ASF1_DROME
ID ASF1_DROME Reviewed; 218 AA.
AC Q9V464;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Histone chaperone asf1;
DE AltName: Full=Anti-silencing function protein 1;
DE AltName: Full=Replication-coupling assembly factor subunit ASF1;
DE Short=RCAF subunit ASF1;
DE AltName: Full=dASF1;
GN Name=asf1; ORFNames=CG9383;
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 42-70; 130-134 AND 144-171,
RP FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10591219; DOI=10.1038/990147;
RA Tyler J.K., Adams C.R., Chen S.-R., Kobayashi R., Kamakaka R.T.,
RA Kadonaga J.T.;
RT "The RCAF complex mediates chromatin assembly during DNA replication and
RT repair.";
RL Nature 402:555-560(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Zimbabwe;
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; TISSUE=Embryo;
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 FUNCTION, INTERACTION WITH CAF1-105, AND SUBCELLULAR LOCATION.
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 [7]
RP FUNCTION, INTERACTION WITH BRM AND MOR, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 19-PHE--LEU-26.
RX PubMed=12381660; DOI=10.1101/gad.231202;
RA Moshkin Y.M., Armstrong J.A., Maeda R.K., Tamkun J.W., Verrijzer P.,
RA Kennison J.A., Karch F.;
RT "Histone chaperone ASF1 cooperates with the Brahma chromatin-remodelling
RT machinery.";
RL Genes Dev. 16:2621-2626(2002).
RN [8]
RP FUNCTION, INTERACTION WITH TLK, AND PHOSPHORYLATION BY TLK.
RX PubMed=14561777; DOI=10.1101/gad.276703;
RA Carrera P., Moshkin Y.M., Groenke S., Sillje H.H.W., Nigg E.A., Jaeckle H.,
RA Karch F.;
RT "Tousled-like kinase functions with the chromatin assembly pathway
RT regulating nuclear divisions.";
RL Genes Dev. 17:2578-2590(2003).
RN [9]
RP FUNCTION.
RX PubMed=16151251; DOI=10.1128/ec.4.9.1583-1590.2005;
RA Tamburini B.A., Carson J.J., Adkins M.W., Tyler J.K.;
RT "Functional conservation and specialization among eukaryotic anti-silencing
RT function 1 histone chaperones.";
RL Eukaryot. Cell 4:1583-1590(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16396992; DOI=10.1096/fj.05-5020fje;
RA Schulz L.L., Tyler J.K.;
RT "The histone chaperone ASF1 localizes to active DNA replication forks to
RT mediate efficient DNA replication.";
RL FASEB J. 20:488-490(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-213, AND
RP IDENTIFICATION BY 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).
RN [12]
RP FUNCTION, AND INTERACTION WITH DAXX.
RX PubMed=28320872; DOI=10.1128/mcb.00597-16;
RA Fromental-Ramain C., Ramain P., Hamiche A.;
RT "The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3
RT Deposition and Heterochromatin Formation.";
RL Mol. Cell. Biol. 37:0-0(2017).
CC -!- FUNCTION: Histone chaperone that facilitates histone deposition and
CC histone exchange and removal during nucleosome assembly and disassembly
CC (PubMed:10591219, PubMed:12381660, PubMed:14561777, PubMed:16151251,
CC PubMed:16396992). Cooperates with chromatin assembly factor 1 (CAF-1)
CC to promote replication-dependent chromatin assembly (PubMed:11533245).
CC Plays a role in the formation of silent heterochromatin
CC (PubMed:12381660, PubMed:28320872). {ECO:0000269|PubMed:10591219,
CC ECO:0000269|PubMed:11533245, ECO:0000269|PubMed:12381660,
CC ECO:0000269|PubMed:14561777, ECO:0000269|PubMed:16151251,
CC ECO:0000269|PubMed:16396992, ECO:0000269|PubMed:28320872}.
CC -!- SUBUNIT: Component of the replication coupling assembly factor (RCAF),
CC composed of asf1, histone H3 and histone H4 (PubMed:10591219).
CC Interacts with the Caf1-105 subunit of the CAF-1 complex
CC (PubMed:11533245). Interacts with brm, mor and tlk (PubMed:12381660,
CC PubMed:14561777). Interacts with Daxx (PubMed:28320872).
CC {ECO:0000269|PubMed:10591219, ECO:0000269|PubMed:11533245,
CC ECO:0000269|PubMed:12381660, ECO:0000269|PubMed:14561777,
CC ECO:0000269|PubMed:28320872}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12381660}. Chromosome
CC {ECO:0000269|PubMed:11533245, ECO:0000269|PubMed:12381660,
CC ECO:0000269|PubMed:16396992}. Note=Localizes to multiple sites on
CC polytene chromosomes including transcriptionally active developmental
CC puffs, the chromocenter and the histone gene cluster (PubMed:12381660).
CC Localizes to active foci of DNA replication throughout S-phase and is
CC lost from stalled replication forks (PubMed:16396992). Not detected on
CC condensed chromatin during mitosis (PubMed:16396992).
CC {ECO:0000269|PubMed:12381660, ECO:0000269|PubMed:16396992}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryos and at lower levels in
CC larvae, pupae and adults. {ECO:0000269|PubMed:10591219}.
CC -!- PTM: Phosphorylated on undefined residues by tlk.
CC {ECO:0000269|PubMed:14561777, ECO:0000269|PubMed:18327897}.
CC -!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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DR EMBL; AF189278; AAF15354.1; -; mRNA.
DR EMBL; AM294236; CAL26140.1; -; Genomic_DNA.
DR EMBL; AM294237; CAL26141.1; -; Genomic_DNA.
DR EMBL; AM294238; CAL26142.1; -; Genomic_DNA.
DR EMBL; AM294239; CAL26143.1; -; Genomic_DNA.
DR EMBL; AM294240; CAL26144.1; -; Genomic_DNA.
DR EMBL; AM294241; CAL26145.1; -; Genomic_DNA.
DR EMBL; AM294242; CAL26146.1; -; Genomic_DNA.
DR EMBL; AM294243; CAL26147.1; -; Genomic_DNA.
DR EMBL; AM294244; CAL26148.1; -; Genomic_DNA.
DR EMBL; AM294245; CAL26149.1; -; Genomic_DNA.
DR EMBL; AM294246; CAL26150.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49131.1; -; Genomic_DNA.
DR EMBL; BT004869; AAO45225.1; -; mRNA.
DR RefSeq; NP_001189131.1; NM_001202202.2.
DR RefSeq; NP_524163.1; NM_079439.4.
DR AlphaFoldDB; Q9V464; -.
DR SMR; Q9V464; -.
DR BioGRID; 65411; 30.
DR DIP; DIP-22309N; -.
DR IntAct; Q9V464; 6.
DR STRING; 7227.FBpp0074715; -.
DR iPTMnet; Q9V464; -.
DR PaxDb; Q9V464; -.
DR PRIDE; Q9V464; -.
DR EnsemblMetazoa; FBtr0074947; FBpp0074715; FBgn0029094.
DR EnsemblMetazoa; FBtr0302381; FBpp0291576; FBgn0029094.
DR GeneID; 40141; -.
DR KEGG; dme:Dmel_CG9383; -.
DR CTD; 40141; -.
DR FlyBase; FBgn0029094; asf1.
DR VEuPathDB; VectorBase:FBgn0029094; -.
DR eggNOG; KOG3265; Eukaryota.
DR GeneTree; ENSGT00390000004692; -.
DR HOGENOM; CLU_060354_1_1_1; -.
DR InParanoid; Q9V464; -.
DR OMA; KINWDYG; -.
DR OrthoDB; 1334998at2759; -.
DR PhylomeDB; Q9V464; -.
DR SignaLink; Q9V464; -.
DR BioGRID-ORCS; 40141; 0 hits in 3 CRISPR screens.
DR ChiTaRS; asf1; fly.
DR GenomeRNAi; 40141; -.
DR PRO; PR:Q9V464; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0029094; Expressed in cleaving embryo and 47 other tissues.
DR ExpressionAtlas; Q9V464; baseline and differential.
DR Genevisible; Q9V464; DM.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0035059; C:RCAF complex; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:FlyBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IDA:UniProtKB.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IBA:GO_Central.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006334; P:nucleosome assembly; IMP:FlyBase.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:FlyBase.
DR Gene3D; 2.60.40.1490; -; 1.
DR InterPro; IPR006818; ASF1-like.
DR InterPro; IPR036747; ASF1-like_sf.
DR PANTHER; PTHR12040; PTHR12040; 2.
DR Pfam; PF04729; ASF1_hist_chap; 1.
DR SUPFAM; SSF101546; SSF101546; 1.
PE 1: Evidence at protein level;
KW Chaperone; Chromatin regulator; Chromosome; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..218
FT /note="Histone chaperone asf1"
FT /id="PRO_0000284025"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 19..26
FT /note="Missing: Impairs binding to histone H3 and histone
FT H4 and transcriptional silencing."
FT /evidence="ECO:0000269|PubMed:12381660"
SQ SEQUENCE 218 AA; 24409 MW; 0AD5CA90118BE1C4 CRC64;
MAKVHITNVV VLDNPSSFFN PFQFELTFEC IEELKEDLEW KMIYVGSAES EEHDQVLDTI
YVGPVPEGRH IFVFQADPPD VSKIPEPDAV GVTIVLLTCS YRGQEFVRVG YYVNNDYADP
EMRENPPTKP LFEKLTRNIL ASKPRVTRFK INWDYGHING NGNGVENGHQ DEMATDGPST
SEAASAVIHP EDDNSLAMPM ENGIKALNEN SNSLAMEC
