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Histone chaperone ASF1 (Anti-silencing function protein 1) (yASF1)

 ASF1_YEAST              Reviewed;         279 AA.
P32447; D6VW69;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
25-OCT-2017, entry version 168.
RecName: Full=Histone chaperone ASF1;
AltName: Full=Anti-silencing function protein 1;
Short=yASF1;
Name=ASF1; Synonyms=CIA1; OrderedLocusNames=YJL115W; ORFNames=J0755;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=9290207;
DOI=10.1002/(SICI)1097-0061(19970915)13:11<1029::AID-YEA160>3.0.CO;2-1;
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;
PubMed=8948101;
DOI=10.1002/(SICI)1097-0061(199611)12:14<1471::AID-YEA30>3.0.CO;2-4;
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 204508 / S288c;
PubMed=8641269;
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]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
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).
[6]
FUNCTION.
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).
[7]
FUNCTION, AND INTERACTION WITH HISTONE H3; HISTONE H4; HIR1 AND HIR2.
PubMed=11412995; DOI=10.1016/S0960-9822(01)00140-3;
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).
[8]
FUNCTION, AND INTERACTION WITH RAD53.
PubMed=11331602; DOI=10.1101/gad.873201;
Hu F., Alcasabas A.A., Elledge S.J.;
"Asf1 links Rad53 to control of chromatin assembly.";
Genes Dev. 15:1061-1066(2001).
[9]
FUNCTION, AND INTERACTION WITH SAS2; SAS4 AND SAS5.
PubMed=11731479; DOI=10.1101/gad.907201;
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).
[10]
FUNCTION, AND INTERACTION WITH SAS2; SAS4 AND SAS5.
PubMed=11731480; DOI=10.1101/gad.929001;
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).
[11]
FUNCTION, INTERACTION WITH HIR1, AND SUBCELLULAR LOCATION.
PubMed=11404324;
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).
[12]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
HISTONE H3; HISTONE H4 AND RAD53.
PubMed=11172707; DOI=10.1016/S1097-2765(01)00150-2;
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).
[13]
FUNCTION, AND INTERACTION WITH HISTONE H3 AND HISTONE H4.
PubMed=11856374; DOI=10.1046/j.1356-9597.2001.00493.x;
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).
[14]
FUNCTION, AND INTERACTION WITH CAC2; HISTONE H3 AND HISTONE H4.
PubMed=11756556; DOI=10.1128/MCB.22.2.614-625.2002;
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).
[15]
FUNCTION, AND INTERACTION WITH BDF1; BDF2; SPT15; TAF1 AND TAF7.
PubMed=12093919; DOI=10.1073/pnas.142627899;
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).
[16]
INTERACTION WITH RAD53.
PubMed=12851493;
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).
[17]
INTERACTION WITH HISTONE H3 AND HISTONE H4.
PubMed=12626510; DOI=10.1074/jbc.M210709200;
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).
[18]
INTERACTION WITH RAD53.
PubMed=12917350; DOI=10.1128/MCB.23.17.6300-6314.2003;
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).
[19]
FUNCTION.
PubMed=14585955; DOI=10.1128/MCB.23.22.7937-7946.2003;
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).
[20]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
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).
[21]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
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).
[22]
FUNCTION.
PubMed=15071494; DOI=10.1038/sj.embor.7400128;
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).
[23]
FUNCTION.
PubMed=15452122; DOI=10.1074/jbc.M406113200;
Adkins M.W., Tyler J.K.;
"The histone chaperone Asf1p mediates global chromatin disassembly in
vivo.";
J. Biol. Chem. 279:52069-52074(2004).
[24]
FUNCTION.
PubMed=15175160; DOI=10.1016/j.molcel.2004.05.016;
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).
[25]
FUNCTION.
PubMed=15542829; DOI=10.1128/MCB.24.23.10180-10192.2004;
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).
[26]
FUNCTION.
PubMed=15542840; DOI=10.1128/MCB.24.23.10313-10327.2004;
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).
[27]
FUNCTION.
PubMed=15766286; DOI=10.1021/bi047523u;
Robinson K.M., Schultz M.C.;
"Gal4-VP16 directs ATP-independent chromatin reorganization in a yeast
chromatin assembly system.";
Biochemistry 44:4551-4561(2005).
[28]
FUNCTION, INTERACTION WITH HIR1; HIR2; HIR3; HPC2; HISTONE H3; HISTONE
H4 AND RAD53, AND MUTAGENESIS OF 36-HIS-ASP-37.
PubMed=16303565; DOI=10.1016/j.cub.2005.10.053;
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).
[29]
FUNCTION.
PubMed=15821127; DOI=10.1128/EC.4.4.673-684.2005;
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).
[30]
FUNCTION, AND INTERACTION WITH RFC1; RFC2; RFC3; RFC4 AND RFC5.
PubMed=15901673; DOI=10.1101/gad.1305005;
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).
[31]
FUNCTION, INTERACTION WITH RAD53, AND SUBCELLULAR LOCATION.
PubMed=16020781; DOI=10.1534/genetics.105.044719;
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).
[32]
FUNCTION.
PubMed=16143623; DOI=10.1534/genetics.105.043000;
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).
[33]
FUNCTION.
PubMed=16039596; DOI=10.1016/j.molcel.2005.05.028;
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).
[34]
FUNCTION.
PubMed=15632066; DOI=10.1128/MCB.25.2.652-660.2005;
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).
[35]
ERRATUM.
Zabaronick S.R., Tyler J.K.;
Mol. Cell. Biol. 25:2871-2871(2005).
[36]
FUNCTION.
PubMed=15891116; DOI=10.1093/nar/gki560;
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).
[37]
FUNCTION.
PubMed=16141196; DOI=10.1093/nar/gki806;
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).
[38]
FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4, AND MUTAGENESIS
OF ASP-37; GLU-39; ASP-54; VAL-94 AND ARG-108.
PubMed=15840725; DOI=10.1073/pnas.0500149102;
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).
[39]
FUNCTION.
PubMed=16815704; DOI=10.1016/j.cub.2006.06.023;
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).
[40]
FUNCTION.
PubMed=16936140; DOI=10.1128/EC.00202-06;
Linger J., Tyler J.K.;
"Global replication-independent histone H4 exchange in budding
yeast.";
Eukaryot. Cell 5:1780-1787(2006).
[41]
FUNCTION, INTERACTION WITH HISTONE H3 AND RAD53, AND MUTAGENESIS OF
VAL-152.
PubMed=16582440; DOI=10.1534/genetics.105.054783;
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).
[42]
FUNCTION.
PubMed=16407267; DOI=10.1074/jbc.M513340200;
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).
[43]
FUNCTION.
PubMed=17046836; DOI=10.1074/jbc.C600265200;
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).
[44]
FUNCTION.
PubMed=16678113; DOI=10.1016/j.molcel.2006.03.014;
Schwabish M.A., Struhl K.;
"Asf1 mediates histone eviction and deposition during elongation by
RNA polymerase II.";
Mol. Cell 22:415-422(2006).
[45]
FUNCTION.
PubMed=16501045; DOI=10.1073/pnas.0511102103;
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).
[46]
FUNCTION, AND MUTAGENESIS OF VAL-45; 53-HIS-ASP-54; VAL-94; LEU-96;
TYR-112; ARG-145 AND THR-147.
PubMed=16627621; DOI=10.1073/pnas.0601676103;
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).
[47]
FUNCTION, AND MUTAGENESIS OF SER-48; VAL-94; TYR-112; ARG-145 AND
THR-147.
PubMed=17107956; DOI=10.1074/jbc.M608025200;
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).
[48]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[49]
FUNCTION, AND INTERACTION WITH RTT109.
PubMed=17320445; DOI=10.1016/j.molcel.2007.02.006;
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).
[50]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
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).
[51]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[52]
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.
PubMed=14680630; DOI=10.1016/j.cub.2003.11.027;
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).
[53]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-169.
PubMed=16428312; DOI=10.1093/jb/mvi182;
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).
[54]
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.
PubMed=17081973; DOI=10.1016/j.cell.2006.08.047;
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).
-!- 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'.
{ECO:0000269|PubMed:10591219, ECO:0000269|PubMed:11172707,
ECO:0000269|PubMed:11331602, ECO:0000269|PubMed:11404324,
ECO:0000269|PubMed:11412995, ECO:0000269|PubMed:11731479,
ECO:0000269|PubMed:11731480, ECO:0000269|PubMed:11756556,
ECO:0000269|PubMed:11856374, ECO:0000269|PubMed:12093919,
ECO:0000269|PubMed:14585955, ECO:0000269|PubMed:14680630,
ECO:0000269|PubMed:15071494, ECO:0000269|PubMed:15175160,
ECO:0000269|PubMed:15452122, ECO:0000269|PubMed:15542829,
ECO:0000269|PubMed:15542840, ECO:0000269|PubMed:15632066,
ECO:0000269|PubMed:15766286, ECO:0000269|PubMed:15821127,
ECO:0000269|PubMed:15840725, ECO:0000269|PubMed:15891116,
ECO:0000269|PubMed:15901673, ECO:0000269|PubMed:16020781,
ECO:0000269|PubMed:16039596, ECO:0000269|PubMed:16141196,
ECO:0000269|PubMed:16143623, ECO:0000269|PubMed:16303565,
ECO:0000269|PubMed:16407267, ECO:0000269|PubMed:16501045,
ECO:0000269|PubMed:16582440, ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:16678113, ECO:0000269|PubMed:16815704,
ECO:0000269|PubMed:16936140, ECO:0000269|PubMed:17046836,
ECO:0000269|PubMed:17107956, ECO:0000269|PubMed:17320445,
ECO:0000269|PubMed:9290207}.
-!- 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. {ECO:0000269|PubMed:11172707,
ECO:0000269|PubMed:11331602, ECO:0000269|PubMed:11404324,
ECO:0000269|PubMed:11412995, ECO:0000269|PubMed:11731479,
ECO:0000269|PubMed:11731480, ECO:0000269|PubMed:11756556,
ECO:0000269|PubMed:11856374, ECO:0000269|PubMed:12093919,
ECO:0000269|PubMed:12626510, ECO:0000269|PubMed:12851493,
ECO:0000269|PubMed:12917350, ECO:0000269|PubMed:14680630,
ECO:0000269|PubMed:15840725, ECO:0000269|PubMed:15901673,
ECO:0000269|PubMed:16020781, ECO:0000269|PubMed:16303565,
ECO:0000269|PubMed:16582440, ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17320445}.
-!- INTERACTION:
P02309:HHF2; NbExp=5; IntAct=EBI-3003, EBI-8113;
P61830:HHT2; NbExp=4; IntAct=EBI-3003, EBI-8098;
P32479:HIR1; NbExp=6; IntAct=EBI-3003, EBI-8316;
P22216:RAD53; NbExp=10; IntAct=EBI-3003, EBI-17843;
P40161:RTT106; NbExp=5; IntAct=EBI-3003, EBI-29119;
P40963:SAS2; NbExp=4; IntAct=EBI-3003, EBI-16476;
Q04003:SAS4; NbExp=5; IntAct=EBI-3003, EBI-38500;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11404324,
ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16020781}.
-!- DEVELOPMENTAL STAGE: Expression peaks in S-phase (at the RNA
level). {ECO:0000269|PubMed:9290207}.
-!- MISCELLANEOUS: Present with 6230 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ASF1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L07593; AAC37512.1; -; Genomic_DNA.
EMBL; Z49390; CAA89410.1; -; Genomic_DNA.
EMBL; AY557874; AAS56200.1; -; Genomic_DNA.
EMBL; BK006943; DAA08685.1; -; Genomic_DNA.
PIR; S30766; S30766.
RefSeq; NP_012420.1; NM_001181548.1.
PDB; 1ROC; X-ray; 1.50 A; A=2-154.
PDB; 1WG3; X-ray; 3.00 A; A=1-169.
PDB; 2HUE; X-ray; 1.70 A; A=2-169.
PDB; 2IDC; X-ray; 2.20 A; A=2-155.
PDB; 2YGV; X-ray; 2.94 A; A/B/C/D=1-156.
PDB; 4EO5; X-ray; 2.35 A; A=2-169.
PDB; 4ZBJ; X-ray; 2.25 A; A=2-169.
PDB; 5EII; X-ray; 2.44 A; G/I=1-156.
PDBsum; 1ROC; -.
PDBsum; 1WG3; -.
PDBsum; 2HUE; -.
PDBsum; 2IDC; -.
PDBsum; 2YGV; -.
PDBsum; 4EO5; -.
PDBsum; 4ZBJ; -.
PDBsum; 5EII; -.
ProteinModelPortal; P32447; -.
SMR; P32447; -.
BioGrid; 33639; 580.
DIP; DIP-2675N; -.
IntAct; P32447; 134.
MINT; MINT-626416; -.
STRING; 4932.YJL115W; -.
iPTMnet; P32447; -.
MaxQB; P32447; -.
PRIDE; P32447; -.
EnsemblFungi; YJL115W; YJL115W; YJL115W.
GeneID; 853327; -.
KEGG; sce:YJL115W; -.
EuPathDB; FungiDB:YJL115W; -.
SGD; S000003651; ASF1.
GeneTree; ENSGT00390000004692; -.
HOGENOM; HOG000197425; -.
InParanoid; P32447; -.
KO; K10753; -.
OMA; NEYTDEA; -.
OrthoDB; EOG092C4LUM; -.
BioCyc; YEAST:G3O-31569-MONOMER; -.
EvolutionaryTrace; P32447; -.
PRO; PR:P32447; -.
Proteomes; UP000002311; Chromosome X.
GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0042393; F:histone binding; IMP:SGD.
GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IGI:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IGI:SGD.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:SGD.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IDA:SGD.
GO; GO:0016573; P:histone acetylation; IMP:SGD.
GO; GO:0043486; P:histone exchange; IMP:SGD.
GO; GO:0033523; P:histone H2B ubiquitination; IMP:SGD.
GO; GO:0006337; P:nucleosome disassembly; IMP:SGD.
GO; GO:0035066; P:positive regulation of histone acetylation; IDA:SGD.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
GO; GO:0010468; P:regulation of gene expression; IMP:SGD.
GO; GO:0001932; P:regulation of protein phosphorylation; IMP:SGD.
GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IMP:SGD.
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.
InterPro; IPR017282; Hist_deposition_Asf1.
PANTHER; PTHR12040; PTHR12040; 1.
Pfam; PF04729; ASF1_hist_chap; 1.
PIRSF; PIRSF037759; Histone_Asf1; 1.
SUPFAM; SSF101546; SSF101546; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Chromatin regulator; Coiled coil;
Complete proteome; Nucleus; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 279 Histone chaperone ASF1.
/FTId=PRO_0000064695.
REGION 1 155 Interaction with histone H3, histone H4,
RAD53 and the RF-C complex.
REGION 1 143 Interaction with HIR1.
COILED 192 243 {ECO:0000255}.
COMPBIAS 170 242 Asp/Glu-rich (highly acidic).
MUTAGEN 6 6 L->M: Enhances transcriptional silencing.
{ECO:0000269|PubMed:17081973}.
MUTAGEN 36 37 HD->AA: Abrogates stimulation of
replication-independent chromatin
assembly by the HIR complex and abrogates
telomeric silencing.
{ECO:0000269|PubMed:14680630,
ECO:0000269|PubMed:16303565}.
MUTAGEN 37 37 D->R: Reduces transcriptional silencing;
when associated with R-39.
{ECO:0000269|PubMed:15840725}.
MUTAGEN 39 39 E->R: Reduces transcriptional silencing;
when associated with R-37.
{ECO:0000269|PubMed:15840725}.
MUTAGEN 45 45 V->D: Reduces acetylation of histone H3
on 'K-56' and enhances sensitivity to
camptothecin.
{ECO:0000269|PubMed:16627621}.
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. {ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
MUTAGEN 53 54 HD->AA: Reduces acetylation of histone H3
on 'K-56' and enhances sensitivity to
camptothecin.
{ECO:0000269|PubMed:16627621}.
MUTAGEN 54 54 D->R: Reduces transcriptional silencing.
{ECO:0000269|PubMed:15840725}.
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.
{ECO:0000269|PubMed:15840725,
ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
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. {ECO:0000269|PubMed:15840725,
ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
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.
{ECO:0000269|PubMed:16627621}.
MUTAGEN 108 108 R->E: Reduces transcriptional silencing.
{ECO:0000269|PubMed:15840725}.
MUTAGEN 109 109 V->M: Reduces interaction with histone H3
and histone H4, enhances transcriptional
silencing and reduces transcriptional
activation.
{ECO:0000269|PubMed:17081973}.
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.
{ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
MUTAGEN 112 112 Y->E: Reduces acetylation of histone H3
on 'K-56' and enhances sensitivity to
bleomycin, camptothecin, HU and MMS.
{ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
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.
{ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
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. {ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
MUTAGEN 146 146 V->L: Reduces interaction with histone H3
and histone H4, enhances transcriptional
silencing and reduces transcriptional
activation.
{ECO:0000269|PubMed:17081973}.
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.
{ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
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.
{ECO:0000269|PubMed:16627621,
ECO:0000269|PubMed:17081973,
ECO:0000269|PubMed:17107956}.
MUTAGEN 152 152 V->VVFLHY: Impairs interaction with
histone H3 and RAD53 and enhances
silencing at telomeres and mating-type
loci. {ECO:0000269|PubMed:16582440}.
STRAND 3 11 {ECO:0000244|PDB:1ROC}.
STRAND 15 17 {ECO:0000244|PDB:1ROC}.
STRAND 22 30 {ECO:0000244|PDB:1ROC}.
STRAND 38 44 {ECO:0000244|PDB:1ROC}.
HELIX 51 53 {ECO:0000244|PDB:2HUE}.
STRAND 55 62 {ECO:0000244|PDB:1ROC}.
STRAND 67 76 {ECO:0000244|PDB:1ROC}.
HELIX 81 83 {ECO:0000244|PDB:1ROC}.
HELIX 87 90 {ECO:0000244|PDB:1ROC}.
STRAND 93 101 {ECO:0000244|PDB:1ROC}.
STRAND 104 119 {ECO:0000244|PDB:1ROC}.
HELIX 120 124 {ECO:0000244|PDB:1ROC}.
HELIX 132 134 {ECO:0000244|PDB:1ROC}.
STRAND 135 139 {ECO:0000244|PDB:1ROC}.
STRAND 145 148 {ECO:0000244|PDB:1ROC}.
TURN 155 157 {ECO:0000244|PDB:2HUE}.
SEQUENCE 279 AA; 31603 MW; 186E76075C0B1644 CRC64;
MSIVSLLGIK VLNNPAKFTD PYEFEITFEC LESLKHDLEW KLTYVGSSRS LDHDQELDSI
LVGPVPVGVN KFVFSADPPS AELIPASELV SVTVILLSCS YDGREFVRVG YYVNNEYDEE
ELRENPPAKV QVDHIVRNIL AEKPRVTRFN IVWDNENEGD LYPPEQPGVD DEEEEDDEEE
DDDEDDEDDE DDDQEDGEGE AEEAAEEEEE EEEKTEDNET NLEEEEEDIE NSDGDEEEGE
EEVGSVDKNE DGNDKKRRKI EGGSTDIEST PKDAARSTN


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