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UniProtKB - Q08465 (YNG1_YEAST)

Entry version 168 (29 Sep 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Protein YNG1

Gene

YNG1

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-binding component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation. YNG1 is required for the HAT activity of NuA3 but not for its integrity. Mediates the interaction of SAS3 with nucleosomes.

2 Publications

Miscellaneous

Present with 861 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei157Histone H3K4me3 bindingBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi158Zinc 1By similarity1
Metal bindingi160Zinc 1By similarity1
Sitei168Histone H3K4me3 bindingBy similarity1
Metal bindingi171Zinc 2By similarity1
Sitei172Histone H3K4me3 bindingBy similarity1
Metal bindingi176Zinc 2By similarity1
Sitei180Histone H3K4me3 bindingBy similarity1
Metal bindingi182Zinc 1; via pros nitrogenBy similarity1
Metal bindingi185Zinc 1By similarity1
Metal bindingi198Zinc 2By similarity1
Metal bindingi202Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri155 – 204PHD-type; degenerateAdd BLAST50

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-3214847, HATs acetylate histones
R-SCE-3899300, SUMOylation of transcription cofactors
R-SCE-6804758, Regulation of TP53 Activity through Acetylation
R-SCE-6811555, PI5P Regulates TP53 Acetylation

<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:
Protein YNG1
Alternative name(s):
ING1 homolog 1
<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:YNG1
Ordered Locus Names:YOR064C
ORF Names:YOR29-15
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000005590, YNG1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YOR064C

<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

Keywords - Cellular componenti

Nucleus

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002402481 – 219Protein YNG1Add BLAST219

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q08465

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

More...PaxDbi		Q08465

PRoteomics IDEntifications database

More...PRIDEi		Q08465

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q08465

<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 H3K4me3 and to a lesser extent with H3K4me2.

Component of the NuA3 complex, composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6.

Interacts with histone H3-K4 trimethylated.

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34463, 153 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1810, NuA3 histone acetyltransferase complex

Database of interacting proteins

More...DIPi		DIP-3833N

Protein interaction database and analysis system

More...IntActi		Q08465, 6 interactors

Molecular INTeraction database

More...MINTi		Q08465

STRING: functional protein association networks

More...STRINGi		4932.YOR064C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q08465, protein

<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

1219
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

More...SMRi		Q08465

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q08465

<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

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PHD-type zinc finger mediates the binding to H3K4me3.1 Publication

<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 ING family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri155 – 204PHD-type; degenerateAdd BLAST50

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1973, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_074406_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q08465

Identification of Orthologs from Complete Genome Data

More...OMAi		RSLWLIQ

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50148

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR028651, ING_fam
IPR011011, Znf_FYVE_PHD
IPR001965, Znf_PHD
IPR013083, Znf_RING/FYVE/PHD

The PANTHER Classification System

More...PANTHERi		PTHR10333, PTHR10333, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00249, PHD, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57903, SSF57903, 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.

Q08465-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEHLANENSD SDIRYSFLST LDHLPCELIR SLRLMQTIDL FKNEEDEPGM 
        60         70         80         90        100
ERACRDLLLV ATYINDLVDD QIHFLKQHKK ELEIQKSVTK NFNSSLENIK 
       110        120        130        140        150
SKLTLEEPGA YKEPKLLLKI NLKKAKSRER KESITSPTIG INQGDVTEGN 
       160        170        180        190        200
NNQEEVYCFC RNVSYGPMVA CDNPACPFEW FHYGCVGLKQ APKGKWYCSK 
       210 
DCKEIANQRS KSKRQKRRK
Length:219
Mass (Da):25,350
Last modified:November 1, 1996 - 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:i5232A71839E2FDA4
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Z70678 Genomic DNA Translation: CAA94549.1
Z74972 Genomic DNA Translation: CAA99257.1
AY557753 Genomic DNA Translation: AAS56079.1
BK006948 Genomic DNA Translation: DAA10843.1

Protein sequence database of the Protein Information Resource

More...PIRi		S66947

NCBI Reference Sequences

More...RefSeqi		NP_014707.1, NM_001183483.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YOR064C_mRNA; YOR064C; YOR064C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854230

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YOR064C

<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
Z70678 Genomic DNA Translation: CAA94549.1
Z74972 Genomic DNA Translation: CAA99257.1
AY557753 Genomic DNA Translation: AAS56079.1
BK006948 Genomic DNA Translation: DAA10843.1
PIRiS66947
RefSeqiNP_014707.1, NM_001183483.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JMINMR-A141-219[»]
2JMJNMR-A141-219[»]
SMRiQ08465
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34463, 153 interactors
ComplexPortaliCPX-1810, NuA3 histone acetyltransferase complex
DIPiDIP-3833N
IntActiQ08465, 6 interactors
MINTiQ08465
STRINGi4932.YOR064C

PTM databases

iPTMnetiQ08465

Proteomic databases

MaxQBiQ08465
PaxDbiQ08465
PRIDEiQ08465

Genome annotation databases

EnsemblFungiiYOR064C_mRNA; YOR064C; YOR064C
GeneIDi854230
KEGGisce:YOR064C

Organism-specific databases

SGDiS000005590, YNG1
VEuPathDBiFungiDB:YOR064C

Phylogenomic databases

eggNOGiKOG1973, Eukaryota
HOGENOMiCLU_074406_1_0_1
InParanoidiQ08465
OMAiRSLWLIQ

Enzyme and pathway databases

ReactomeiR-SCE-3214847, HATs acetylate histones
R-SCE-3899300, SUMOylation of transcription cofactors
R-SCE-6804758, Regulation of TP53 Activity through Acetylation
R-SCE-6811555, PI5P Regulates TP53 Acetylation

Miscellaneous databases

EvolutionaryTraceiQ08465

Protein Ontology

More...PROi		PR:Q08465
RNActiQ08465, protein

Family and domain databases

Gene3Di3.30.40.10, 1 hit
IDEALiIID50148
InterProiView protein in InterPro
IPR028651, ING_fam
IPR011011, Znf_FYVE_PHD
IPR001965, Znf_PHD
IPR013083, Znf_RING/FYVE/PHD
PANTHERiPTHR10333, PTHR10333, 2 hits
SMARTiView protein in SMART
SM00249, PHD, 1 hit
SUPFAMiSSF57903, SSF57903, 1 hit

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 nameiYNG1_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: Q08465
Secondary accession number(s): D6W2C7, O00025
<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: June 13, 2006
Last sequence update: November 1, 1996
Last modified: September 29, 2021
This is version 168 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, Reference proteome

Documents

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