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Q24572

- CAF1_DROME

UniProt

Q24572 - CAF1_DROME

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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

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 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
Complete GO annotation...

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
Complete GO annotation...

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.
ExpressionAtlasiQ24572. differential.

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

        10         20         30         40         50
MVDRSDNAAE SFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT
60 70 80 90 100
AQWLPDVTKQ DGKDYSVHRL ILGTHTSDEQ NHLLIASVQL PSEDAQFDGS
110 120 130 140 150
HYDNEKGEFG GFGSVCGKIE IEIKINHEGE VNRARYMPQN ACVIATKTPS
160 170 180 190 200
SDVLVFDYTK HPSKPEPSGE CQPDLRLRGH QKEGYGLSWN PNLNGYLLSA
210 220 230 240 250
SDDHTICLWD INATPKEHRV IDAKNIFTGH TAVVEDVAWH LLHESLFGSV
260 270 280 290 300
ADDQKLMIWD TRNNNTSKPS HTVDAHTAEV NCLSFNPYSE FILATGSADK
310 320 330 340 350
TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLHVWD
360 370 380 390 400
LSKIGEEQST EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWIICSVSED
410 420 430
NIMQVWQMAE NVYNDEEPEI PASELETNTA
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.
ExpressionAtlasi Q24572. differential.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 142 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