRD complex, Caf1-55 may interact
CC directly with Mi-2, MTA1-like and HDAC1/Rpd3. The NuRD complex may also
CC associate with the methyl-DNA binding protein MBD-like via Caf1-55 and
CC Mi-2. Component of the NURF complex, composed of Caf1-55, E(bx), Nurf-
CC 38 and Iswi. Component of the Esc/E(z) complex, composed of Caf1-55,
CC esc, E(z), Su(z)1, and possibly Pho1. The Esc/E(z) complex may also
CC associate with Pcl and HDAC1/Rpd3 during early embryogenesis. Interacts
CC with Rbf and Rbf2. Component of the DREAM complex at least composed of
CC Myb, Caf1-55, mip40, mip120, mip130, E2f2, Dp, Rbf, Rbf2, lin-52,
CC HDAC1/Rpd3 and l(3)mbt. {ECO:0000269|PubMed:11124122,
CC ECO:0000269|PubMed:11533245, ECO:0000269|PubMed:12408863,
CC ECO:0000269|PubMed:12408864, ECO:0000269|PubMed:12490953,
CC ECO:0000269|PubMed:12533794, ECO:0000269|PubMed:12697833,
CC ECO:0000269|PubMed:15456884, ECO:0000269|PubMed:15479636,
CC ECO:0000269|PubMed:15516265, ECO:0000269|PubMed:15545624,
CC ECO:0000269|PubMed:9419341, ECO:0000269|PubMed:9784495}.
CC -!- INTERACTION:
CC Q24572; Q9V6Q2: cid; NbExp=6; IntAct=EBI-75924, EBI-129287;
CC Q24572; P42124: E(z); NbExp=7; IntAct=EBI-75924, EBI-112315;
CC Q24572; Q24338: esc; NbExp=11; IntAct=EBI-75924, EBI-88911;
CC Q24572; Q94517: HDAC1; NbExp=4; IntAct=EBI-75924, EBI-302197;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8887645,
CC ECO:0000269|PubMed:9419341}.
CC -!- DEVELOPMENTAL STAGE: Highest level during early embryogenesis and then
CC decreases in larvae, pupae and adults. {ECO:0000269|PubMed:8887645}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
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DR EMBL; U62388; AAB37257.1; -; mRNA.
DR EMBL; AM294392; CAL26322.1; -; Genomic_DNA.
DR EMBL; AM294393; CAL26323.1; -; Genomic_DNA.
DR EMBL; AM294394; CAL26324.1; -; Genomic_DNA.
DR EMBL; AM294395; CAL26325.1; -; Genomic_DNA.
DR EMBL; AM294396; CAL26330.1; -; Genomic_DNA.
DR EMBL; AM294397; CAL26335.1; -; Genomic_DNA.
DR EMBL; AM294398; CAL26337.1; -; Genomic_DNA.
DR EMBL; AM294399; CAL26338.1; -; Genomic_DNA.
DR EMBL; AM294400; CAL26339.1; -; Genomic_DNA.
DR EMBL; AM294401; CAL26340.1; -; Genomic_DNA.
DR EMBL; AM294402; CAL26341.1; -; Genomic_DNA.
DR EMBL; AM294403; CAL26342.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF55146.1; -; Genomic_DNA.
DR EMBL; AY061408; AAL28956.1; -; mRNA.
DR RefSeq; NP_524354.1; NM_079630.4.
DR PDB; 2XYI; X-ray; 1.75 A; A=1-430.
DR PDB; 2YB8; X-ray; 2.30 A; B=1-418.
DR PDB; 2YBA; X-ray; 2.55 A; A/B=1-418.
DR PDB; 3C99; X-ray; 2.90 A; A=1-430.
DR PDB; 3C9C; X-ray; 3.20 A; A=1-430.
DR PDBsum; 2XYI; -.
DR PDBsum; 2YB8; -.
DR PDBsum; 2YBA; -.
DR PDBsum; 3C99; -.
DR PDBsum; 3C9C; -.
DR AlphaFoldDB; Q24572; -.
DR SMR; Q24572; -.
DR BioGRID; 66900; 76.
DR DIP; DIP-23697N; -.
DR IntAct; Q24572; 25.
DR MINT; Q24572; -.
DR STRING; 7227.FBpp0082511; -.
DR iPTMnet; Q24572; -.
DR PaxDb; Q24572; -.
DR PRIDE; Q24572; -.
DR DNASU; 41836; -.
DR EnsemblMetazoa; FBtr0083052; FBpp0082511; FBgn0263979.
DR GeneID; 41836; -.
DR KEGG; dme:Dmel_CG4236; -.
DR CTD; 41836; -.
DR FlyBase; FBgn0263979; Caf1-55.
DR VEuPathDB; VectorBase:FBgn0263979; -.
DR eggNOG; KOG0264; Eukaryota.
DR GeneTree; ENSGT00940000154748; -.
DR InParanoid; Q24572; -.
DR OMA; PHEEGCL; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; Q24572; -.
DR Reactome; R-DME-1538133; G0 and Early G1.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-3214815; HDACs deacetylate histones.
DR Reactome; R-DME-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-DME-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DME-8951664; Neddylation.
DR SignaLink; Q24572; -.
DR BioGRID-ORCS; 41836; 1 hit in 3 CRISPR screens.
DR EvolutionaryTrace; Q24572; -.
DR GenomeRNAi; 41836; -.
DR PRO; PR:Q24572; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0263979; Expressed in egg cell and 38 other tissues.
DR ExpressionAtlas; Q24572; baseline and differential.
DR Genevisible; Q24572; DM.
DR GO; GO:0033186; C:CAF-1 complex; IDA:FlyBase.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:FlyBase.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:FlyBase.
DR GO; GO:0031523; C:Myb complex; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0016581; C:NuRD complex; IDA:FlyBase.
DR GO; GO:0016589; C:NURF complex; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0070822; C:Sin3-type complex; IDA:FlyBase.
DR GO; GO:0005667; C:transcription regulator complex; IPI:FlyBase.
DR GO; GO:0042393; F:histone binding; IDA:FlyBase.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:FlyBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:FlyBase.
DR GO; GO:0031497; P:chromatin assembly; IDA:FlyBase.
DR GO; GO:0006338; P:chromatin remodeling; IDA:FlyBase.
DR GO; GO:0007307; P:eggshell chorion gene amplification; IC:FlyBase.
DR GO; GO:0140718; P:facultative heterochromatin assembly; IC:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IPI:FlyBase.
DR GO; GO:0016573; P:histone acetylation; IDA:FlyBase.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:FlyBase.
DR GO; GO:0006334; P:nucleosome assembly; IDA:FlyBase.
DR GO; GO:0034728; P:nucleosome organization; IDA:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007379; P:segment specification; IMP:FlyBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..430
FT /note="Chromatin assembly factor 1 p55 subunit"
FT /id="PRO_0000050895"
FT REPEAT 126..159
FT /note="WD 1"
FT REPEAT 179..210
FT /note="WD 2"
FT REPEAT 229..260
FT /note="WD 3"
FT REPEAT 275..306
FT /note="WD 4"
FT REPEAT 319..350
FT /note="WD 5"
FT REPEAT 376..407
FT /note="WD 6"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT HELIX 12..35
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 119..129
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:2XYI"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2YB8"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:2XYI"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:2XYI"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3C99"
FT STRAND 314..318
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:2YB8"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:2XYI"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:2XYI"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:2XYI"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:2XYI"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:2XYI"
SQ SEQUENCE 430 AA; 48635 MW; 90C5FB959F1660D5 CRC64;
MVDRSDNAAE SFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTKQ
DGKDYSVHRL ILGTHTSDEQ NHLLIASVQL PSEDAQFDGS HYDNEKGEFG GFGSVCGKIE
IEIKINHEGE VNRARYMPQN ACVIATKTPS SDVLVFDYTK HPSKPEPSGE CQPDLRLRGH
QKEGYGLSWN PNLNGYLLSA SDDHTICLWD INATPKEHRV IDAKNIFTGH TAVVEDVAWH
LLHESLFGSV ADDQKLMIWD TRNNNTSKPS HTVDAHTAEV NCLSFNPYSE FILATGSADK
TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLHVWD LSKIGEEQST
EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWIICSVSED NIMQVWQMAE NVYNDEEPEI
PASELETNTA
