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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 protein phosphorylation 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)DescriptionActionsGraphical viewLength
Mutagenesisi6L → M: Enhances transcriptional silencing. 1 Publication1
Mutagenesisi36 – 37HD → AA: Abrogates stimulation of replication-independent chromatin assembly by the HIR complex and abrogates telomeric silencing. 2 Publications2
Mutagenesisi37D → R: Reduces transcriptional silencing; when associated with R-39. 1 Publication1
Mutagenesisi39E → R: Reduces transcriptional silencing; when associated with R-37. 1 Publication1
Mutagenesisi45V → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. 1 Publication1
Mutagenesisi48S → 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 Publications1
Mutagenesisi53 – 54HD → AA: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to camptothecin. 1 Publication2
Mutagenesisi54D → R: Reduces transcriptional silencing. 1 Publication1
Mutagenesisi94V → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with D-96. 4 Publications1
Mutagenesisi94V → 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 Publications1
Mutagenesisi96L → D: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with D-94. 1 Publication1
Mutagenesisi108R → E: Reduces transcriptional silencing. 1 Publication1
Mutagenesisi109V → M: Reduces interaction with histone H3 and histone H4, enhances transcriptional silencing and reduces transcriptional activation. 1 Publication1
Mutagenesisi112Y → 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 Publications1
Mutagenesisi112Y → E: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS. 3 Publications1
Mutagenesisi145R → A: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with A-147. 3 Publications1
Mutagenesisi145R → 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 Publications1
Mutagenesisi146V → L: Reduces interaction with histone H3 and histone H4, enhances transcriptional silencing and reduces transcriptional activation. 1 Publication1
Mutagenesisi147T → A: Reduces acetylation of histone H3 on 'K-56' and enhances sensitivity to bleomycin, camptothecin, HU and MMS; when associated with A-145. 3 Publications1
Mutagenesisi147T → 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 Publications1
Mutagenesisi152V → VVFLHY: Impairs interaction with histone H3 and RAD53 and enhances silencing at telomeres and mating-type loci. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000646951 – 279Histone chaperone ASF1Add BLAST279

Proteomic databases

MaxQBiP32447.
PRIDEiP32447.

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 interactors.
DIPiDIP-2675N.
IntActiP32447. 134 interactors.
MINTiMINT-626416.

Structurei

Secondary structure

1279
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 11Combined sources9
Beta strandi15 – 17Combined sources3
Beta strandi22 – 30Combined sources9
Beta strandi38 – 44Combined sources7
Helixi51 – 53Combined sources3
Beta strandi55 – 62Combined sources8
Beta strandi67 – 76Combined sources10
Helixi81 – 83Combined sources3
Helixi87 – 90Combined sources4
Beta strandi93 – 101Combined sources9
Beta strandi104 – 119Combined sources16
Helixi120 – 124Combined sources5
Helixi132 – 134Combined sources3
Beta strandi135 – 139Combined sources5
Beta strandi145 – 148Combined sources4
Turni155 – 157Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32447.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 155Interaction with histone H3, histone H4, RAD53 and the RF-C complexAdd BLAST155
Regioni1 – 143Interaction with HIR1Add BLAST143

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili192 – 243Sequence analysisAdd BLAST52

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi170 – 242Asp/Glu-rich (highly acidic)Add BLAST73

Sequence similaritiesi

Belongs to the ASF1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

GeneTreeiENSGT00390000004692.
HOGENOMiHOG000197425.
InParanoidiP32447.
KOiK10753.
OMAiNEYTDEA.
OrthoDBiEOG092C4LUM.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiP32447.

Proteomic databases

MaxQBiP32447.
PRIDEiP32447.

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.
OrthoDBiEOG092C4LUM.

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...

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: November 30, 2016
This is version 160 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.