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Entry version 183 (03 Jul 2019)
Sequence version 1 (01 Oct 1993)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone, Chromatin regulator
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31569-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone chaperone ASF1
Alternative name(s):
Anti-silencing function protein 1
Short name:
yASF1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ASF1
Synonyms:CIA1
Ordered Locus Names:YJL115W
ORF Names:J0755
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YJL115W

Saccharomyces Genome Database

More...
SGDi
S000003651 ASF1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000646951 – 279Histone chaperone ASF1Add BLAST279

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32447

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P32447

PRoteomics IDEntifications database

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PRIDEi
P32447

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32447

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33639, 643 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1322 RAD53-ASF1 complex

Database of interacting proteins

More...
DIPi
DIP-2675N

Protein interaction database and analysis system

More...
IntActi
P32447, 134 interactors

Molecular INTeraction database

More...
MINTi
P32447

STRING: functional protein association networks

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STRINGi
4932.YJL115W

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1279
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P32447

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P32447

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili192 – 243Sequence analysisAdd BLAST52

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi170 – 242Asp/Glu-rich (highly acidic)Add BLAST73

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ASF1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000004692

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000197425

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32447

KEGG Orthology (KO)

More...
KOi
K10753

Identification of Orthologs from Complete Genome Data

More...
OMAi
SYDEREF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.1490, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006818 ASF1-like
IPR036747 ASF1-like_sf
IPR017282 Hist_deposition_Asf1

The PANTHER Classification System

More...
PANTHERi
PTHR12040 PTHR12040, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04729 ASF1_hist_chap, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037759 Histone_Asf1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF101546 SSF101546, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i186E76075C0B1644
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

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PIRi
S30766

NCBI Reference Sequences

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RefSeqi
NP_012420.1, NM_001181548.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJL115W_mRNA; YJL115W_mRNA; YJL115W

Database of genes from NCBI RefSeq genomes

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GeneIDi
853327

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJL115W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
5EIIX-ray2.44G/I1-156[»]
5UCBX-ray1.52B2-154[»]
5UEAX-ray1.70D/X2-154[»]
5UEKX-ray1.70A2-154[»]
6AYZX-ray2.10A/M2-154[»]
6AZ2X-ray2.48B/D2-154[»]
6F0YNMR-A2-169[»]
SMRiP32447
ModBaseiSearch...

Protein-protein interaction databases

BioGridi33639, 643 interactors
ComplexPortaliCPX-1322 RAD53-ASF1 complex
DIPiDIP-2675N
IntActiP32447, 134 interactors
MINTiP32447
STRINGi4932.YJL115W

PTM databases

iPTMnetiP32447

Proteomic databases

MaxQBiP32447
PaxDbiP32447
PRIDEiP32447

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P32447
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL115W_mRNA; YJL115W_mRNA; YJL115W
GeneIDi853327
KEGGisce:YJL115W

Organism-specific databases

EuPathDBiFungiDB:YJL115W
SGDiS000003651 ASF1

Phylogenomic databases

GeneTreeiENSGT00390000004692
HOGENOMiHOG000197425
InParanoidiP32447
KOiK10753
OMAiSYDEREF

Enzyme and pathway databases

BioCyciYEAST:G3O-31569-MONOMER

Miscellaneous databases

EvolutionaryTraceiP32447

Protein Ontology

More...
PROi
PR:P32447

Family and domain databases

Gene3Di2.60.40.1490, 1 hit
InterProiView protein in InterPro
IPR006818 ASF1-like
IPR036747 ASF1-like_sf
IPR017282 Hist_deposition_Asf1
PANTHERiPTHR12040 PTHR12040, 1 hit
PfamiView protein in Pfam
PF04729 ASF1_hist_chap, 1 hit
PIRSFiPIRSF037759 Histone_Asf1, 1 hit
SUPFAMiSSF101546 SSF101546, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiASF1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P32447
Secondary accession number(s): D6VW69
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 3, 2019
This is version 183 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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 chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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