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Protein

Histone chaperone ASF1

Gene

ASF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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'.39 Publications

GO - Molecular functioni

  • histone binding Source: SGD

GO - Biological processi

  • chromatin silencing at silent mating-type cassette Source: SGD
  • chromatin silencing at telomere Source: SGD
  • DNA replication-dependent nucleosome assembly Source: SGD
  • DNA replication-independent nucleosome assembly Source: SGD
  • histone acetylation Source: SGD
  • histone exchange Source: SGD
  • histone H2B ubiquitination Source: SGD
  • nucleosome disassembly Source: SGD
  • positive regulation of histone acetylation Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  • regulation of gene expression Source: SGD
  • regulation of transcription from RNA polymerase II promoter in response to stress Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-31569-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone chaperone ASF1
Alternative name(s):
Anti-silencing function protein 1
Short name:
yASF1
Gene namesi
Name:ASF1
Synonyms:CIA1
Ordered Locus Names:YJL115W
ORF Names:J0755
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL115W.
SGDiS000003651. ASF1.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi6 – 61L → M: Enhances transcriptional silencing. 1 Publication
Mutagenesisi36 – 372HD → AA: Abrogates stimulation of replication-independent chromatin assembly by the HIR complex and abrogates telomeric silencing. 2 Publications
Mutagenesisi37 – 371D → R: Reduces transcriptional silencing; when associated with R-39. 1 Publication
Mutagenesisi39 – 391E → R: Reduces transcriptional silencing; when associated with R-37. 1 Publication
Mutagenesisi45 – 451V → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. 1 Publication
Mutagenesisi48 – 481S → 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. 2 Publications
Mutagenesisi53 – 542HD → AA: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. 1 Publication
Mutagenesisi54 – 541D → R: Reduces transcriptional silencing. 1 Publication
Mutagenesisi94 – 941V → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with D-96. 4 Publications
Mutagenesisi94 – 941V → 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. 4 Publications
Mutagenesisi96 – 961L → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with D-94. 1 Publication
Mutagenesisi108 – 1081R → E: Reduces transcriptional silencing. 1 Publication
Mutagenesisi109 – 1091V → M: Reduces interaction with histone H3 and histone H4, enhances transcriptional silencing and reduces transcriptional activation. 1 Publication
Mutagenesisi112 – 1121Y → 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. 3 Publications
Mutagenesisi112 – 1121Y → E: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS. 3 Publications
Mutagenesisi145 – 1451R → A: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with A-147. 3 Publications
Mutagenesisi145 – 1451R → 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. 3 Publications
Mutagenesisi146 – 1461V → L: Reduces interaction with histone H3 and histone H4, enhances transcriptional silencing and reduces transcriptional activation. 1 Publication
Mutagenesisi147 – 1471T → A: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with A-145. 3 Publications
Mutagenesisi147 – 1471T → 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. 3 Publications
Mutagenesisi152 – 1521V → VVFLHY: Impairs interaction with histone H3 and RAD53 and enhances silencing at telomeres and mating-type loci. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Histone chaperone ASF1PRO_0000064695Add
BLAST

Proteomic databases

MaxQBiP32447.

PTM databases

iPTMnetiP32447.

Expressioni

Developmental stagei

Expression peaks in S-phase (at the RNA level).1 Publication

Interactioni

Subunit structurei

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 RTT109.20 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HHF2P023095EBI-3003,EBI-8113
HHT2P618304EBI-3003,EBI-8098
HIR1P324796EBI-3003,EBI-8316
RAD53P222168EBI-3003,EBI-17843
RTT106P401615EBI-3003,EBI-29119
SAS2P409634EBI-3003,EBI-16476
SAS4Q040035EBI-3003,EBI-38500

GO - Molecular functioni

  • histone binding Source: SGD

Protein-protein interaction databases

BioGridi33639. 351 interactions.
DIPiDIP-2675N.
IntActiP32447. 134 interactions.
MINTiMINT-626416.

Structurei

Secondary structure

1
279
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 119Combined sources
Beta strandi15 – 173Combined sources
Beta strandi22 – 309Combined sources
Beta strandi38 – 447Combined sources
Helixi51 – 533Combined sources
Beta strandi55 – 628Combined sources
Beta strandi67 – 7610Combined sources
Helixi81 – 833Combined sources
Helixi87 – 904Combined sources
Beta strandi93 – 1019Combined sources
Beta strandi104 – 11916Combined sources
Helixi120 – 1245Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi145 – 1484Combined sources
Turni155 – 1573Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ROCX-ray1.50A2-154[»]
1WG3X-ray3.00A1-169[»]
2HUEX-ray1.70A2-169[»]
2IDCX-ray2.20A2-155[»]
2YGVX-ray2.94A/B/C/D1-156[»]
4EO5X-ray2.35A2-169[»]
4ZBJX-ray2.25A2-169[»]
ProteinModelPortaliP32447.
SMRiP32447. Positions 2-154.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32447.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 155155Interaction with histone H3, histone H4, RAD53 and the RF-C complexAdd
BLAST
Regioni1 – 143143Interaction with HIR1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili192 – 24352Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi170 – 24273Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
InParanoidiP32447.
KOiK10753.
OMAiNEYTDEA.
OrthoDBiEOG70CRJQ.

Family and domain databases

Gene3Di2.60.40.1490. 1 hit.
InterProiIPR006818. ASF1-like.
IPR017282. Hist_deposition_Asf1.
[Graphical view]
PANTHERiPTHR12040. PTHR12040. 1 hit.
PfamiPF04729. ASF1_hist_chap. 1 hit.
[Graphical view]
PIRSFiPIRSF037759. Histone_Asf1. 1 hit.
SUPFAMiSSF101546. SSF101546. 1 hit.

Sequencei

Sequence statusi: Complete.

P32447-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIVSLLGIK VLNNPAKFTD PYEFEITFEC LESLKHDLEW KLTYVGSSRS
60 70 80 90 100
LDHDQELDSI LVGPVPVGVN KFVFSADPPS AELIPASELV SVTVILLSCS
110 120 130 140 150
YDGREFVRVG YYVNNEYDEE ELRENPPAKV QVDHIVRNIL AEKPRVTRFN
160 170 180 190 200
IVWDNENEGD LYPPEQPGVD DEEEEDDEEE DDDEDDEDDE DDDQEDGEGE
210 220 230 240 250
AEEAAEEEEE EEEKTEDNET NLEEEEEDIE NSDGDEEEGE EEVGSVDKNE
260 270
DGNDKKRRKI EGGSTDIEST PKDAARSTN
Length:279
Mass (Da):31,603
Last modified:October 1, 1993 - v1
Checksum:i186E76075C0B1644
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07593 Genomic DNA. Translation: AAC37512.1.
Z49390 Genomic DNA. Translation: CAA89410.1.
AY557874 Genomic DNA. Translation: AAS56200.1.
BK006943 Genomic DNA. Translation: DAA08685.1.
PIRiS30766.
RefSeqiNP_012420.1. NM_001181548.1.

Genome annotation databases

EnsemblFungiiYJL115W; YJL115W; YJL115W.
GeneIDi853327.
KEGGisce:YJL115W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07593 Genomic DNA. Translation: AAC37512.1.
Z49390 Genomic DNA. Translation: CAA89410.1.
AY557874 Genomic DNA. Translation: AAS56200.1.
BK006943 Genomic DNA. Translation: DAA08685.1.
PIRiS30766.
RefSeqiNP_012420.1. NM_001181548.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ROCX-ray1.50A2-154[»]
1WG3X-ray3.00A1-169[»]
2HUEX-ray1.70A2-169[»]
2IDCX-ray2.20A2-155[»]
2YGVX-ray2.94A/B/C/D1-156[»]
4EO5X-ray2.35A2-169[»]
4ZBJX-ray2.25A2-169[»]
ProteinModelPortaliP32447.
SMRiP32447. Positions 2-154.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33639. 351 interactions.
DIPiDIP-2675N.
IntActiP32447. 134 interactions.
MINTiMINT-626416.

PTM databases

iPTMnetiP32447.

Proteomic databases

MaxQBiP32447.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL115W; YJL115W; YJL115W.
GeneIDi853327.
KEGGisce:YJL115W.

Organism-specific databases

EuPathDBiFungiDB:YJL115W.
SGDiS000003651. ASF1.

Phylogenomic databases

GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
InParanoidiP32447.
KOiK10753.
OMAiNEYTDEA.
OrthoDBiEOG70CRJQ.

Enzyme and pathway databases

BioCyciYEAST:G3O-31569-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32447.
PROiP32447.

Family and domain databases

Gene3Di2.60.40.1490. 1 hit.
InterProiIPR006818. ASF1-like.
IPR017282. Hist_deposition_Asf1.
[Graphical view]
PANTHERiPTHR12040. PTHR12040. 1 hit.
PfamiPF04729. ASF1_hist_chap. 1 hit.
[Graphical view]
PIRSFiPIRSF037759. Histone_Asf1. 1 hit.
SUPFAMiSSF101546. SSF101546. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONE H3; HISTONE H4; HIR1 AND HIR2.
  8. "Asf1 links Rad53 to control of chromatin assembly."
    Hu F., Alcasabas A.A., Elledge S.J.
    Genes Dev. 15:1061-1066(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAD53.
  9. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SAS2; SAS4 AND SAS5.
  10. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SAS2; SAS4 AND SAS5.
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIR1, SUBCELLULAR LOCATION.
  12. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HISTONE H3; HISTONE H4 AND RAD53.
  13. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4.
  14. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CAC2; HISTONE H3 AND HISTONE H4.
  15. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BDF1; BDF2; SPT15; TAF1 AND TAF7.
  16. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD53.
  17. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HISTONE H3 AND HISTONE H4.
  18. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD53.
  19. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  21. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  22. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "The histone chaperone Asf1p mediates global chromatin disassembly in vivo."
    Adkins M.W., Tyler J.K.
    J. Biol. Chem. 279:52069-52074(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  27. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIR1; HIR2; HIR3; HPC2; HISTONE H3; HISTONE H4 AND RAD53, MUTAGENESIS OF 36-HIS-ASP-37.
  29. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RFC1; RFC2; RFC3; RFC4 AND RFC5.
  31. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAD53, SUBCELLULAR LOCATION.
  32. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  33. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  34. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  35. Erratum
    Zabaronick S.R., Tyler J.K.
    Mol. Cell. Biol. 25:2871-2871(2005)
  36. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  37. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  38. Cited for: FUNCTION, INTERACTION WITH HISTONE H3 AND HISTONE H4, MUTAGENESIS OF ASP-37; GLU-39; ASP-54; VAL-94 AND ARG-108.
  39. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  40. "Global replication-independent histone H4 exchange in budding yeast."
    Linger J., Tyler J.K.
    Eukaryot. Cell 5:1780-1787(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  41. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HISTONE H3 AND RAD53, MUTAGENESIS OF VAL-152.
  42. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  43. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  44. "Asf1 mediates histone eviction and deposition during elongation by RNA polymerase II."
    Schwabish M.A., Struhl K.
    Mol. Cell 22:415-422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  45. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  46. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF VAL-45; 53-HIS-ASP-54; VAL-94; LEU-96; TYR-112; ARG-145 AND THR-147.
  47. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-48; VAL-94; TYR-112; ARG-145 AND THR-147.
  48. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  49. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RTT109.
  50. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  51. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  52. 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.
  53. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-169.
  54. "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] [Europe PMC] [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.

Entry informationi

Entry nameiASF1_YEAST
AccessioniPrimary (citable) accession number: P32447
Secondary accession number(s): D6VW69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 6, 2016
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6230 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.