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Entry version 154 (13 Nov 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Histone H3.3

Gene

H3-3a

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

Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.By similarity

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

GO - Biological processi

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

Molecular functionDNA-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-212300 PRC2 methylates histones and DNA
R-MMU-2299718 Condensation of Prophase Chromosomes
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
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-73772 RNA Polymerase I Promoter Escape
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 H3.3
<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:H3-3aBy similarity
Synonyms:H3.3a, H3f3aImported
AND
Name:H3-3bBy similarity
Synonyms:H3.3b, H3f3bImported
<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> Componentsi: Chromosome 1, Chromosome 11

Organism-specific databases

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

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MGIi
MGI:1097686 H3f3a
MGI:1101768 H3f3b

<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 & Seán O’Donoghue; 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 <a href="http://www.uniprot.org/help/ptm_processing_section">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 methionineiRemovedCurated
<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_00002212512 – 136Histone H3.3Add 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 residuei3Asymmetric dimethylarginine; by PRMT6; alternateBy similarity1
Modified residuei3Citrulline; alternateBy similarity1
Modified residuei4Phosphothreonine; by HASPIN1 Publication1
Modified residuei5Allysine; alternateBy similarity1
Modified residuei5N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei5N6,N6-dimethyllysine; alternate1 Publication1
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; alternate1 Publication1
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 PKCBy similarity1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate3 Publications1
Modified residuei15N6-glutaryllysine; alternateBy similarity1
Modified residuei15N6-succinyllysine; alternateBy similarity1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternate3 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-glutaryllysine; alternateBy similarity1
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-glutaryllysine; alternateBy similarity1
Modified residuei24N6-methyllysine; alternate1 Publication1
Modified residuei27CitrullineBy similarity1
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-glutaryllysine; alternateBy similarity1
Modified residuei28N6-methyllysine; alternate2 Publications1
Modified residuei29ADP-ribosylserine; alternateBy similarity1
Modified residuei29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA56 Publications1
Modified residuei32PhosphoserineBy similarity1
Modified residuei37N6,N6,N6-trimethyllysine; alternateBy similarity1
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-glutaryllysine; alternateBy similarity1
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-glutaryllysine; alternateBy similarity1
Modified residuei80N6-methyllysine; alternate2 Publications1
Modified residuei80N6-succinyllysine; alternate1 Publication1
Modified residuei81PhosphothreonineBy similarity1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysine; alternateBy similarity1
Modified residuei116N6-glutaryllysine; alternateBy similarity1
Modified residuei123N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei123N6-acetyllysine; alternateBy similarity1
Modified residuei123N6-butyryllysine; alternate1 Publication1
Modified residuei123N6-glutaryllysine; alternateBy similarity1
Modified residuei123N6-methyllysine; alternate1 Publication1
Modified residuei123N6-succinyllysine; alternateBy similarity1

<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.6 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.5 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
Specifically enriched in modifications associated with active chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-80. 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), which are linked to gene repression, are underrepresented. 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.9 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 Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin. Phosphorylation on Ser-32 (H3S31ph) is specific to regions bordering centromeres in metaphase chromosomes. metaphase chromosomes.10 Publications
Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination.1 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
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
P84244

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P84244

MaxQB - The MaxQuant DataBase

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MaxQBi
P84244

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

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PaxDbi
P84244

PeptideAtlas

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PeptideAtlasi
P84244

PRoteomics IDEntifications database

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PRIDEi
P84244

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P84244

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

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PhosphoSitePlusi
P84244

SwissPalm database of S-palmitoylation events

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SwissPalmi
P84244

<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 throughout the cell cycle independently of DNA synthesis.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000016559 Expressed in 293 organ(s), highest expression level in female gonad

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P84244 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P84244 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.

Interacts with HIRA, a chaperone required for its incorporation into nucleosomes.

Interacts with ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3).

By similarity

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>Sitei32Interaction with ZMYND11By similarity1

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
200196, 26 interactors
200199, 4 interactors

Database of interacting proteins

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DIPi
DIP-35190N

Protein interaction database and analysis system

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IntActi
P84244, 40 interactors

Molecular INTeraction database

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MINTi
P84244

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000124509

<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

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SMRi
P84244

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

<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

Specific interaction of trimethylated form at 'Lys-36' (H3.3K36me3) with ZMYND11 is mediated by the encapsulation of Ser-32 residue with a composite pocket formed by the tandem bromo-PWWP domains (By similarity). Interacts with ZMYND11; when trimethylated at 'Lys-36' (H3.3K36me3).By similarity

<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
ENSGT00950000182954

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P84244

KEGG Orthology (KO)

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KOi
K11253

Identification of Orthologs from Complete Genome Data

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OMAi
CTMARTK

Database of Orthologous Groups

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OrthoDBi
1564596at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P84244

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>. 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>Sequence (1+)i

<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.

<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 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.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P84244-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,328
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:i5158ED279E6F9E1C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E0CZ27E0CZ27_MOUSE
Histone H3
H3f3a
119Annotation score:

Annotation score:2 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>
F8WI35F8WI35_MOUSE
Histone H3
H3f3a
135Annotation score:

Annotation score:2 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>
E0CYN1E0CYN1_MOUSE
H3.3 histone A
H3f3a
52Annotation score:

Annotation score:2 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>
E0CYR7E0CYR7_MOUSE
H3.3 histone A
H3f3a
55Annotation score:

Annotation score:2 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH92300 differs from that shown. Reason: Frameshift.Curated
The sequence BAB27616 differs from that shown. Reason: Frameshift.Curated
The sequence BAE35387 differs from that shown. Reason: Frameshift.Curated

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 conflicti75I → T in AAH21768 (PubMed:15489334).Curated1
Sequence conflicti99A → E in BAE31789 (PubMed:16141072).Curated1
Sequence conflicti99A → E in BAE30411 (PubMed:16141072).Curated1
Sequence conflicti129R → C in X91866 (PubMed:9174168).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
X13605 mRNA Translation: CAA31940.1
Z85979 mRNA Translation: CAB06625.1
X91866 mRNA No translation available.
AK002928 mRNA Translation: BAB22464.1
AK011431 mRNA Translation: BAB27616.1 Frameshift.
AK037900 mRNA Translation: BAC29895.1
AK088075 mRNA Translation: BAC40130.1
AK135839 mRNA Translation: BAE22687.1
AK150467 mRNA Translation: BAE29584.1
AK150468 mRNA Translation: BAE29585.1
AK150591 mRNA Translation: BAE29685.1
AK150928 mRNA Translation: BAE29966.1
AK151274 mRNA Translation: BAE30261.1
AK151336 mRNA Translation: BAE30314.1
AK151451 mRNA Translation: BAE30411.1
AK151634 mRNA Translation: BAE30566.1
AK151658 mRNA Translation: BAE30586.1
AK151661 mRNA Translation: BAE30589.1
AK151869 mRNA Translation: BAE30757.1
AK152293 mRNA Translation: BAE31102.1
AK152453 mRNA Translation: BAE31231.1
AK152455 mRNA Translation: BAE31233.1
AK152623 mRNA Translation: BAE31366.1
AK152911 mRNA Translation: BAE31590.1
AK153034 mRNA Translation: BAE31666.1
AK153189 mRNA Translation: BAE31789.1
AK153239 mRNA Translation: BAE31831.1
AK153294 mRNA Translation: BAE31877.1
AK153371 mRNA Translation: BAE31939.1
AK153530 mRNA Translation: BAE32069.1
AK159615 mRNA Translation: BAE35232.1
AK159807 mRNA Translation: BAE35387.1 Frameshift.
AK159850 mRNA Translation: BAE35427.1
AK160677 mRNA Translation: BAE35953.1
AK161675 mRNA Translation: BAE36524.1
AK162040 mRNA Translation: BAE36694.1
AK163244 mRNA Translation: BAE37253.1
AK167828 mRNA Translation: BAE39850.1
AK167879 mRNA Translation: BAE39892.1
AK168197 mRNA Translation: BAE40157.1
AK168698 mRNA Translation: BAE40542.1
AK169042 mRNA Translation: BAE40831.1
AK169226 mRNA Translation: BAE40995.1
BC002268 mRNA Translation: AAH02268.1
BC012687 mRNA Translation: AAH12687.1
BC021768 mRNA Translation: AAH21768.1
BC037730 mRNA Translation: AAH37730.1
BC083353 mRNA Translation: AAH83353.1
BC088835 mRNA Translation: AAH88835.1
BC092043 mRNA Translation: AAH92043.1
BC092300 mRNA Translation: AAH92300.1 Frameshift.
BC106177 mRNA Translation: AAI06178.1
AY383567 Genomic DNA Translation: AAQ96274.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS15573.1
CCDS36377.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S04186

NCBI Reference Sequences

More...
RefSeqi
NP_032236.1, NM_008210.5
NP_032237.1, NM_008211.3
XP_006532311.1, XM_006532248.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000016703; ENSMUSP00000016703; ENSMUSG00000016559
ENSMUST00000106454; ENSMUSP00000102062; ENSMUSG00000016559
ENSMUST00000161308; ENSMUSP00000124509; ENSMUSG00000060743
ENSMUST00000162814; ENSMUSP00000125104; ENSMUSG00000060743

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
15078
15081

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:15078
mmu:15081

UCSC genome browser

More...
UCSCi
uc007dwr.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
X13605 mRNA Translation: CAA31940.1
Z85979 mRNA Translation: CAB06625.1
X91866 mRNA No translation available.
AK002928 mRNA Translation: BAB22464.1
AK011431 mRNA Translation: BAB27616.1 Frameshift.
AK037900 mRNA Translation: BAC29895.1
AK088075 mRNA Translation: BAC40130.1
AK135839 mRNA Translation: BAE22687.1
AK150467 mRNA Translation: BAE29584.1
AK150468 mRNA Translation: BAE29585.1
AK150591 mRNA Translation: BAE29685.1
AK150928 mRNA Translation: BAE29966.1
AK151274 mRNA Translation: BAE30261.1
AK151336 mRNA Translation: BAE30314.1
AK151451 mRNA Translation: BAE30411.1
AK151634 mRNA Translation: BAE30566.1
AK151658 mRNA Translation: BAE30586.1
AK151661 mRNA Translation: BAE30589.1
AK151869 mRNA Translation: BAE30757.1
AK152293 mRNA Translation: BAE31102.1
AK152453 mRNA Translation: BAE31231.1
AK152455 mRNA Translation: BAE31233.1
AK152623 mRNA Translation: BAE31366.1
AK152911 mRNA Translation: BAE31590.1
AK153034 mRNA Translation: BAE31666.1
AK153189 mRNA Translation: BAE31789.1
AK153239 mRNA Translation: BAE31831.1
AK153294 mRNA Translation: BAE31877.1
AK153371 mRNA Translation: BAE31939.1
AK153530 mRNA Translation: BAE32069.1
AK159615 mRNA Translation: BAE35232.1
AK159807 mRNA Translation: BAE35387.1 Frameshift.
AK159850 mRNA Translation: BAE35427.1
AK160677 mRNA Translation: BAE35953.1
AK161675 mRNA Translation: BAE36524.1
AK162040 mRNA Translation: BAE36694.1
AK163244 mRNA Translation: BAE37253.1
AK167828 mRNA Translation: BAE39850.1
AK167879 mRNA Translation: BAE39892.1
AK168197 mRNA Translation: BAE40157.1
AK168698 mRNA Translation: BAE40542.1
AK169042 mRNA Translation: BAE40831.1
AK169226 mRNA Translation: BAE40995.1
BC002268 mRNA Translation: AAH02268.1
BC012687 mRNA Translation: AAH12687.1
BC021768 mRNA Translation: AAH21768.1
BC037730 mRNA Translation: AAH37730.1
BC083353 mRNA Translation: AAH83353.1
BC088835 mRNA Translation: AAH88835.1
BC092043 mRNA Translation: AAH92043.1
BC092300 mRNA Translation: AAH92300.1 Frameshift.
BC106177 mRNA Translation: AAI06178.1
AY383567 Genomic DNA Translation: AAQ96274.1
CCDSiCCDS15573.1
CCDS36377.1
PIRiS04186
RefSeqiNP_032236.1, NM_008210.5
NP_032237.1, NM_008211.3
XP_006532311.1, XM_006532248.2

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
2RVNNMR-B2-18[»]
5XM0X-ray2.87A/E1-136[»]
5XM1X-ray3.45A/E1-136[»]
SMRiP84244
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi200196, 26 interactors
200199, 4 interactors
DIPiDIP-35190N
IntActiP84244, 40 interactors
MINTiP84244
STRINGi10090.ENSMUSP00000124509

PTM databases

iPTMnetiP84244
PhosphoSitePlusiP84244
SwissPalmiP84244

Proteomic databases

EPDiP84244
jPOSTiP84244
MaxQBiP84244
PaxDbiP84244
PeptideAtlasiP84244
PRIDEiP84244

Genome annotation databases

EnsembliENSMUST00000016703; ENSMUSP00000016703; ENSMUSG00000016559
ENSMUST00000106454; ENSMUSP00000102062; ENSMUSG00000016559
ENSMUST00000161308; ENSMUSP00000124509; ENSMUSG00000060743
ENSMUST00000162814; ENSMUSP00000125104; ENSMUSG00000060743
GeneIDi15078
15081
KEGGimmu:15078
mmu:15081
UCSCiuc007dwr.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
15078
15081
MGIiMGI:1097686 H3f3a
MGI:1101768 H3f3b

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00950000182954
InParanoidiP84244
KOiK11253
OMAiCTMARTK
OrthoDBi1564596at2759
PhylomeDBiP84244
TreeFamiTF314241

Enzyme and pathway databases

ReactomeiR-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-212300 PRC2 methylates histones and DNA
R-MMU-2299718 Condensation of Prophase Chromosomes
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
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-73772 RNA Polymerase I Promoter Escape
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
H3f3a mouse
H3f3b mouse

Protein Ontology

More...
PROi
PR:P84244

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000016559 Expressed in 293 organ(s), highest expression level in female gonad
ExpressionAtlasiP84244 baseline and differential
GenevisibleiP84244 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...

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 nameiH33_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: P84244
Secondary accession number(s): P06351
, P33155, Q3TW79, Q3U6D6, Q569U8, Q5HZY8, Q6TXQ5, Q8VDJ2, Q9D0H3, Q9V3W4
<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: January 1, 1988
Last sequence update: January 23, 2007
Last modified: November 13, 2019
This is version 154 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, Reference proteome

Documents

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