Reviewed, UniProtKB/Swiss-Prot P32447 (ASF1_YEAST)

Names and origin

Protein names

Recommended name:
    Histone chaperone ASF1
Alternative name(s):
    Anti-silencing function protein 1
      Short name=yASF1

Gene names

Name:	ASF1
Synonyms:	CIA1
Ordered Locus Names:	YJL115W
ORF Names:	J0755

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	279 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. 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'. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.50
Subunit structure	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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.27 Ref.29 Ref.30 Ref.37 Ref.40 Ref.47 Ref.50 Ref.15 Ref.16 Ref.17
Subcellular location	Nucleus. Ref.10 Ref.30 Ref.19
Developmental stage	Expression peaks in S-phase (at the RNA level). Ref.1
Miscellaneous	Present with 6230 molecules/cell in log phase SD medium. Ref.20
Sequence similarities	Belongs to the ASF1 family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil
Molecular function	Chaperone Chromatin regulator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	DNA replication-dependent nucleosome assembly Ref.6 Inferred from direct assay. Source: SGD DNA replication-independent nucleosome assembly Ref.27 Inferred from direct assay. Source: SGD chromatin silencing at silent mating-type cassette Ref.37 Inferred from genetic interaction. Source: SGD chromatin silencing at telomere Ref.37 Inferred from genetic interaction. Source: SGD histone acetylation Ref.45 Inferred from mutant phenotype. Source: SGD histone exchange Inferred from mutant phenotype. Source: SGD negative regulation of transposition, RNA-mediated Inferred from mutant phenotype. Source: SGD nucleosome disassembly Ref.43 Inferred from mutant phenotype. Source: SGD positive regulation of histone acetylation Inferred from direct assay. Source: SGD transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromatin assembly complex Ref.8 Inferred from direct assay. Source: SGD
Molecular function	histone binding Ref.37 Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HHF1	P02309	1	EBI-3003,EBI-8113
HHT1	P61830	1	EBI-3003,EBI-8098
HIR1	P32479	2	EBI-3003,EBI-8316
RAD53	P22216	1	EBI-3003,EBI-17843
RSP5	P39940	1	EBI-3003,EBI-16219
SAS2	P40963	1	EBI-3003,EBI-16476
SAS4	Q04003	3	EBI-3003,EBI-38500

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 279

279

Histone chaperone ASF1

PRO_0000064695

Regions

Region

1 – 155

155

Interaction with histone H3, histone H4, RAD53 and the RF-C complex

Region

1 – 143

143

Interaction with HIR1

Coiled coil

192 – 243

52

Potential

Compositional bias

170 – 242

73

Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue

264

1

Phosphoserine Ref.48 Ref.49

Modified residue

265

1

Phosphothreonine Ref.48 Ref.49

Modified residue

269

1

Phosphoserine Ref.49

Modified residue

270

1

Phosphothreonine Ref.48

Experimental info

Mutagenesis

6

1

L → M: Enhances transcriptional silencing. Ref.27 Ref.50 Ref.52

Mutagenesis

36 – 37

2

HD → AA: Abrogates stimulation of replication-independent chromatin assembly by the HIR complex and abrogates telomeric silencing. Ref.27 Ref.37 Ref.50

Mutagenesis

37

1

D → R: Reduces transcriptional silencing; when associated with R-39. Ref.27 Ref.37 Ref.50

Mutagenesis

39

1

E → R: Reduces transcriptional silencing; when associated with R-37. Ref.27 Ref.37 Ref.50

Mutagenesis

45

1

V → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. Ref.27 Ref.45 Ref.50

Mutagenesis

48

1

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. Ref.27 Ref.46 Ref.50 Ref.52

Mutagenesis

53 – 54

2

HD → AA: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. Ref.27 Ref.37 Ref.50

Mutagenesis

54

1

D → R: Reduces transcriptional silencing. Ref.27 Ref.37 Ref.50

Mutagenesis

94

1

V → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with D-96. Ref.27 Ref.37 Ref.45 Ref.46 Ref.50 Ref.52

Mutagenesis

94

1

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. Ref.27 Ref.37 Ref.45 Ref.46 Ref.50 Ref.52

Mutagenesis

96

1

L → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with D-94. Ref.27 Ref.45 Ref.50

Mutagenesis

108

1

R → E: Reduces transcriptional silencing. Ref.27 Ref.37 Ref.50

Mutagenesis

109

1

V → M: Reduces interaction with histone H3 and histone H4, enhances transcriptional silencing and reduces transcriptional activation. Ref.27 Ref.50 Ref.52

Mutagenesis

112

1

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. Ref.27 Ref.45 Ref.46 Ref.50 Ref.52

Mutagenesis

112

1

Y → E: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS. Ref.27 Ref.45 Ref.46 Ref.50 Ref.52

Mutagenesis

145

1

R → A: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with A-147. Ref.27 Ref.45 Ref.46 Ref.50 Ref.52

Mutagenesis

145

1

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. Ref.27 Ref.45 Ref.46 Ref.50 Ref.52

Mutagenesis

146

1

V → L: Reduces interaction with histone H3 and histone H4, enhances transcriptional silencing and reduces transcriptional activation. Ref.27 Ref.50 Ref.52

Mutagenesis

147

1

T → A: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with A-145. Ref.27 Ref.45 Ref.46 Ref.50 Ref.52

Mutagenesis

147

1

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. Ref.27 Ref.45 Ref.46 Ref.50 Ref.52

Mutagenesis

152

1

V → VVFLHY: Impairs interaction with histone H3 and RAD53 and enhances silencing at telomeres and mating-type loci. Ref.27 Ref.40 Ref.50

Secondary structure

1

.

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279

Helix Strand Turn

Details...

Beta strand

3 – 11

9

Beta strand

15 – 17

3

Beta strand

22 – 30

9

Beta strand

38 – 44

7

Beta strand

55 – 62

8

Beta strand

67 – 76

10

Helix

81 – 83

3

Helix

87 – 90

4

Beta strand

93 – 101

9

Beta strand

104 – 119

16

Helix

120 – 124

5

Helix

132 – 134

3

Beta strand

135 – 139

5

Beta strand

145 – 148

4

Turn

155 – 157

3

Sequences

	Sequence		Length	Mass (Da)
	P32447-1 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 186E76075C0B1644	FASTA	279	31,603
	10 20 30 40 50 60 MSIVSLLGIK VLNNPAKFTD PYEFEITFEC LESLKHDLEW KLTYVGSSRS LDHDQELDSI 70 80 90 100 110 120 LVGPVPVGVN KFVFSADPPS AELIPASELV SVTVILLSCS YDGREFVRVG YYVNNEYDEE 130 140 150 160 170 180 ELRENPPAKV QVDHIVRNIL AEKPRVTRFN IVWDNENEGD LYPPEQPGVD DEEEEDDEEE 190 200 210 220 230 240 DDDEDDEDDE DDDQEDGEGE AEEAAEEEEE EEEKTEDNET NLEEEEEDIE NSDGDEEEGE 250 260 270 EEVGSVDKNE DGNDKKRRKI EGGSTDIEST PKDAARSTN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two new S-phase-specific genes from Saccharomyces cerevisiae." Le S., Davis C., Konopka J.B., Sternglanz R. Yeast 13:1029-1042(1997) [PubMed: 9290207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE.
[2]	"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." Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C. Yeast 12:1471-1474(1996) [PubMed: 8948101] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." 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. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: FUNCTION.
[6]	"Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for heterochromatic silencing." Sharp J.A., Fouts E.T., Krawitz D.C., Kaufman P.D. Curr. Biol. 11:463-473(2001) [PubMed: 11412995] [Abstract] Cited for: FUNCTION, INTERACTION WITH HISTONE H3; HISTONE H4; HIR1 AND HIR2.
[7]	"Asf1 links Rad53 to control of chromatin assembly." Hu F., Alcasabas A.A., Elledge S.J. Genes Dev. 15:1061-1066(2001) [PubMed: 11331602] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAD53.
[8]	"The yeast SAS (something about silencing) protein complex contains a MYST-type putative acetyltransferase and functions with chromatin assembly factor ASF1." Osada S., Sutton A., Muster N., Brown C.E., Yates J.R. III, Sternglanz R., Workman J.L. Genes Dev. 15:3155-3168(2001) [PubMed: 11731479] [Abstract] Cited for: FUNCTION, INTERACTION WITH SAS2; SAS4 AND SAS5.
[9]	"The silencing complex SAS-I links histone acetylation to the assembly of repressed chromatin by CAF-I and Asf1 in Saccharomyces cerevisiae." Meijsing S.H., Ehrenhofer-Murray A.E. Genes Dev. 15:3169-3182(2001) [PubMed: 11731480] [Abstract] Cited for: FUNCTION, INTERACTION WITH SAS2; SAS4 AND SAS5.
[10]	"Yeast ASF1 protein is required for cell cycle regulation of histone gene transcription." Sutton A., Bucaria J., Osley M.A., Sternglanz R. Genetics 158:587-596(2001) [PubMed: 11404324] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIR1, SUBCELLULAR LOCATION.
[11]	"Dynamic interaction of DNA damage checkpoint protein Rad53 with chromatin assembly factor Asf1." Emili A., Schieltz D.M., Yates J.R. III, Hartwell L.H. Mol. Cell 7:13-20(2001) [PubMed: 11172707] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HISTONE H3; HISTONE H4 AND RAD53.
[12]	"Polyanionic stretch-deleted histone chaperone cia1/Asf1p is functional both in vivo and in vitro." Umehara T., Chimura T., Ichikawa N., Horikoshi M. Genes Cells 7:59-73(2002) [PubMed: 11856374] [Abstract] Cited for: FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4.
[13]	"Chromatin assembly factor I mutants defective for PCNA binding require Asf1/Hir proteins for silencing." Krawitz D.C., Kama T., Kaufman P.D. Mol. Cell. Biol. 22:614-625(2002) [PubMed: 11756556] [Abstract] Cited for: FUNCTION, INTERACTION WITH CAC2; HISTONE H3 AND HISTONE H4.
[14]	"Identification and characterization of CIA/ASF1 as an interactor of bromodomains associated with TFIID." Chimura T., Kuzuhara T., Horikoshi M. Proc. Natl. Acad. Sci. U.S.A. 99:9334-9339(2002) [PubMed: 12093919] [Abstract] Cited for: FUNCTION, INTERACTION WITH BDF1; BDF2; SPT15; TAF1 AND TAF7.
[15]	"FHA domain-mediated DNA checkpoint regulation of Rad53." Schwartz M.F., Lee S.-J., Duong J.K., Eminaga S., Stern D.F. Cell Cycle 2:384-396(2003) [PubMed: 12851493] [Abstract] Cited for: INTERACTION WITH RAD53.
[16]	"Sas4 and Sas5 are required for the histone acetyltransferase activity of Sas2 in the SAS complex." Sutton A., Shia W.-J., Band D., Kaufman P.D., Osada S., Workman J.L., Sternglanz R. J. Biol. Chem. 278:16887-16892(2003) [PubMed: 12626510] [Abstract] Cited for: INTERACTION WITH HISTONE H3 AND HISTONE H4.
[17]	"Rad53 phosphorylation site clusters are important for Rad53 regulation and signaling." Lee S.-J., Schwartz M.F., Duong J.K., Stern D.F. Mol. Cell. Biol. 23:6300-6314(2003) [PubMed: 12917350] [Abstract] Cited for: INTERACTION WITH RAD53.
[18]	"Replication-independent assembly of nucleosome arrays in a novel yeast chromatin reconstitution system involves antisilencing factor Asf1p and chromodomain protein Chd1p." Robinson K.M., Schultz M.C. Mol. Cell. Biol. 23:7937-7946(2003) [PubMed: 14585955] [Abstract] Cited for: FUNCTION.
[19]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[20]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[21]	"The absence of the yeast chromatin assembly factor Asf1 increases genomic instability and sister chromatid exchange." Prado F., Cortes-Ledesma F., Aguilera A. EMBO Rep. 5:497-502(2004) [PubMed: 15071494] [Abstract] Cited for: FUNCTION.
[22]	"The histone chaperone Asf1p mediates global chromatin disassembly in vivo." Adkins M.W., Tyler J.K. J. Biol. Chem. 279:52069-52074(2004) [PubMed: 15452122] [Abstract] Cited for: FUNCTION.
[23]	"Chromatin disassembly mediated by the histone chaperone Asf1 is essential for transcriptional activation of the yeast PHO5 and PHO8 genes." Adkins M.W., Howar S.R., Tyler J.K. Mol. Cell 14:657-666(2004) [PubMed: 15175160] [Abstract] Cited for: FUNCTION.
[24]	"Yeast chromatin assembly complex 1 protein excludes nonacetylatable forms of histone H4 from chromatin and the nucleus." Glowczewski L., Waterborg J.H., Berman J.G. Mol. Cell. Biol. 24:10180-10192(2004) [PubMed: 15542829] [Abstract] Cited for: FUNCTION.
[25]	"Activation of the DNA damage checkpoint in yeast lacking the histone chaperone anti-silencing function 1." Ramey C.J., Howar S., Adkins M., Linger J., Spicer J., Tyler J.K. Mol. Cell. Biol. 24:10313-10327(2004) [PubMed: 15542840] [Abstract] Cited for: FUNCTION.
[26]	"Gal4-VP16 directs ATP-independent chromatin reorganization in a yeast chromatin assembly system." Robinson K.M., Schultz M.C. Biochemistry 44:4551-4561(2005) [PubMed: 15766286] [Abstract] Cited for: FUNCTION.
[27]	"Replication-independent histone deposition by the HIR complex and Asf1." Green E.M., Antczak A.J., Bailey A.O., Franco A.A., Wu K.J., Yates J.R. III, Kaufman P.D. Curr. Biol. 15:2044-2049(2005) [PubMed: 16303565] [Abstract] Cited for: FUNCTION, INTERACTION WITH HIR1; HIR2; HIR3; HPC2; HISTONE H3; HISTONE H4 AND RAD53, MUTAGENESIS OF 36-HIS-ASP-37.
[28]	"Contribution of CAF-I to anaphase-promoting-complex-mediated mitotic chromatin assembly in Saccharomyces cerevisiae." Harkness T.A.A., Arnason T.G., Legrand C., Pisclevich M.G., Davies G.F., Turner E.L. Eukaryot. Cell 4:673-684(2005) [PubMed: 15821127] [Abstract] Cited for: FUNCTION.
[29]	"Histone deposition protein Asf1 maintains DNA replisome integrity and interacts with replication factor C." Franco A.A., Lam W.M., Burgers P.M., Kaufman P.D. Genes Dev. 19:1365-1375(2005) [PubMed: 15901673] [Abstract] Cited for: FUNCTION, INTERACTION WITH RFC1; RFC2; RFC3; RFC4 AND RFC5.
[30]	"Regulation of histone deposition proteins Asf1/Hir1 by multiple DNA damage checkpoint kinases in Saccharomyces cerevisiae." Sharp J.A., Rizki G., Kaufman P.D. Genetics 171:885-899(2005) [PubMed: 16020781] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAD53, SUBCELLULAR LOCATION.
[31]	"The yeast histone chaperone chromatin assembly factor 1 protects against double-strand DNA-damaging agents." Linger J., Tyler J.K. Genetics 171:1513-1522(2005) [PubMed: 16143623] [Abstract] Cited for: FUNCTION.
[32]	"Histones are incorporated in trans during reassembly of the yeast PHO5 promoter." Schermer U.J., Korber P., Hoerz W. Mol. Cell 19:279-285(2005) [PubMed: 16039596] [Abstract] Cited for: FUNCTION.
[33]	"The histone chaperone anti-silencing function 1 is a global regulator of transcription independent of passage through S phase." Zabaronick S.R., Tyler J.K. Mol. Cell. Biol. 25:652-660(2005) [PubMed: 15632066] [Abstract] Cited for: FUNCTION.
[34]	Erratum Zabaronick S.R., Tyler J.K. Mol. Cell. Biol. 25:2871-2871(2005)
[35]	"Chromatin assembly factor Asf1p-dependent occupancy of the SAS histone acetyltransferase complex at the silent mating-type locus HMLalpha." Osada S., Kurita M., Nishikawa J., Nishihara T. Nucleic Acids Res. 33:2742-2750(2005) [PubMed: 15891116] [Abstract] Cited for: FUNCTION.
[36]	"Reduction of nucleosome assembly during new DNA synthesis impairs both major pathways of double-strand break repair." Lewis L.K., Karthikeyan G., Cassiano J., Resnick M.A. Nucleic Acids Res. 33:4928-4939(2005) [PubMed: 16141196] [Abstract] Cited for: FUNCTION.
[37]	"Structural basis for the interaction of Asf1 with histone H3 and its functional implications." Mousson F., Lautrette A., Thuret J.-Y., Agez M., Courbeyrette R., Amigues B., Becker E., Neumann J.-M., Guerois R., Mann C., Ochsenbein F. Proc. Natl. Acad. Sci. U.S.A. 102:5975-5980(2005) [PubMed: 15840725] [Abstract] Cited for: FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4, MUTAGENESIS OF ASP-37; GLU-39; ASP-54; VAL-94 AND ARG-108.
[38]	"The sirtuins Hst3 and Hst4p preserve genome integrity by controlling histone H3 lysine 56 deacetylation." Celic I., Masumoto H., Griffith W.P., Meluh P., Cotter R.J., Boeke J.D., Verreault A. Curr. Biol. 16:1280-1289(2006) [PubMed: 16815704] [Abstract] Cited for: FUNCTION.
[39]	"Global replication-independent histone H4 exchange in budding yeast." Linger J., Tyler J.K. Eukaryot. Cell 5:1780-1787(2006) [PubMed: 16936140] [Abstract] Cited for: FUNCTION.
[40]	"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." Tamburini B.A., Carson J.J., Linger J.G., Tyler J.K. Genetics 173:599-610(2006) [PubMed: 16582440] [Abstract] Cited for: FUNCTION, INTERACTION WITH HISTONE H3 AND RAD53, MUTAGENESIS OF VAL-152.
[41]	"The histone chaperone Asf1 increases the rate of histone eviction at the yeast PHO5 and PHO8 promoters." Korber P., Barbaric S., Luckenbach T., Schmid A., Schermer U.J., Blaschke D., Hoerz W. J. Biol. Chem. 281:5539-5545(2006) [PubMed: 16407267] [Abstract] Cited for: FUNCTION.
[42]	"Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II." Schneider J., Bajwa P., Johnson F.C., Bhaumik S.R., Shilatifard A. J. Biol. Chem. 281:37270-37274(2006) [PubMed: 17046836] [Abstract] Cited for: FUNCTION.
[43]	"Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II." Schwabish M.A., Struhl K. Mol. Cell 22:415-422(2006) [PubMed: 16678113] [Abstract] Cited for: FUNCTION.
[44]	"Checkpoint functions are required for normal S-phase progression in Saccharomyces cerevisiae RCAF- and CAF-I-defective mutants." Kats E.S., Albuquerque C.P., Zhou H., Kolodner R.D. Proc. Natl. Acad. Sci. U.S.A. 103:3710-3715(2006) [PubMed: 16501045] [Abstract] Cited for: FUNCTION.
[45]	"Histone chaperone Asf1 is required for histone H3 lysine 56 acetylation, a modification associated with S phase in mitosis and meiosis." 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. Proc. Natl. Acad. Sci. U.S.A. 103:6988-6993(2006) [PubMed: 16627621] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF VAL-45; 53-HIS-ASP-54; VAL-94; LEU-96; TYR-112; ARG-145 AND THR-147.
[46]	"The histone chaperone anti-silencing function 1 stimulates the acetylation of newly synthesized histone H3 in S-phase." Adkins M.W., Carson J.J., English C.M., Ramey C.J., Tyler J.K. J. Biol. Chem. 282:1334-1340(2007) [PubMed: 17107956] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-48; VAL-94; TYR-112; ARG-145 AND THR-147.
[47]	"Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes." Tsubota T., Berndsen C.E., Erkmann J.A., Smith C.L., Yang L., Freitas M.A., Denu J.M., Kaufman P.D. Mol. Cell 25:703-712(2007) [PubMed: 17320445] [Abstract] Cited for: FUNCTION, INTERACTION WITH RTT109.
[48]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; THR-265 AND THR-270, MASS SPECTROMETRY.
[49]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; THR-265 AND SER-269, MASS SPECTROMETRY.
[50]	"Structure and function of the conserved core of histone deposition protein Asf1." 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. Curr. Biol. 13:2148-2158(2003) [PubMed: 14680630] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-154, FUNCTION, INTERACTION WITH HISTONE H3; HISTONE H4 AND RAD53, MUTAGENESIS OF 36-HIS-ASP-37.
[51]	"Structural similarity between histone chaperone Cia1p/Asf1p and DNA-binding protein NF-kappaB." Padmanabhan B., Kataoka K., Umehara T., Adachi N., Yokoyama S., Horikoshi M. J. Biochem. 138:821-829(2005) [PubMed: 16428312] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-169.
[52]	"Structural basis for the histone chaperone activity of Asf1." English C.M., Adkins M.W., Carson J.J., Churchill M.E.A., Tyler J.K. Cell 127:495-508(2006) [PubMed: 17081973] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-169 IN COMPLEX WITH THE HISTONE H3/H4 HETERODIMER, MUTAGENESIS OF LEU-6; SER-48; VAL-94; VAL-109; TYR-112; ARG-145; VAL-146 AND THR-147.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L07593 Genomic DNA. Translation: AAC37512.1.
Z49390 Genomic DNA. Translation: CAA89410.1.
AY557874 Genomic DNA. Translation: AAS56200.1.

PIR

S30766.

RefSeq

NP_012420.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ROC	X-ray	1.50	A	2-154	[»]
1WG3	X-ray	3.00	A	1-169	[»]
2HUE	X-ray	1.70	A	2-169	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2675N.

IntAct

P32447. 19 interactions.

Proteomic databases

PeptideAtlas

P32447.

PRIDE

P32447.

Genome annotation databases

Ensembl

YJL115W. Saccharomyces cerevisiae. [Contig view]

GeneID

853327.

GenomeReviews

Gene locus YJL115W in contig Y13136_GR.

KEGG

sce:YJL115W.

NMPDR

fig|4932.3.peg.3389.

Organism-specific databases

CYGD

YJL115w.

SGD

S000003651. ASF1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P32447.

OMA

P32447. VILLSCS.

Gene expression databases

ArrayExpress

P32447.

GermOnline

YJL115W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR017282. Hist_deposition_Asf1.
IPR006818. Histone_chaperone_ASF1-like.
[Graphical view]

Gene3D

G3DSA:2.60.40.1490. Anti-silence. 1 hit.

PANTHER

PTHR12040. Anti-silence. 1 hit.

Pfam

PF04729. ASF1_hist_chap. 1 hit.
[Graphical view]

PIRSF

PIRSF037759. Histone_Asf1. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

973687.

Entry information

Entry name

ASF1_YEAST

Accession

Primary (citable) accession number: P32447

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)