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Q24572 (CAF1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Caf1
ORF Names:CG4236
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.6 Ref.9 Ref.14 Ref.20

Subunit structure

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. Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

Nucleus Ref.1 Ref.6.

Developmental stage

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

Sequence similarities

Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.

Contains 6 WD repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
WD repeat
   Molecular functionChromatin regulator
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Traceable author statement PubMed 9230310. Source: FlyBase

chromatin assembly

Inferred from direct assay Ref.1. Source: FlyBase

chromatin silencing

Inferred from physical interaction Ref.10. Source: FlyBase

dendrite morphogenesis

Inferred from mutant phenotype PubMed 16547170. Source: FlyBase

eggshell chorion gene amplification

Inferred by curator Ref.14. Source: FlyBase

histone H3-K27 methylation

Inferred by curator Ref.12Ref.13. Source: GOC

histone H3-K9 methylation

Inferred by curator Ref.12. Source: GOC

histone acetylation

Inferred from direct assay Ref.6. Source: FlyBase

histone methylation

Inferred from direct assay Ref.12Ref.13. Source: FlyBase

mitotic cytokinesis

Inferred from mutant phenotype PubMed 15380073. Source: FlyBase

muscle organ development

Inferred from mutant phenotype PubMed 16547170. Source: FlyBase

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.19. Source: FlyBase

neuron development

Inferred from mutant phenotype PubMed 16547170. Source: FlyBase

neuron projection morphogenesis

Inferred from mutant phenotype PubMed 18604272. Source: FlyBase

nucleosome assembly

Inferred from direct assay PubMed 10591219PubMed 9230310. Source: FlyBase

nucleosome mobilization

Inferred from direct assay PubMed 10399912. Source: FlyBase

nucleosome positioning

Inferred from direct assay Ref.7. Source: FlyBase

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 22241697. Source: FlyBase

regulation of mitotic cell cycle

Inferred from mutant phenotype PubMed 12077326. Source: FlyBase

segment specification

Inferred from mutant phenotype PubMed 21490066. Source: FlyBase

transcription, DNA-templated

Inferred from direct assay PubMed 11279013. Source: FlyBase

   Cellular_componentCAF-1 complex

Inferred from direct assay Ref.1. Source: FlyBase

ESC/E(Z) complex

Inferred from direct assay Ref.12Ref.13PubMed 18276122PubMed 22354997. Source: FlyBase

Myb complex

Inferred from direct assay Ref.14Ref.18Ref.19. Source: FlyBase

NURF complex

Inferred from physical interaction Ref.6. Source: FlyBase

NuRD complex

Inferred from direct assay Ref.17PubMed 20733004. Source: FlyBase

Sin3-type complex

Inferred from direct assay PubMed 20566628. Source: FlyBase

histone methyltransferase complex

Inferred from direct assay PubMed 16055700. Source: FlyBase

nucleus

Inferred from direct assay Ref.10Ref.12Ref.1Ref.6. Source: FlyBase

polytene chromosome

Inferred from direct assay Ref.6. Source: FlyBase

transcription factor complex

Inferred from physical interaction PubMed 12459787. Source: FlyBase

   Molecular_functionhistone acetyltransferase binding

Inferred from physical interaction Ref.6. Source: FlyBase

histone binding

Inferred from direct assay PubMed 21550984. Source: FlyBase

histone deacetylase binding

Inferred from direct assay Ref.1. Source: FlyBase

protein homodimerization activity

Inferred from physical interaction Ref.17. Source: FlyBase

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Probable histone-binding protein Caf1
PRO_0000050895

Regions

Repeat126 – 15934WD 1
Repeat179 – 21032WD 2
Repeat229 – 26032WD 3
Repeat275 – 30632WD 4
Repeat319 – 35032WD 5
Repeat376 – 40732WD 6

Amino acid modifications

Modified residue111Phosphoserine Ref.21
Modified residue1001Phosphoserine Ref.22

Secondary structure

............................................................................... 430
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q24572 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 90C5FB959F1660D5

FASTA43048,635
        10         20         30         40         50         60 
MVDRSDNAAE SFDDAVEERV INEEYKIWKK NTPFLYDLVM THALEWPSLT AQWLPDVTKQ 

        70         80         90        100        110        120 
DGKDYSVHRL ILGTHTSDEQ NHLLIASVQL PSEDAQFDGS HYDNEKGEFG GFGSVCGKIE 

       130        140        150        160        170        180 
IEIKINHEGE VNRARYMPQN ACVIATKTPS SDVLVFDYTK HPSKPEPSGE CQPDLRLRGH 

       190        200        210        220        230        240 
QKEGYGLSWN PNLNGYLLSA SDDHTICLWD INATPKEHRV IDAKNIFTGH TAVVEDVAWH 

       250        260        270        280        290        300 
LLHESLFGSV ADDQKLMIWD TRNNNTSKPS HTVDAHTAEV NCLSFNPYSE FILATGSADK 

       310        320        330        340        350        360 
TVALWDLRNL KLKLHSFESH KDEIFQVQWS PHNETILASS GTDRRLHVWD LSKIGEEQST 

       370        380        390        400        410        420 
EDAEDGPPEL LFIHGGHTAK ISDFSWNPNE PWIICSVSED NIMQVWQMAE NVYNDEEPEI 

       430 
PASELETNTA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_524354.1. NM_079630.4.
UniGeneDm.1657.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XYIX-ray1.75A1-430[»]
2YB8X-ray2.30B1-418[»]
2YBAX-ray2.55A/B1-418[»]
3C99X-ray2.90A1-430[»]
3C9CX-ray3.20A1-430[»]
ProteinModelPortalQ24572.
SMRQ24572. Positions 9-415.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66900. 35 interactions.
DIPDIP-23697N.
IntActQ24572. 20 interactions.
MINTMINT-252601.
STRING7227.FBpp0082511.

Proteomic databases

PaxDbQ24572.
PRIDEQ24572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0083052; FBpp0082511; FBgn0263979.
GeneID41836.
KEGGdme:Dmel_CG4236.

Organism-specific databases

CTD41836.
FlyBaseFBgn0263979. Caf1.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00570000079069.
InParanoidQ24572.
KOK10752.
OMACQPDLRL.
PhylomeDBQ24572.

Enzyme and pathway databases

SignaLinkQ24572.

Gene expression databases

BgeeQ24572.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. 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]
PfamPF12265. CAF1C_H4-bd. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ24572.
GenomeRNAi41836.
NextBio825799.
PROQ24572.

Entry information

Entry nameCAF1_DROME
AccessionPrimary (citable) accession number: Q24572
Secondary accession number(s): A0AP04, Q9VFB4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase