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UniProtKB/Swiss-Prot entry P32447

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Entry information
Entry name ASF1_YEAST
Primary accession number P32447
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1993
Sequence was last modified on October 1, 1993 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 81)
Name and origin of the protein
Protein name Histone chaperone ASF1
Synonyms Anti-silencing function protein 1
yASF1
Gene name
Name: ASF1
Synonyms: CIA1
OrderedLocusNames: YJL115W
ORFNames: J0755
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
DOI=10.1002/(SICI)1097-0061(19970915)13:11<1029::AID-YEA160>3.0.CO;2-1; PubMed=9290207 [NCBI, ExPASy, EBI, Israel, Japan]
Le S., Davis C., Konopka J.B., Sternglanz R.;
"Two new S-phase-specific genes from Saccharomyces cerevisiae.";
Yeast 13:1029-1042(1997).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1002/(SICI)1097-0061(199611)12:14<1471::AID-YEA30>3.3.CO;2-W; PubMed=8948101 [NCBI, ExPASy, EBI, Israel, Japan]
Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
"Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19 open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14, RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta elements and a Ty4 transposon.";
Yeast 12:1471-1474(1996).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8641269 [NCBI, ExPASy, EBI, Israel, Japan]
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
EMBO J. 15:2031-2049(1996).
[4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
 FUNCTION.
DOI=10.1038/990147; PubMed=10591219 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
 FUNCTION, AND INTERACTION WITH HISTONE H3; HISTONE H4; HIR1 AND HIR2.
DOI=10.1016/S0960-9822(01)00140-3; PubMed=11412995 [NCBI, ExPASy, EBI, Israel, Japan]
Sharp J.A., Fouts E.T., Krawitz D.C., Kaufman P.D.;
"Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing.";
Curr. Biol. 11:463-473(2001).
[7]
 FUNCTION, AND INTERACTION WITH RAD53.
DOI=10.1101/gad.873201; PubMed=11331602 [NCBI, ExPASy, EBI, Israel, Japan]
Hu F., Alcasabas A.A., Elledge S.J.;
"Asf1 links Rad53 to control of chromatin assembly.";
Genes Dev. 15:1061-1066(2001).
[8]
 FUNCTION, AND INTERACTION WITH SAS2; SAS4 AND SAS5.
DOI=10.1101/gad.907201; PubMed=11731479 [NCBI, ExPASy, EBI, Israel, Japan]
Osada S., Sutton A., Muster N., Brown C.E., Yates J.R. III, Sternglanz R., Workman J.L.;
"The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1.";
Genes Dev. 15:3155-3168(2001).
[9]
 FUNCTION, AND INTERACTION WITH SAS2; SAS4 AND SAS5.
DOI=10.1101/gad.929001; PubMed=11731480 [NCBI, ExPASy, EBI, Israel, Japan]
Meijsing S.H., Ehrenhofer-Murray A.E.;
"The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae.";
Genes Dev. 15:3169-3182(2001).
[10]
 FUNCTION, INTERACTION WITH HIR1, AND SUBCELLULAR LOCATION.
PubMed=11404324 [NCBI, ExPASy, EBI, Israel, Japan]
Sutton A., Bucaria J., Osley M.A., Sternglanz R.;
"Yeast ASF1 protein is required for cell cycle regulation of histone gene transcription.";
Genetics 158:587-596(2001).
[11]
 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH HISTONE H3; HISTONE H4 AND RAD53.
DOI=10.1016/S1097-2765(01)00150-2; PubMed=11172707 [NCBI, ExPASy, EBI, Israel, Japan]
Emili A., Schieltz D.M., Yates J.R. III, Hartwell L.H.;
"Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1.";
Mol. Cell 7:13-20(2001).
[12]
 FUNCTION, AND INTERACTION WITH HISTONE H3 AND HISTONE H4.
DOI=10.1046/j.1356-9597.2001.00493.x; PubMed=11856374 [NCBI, ExPASy, EBI, Israel, Japan]
Umehara T., Chimura T., Ichikawa N., Horikoshi M.;
"Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro.";
Genes Cells 7:59-73(2002).
[13]
 FUNCTION, AND INTERACTION WITH CAC2; HISTONE H3 AND HISTONE H4.
DOI=10.1128/MCB.22.2.614-625.2002; PubMed=11756556 [NCBI, ExPASy, EBI, Israel, Japan]
Krawitz D.C., Kama T., Kaufman P.D.;
"Chromatin assembly factor I mutants defective for PCNA binding require Asf1/Hir proteins for silencing.";
Mol. Cell. Biol. 22:614-625(2002).
[14]
 FUNCTION, AND INTERACTION WITH BDF1; BDF2; SPT15; TAF1 AND TAF7.
DOI=10.1073/pnas.142627899; PubMed=12093919 [NCBI, ExPASy, EBI, Israel, Japan]
Chimura T., Kuzuhara T., Horikoshi M.;
"Identification and characterization of CIA/ASF1 as an interactor of bromodomains associated with TFIID.";
Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002).
[15]
 INTERACTION WITH RAD53.
PubMed=12851493 [NCBI, ExPASy, EBI, Israel, Japan]
Schwartz M.F., Lee S.-J., Duong J.K., Eminaga S., Stern D.F.;
"FHA domain-mediated DNA checkpoint regulation of Rad53.";
Cell Cycle 2:384-396(2003).
[16]
 INTERACTION WITH HISTONE H3 AND HISTONE H4.
DOI=10.1074/jbc.M210709200; PubMed=12626510 [NCBI, ExPASy, EBI, Israel, Japan]
Sutton A., Shia W.-J., Band D., Kaufman P.D., Osada S., Workman J.L., Sternglanz R.;
"Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex.";
J. Biol. Chem. 278:16887-16892(2003).
[17]
 INTERACTION WITH RAD53.
DOI=10.1128/MCB.23.17.6300-6314.2003; PubMed=12917350 [NCBI, ExPASy, EBI, Israel, Japan]
Lee S.-J., Schwartz M.F., Duong J.K., Stern D.F.;
"Rad53 phosphorylation site clusters are important for Rad53 regulation and signaling.";
Mol. Cell. Biol. 23:6300-6314(2003).
[18]
 FUNCTION.
DOI=10.1128/MCB.23.22.7937-7946.2003; PubMed=14585955 [NCBI, ExPASy, EBI, Israel, Japan]
Robinson K.M., Schultz M.C.;
"Replication-independent assembly of nucleosome arrays in a novel yeast chromatin reconstitution system involves antisilencing factor Asf1p and chromodomain protein Chd1p.";
Mol. Cell. Biol. 23:7937-7946(2003).
[19]
 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[20]
 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[21]
 FUNCTION.
DOI=10.1038/sj.embor.7400128; PubMed=15071494 [NCBI, ExPASy, EBI, Israel, Japan]
Prado F., Cortes-Ledesma F., Aguilera A.;
"The absence of the yeast chromatin assembly factor Asf1 increases genomic instability and sister chromatid exchange.";
EMBO Rep. 5:497-502(2004).
[22]
 FUNCTION.
DOI=10.1074/jbc.M406113200; PubMed=15452122 [NCBI, ExPASy, EBI, Israel, Japan]
Adkins M.W., Tyler J.K.;
"The histone chaperone Asf1p mediates global chromatin disassembly in vivo.";
J. Biol. Chem. 279:52069-52074(2004).
[23]
 FUNCTION.
DOI=10.1016/j.molcel.2004.05.016; PubMed=15175160 [NCBI, ExPASy, EBI, Israel, Japan]
Adkins M.W., Howar S.R., Tyler J.K.;
"Chromatin disassembly mediated by the histone chaperone Asf1 is essential for transcriptional activation of the yeast PHO5 and PHO8 genes.";
Mol. Cell 14:657-666(2004).
[24]
 FUNCTION.
DOI=10.1128/MCB.24.23.10180-10192.2004; PubMed=15542829 [NCBI, ExPASy, EBI, Israel, Japan]
Glowczewski L., Waterborg J.H., Berman J.G.;
"Yeast chromatin assembly complex 1 protein excludes nonacetylatable forms of histone H4 from chromatin and the nucleus.";
Mol. Cell. Biol. 24:10180-10192(2004).
[25]
 FUNCTION.
DOI=10.1128/MCB.24.23.10313-10327.2004; PubMed=15542840 [NCBI, ExPASy, EBI, Israel, Japan]
Ramey C.J., Howar S., Adkins M., Linger J., Spicer J., Tyler J.K.;
"Activation of the DNA damage checkpoint in yeast lacking the histone chaperone anti-silencing function 1.";
Mol. Cell. Biol. 24:10313-10327(2004).
[26]
 FUNCTION.
DOI=10.1021/bi047523u; PubMed=15766286 [NCBI, ExPASy, EBI, Israel, Japan]
Robinson K.M., Schultz M.C.;
"Gal4-VP16 directs ATP-independent chromatin reorganization in a yeast chromatin assembly system.";
Biochemistry 44:4551-4561(2005).
[27]
 FUNCTION, INTERACTION WITH HIR1; HIR2; HIR3; HPC2; HISTONE H3; HISTONE H4 AND RAD53, AND MUTAGENESIS OF 36-HIS-ASP-37.
DOI=10.1016/j.cub.2005.10.053; PubMed=16303565 [NCBI, ExPASy, EBI, Israel, Japan]
Green E.M., Antczak A.J., Bailey A.O., Franco A.A., Wu K.J., Yates J.R. III, Kaufman P.D.;
"Replication-independent histone deposition by the HIR complex and Asf1.";
Curr. Biol. 15:2044-2049(2005).
[28]
 FUNCTION.
DOI=10.1128/EC.4.4.673-684.2005; PubMed=15821127 [NCBI, ExPASy, EBI, Israel, Japan]
Harkness T.A.A., Arnason T.G., Legrand C., Pisclevich M.G., Davies G.F., Turner E.L.;
"Contribution of CAF-I to anaphase-promoting-complex-mediated mitotic chromatin assembly in Saccharomyces cerevisiae.";
Eukaryot. Cell 4:673-684(2005).
[29]
 FUNCTION, AND INTERACTION WITH RFC1; RFC2; RFC3; RFC4 AND RFC5.
DOI=10.1101/gad.1305005; PubMed=15901673 [NCBI, ExPASy, EBI, Israel, Japan]
Franco A.A., Lam W.M., Burgers P.M., Kaufman P.D.;
"Histone deposition protein Asf1 maintains DNA replisome integrity and interacts with replication factor C.";
Genes Dev. 19:1365-1375(2005).
[30]
 FUNCTION, INTERACTION WITH RAD53, AND SUBCELLULAR LOCATION.
DOI=10.1534/genetics.105.044719; PubMed=16020781 [NCBI, ExPASy, EBI, Israel, Japan]
Sharp J.A., Rizki G., Kaufman P.D.;
"Regulation of histone deposition proteins Asf1/Hir1 by multiple DNA damage checkpoint kinases in Saccharomyces cerevisiae.";
Genetics 171:885-899(2005).
[31]
 FUNCTION.
DOI=10.1534/genetics.105.043000; PubMed=16143623 [NCBI, ExPASy, EBI, Israel, Japan]
Linger J., Tyler J.K.;
"The yeast histone chaperone chromatin assembly factor 1 protects against double-strand DNA-damaging agents.";
Genetics 171:1513-1522(2005).
[32]
 FUNCTION.
DOI=10.1016/j.molcel.2005.05.028; PubMed=16039596 [NCBI, ExPASy, EBI, Israel, Japan]
Schermer U.J., Korber P., Hoerz W.;
"Histones are incorporated in trans during reassembly of the yeast PHO5 promoter.";
Mol. Cell 19:279-285(2005).
[33]
 FUNCTION.
DOI=10.1128/MCB.25.2.652-660.2005; PubMed=15632066 [NCBI, ExPASy, EBI, Israel, Japan]
Zabaronick S.R., Tyler J.K.;
"The histone chaperone anti-silencing function 1 is a global regulator of transcription independent of passage through S phase.";
Mol. Cell. Biol. 25:652-660(2005).
[34]
 ERRATUM.
Zabaronick S.R., Tyler J.K.;
Mol. Cell. Biol. 25:2871-2871(2005).
[35]
 FUNCTION.
DOI=10.1093/nar/gki560; PubMed=15891116 [NCBI, ExPASy, EBI, Israel, Japan]
Osada S., Kurita M., Nishikawa J., Nishihara T.;
"Chromatin assembly factor Asf1p-dependent occupancy of the SAS histone acetyltransferase complex at the silent mating-type locus HMLalpha.";
Nucleic Acids Res. 33:2742-2750(2005).
[36]
 FUNCTION.
DOI=10.1093/nar/gki806; PubMed=16141196 [NCBI, ExPASy, EBI, Israel, Japan]
Lewis L.K., Karthikeyan G., Cassiano J., Resnick M.A.;
"Reduction of nucleosome assembly during new DNA synthesis impairs both major pathways of double-strand break repair.";
Nucleic Acids Res. 33:4928-4939(2005).
[37]
 FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4, AND MUTAGENESIS OF ASP-37; GLU-39; ASP-54; VAL-94 AND ARG-108.
DOI=10.1073/pnas.0500149102; PubMed=15840725 [NCBI, ExPASy, EBI, Israel, Japan]
Mousson F., Lautrette A., Thuret J.-Y., Agez M., Courbeyrette R., Amigues B., Becker E., Neumann J.-M., Guerois R., Mann C., Ochsenbein F.;
"Structural basis for the interaction of Asf1 with histone H3 and its functional implications.";
Proc. Natl. Acad. Sci. U.S.A. 102:5975-5980(2005).
[38]
 FUNCTION.
DOI=10.1016/j.cub.2006.06.023; PubMed=16815704 [NCBI, ExPASy, EBI, Israel, Japan]
Celic I., Masumoto H., Griffith W.P., Meluh P., Cotter R.J., Boeke J.D., Verreault A.;
"The sirtuins Hst3 and Hst4p preserve genome integrity by controlling histone H3 lysine 56 deacetylation.";
Curr. Biol. 16:1280-1289(2006).
[39]
 FUNCTION.
DOI=10.1128/EC.00202-06; PubMed=16936140 [NCBI, ExPASy, EBI, Israel, Japan]
Linger J., Tyler J.K.;
"Global replication-independent histone H4 exchange in budding yeast.";
Eukaryot. Cell 5:1780-1787(2006).
[40]
 FUNCTION, INTERACTION WITH HISTONE H3 AND RAD53, AND MUTAGENESIS OF VAL-152.
DOI=10.1534/genetics.105.054783; PubMed=16582440 [NCBI, ExPASy, EBI, Israel, Japan]
Tamburini B.A., Carson J.J., Linger J.G., Tyler J.K.;
"Dominant mutants of the Saccharomyces cerevisiae ASF1 histone chaperone bypass the need for CAF-1 in transcriptional silencing by altering histone and Sir protein recruitment.";
Genetics 173:599-610(2006).
[41]
 FUNCTION.
DOI=10.1074/jbc.M513340200; PubMed=16407267 [NCBI, ExPASy, EBI, Israel, Japan]
Korber P., Barbaric S., Luckenbach T., Schmid A., Schermer U.J., Blaschke D., Hoerz W.;
"The histone chaperone Asf1 increases the rate of histone eviction at the yeast PHO5 and PHO8 promoters.";
J. Biol. Chem. 281:5539-5545(2006).
[42]
 FUNCTION.
DOI=10.1074/jbc.C600265200; PubMed=17046836 [NCBI, ExPASy, EBI, Israel, Japan]
Schneider J., Bajwa P., Johnson F.C., Bhaumik S.R., Shilatifard A.;
"Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II.";
J. Biol. Chem. 281:37270-37274(2006).
[43]
 FUNCTION.
DOI=10.1016/j.molcel.2006.03.014; PubMed=16678113 [NCBI, ExPASy, EBI, Israel, Japan]
Schwabish M.A., Struhl K.;
"Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II.";
Mol. Cell 22:415-422(2006).
[44]
 FUNCTION.
DOI=10.1073/pnas.0511102103; PubMed=16501045 [NCBI, ExPASy, EBI, Israel, Japan]
Kats E.S., Albuquerque C.P., Zhou H., Kolodner R.D.;
"Checkpoint functions are required for normal S-phase progression in Saccharomyces cerevisiae RCAF- and CAF-I-defective mutants.";
Proc. Natl. Acad. Sci. U.S.A. 103:3710-3715(2006).
[45]
 FUNCTION, AND MUTAGENESIS OF VAL-45; 53-HIS-ASP-54; VAL-94; LEU-96; TYR-112; ARG-145 AND THR-147.
DOI=10.1073/pnas.0601676103; PubMed=16627621 [NCBI, ExPASy, EBI, Israel, Japan]
Recht J., Tsubota T., Tanny J.C., Diaz R.L., Berger J.M., Zhang X., Garcia B.A., Shabanowitz J., Burlingame A.L., Hunt D.F., Kaufman P.D., Allis C.D.;
"Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis.";
Proc. Natl. Acad. Sci. U.S.A. 103:6988-6993(2006).
[46]
 FUNCTION, AND MUTAGENESIS OF SER-48; VAL-94; TYR-112; ARG-145 AND THR-147.
DOI=10.1074/jbc.M608025200; PubMed=17107956 [NCBI, ExPASy, EBI, Israel, Japan]
Adkins M.W., Carson J.J., English C.M., Ramey C.J., Tyler J.K.;
"The histone chaperone anti-silencing function 1 stimulates the acetylation of newly synthesized histone H3 in S-phase.";
J. Biol. Chem. 282:1334-1340(2007).
[47]
 FUNCTION, AND INTERACTION WITH RTT109.
DOI=10.1016/j.molcel.2007.02.006; PubMed=17320445 [NCBI, ExPASy, EBI, Israel, Japan]
Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L., Freitas M.A., Denu J.M., Kaufman P.D.;
"Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes.";
Mol. Cell 25:703-712(2007).
[48]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; THR-265 AND THR-270, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[49]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; THR-265 AND SER-269, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[50]
 X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-154, FUNCTION, INTERACTION WITH HISTONE H3; HISTONE H4 AND RAD53, AND MUTAGENESIS OF 36-HIS-ASP-37.
DOI=10.1016/j.cub.2003.11.027; PubMed=14680630 [NCBI, ExPASy, EBI, Israel, Japan]
Daganzo S.M., Erzberger J.P., Lam W.M., Skordalakes E., Zhang R., Franco A.A., Brill S.J., Adams P.D., Berger J.M., Kaufman P.D.;
"Structure and function of the conserved core of histone deposition protein Asf1.";
Curr. Biol. 13:2148-2158(2003).
[51]
 X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-169.
DOI=10.1093/jb/mvi182; PubMed=16428312 [NCBI, ExPASy, EBI, Israel, Japan]
Padmanabhan B., Kataoka K., Umehara T., Adachi N., Yokoyama S., Horikoshi M.;
"Structural similarity between histone chaperone Cia1p/Asf1p and DNA-binding protein NF-kappaB.";
J. Biochem. 138:821-829(2005).
[52]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-169 IN COMPLEX WITH THE HISTONE H3/H4 HETERODIMER, AND MUTAGENESIS OF LEU-6; SER-48; VAL-94; VAL-109; TYR-112; ARG-145; VAL-146 AND THR-147.
DOI=10.1016/j.cell.2006.08.047; PubMed=17081973 [NCBI, ExPASy, EBI, Israel, Japan]
English C.M., Adkins M.W., Carson J.J., Churchill M.E.A., Tyler J.K.;
"Structural basis for the histone chaperone activity of Asf1.";
Cell 127:495-508(2006).
Comments
  • FUNCTION: Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair. May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks. Also required for acetylation of histone H3 on 'Lys-9' and 'Lys-56'.
  • SUBUNIT: Interacts with histone H3/H4 heterodimers via both histone H3 and histone H4. Interacts with RAD53 and this may impair interaction with histones and chromatin assembly. Interaction with RAD53 is reduced upon activation of DNA damage or replication checkpoints and loss of RAD53 may in turn facilitate interaction with histones and chromatin assembly. Interacts with the CAC2 subunit of chromatin assembly factor 1 (CAF-1). Interacts with the HIR1, HIR2, HIR3 and HPC2 subunits of the HIR complex. Interacts with the RFC1, RFC2, RFC3, RFC4 and RFC5 subunits of the replication factor C (RF-C/RFC) complex. The RF-C complex may recruit this protein to DNA. Interacts with the SAS2, SAS4 and SAS5 subunits of the SAS/SAS-I complex. Interacts with the BDF1, BDF2, SPT15, TAF1 and TAF7 subunits of the TFIID complex. Interacts with RTT109.
  • INTERACTION:
    P32479:HIR1; NbExp=2; IntAct=EBI-3003, EBI-8316;
    P22216:RAD53; NbExp=1; IntAct=EBI-3003, EBI-17843;
    P39940:RSP5; NbExp=1; IntAct=EBI-3003, EBI-16219;
    P40963:SAS2; NbExp=1; IntAct=EBI-3003, EBI-16476;
    Q04003:SAS4; NbExp=3; IntAct=EBI-3003, EBI-38500;
  • SUBCELLULAR LOCATION: Nucleus.
  • DEVELOPMENTAL STAGE: Expression peaks in S-phase (at the RNA level).
  • MISCELLANEOUS: Present with 6230 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the ASF1 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L07593; AAC37512.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49390; CAA89410.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557874; AAS56200.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S30766; S30766.
RefSeq NP_012420.1; -.
3D structure databases
PDB
1ROC; X-ray; 1.50 A; A=2-154.[ExPASy / RCSB / EBI]
1WG3; X-ray; 3.00 A; A=1-169.[ExPASy / RCSB / EBI]
2HUE; X-ray; 1.70 A; A=2-169.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1ROC; -.
1WG3; -.
2HUE; -.
ModBase P32447.
Protein-protein interaction databases
DIP DIP:2675N; -.
IntAct P32447; -.
Organism-specific databases
CYGD YJL115w; -.
SGD S000003651; ASF1.
Yeast-GFP YJL115W.
Gene expression databases
ArrayExpress P32447; -.
GermOnline YJL115W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005678; Cellular component: chromatin assembly complex (inferred from direct assay from SGD).
GO:0042393; Molecular function: histone binding (inferred from mutant phenotype from SGD).
GO:0030466; Biological process: chromatin silencing at silent mating-type cassette (inferred from genetic interaction from SGD).
GO:0006348; Biological process: chromatin silencing at telomere (inferred from genetic interaction from SGD).
GO:0006335; Biological process: DNA replication-dependent nucleosome assembly (inferred from direct assay from SGD).
GO:0006336; Biological process: DNA replication-independent nucleosome assembly (inferred from direct assay from SGD).
GO:0043486; Biological process: histone exchange (inferred from mutant phenotype from SGD).
GO:0010526; Biological process: negative regulation of transposition, RNA-mediated (inferred from mutant phenotype from SGD).
GO:0006337; Biological process: nucleosome disassembly (inferred from mutant phenotype from SGD).
GO:0035066; Biological process: positive regulation of histone acetylation (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR006818; Anti-silence.
IPR017282; Hist_deposition_Asf1.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.1490; Anti-silence; 1.
PANTHER PTHR12040; Anti-silence; 1.
Pfam PF04729; Anti-silence; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF037759; Histone_Asf1; 1.
BLOCKS P32447.
ProtoNet P32447.
Proteomic databases
PeptideAtlas P32447; -.
Genome annotation databases
Ensembl YJL115W; Saccharomyces cerevisiae. [Contig view]
GeneID 853327; -.
GenomeReviews Y13136_GR; YJL115W.
KEGG sce:YJL115W; -.
NMPDR fig|4932.3.peg.3389; -.
Phylogenomic databases
HOGENOM P32447; -.
Other
LinkHub P32447; -.
NextBio 973687; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chaperone; Chromatin regulator; Coiled coil; Complete proteome; Nucleus; Phosphoprotein; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   279  279     Histone chaperone ASF1. PRO_0000064695
REGION   1   155  155     Interaction with histone H3, histone H4, RAD53 and the RF-C complex. 
REGION   1   143  143     Interaction with HIR1. 
COILED   192   243  52     Potential. 
COMPBIAS   170   242  73     Asp/Glu-rich (highly acidic). 
MOD_RES   264   264        Phosphoserine. 
MOD_RES   265   265        Phosphothreonine. 
MOD_RES   269   269        Phosphoserine. 
MOD_RES   270   270        Phosphothreonine. 
MUTAGEN   6     6        L->M: Enhances transcriptional silencing. 
MUTAGEN   36    37        HD->AA: Abrogates stimulation of replication-independent chromatin assembly by the HIR complex and abrogates telomeric silencing. 
MUTAGEN   37    37        D->R: Reduces transcriptional silencing; when associated with R-39. 
MUTAGEN   39    39        E->R: Reduces transcriptional silencing; when associated with R-37. 
MUTAGEN   45    45        V->D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. 
MUTAGEN   48    48        S->R: Abrogates interaction with histone H3 and histone H4 and enhances transcriptional silencing. Reduces acetylation of histone H3 on 'K-9' and 'K-56'; when associated with E-145 or E-147. 
MUTAGEN   53    54        HD->AA: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. 
MUTAGEN   54    54        D->R: Reduces transcriptional silencing. 
MUTAGEN   94    94        V->D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with D-96. 
MUTAGEN   94    94        V->R: Abrogates interaction with histone H3 and histone H4, abrogates transcriptional silencing, reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS. 
MUTAGEN   96    96        L->D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with D-94. 
MUTAGEN   108   108        R->E: Reduces transcriptional silencing. 
MUTAGEN   109   109        V->M: Reduces interaction with histone H3 and histone H4, enhances transcriptional silencing and reduces transcriptional activation. 
MUTAGEN   112   112        Y->A: Abrogates interaction with histone H3 and histone H4 and enhances transcriptional silencing. Abrogates transcriptional silencing, reduces transcriptional activation, reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS; when associated with E-145 or E-147. 
MUTAGEN   112   112        Y->E: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS. 
MUTAGEN   145   145        R->A: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with A-147. 
MUTAGEN   145   145        R->E: Abrogates interaction with histone H3 and histone H4, abrogates transcriptional silencing, reduces transcriptional activation, reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS; when associated with R-48; E-112 or E-147. 
MUTAGEN   146   146        V->L: Reduces interaction with histone H3 and histone H4, enhances transcriptional silencing and reduces transcriptional activation. 
MUTAGEN   147   147        T->A: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with A-145. 
MUTAGEN   147   147        T->E: Enhances transcriptional silencing. Abrogates interaction with histone H3 and histone H4, abrogates transcriptional silencing, reduces transcriptional activation, reduces acetylation of histone H3 on 'K-9' and 'K-56' and enhances sensitivity to HU and MMS; when associated with R-48; A-112 or E-145.