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Entry version 157 (13 Feb 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Histone H3.1

Gene

Hist1h3a

more
Organism
Mus musculus (Mouse)
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.

Miscellaneous

This histone is only present in mammals.

<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

  • nucleosomal DNA binding Source: GO_Central
  • protein heterodimerization activity Source: InterPro

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 functionDNA-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1266695 Interleukin-7 signaling
R-MMU-212300 PRC2 methylates histones and DNA
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-3214815 HDACs deacetylate histones
R-MMU-3214841 PKMTs methylate histone lysines
R-MMU-3214842 HDMs demethylate histones
R-MMU-3214847 HATs acetylate histones
R-MMU-3214858 RMTs methylate histone arginines
R-MMU-3247509 Chromatin modifying enzymes
R-MMU-427359 SIRT1 negatively regulates rRNA expression
R-MMU-427413 NoRC negatively regulates rRNA expression
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5578749 Transcriptional regulation by small RNAs
R-MMU-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-MMU-73728 RNA Polymerase I Promoter Opening
R-MMU-73777 RNA Polymerase I Chain Elongation
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9018519 Estrogen-dependent gene expression
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

<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 H3.1
<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:Hist1h3a
Synonyms:H3a
AND
Name:Hist1h3g
Synonyms:H3.1-221, H3g
AND
Name:Hist1h3h
Synonyms:H3.1-291, H3h
AND
Name:Hist1h3i
Synonyms:H3.1-I, H3i
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 13

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:2668828 Hist1h3a
MGI:2145541 Hist1h3g
MGI:2448349 Hist1h3h
MGI:2448350 Hist1h3i

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002212491 – 136Histone H3.1Add BLAST136

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 residuei3Asymmetric dimethylarginine; by PRMT6; alternateBy similarity1
Modified residuei3Citrulline; alternate1 Publication1
Modified residuei3Phosphoarginine; alternateCurated1
Modified residuei4Phosphothreonine; by HASPIN1 Publication1
Modified residuei5Allysine; alternateBy similarity1
Modified residuei5N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei5N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei5N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei5N6-acetyllysine; alternate1 Publication1
Modified residuei5N6-crotonyllysine; alternate1 Publication1
Modified residuei5N6-methyllysine; alternate2 Publications1
Modified residuei7Phosphothreonine; by PKCBy similarity1
Modified residuei9Citrulline; alternate1 Publication1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternate1 Publication1
Modified residuei10N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei10N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-acetyllysine; alternate2 Publications1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate2 Publications1
Modified residuei11ADP-ribosylserine; alternateBy similarity1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA55 Publications1
Modified residuei12Phosphothreonine; by PKC and CHEK1By similarity1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate3 Publications1
Modified residuei15N6-succinyllysine; alternateBy similarity1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternate4 Publications1
Modified residuei18Citrulline; alternate1 Publication1
Modified residuei19N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei19N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei19N6-acetyllysine; alternate3 Publications1
Modified residuei19N6-butyryllysine; alternate1 Publication1
Modified residuei19N6-crotonyllysine; alternate1 Publication1
Modified residuei19N6-methyllysine; alternate1 Publication1
Modified residuei24N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei24N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei24N6-acetyllysine; alternate3 Publications1
Modified residuei24N6-butyryllysine; alternate1 Publication1
Modified residuei24N6-crotonyllysine; alternate1 Publication1
Modified residuei24N6-methyllysine; alternate1 Publication1
Modified residuei27Citrulline1 Publication1
Modified residuei28N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei28N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei28N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei28N6-acetyllysine; alternate1 Publication1
Modified residuei28N6-butyryllysine; alternate1 Publication1
Modified residuei28N6-crotonyllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate2 Publications1
Modified residuei29ADP-ribosylserine; alternateBy similarity1
Modified residuei29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA56 Publications1
Modified residuei37N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei37N6-acetyllysine; alternate1 Publication1
Modified residuei37N6-butyryllysine; alternate1 Publication1
Modified residuei37N6-methyllysine; alternate2 Publications1
Modified residuei38N6-butyryllysine; alternate1 Publication1
Modified residuei38N6-methyllysine; alternateBy similarity1
Modified residuei42PhosphotyrosineBy similarity1
Modified residuei57N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei57N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei57N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei57N6-acetyllysine; alternateBy similarity1
Modified residuei57N6-crotonyllysine; alternate1 Publication1
Modified residuei57N6-methyllysine; by EHMT2; alternateBy similarity1
Modified residuei57N6-succinyllysine; alternate1 Publication1
Modified residuei58PhosphoserineBy similarity1
Modified residuei65N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei65N6-methyllysine; alternateBy similarity1
Modified residuei80N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei80N6,N6-dimethyllysine; alternate2 Publications1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei80N6-acetyllysine; alternateBy similarity1
Modified residuei80N6-butyryllysine; alternate1 Publication1
Modified residuei80N6-methyllysine; alternate2 Publications1
Modified residuei80N6-succinyllysine; alternate1 Publication1
Modified residuei81PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysineBy similarity1
Modified residuei123N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei123N6-acetyllysine; alternateBy similarity1
Modified residuei123N6-butyryllysine; alternate1 Publication1
Modified residuei123N6-methyllysine; alternate1 Publication1
Modified residuei123N6-succinyllysine; alternateBy similarity1
Modified residuei129PhosphoarginineCurated1
Modified residuei130PhosphoarginineCurated1
Modified residuei132PhosphoarginineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability.7 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.6 Publications
Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).By similarity
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.10 Publications
Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.12 Publications
Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination.By similarity1 Publication
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity).By similarity
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication
Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis.1 Publication
Hydroxybutyrylation of histones is induced by starvation. It is linked to gene activation and may replace histone acetylation on the promoter of specific genes in response to fasting.1 Publication
Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation.By similarity
Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P68433

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P68433

MaxQB - The MaxQuant DataBase

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MaxQBi
P68433

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

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PaxDbi
P68433

PRoteomics IDEntifications database

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PRIDEi
P68433

Consortium for Top Down Proteomics

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TopDownProteomicsi
P68433

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P68433

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P68433

<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

Expressed during S phase, then expression strongly decreases as cell division slows down during the process of differentiation.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000069265 Expressed in 15 organ(s), highest expression level in testis

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P68433 MM

<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

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.

<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)

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BioGridi
237523, 2 interactors

Protein interaction database and analysis system

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IntActi
P68433, 26 interactors

Molecular INTeraction database

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MINTi
P68433

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000097295

<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

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
1GUWNMR-B2-17[»]
1U35X-ray3.00A/E1-136[»]
2V83X-ray2.40D/E2-10[»]
2W5ZX-ray2.20C2-9[»]
2WP1X-ray2.10P/Q15-24[»]
2XL3X-ray2.70D/F2-9[»]
4EZHX-ray2.52C/D25-35[»]
5B1LX-ray2.35A/E1-136[»]
5B1MX-ray2.34A/E1-136[»]
5IX1X-ray2.60P/Q2-16[»]
5IX2X-ray2.90P/Q2-33[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P68433

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

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SMRi
P68433

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P68433

<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

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eggNOGi
KOG1745 Eukaryota
COG2036 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153149
ENSGT00940000153611

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001172

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P68433

KEGG Orthology (KO)

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KOi
K11253

Identification of Orthologs from Complete Genome Data

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OMAi
RRXEASE

Database of Orthologous Groups

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OrthoDBi
1564596at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P68433

TreeFam database of animal gene trees

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TreeFami
TF314241

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

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PANTHERi
PTHR11426 PTHR11426, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00125 Histone, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00622 HISTONEH3

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00428 H3, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47113 SSF47113, 1 hit

PROSITE; a protein domain and family database

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

P68433-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,404
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:i9B89008EA50A0EF6
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X01684 Genomic DNA Translation: CAA25839.1
M32460 Genomic DNA Translation: AAA37811.1
M32462 Genomic DNA Translation: AAA37813.1
X16496 Genomic DNA Translation: CAA34512.1
U62670 Genomic DNA Translation: AAB04763.1
U62672 Genomic DNA Translation: AAB04765.1
AY158944 Genomic DNA Translation: AAO06254.1
AY158945 Genomic DNA Translation: AAO06255.1
AY158946 Genomic DNA Translation: AAO06256.1
AY158952 Genomic DNA Translation: AAO06262.1
Y12290 Genomic DNA Translation: CAA72968.1
AK006742 mRNA Translation: BAB24722.1
AK018952 mRNA Translation: BAB31493.1
AK155722 mRNA Translation: BAE33402.1
AL590388 Genomic DNA Translation: CAI25837.1
AL589651 Genomic DNA Translation: CAI24113.1
AL589651 Genomic DNA Translation: CAI24105.1
BC107285 mRNA Translation: AAI07286.1
BC107287 mRNA Translation: AAI07288.1
BC115816 mRNA Translation: AAI15817.1
BC116383 mRNA Translation: AAI16384.1
BC125355 mRNA Translation: AAI25356.1
BC125357 mRNA Translation: AAI25358.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS26289.1
CCDS26296.1
CCDS26342.1
CCDS26368.1

Protein sequence database of the Protein Information Resource

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PIRi
A39525
S06755

NCBI Reference Sequences

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RefSeqi
NP_038578.2, NM_013550.5
NP_659539.1, NM_145073.2
NP_835513.1, NM_178206.2
NP_835514.1, NM_178207.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.221301
Mm.261657
Mm.377874
Mm.390558
Mm.397328

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000099517
ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265
ENSMUST00000188775; ENSMUSP00000140394; ENSMUSG00000101355
ENSMUST00000189457; ENSMUSP00000139663; ENSMUSG00000101972

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
319152
319153
360198
97908

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:319152
mmu:319153
mmu:360198
mmu:97908

UCSC genome browser

More...
UCSCi
uc007prc.1 mouse

<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
X01684 Genomic DNA Translation: CAA25839.1
M32460 Genomic DNA Translation: AAA37811.1
M32462 Genomic DNA Translation: AAA37813.1
X16496 Genomic DNA Translation: CAA34512.1
U62670 Genomic DNA Translation: AAB04763.1
U62672 Genomic DNA Translation: AAB04765.1
AY158944 Genomic DNA Translation: AAO06254.1
AY158945 Genomic DNA Translation: AAO06255.1
AY158946 Genomic DNA Translation: AAO06256.1
AY158952 Genomic DNA Translation: AAO06262.1
Y12290 Genomic DNA Translation: CAA72968.1
AK006742 mRNA Translation: BAB24722.1
AK018952 mRNA Translation: BAB31493.1
AK155722 mRNA Translation: BAE33402.1
AL590388 Genomic DNA Translation: CAI25837.1
AL589651 Genomic DNA Translation: CAI24113.1
AL589651 Genomic DNA Translation: CAI24105.1
BC107285 mRNA Translation: AAI07286.1
BC107287 mRNA Translation: AAI07288.1
BC115816 mRNA Translation: AAI15817.1
BC116383 mRNA Translation: AAI16384.1
BC125355 mRNA Translation: AAI25356.1
BC125357 mRNA Translation: AAI25358.1
CCDSiCCDS26289.1
CCDS26296.1
CCDS26342.1
CCDS26368.1
PIRiA39525
S06755
RefSeqiNP_038578.2, NM_013550.5
NP_659539.1, NM_145073.2
NP_835513.1, NM_178206.2
NP_835514.1, NM_178207.2
UniGeneiMm.221301
Mm.261657
Mm.377874
Mm.390558
Mm.397328

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GUWNMR-B2-17[»]
1U35X-ray3.00A/E1-136[»]
2V83X-ray2.40D/E2-10[»]
2W5ZX-ray2.20C2-9[»]
2WP1X-ray2.10P/Q15-24[»]
2XL3X-ray2.70D/F2-9[»]
4EZHX-ray2.52C/D25-35[»]
5B1LX-ray2.35A/E1-136[»]
5B1MX-ray2.34A/E1-136[»]
5IX1X-ray2.60P/Q2-16[»]
5IX2X-ray2.90P/Q2-33[»]
ProteinModelPortaliP68433
SMRiP68433
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi237523, 2 interactors
IntActiP68433, 26 interactors
MINTiP68433
STRINGi10090.ENSMUSP00000097295

PTM databases

iPTMnetiP68433
PhosphoSitePlusiP68433

Proteomic databases

EPDiP68433
jPOSTiP68433
MaxQBiP68433
PaxDbiP68433
PRIDEiP68433
TopDownProteomicsiP68433

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000099517
ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265
ENSMUST00000188775; ENSMUSP00000140394; ENSMUSG00000101355
ENSMUST00000189457; ENSMUSP00000139663; ENSMUSG00000101972
GeneIDi319152
319153
360198
97908
KEGGimmu:319152
mmu:319153
mmu:360198
mmu:97908
UCSCiuc007prc.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8350
8354
8355
8357
MGIiMGI:2668828 Hist1h3a
MGI:2145541 Hist1h3g
MGI:2448349 Hist1h3h
MGI:2448350 Hist1h3i

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00940000153149
ENSGT00940000153611
HOVERGENiHBG001172
InParanoidiP68433
KOiK11253
OMAiRRXEASE
OrthoDBi1564596at2759
PhylomeDBiP68433
TreeFamiTF314241

Enzyme and pathway databases

ReactomeiR-MMU-1266695 Interleukin-7 signaling
R-MMU-212300 PRC2 methylates histones and DNA
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-3214815 HDACs deacetylate histones
R-MMU-3214841 PKMTs methylate histone lysines
R-MMU-3214842 HDMs demethylate histones
R-MMU-3214847 HATs acetylate histones
R-MMU-3214858 RMTs methylate histone arginines
R-MMU-3247509 Chromatin modifying enzymes
R-MMU-427359 SIRT1 negatively regulates rRNA expression
R-MMU-427413 NoRC negatively regulates rRNA expression
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5578749 Transcriptional regulation by small RNAs
R-MMU-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-MMU-73728 RNA Polymerase I Promoter Opening
R-MMU-73777 RNA Polymerase I Chain Elongation
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9018519 Estrogen-dependent gene expression
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Zfp106 mouse
EvolutionaryTraceiP68433

Protein Ontology

More...
PROi
PR:P68433

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000069265 Expressed in 15 organ(s), highest expression level in testis
GenevisibleiP68433 MM

Family and domain databases

Gene3Di1.10.20.10, 1 hit
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...

<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 nameiH31_MOUSE
<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: P68433
Secondary accession number(s): P02295
, P02296, P16106, Q05A97, Q3B7Z8, Q3B7Z9, Q5T009
<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: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 157 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 programChordata 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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