Q9V464 (ASF1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone chaperone asf1

Alternative name(s):
Anti-silencing function protein 1
Replication-coupling assembly factor subunit ASF1
Short name=RCAF subunit ASF1
dASF1

Gene names

Name:	asf1
ORF Names:	CG9383

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	218 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. Plays a role in the formation of silent heterochromatin. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Subunit structure	Component of the replication coupling assembly factor (RCAF), composed of asf1, histone H3 and histone H4. Interacts with the Caf1-105 subunit of the CAF-1 complex. Interacts with brm, mor and tlk. Ref.1 Ref.6 Ref.7 Ref.8
Subcellular location	Nucleus. Chromosome. Note: Localizes to multiple sites on polytene chromosomes including transcriptionally active developmental puffs, the chromocenter and the histone gene cluster. Localizes to active foci of DNA replication throughout S-phase and is lost from stalled replication forks. Not detected on condensed chromatin during mitosis. Ref.6 Ref.7 Ref.10
Developmental stage	Highly expressed in embryos and at lower levels in larvae, pupae and adults. Ref.1
Post-translational modification	Phosphorylated on undefined residues by tlk. Ref.8 Ref.11
Sequence similarities	Belongs to the ASF1 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Molecular function	Chaperone Chromatin regulator
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW dendrite morphogenesis Inferred from mutant phenotype. Source: FlyBase muscle organ development Inferred from mutant phenotype. Source: FlyBase nucleosome assembly Inferred from mutant phenotype Ref.1. Source: FlyBase regulation of nuclear mRNA splicing, via spliceosome Inferred from mutant phenotype. Source: FlyBase regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	RCAF complex Inferred from direct assay Ref.6. Source: UniProtKB chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction Ref.1Ref.6Ref.7Ref.8. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 218	218	Histone chaperone asf1		PRO_0000284025
Amino acid modifications
	Modified residue	211	1	Phosphoserine Ref.11
	Modified residue	213	1	Phosphoserine Ref.11
Experimental info
	Mutagenesis	19 – 26	8	Missing: Impairs binding to histone H3 and histone H4 and transcriptional silencing. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q9V464 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 0AD5CA90118BE1C4	FASTA	218	24,409
	10 20 30 40 50 60 MAKVHITNVV VLDNPSSFFN PFQFELTFEC IEELKEDLEW KMIYVGSAES EEHDQVLDTI 70 80 90 100 110 120 YVGPVPEGRH IFVFQADPPD VSKIPEPDAV GVTIVLLTCS YRGQEFVRVG YYVNNDYADP 130 140 150 160 170 180 EMRENPPTKP LFEKLTRNIL ASKPRVTRFK INWDYGHING NGNGVENGHQ DEMATDGPST 190 200 210 SEAASAVIHP EDDNSLAMPM ENGIKALNEN SNSLAMEC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The RCAF complex mediates chromatin assembly during DNA replication and repair." Tyler J.K., Adams C.R., Chen S.-R., Kobayashi R., Kamakaka R.T., Kadonaga J.T. Nature 402:555-560(1999) [PubMed: 10591219] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-70; 130-134 AND 144-171, FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4, DEVELOPMENTAL STAGE.
[2]	"Widespread adaptive evolution of Drosophila genes with sex-biased expression." Proeschel M., Zhang Z., Parsch J. Genetics 174:893-900(2006) [PubMed: 16951084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Zimbabwe.
[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: 10731132] [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. , 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: 12537572] [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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"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: 11533245] [Abstract] Cited for: FUNCTION, INTERACTION WITH CAF1-105, SUBCELLULAR LOCATION.
[7]	"Histone chaperone ASF1 cooperates with the Brahma chromatin-remodelling machinery." Moshkin Y.M., Armstrong J.A., Maeda R.K., Tamkun J.W., Verrijzer P., Kennison J.A., Karch F. Genes Dev. 16:2621-2626(2002) [PubMed: 12381660] [Abstract] Cited for: FUNCTION, INTERACTION WITH BRM AND MOR, SUBCELLULAR LOCATION, MUTAGENESIS OF 19-PHE--LEU-26.
[8]	"Tousled-like kinase functions with the chromatin assembly pathway regulating nuclear divisions." Carrera P., Moshkin Y.M., Groenke S., Sillje H.H.W., Nigg E.A., Jaeckle H., Karch F. Genes Dev. 17:2578-2590(2003) [PubMed: 14561777] [Abstract] Cited for: FUNCTION, INTERACTION WITH TLK, PHOSPHORYLATION BY TLK.
[9]	"Functional conservation and specialization among eukaryotic anti-silencing function 1 histone chaperones." Tamburini B.A., Carson J.J., Adkins M.W., Tyler J.K. Eukaryot. Cell 4:1583-1590(2005) [PubMed: 16151251] [Abstract] Cited for: FUNCTION.
[10]	"The histone chaperone ASF1 localizes to active DNA replication forks to mediate efficient DNA replication." Schulz L.L., Tyler J.K. FASEB J. 20:488-490(2006) [PubMed: 16396992] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"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: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-213, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF189278 mRNA. Translation: AAF15354.1. AM294236 Genomic DNA. Translation: CAL26140.1. AM294237 Genomic DNA. Translation: CAL26141.1. AM294238 Genomic DNA. Translation: CAL26142.1. AM294239 Genomic DNA. Translation: CAL26143.1. AM294240 Genomic DNA. Translation: CAL26144.1. AM294241 Genomic DNA. Translation: CAL26145.1. AM294242 Genomic DNA. Translation: CAL26146.1. AM294243 Genomic DNA. Translation: CAL26147.1. AM294244 Genomic DNA. Translation: CAL26148.1. AM294245 Genomic DNA. Translation: CAL26149.1. AM294246 Genomic DNA. Translation: CAL26150.1. AE014296 Genomic DNA. Translation: AAF49131.1. BT004869 mRNA. Translation: AAO45225.1.
RefSeq	NP_001189131.1. NM_001202202.1. NP_524163.1. NM_079439.3.
3D structure databases
HSSP	HSSP built from PDB template 1TEY based on UniProtKB Q9Y294.
ProteinModelPortal	Q9V464.
SMR	Q9V464. Positions 1-153.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-22309N.
IntAct	Q9V464. 4 interactions.
MINT	MINT-840234.
STRING	Q9V464.
Proteomic databases
PRIDE	Q9V464.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0074947; FBpp0074715; FBgn0029094. FBtr0302381; FBpp0291576; FBgn0029094.
GeneID	40141.
KEGG	dme:Dmel_CG9383.
NMPDR	fig|7227.3.peg.10584.
Organism-specific databases
CTD	40141.
FlyBase	FBgn0029094. asf1.
Phylogenomic databases
eggNOG	inNOG07630.
GeneTree	EMGT00050000015648.
InParanoid	Q9V464.
OMA	ESEEHDQ.
OrthoDB	EOG43N5VQ.
PhylomeDB	Q9V464.
Gene expression databases
ArrayExpress	Q9V464.
Bgee	Q9V464.
Family and domain databases
InterPro	IPR006818. Histone_chaperone_ASF1-like. [Graphical view]
Gene3D	G3DSA:2.60.40.1490. Anti-silence. 1 hit.
KO	K10753.
PANTHER	PTHR12040. Anti-silence. 1 hit.
Pfam	PF04729. ASF1_hist_chap. 1 hit. [Graphical view]
SUPFAM	SSF101546. Anti-silence. 1 hit.
ProtoNet	Search...
Other
NextBio	817207.

Entry information

Entry name

ASF1_DROME

Accession

Primary (citable) accession number: Q9V464

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 17, 2007
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project