Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P61830 (H3_YEAST)

Entry version 179 (07 Apr 2021)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

Histone H3

Gene

HHT1

more
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

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP, UAF seems to stimulate basal transcription to a fully activated level.

Miscellaneous

Present with 213000 molecules/cell in log phase SD medium.1 Publication

Caution

To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9ac = acetylated Lys-10; H3K9me1 = monomethylated Lys-10; H3S10ph = phosphorylated Ser-11; H3K14ac = acetylated Lys-15; H3K14me2 = dimethylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27ac = acetylated Lys-28; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3K36ac = acetylated Lys-37; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37; H3K56ac = acetylated Lys-57; H3K64ac = acetylated Lys-65; H3K79me1/2/3 = mono-, di- and trimethylated Lys-80.Curated

<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

Molecular functionDNA-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-2559580, Oxidative Stress Induced Senescence
R-SCE-3214815, HDACs deacetylate histones
R-SCE-427359, SIRT1 negatively regulates rRNA expression
R-SCE-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-SCE-73772, RNA Polymerase I Promoter Escape
R-SCE-9018519, Estrogen-dependent gene expression

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P61830

<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%5Fand%5Ftaxonomy%5Fsection">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 H3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:HHT1
Ordered Locus Names:YBR010W
ORF Names:YBR0201
AND
Name:HHT2
Synonyms:SIN2
Ordered Locus Names:YNL031C
ORF Names:N2749
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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> Componentsi: Chromosome II, Chromosome XIV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000000214, HHT1
S000004976, HHT2

<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

Chromosome, Nucleosome core, 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi11S → A: Impairs histone H3 phosphorylation and reduces transcription of some GCN5 regulated genes. 2 Publications1
Mutagenesisi53R → A, K or Q: Lethal. 1 Publication1
Mutagenesisi57K → A, Q or R: Increases sensitivity to genotoxic agents inducing DNA breaks during replication. 3 Publications1
Mutagenesisi80K → A, P or Q: Compromises telomeric silencing. 2 Publications1
Mutagenesisi119T → A or E: Lethal. 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
<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_00002213702 – 136Histone H3Add BLAST135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei5N6,N6,N6-trimethyllysine; alternate11 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate11 Publications1
Modified residuei5N6-methyllysine; alternate11 Publications1
Modified residuei10N6-acetyllysine; alternate5 Publications1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate1 Publication1
Modified residuei11Phosphoserine3 Publications1
Modified residuei15N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate8 Publications1
Modified residuei15N6-butyryllysine; alternate2 Publications1
Modified residuei19N6-acetyllysine; alternate5 Publications1
Modified residuei19N6-butyryllysine; alternate1 Publication1
Modified residuei19N6-methyllysine; alternate1 Publication1
Modified residuei24N6-acetyllysine; alternate3 Publications1
Modified residuei24N6-butyryllysine; alternate1 Publication1
Modified residuei24N6-methyllysine; alternate1 Publication1
Modified residuei24N6-propionyllysine; alternate1 Publication1
Modified residuei28N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei28N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei28N6-acetyllysine; alternate3 Publications1
Modified residuei28N6-butyryllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate1 Publication1
Modified residuei37N6,N6,N6-trimethyllysine; alternate7 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate8 Publications1
Modified residuei37N6-acetyllysine; alternate3 Publications1
Modified residuei37N6-methyllysine; alternate8 Publications1
Modified residuei38N6-acetyllysine; alternate1 Publication1
Modified residuei38N6-methyllysine; alternate1 Publication1
Modified residuei57N6-acetyllysine6 Publications1
Modified residuei57N6-malonyllysine; alternate1 Publication1
Modified residuei57N6-propionyllysine; alternate1 Publication1
Modified residuei65N6-acetyllysine1 Publication1
Modified residuei80N6,N6,N6-trimethyllysine; alternate6 Publications1
Modified residuei80N6,N6-dimethyllysine; alternate6 Publications1
Modified residuei80N6-methyllysine; alternate6 Publications1
Modified residuei80N6-succinyllysine; alternate1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by IPL1 to form H3S10ph in a cell cycle-dependent manner during mitosis and meiosis. H3S10ph is also formed by SNF1, promotes subsequent H3K14ac formation by GCN5, and is required for transcriptional activation through TBP recruitment to the promoters. Dephosphorylation is performed by GLC7.3 Publications
Mono-, di- and trimethylated by the COMPASS complex to form H3K4me1/2/3. H3K4me activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance. H3K4me enrichment correlates with transcription levels, and occurs in a 5' to 3' gradient with H3K4me3 enrichment at the 5'-end of genes, shifting to H3K4me2 and then H3K4me1. Methylated by SET2 to form H3K36me. H3K36me represses gene expression. Methylated by DOT1 to form H3K79me. H3K79me is required for association of SIR proteins with telomeric regions and for telomeric silencing. The COMPASS-mediated formation of H3K4me2/3 and the DOT1-mediated formation of H3K79me require H2BK123ub1.20 Publications
Acetylation of histone H3 leads to transcriptional activation. H3K14ac formation by GCN5, a component of the SAGA complex, is promoted by H3S10ph. Further acetylated by GCN5 to form H3K9ac, H3K18ac, H3K23ac, H3K27ac and H3K36ac. H3K14ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. H3K56ac formation occurs predominantly in newly synthesized H3 molecules during G1, S and G2/M of the cell cycle and may be involved in DNA repair.13 Publications
Crotonylation (Kcr) marks active promoters and enhancers and confers resistance to transcriptional repressors.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P61830

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

More...PaxDbi		P61830

PRoteomics IDEntifications database

More...PRIDEi		P61830

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P61830

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P61830

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Histone H3 is a component of the UAF (upstream activation factor) complex, which consists of UAF30, RRN5, RRN9, RRN10, and histones H3 and H4.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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		32711, 838 interactors
35796, 697 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1101, RNA polymerase I upstream activating factor complex
CPX-1610, Nucleosome, variant HTA2-HTB2
CPX-1611, Nucleosome, variant HTA2-HTB1
CPX-1612, Nucleosome, variant HTA1-HTB1
CPX-1613, Nucleosome, variant HTZ1-HTB1
CPX-1614, Nucleosome, variant HTZ1-HTB2
CPX-2566, Nucleosome, variant HTA1-HTB2

Database of interacting proteins

More...DIPi		DIP-417N

Protein interaction database and analysis system

More...IntActi		P61830, 153 interactors

Molecular INTeraction database

More...MINTi		P61830

STRING: functional protein association networks

More...STRINGi		4932.YNL031C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P61830, 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

1136
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		P61830

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		P61830

<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 information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1745, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT01020000230348

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_078295_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P61830

Identification of Orthologs from Complete Genome Data

More...OMAi		CTMARTK

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.20.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50143

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009072, Histone-fold
IPR007125, Histone_H2A/H2B/H3
IPR000164, Histone_H3/CENP-A

The PANTHER Classification System

More...PANTHERi		PTHR11426, PTHR11426, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00125, Histone, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00622, HISTONEH3

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00428, H3, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47113, SSF47113, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00322, HISTONE_H3_1, 1 hit
PS00959, HISTONE_H3_2, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P61830-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LASKAARKSA PSTGGVKKPH RYKPGTVALR 
        60         70         80         90        100
EIRRFQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAI GALQESVEAY 
       110        120        130 
LVSLFEDTNL AAIHAKRVTI QKKDIKLARR LRGERS
Length:136
Mass (Da):15,356
Last modified:January 23, 2007 - v2
<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:iA6115FEB480AC67A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti124D → E AA sequence (PubMed:7035169).Curated1

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
X00724 Genomic DNA Translation: CAA25310.1
X00725 Genomic DNA Translation: CAA25312.1
Z35879 Genomic DNA Translation: CAA84948.1
Z71306 Genomic DNA Translation: CAA95893.1
Z71307 Genomic DNA Translation: CAA95894.1
AY558343 Genomic DNA Translation: AAS56669.1
AY692987 Genomic DNA Translation: AAT93006.1
AY554000 Genomic DNA Translation: AAS64341.1
AY554001 Genomic DNA Translation: AAS64342.1
AY554002 Genomic DNA Translation: AAS64343.1
AY554003 Genomic DNA Translation: AAS64344.1
AY554004 Genomic DNA Translation: AAS64345.1
AY554005 Genomic DNA Translation: AAS64346.1
AY554006 Genomic DNA Translation: AAS64347.1
AY554007 Genomic DNA Translation: AAS64348.1
AY554008 Genomic DNA Translation: AAS64349.1
BK006936 Genomic DNA Translation: DAA07131.1
BK006947 Genomic DNA Translation: DAA10514.1

Protein sequence database of the Protein Information Resource

More...PIRi		S45265, HSBY3

NCBI Reference Sequences

More...RefSeqi		NP_009564.1, NM_001178358.1
NP_014367.1, NM_001182870.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YBR010W_mRNA; YBR010W; YBR010W
YNL031C_mRNA; YNL031C; YNL031C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		852295
855700

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YBR010W
sce:YNL031C

<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
X00724 Genomic DNA Translation: CAA25310.1
X00725 Genomic DNA Translation: CAA25312.1
Z35879 Genomic DNA Translation: CAA84948.1
Z71306 Genomic DNA Translation: CAA95893.1
Z71307 Genomic DNA Translation: CAA95894.1
AY558343 Genomic DNA Translation: AAS56669.1
AY692987 Genomic DNA Translation: AAT93006.1
AY554000 Genomic DNA Translation: AAS64341.1
AY554001 Genomic DNA Translation: AAS64342.1
AY554002 Genomic DNA Translation: AAS64343.1
AY554003 Genomic DNA Translation: AAS64344.1
AY554004 Genomic DNA Translation: AAS64345.1
AY554005 Genomic DNA Translation: AAS64346.1
AY554006 Genomic DNA Translation: AAS64347.1
AY554007 Genomic DNA Translation: AAS64348.1
AY554008 Genomic DNA Translation: AAS64349.1
BK006936 Genomic DNA Translation: DAA07131.1
BK006947 Genomic DNA Translation: DAA10514.1
PIRiS45265, HSBY3
RefSeqiNP_009564.1, NM_001178358.1
NP_014367.1, NM_001182870.1

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
1ID3X-ray3.10A/E2-136[»]
1M1DX-ray2.20B/D2-21[»]
1PEGX-ray2.59P/Q2-16[»]
1PU9X-ray2.30B6-24[»]
1PUAX-ray2.30B6-24[»]
1QSNX-ray2.20B10-20[»]
2CNXX-ray2.10P2-6[»]
2H2GX-ray1.63B114-124[»]
2IDCX-ray2.20A119-135[»]
2JMJNMR-P2-10[»]
2RNWNMR-B2-16[»]
2RNXNMR-B32-43[»]
2RSNNMR-B2-18[»]
3MP1X-ray2.60P2-6[»]
3MP6X-ray1.48P2-5[»]
3Q33X-ray2.80D2-15[»]
4JJNX-ray3.09A/E2-136[»]
4KUDX-ray3.20A/E1-136[»]
4PSXX-ray2.51P/Y2-16[»]
5D7EX-ray1.90C6-12[»]
5IOKX-ray2.22C6-12[»]
5ZBAX-ray3.50C1-136[»]
5ZBBX-ray3.60C1-136[»]
6GEJelectron microscopy3.60A/B1-136[»]
6GENelectron microscopy3.60A/B1-136[»]
6J2PX-ray2.85E/F/G/H2-8[»]
6KMJX-ray1.40C7-22[»]
SMRiP61830
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi32711, 838 interactors
35796, 697 interactors
ComplexPortaliCPX-1101, RNA polymerase I upstream activating factor complex
CPX-1610, Nucleosome, variant HTA2-HTB2
CPX-1611, Nucleosome, variant HTA2-HTB1
CPX-1612, Nucleosome, variant HTA1-HTB1
CPX-1613, Nucleosome, variant HTZ1-HTB1
CPX-1614, Nucleosome, variant HTZ1-HTB2
CPX-2566, Nucleosome, variant HTA1-HTB2
DIPiDIP-417N
IntActiP61830, 153 interactors
MINTiP61830
STRINGi4932.YNL031C

PTM databases

CarbonylDBiP61830
iPTMnetiP61830

Proteomic databases

MaxQBiP61830
PaxDbiP61830
PRIDEiP61830

Genome annotation databases

EnsemblFungiiYBR010W_mRNA; YBR010W; YBR010W
YNL031C_mRNA; YNL031C; YNL031C
GeneIDi852295
855700
KEGGisce:YBR010W
sce:YNL031C

Organism-specific databases

SGDiS000000214, HHT1
S000004976, HHT2

Phylogenomic databases

eggNOGiKOG1745, Eukaryota
GeneTreeiENSGT01020000230348
HOGENOMiCLU_078295_4_0_1
InParanoidiP61830
OMAiCTMARTK

Enzyme and pathway databases

ReactomeiR-SCE-2559580, Oxidative Stress Induced Senescence
R-SCE-3214815, HDACs deacetylate histones
R-SCE-427359, SIRT1 negatively regulates rRNA expression
R-SCE-5625886, Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-SCE-73772, RNA Polymerase I Promoter Escape
R-SCE-9018519, Estrogen-dependent gene expression
SABIO-RKiP61830

Miscellaneous databases

EvolutionaryTraceiP61830

Protein Ontology

More...PROi		PR:P61830
RNActiP61830, protein

Family and domain databases

Gene3Di1.10.20.10, 1 hit
IDEALiIID50143
InterProiView protein in InterPro
IPR009072, Histone-fold
IPR007125, Histone_H2A/H2B/H3
IPR000164, Histone_H3/CENP-A
PANTHERiPTHR11426, PTHR11426, 1 hit
PfamiView protein in Pfam
PF00125, Histone, 1 hit
PRINTSiPR00622, HISTONEH3
SMARTiView protein in SMART
SM00428, H3, 1 hit
SUPFAMiSSF47113, SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00322, HISTONE_H3_1, 1 hit
PS00959, HISTONE_H3_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...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 nameiH3_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: P61830
Secondary accession number(s): D6VQ11
, E9PAG1, P02303, P13996, Q6B1U3, Q6Q7G9
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 7, 2021
This is version 179 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again