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Histone chaperone asf1 (Anti-silencing function protein 1) (Replication-coupling assembly factor subunit ASF1) (RCAF subunit ASF1) (dASF1)

 ASF1_DROME              Reviewed;         218 AA.
Q9V464;
17-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
23-MAY-2018, entry version 130.
RecName: Full=Histone chaperone asf1;
AltName: Full=Anti-silencing function protein 1;
AltName: Full=Replication-coupling assembly factor subunit ASF1;
Short=RCAF subunit ASF1;
AltName: Full=dASF1;
Name=asf1; ORFNames=CG9383;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 42-70; 130-134 AND
144-171, FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4, AND
DEVELOPMENTAL STAGE.
PubMed=10591219; DOI=10.1038/990147;
Tyler J.K., Adams C.R., Chen S.-R., Kobayashi R., Kamakaka R.T.,
Kadonaga J.T.;
"The RCAF complex mediates chromatin assembly during DNA replication
and repair.";
Nature 402:555-560(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Zimbabwe;
PubMed=16951084; DOI=10.1534/genetics.106.058008;
Proeschel M., Zhang Z., Parsch J.;
"Widespread adaptive evolution of Drosophila genes with sex-biased
expression.";
Genetics 174:893-900(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION, INTERACTION WITH CAF1-105, AND SUBCELLULAR LOCATION.
PubMed=11533245; DOI=10.1128/MCB.21.19.6574-6584.2001;
Tyler J.K., Collins K.A., Prasad-Sinha J., Amiott E., Bulger M.,
Harte P.J., Kobayashi R., Kadonaga J.T.;
"Interaction between the Drosophila CAF-1 and ASF1 chromatin assembly
factors.";
Mol. Cell. Biol. 21:6574-6584(2001).
[7]
FUNCTION, INTERACTION WITH BRM AND MOR, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF 19-PHE--LEU-26.
PubMed=12381660; DOI=10.1101/gad.231202;
Moshkin Y.M., Armstrong J.A., Maeda R.K., Tamkun J.W., Verrijzer P.,
Kennison J.A., Karch F.;
"Histone chaperone ASF1 cooperates with the Brahma chromatin-
remodelling machinery.";
Genes Dev. 16:2621-2626(2002).
[8]
FUNCTION, INTERACTION WITH TLK, AND PHOSPHORYLATION BY TLK.
PubMed=14561777; DOI=10.1101/gad.276703;
Carrera P., Moshkin Y.M., Groenke S., Sillje H.H.W., Nigg E.A.,
Jaeckle H., Karch F.;
"Tousled-like kinase functions with the chromatin assembly pathway
regulating nuclear divisions.";
Genes Dev. 17:2578-2590(2003).
[9]
FUNCTION.
PubMed=16151251; DOI=10.1128/EC.4.9.1583-1590.2005;
Tamburini B.A., Carson J.J., Adkins M.W., Tyler J.K.;
"Functional conservation and specialization among eukaryotic anti-
silencing function 1 histone chaperones.";
Eukaryot. Cell 4:1583-1590(2005).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16396992; DOI=10.1096/fj.05-5020fje;
Schulz L.L., Tyler J.K.;
"The histone chaperone ASF1 localizes to active DNA replication forks
to mediate efficient DNA replication.";
FASEB J. 20:488-490(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-213, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- 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.
{ECO:0000269|PubMed:10591219, ECO:0000269|PubMed:11533245,
ECO:0000269|PubMed:12381660, ECO:0000269|PubMed:14561777,
ECO:0000269|PubMed:16151251, ECO:0000269|PubMed:16396992}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10591219,
ECO:0000269|PubMed:11533245, ECO:0000269|PubMed:12381660,
ECO:0000269|PubMed:14561777}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12381660}.
Chromosome {ECO:0000269|PubMed:11533245,
ECO:0000269|PubMed:12381660, ECO:0000269|PubMed:16396992}.
Note=Localizes to multiple sites on polytene chromosomes including
transcriptionally active developmental puffs, the chromocenter and
the histone gene cluster (PubMed:12381660). Localizes to active
foci of DNA replication throughout S-phase and is lost from
stalled replication forks (PubMed:16396992). Not detected on
condensed chromatin during mitosis (PubMed:16396992).
{ECO:0000269|PubMed:12381660, ECO:0000269|PubMed:16396992}.
-!- DEVELOPMENTAL STAGE: Highly expressed in embryos and at lower
levels in larvae, pupae and adults. {ECO:0000269|PubMed:10591219}.
-!- PTM: Phosphorylated on undefined residues by tlk.
{ECO:0000269|PubMed:14561777, ECO:0000269|PubMed:18327897}.
-!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
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EMBL; AF189278; AAF15354.1; -; mRNA.
EMBL; AM294236; CAL26140.1; -; Genomic_DNA.
EMBL; AM294237; CAL26141.1; -; Genomic_DNA.
EMBL; AM294238; CAL26142.1; -; Genomic_DNA.
EMBL; AM294239; CAL26143.1; -; Genomic_DNA.
EMBL; AM294240; CAL26144.1; -; Genomic_DNA.
EMBL; AM294241; CAL26145.1; -; Genomic_DNA.
EMBL; AM294242; CAL26146.1; -; Genomic_DNA.
EMBL; AM294243; CAL26147.1; -; Genomic_DNA.
EMBL; AM294244; CAL26148.1; -; Genomic_DNA.
EMBL; AM294245; CAL26149.1; -; Genomic_DNA.
EMBL; AM294246; CAL26150.1; -; Genomic_DNA.
EMBL; AE014296; AAF49131.1; -; Genomic_DNA.
EMBL; BT004869; AAO45225.1; -; mRNA.
RefSeq; NP_001189131.1; NM_001202202.2.
RefSeq; NP_524163.1; NM_079439.4.
UniGene; Dm.2521; -.
ProteinModelPortal; Q9V464; -.
SMR; Q9V464; -.
BioGrid; 65411; 26.
DIP; DIP-22309N; -.
IntAct; Q9V464; 6.
STRING; 7227.FBpp0074715; -.
iPTMnet; Q9V464; -.
PaxDb; Q9V464; -.
PRIDE; Q9V464; -.
EnsemblMetazoa; FBtr0074947; FBpp0074715; FBgn0029094.
EnsemblMetazoa; FBtr0302381; FBpp0291576; FBgn0029094.
GeneID; 40141; -.
KEGG; dme:Dmel_CG9383; -.
CTD; 40141; -.
FlyBase; FBgn0029094; asf1.
eggNOG; KOG3265; Eukaryota.
eggNOG; COG5137; LUCA.
GeneTree; ENSGT00390000004692; -.
InParanoid; Q9V464; -.
KO; K10753; -.
OMA; FNPFQFE; -.
OrthoDB; EOG091G0K07; -.
PhylomeDB; Q9V464; -.
ChiTaRS; asf1; fly.
GenomeRNAi; 40141; -.
PRO; PR:Q9V464; -.
Proteomes; UP000000803; Chromosome 3L.
Bgee; FBgn0029094; -.
ExpressionAtlas; Q9V464; baseline and differential.
Genevisible; Q9V464; DM.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0035059; C:RCAF complex; IDA:UniProtKB.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:FlyBase.
GO; GO:0006325; P:chromatin organization; IDA:UniProtKB.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:FlyBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase.
GO; GO:0006334; P:nucleosome assembly; IMP:FlyBase.
GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.60.40.1490; -; 1.
InterPro; IPR006818; ASF1-like.
InterPro; IPR036747; ASF1-like_sf.
PANTHER; PTHR12040; PTHR12040; 1.
Pfam; PF04729; ASF1_hist_chap; 1.
SUPFAM; SSF101546; SSF101546; 1.
1: Evidence at protein level;
Chaperone; Chromatin regulator; Chromosome; Complete proteome;
Direct protein sequencing; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation.
CHAIN 1 218 Histone chaperone asf1.
/FTId=PRO_0000284025.
MOD_RES 211 211 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
MUTAGEN 19 26 Missing: Impairs binding to histone H3
and histone H4 and transcriptional
silencing. {ECO:0000269|PubMed:12381660}.
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


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