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UniProtKB - P84243 (H33_HUMAN)

Entry version 164 (10 Apr 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Histone H3.3

Gene

H3F3A

more
Organism
Homo sapiens (Human)
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.3 Publications

Caution

The original paper reporting lysine deamination at Lys-5 by LOXL2 has been retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148). However, this modification was confirmed in a subsequent publication (PubMed:27735137).2 Publications1 Publication

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-212300 PRC2 methylates histones and DNA
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-427359 SIRT1 negatively regulates rRNA expression
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5334118 DNA methylation
R-HSA-5578749 Transcriptional regulation by small RNAs
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-HSA-73728 RNA Polymerase I Promoter Opening
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

SIGNOR Signaling Network Open Resource

More...SIGNORi		P84243

<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:H3F3A
Synonyms:H3.3A, H3F3
ORF Names:PP781
AND
Name:H3F3B
Synonyms:H3.3B
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000132475.8
HostDB:ENSG00000163041.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:4764 H3F3A
HGNC:4765 H3F3B

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601058 gene
601128 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P84243

<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 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Glioma (GLM)3 Publications
The gene represented in this entry is involved in disease pathogenesis. H3F3A mutations affecting residues involved in post-translational modifications of histone H3.3 are recurrent in malignant, aggressive gliomas including glioblastoma multiforme (GBM) and diffuse intrinsic pontine glioma (DIPG) (PubMed:22286061, PubMed:22286216). The mechanism through which mutations lead to tumorigenesis involves altered histones methylation, impaired regulation of Polycomb repressive complex 2 (PRC2) activity, and aberrant epigenetic regulation of gene expression (PubMed:23539269, PubMed:23539183, PubMed:23603901).5 Publications
Disease descriptionGliomas are benign or malignant central nervous system neoplasms derived from glial cells. They comprise astrocytomas and glioblastoma multiforme that are derived from astrocytes, oligodendrogliomas derived from oligodendrocytes and ependymomas derived from ependymocytes.
See also OMIM:137800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_07902128K → M in GLM; glioblastoma multiforme samples and diffuse intrinsic pontine glioma; somatic mutation; more prevalent in pediatric than adult malignancies; results in reduced allosteric activation of PRC2 causing a global decrease of H3K27me3 levels; has no effect on H3K4me3 or H3K36me3 levels. 3 PublicationsCorresponds to variant dbSNP:rs1057519903EnsemblClinVar.1
Natural variantiVAR_07902235G → R in GLM; glioblastoma multiforme samples; somatic mutation; also found in osteosarcoma samples; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. 2 Publications1
Natural variantiVAR_07902335G → V in GLM; glioblastoma multiforme samples; somatic mutation; affects regulation of gene expression and results in up-regulation of MYCN; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. 3 Publications1
H3F3A and H3F3B mutations affecting residues involved in post-translational modifications of histone H3.3 are implicated in the pathogenesis of some bone and cartilage neoplasms. Mutations have been found with high prevalence in chondroblastoma and giant cell tumors of bone, and with low frequency in osteosarcoma, conventional chondrosarcoma and clear cell chondrosarcoma. Chondroblastoma samples frequently carry a H3F3B mutation affecting residue Lys-37 (H3K36), although H3F3A is mutated in some cases. Most giant cell tumors of bone harbor H3F3A mutations affecting residue Gly-35 (H3G34).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi43R → K: Reduced binding of histone H1 to histone H3.3-containing nucleosomes. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		3020
3021

MalaCards human disease database

More...MalaCardsi		H3F3A
MIMi137800 phenotype

Open Targets

More...OpenTargetsi		ENSG00000132475
ENSG00000163041

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29140

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		H3F3A

Domain mapping of disease mutations (DMDM)

More...DMDMi		55977062

<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_00002212472 – 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; alternate3 Publications1
Modified residuei3Citrulline; alternate1 Publication1
Modified residuei4Phosphothreonine; by HASPIN2 Publications1
Modified residuei5Allysine; alternate1 Publication1
Modified residuei5N6,N6,N6-trimethyllysine; alternate4 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate4 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; alternate4 Publications1
Modified residuei7Phosphothreonine; by PKC1 Publication1
Modified residuei9Citrulline; alternate2 Publications1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei10N6,N6,N6-trimethyllysine; alternate6 Publications1
Modified residuei10N6,N6-dimethyllysine; alternate6 Publications1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-acetyllysine; alternate5 Publications1
Modified residuei10N6-butyryllysine; alternate1 Publication1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate6 Publications1
Modified residuei11ADP-ribosylserine; alternate2 Publications1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications1
Modified residuei12Phosphothreonine; by PKC2 Publications1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate5 Publications1
Modified residuei15N6-succinyllysine; alternate1 Publication1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternate3 Publications1
Modified residuei18Citrulline; alternate3 Publications1
Modified residuei19N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei19N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei19N6-acetyllysine; alternate2 Publications1
Modified residuei19N6-butyryllysine; alternate1 Publication1
Modified residuei19N6-crotonyllysine; alternate1 Publication1
Modified residuei19N6-methyllysine; alternate2 Publications1
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; alternate4 Publications1
Modified residuei28N6,N6-dimethyllysine; alternateCombined sources4 Publications1
Modified residuei28N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei28N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei28N6-acetyllysine; alternateCombined sources2 Publications1
Modified residuei28N6-crotonyllysine; alternate1 Publication1
Modified residuei28N6-methyllysine; alternate4 Publications1
Modified residuei29ADP-ribosylserine; alternate2 Publications1
Modified residuei29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA56 Publications1
Modified residuei32Phosphoserine2 Publications1
Modified residuei37N6,N6,N6-trimethyllysine; alternate4 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate4 Publications1
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei37N6-acetyllysine; alternate2 Publications1
Modified residuei37N6-methyllysine; alternate4 Publications1
Modified residuei38N6-methyllysineBy similarity1
Modified residuei42Phosphotyrosine1 Publication1
Modified residuei57N6,N6,N6-trimethyllysine; alternate2 Publications1
Modified residuei57N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei57N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei57N6-acetyllysine; alternate1 Publication1
Modified residuei57N6-crotonyllysine; alternate1 Publication1
Modified residuei57N6-methyllysine; by EHMT2; alternate2 Publications1
Modified residuei57N6-succinyllysine; alternate1 Publication1
Modified residuei58Phosphoserine1 Publication1
Modified residuei65N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei65N6-methyllysine; alternate2 Publications1
Modified residuei80N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei80N6,N6-dimethyllysine; alternate3 Publications1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei80N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei80N6-acetyllysine; alternate1 Publication1
Modified residuei80N6-methyllysine; alternate3 Publications1
Modified residuei80N6-succinyllysine; alternate2 Publications1
Modified residuei81Phosphothreonine1 Publication1
Modified residuei87PhosphoserineCombined sources1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysine1 Publication1
Modified residuei123N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei123N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei123N6-acetyllysine; alternate2 Publications1
Modified residuei123N6-methyllysine; alternate2 Publications1
Modified residuei123N6-succinyllysine; alternate1 Publication1

<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.11 Publications
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.4 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.10 Publications
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.15 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.17 Publications
Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination (By similarity).By similarity
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.1 Publication
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.By similarity
Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes (PubMed:29211711). It gives a specific tag for epigenetic transcription activation (PubMed:29211711).1 Publication
Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802). Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac) (PubMed:30257210).2 Publications

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P84243

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P84243

MaxQB - The MaxQuant DataBase

More...MaxQBi		P84243

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

More...PaxDbi		P84243

PeptideAtlas

More...PeptideAtlasi		P84243

PRoteomics IDEntifications database

More...PRIDEi		P84243

ProteomicsDB human proteome resource

More...ProteomicsDBi		57757

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P84243

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P84243

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

More...PhosphoSitePlusi		P84243

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P84243

<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.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000132475 Expressed in 238 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P84243 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P84243 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB011481
CAB037166
CAB037178
CAB037187
CAB037221
HPA042570

<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).2 Publications

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 ZMYND111 Publication1

<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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		109272, 138 interactors
109273, 30 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P84243

Database of interacting proteins

More...DIPi		DIP-40046N

Protein interaction database and analysis system

More...IntActi		P84243, 61 interactors

Molecular INTeraction database

More...MINTi		P84243

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000355778

<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

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L43NMR-A2-13[»]
3ASKX-ray2.90P/Q/R2-14[»]
3ASLX-ray1.41B2-12[»]
3AV2X-ray2.80A/E1-136[»]
3JVKX-ray1.80C13-20[»]
3MUKX-ray1.75D22-29[»]
3MULX-ray1.65D13-20[»]
3QL9X-ray0.93C2-16[»]
3QLAX-ray1.60C/F2-16[»]
3QLCX-ray2.50C/D2-16[»]
3WTPX-ray2.67E1-136[»]
4GNEX-ray1.47B2-8[»]
4GNFX-ray1.55C2-16[»]
4GNGX-ray1.73B/F2-16[»]
4GU0X-ray3.10E/F2-27[»]
4GURX-ray2.51C2-22[»]
4GUSX-ray2.23C2-22[»]
4GY5X-ray2.96E/F2-18[»]
4H9NX-ray1.95A2-136[»]
4H9OX-ray2.05A2-136[»]
4H9PX-ray2.20A2-136[»]
4H9QX-ray1.95A2-136[»]
4H9RX-ray2.20A2-136[»]
4H9SX-ray2.60A/B2-136[»]
4HGAX-ray2.80B1-136[»]
4L58X-ray1.48B2-13[»]
4N4IX-ray2.00B20-43[»]
4O62X-ray1.78D2-12[»]
4QQ4X-ray1.75C/D2-16[»]
4TMPX-ray2.30B/D2-12[»]
4U7TX-ray2.90F/G2-13[»]
4W5AX-ray2.60C/D/F2-16[»]
5B32X-ray2.35A/E1-136[»]
5B33X-ray2.92A/E1-136[»]
5BNVX-ray2.79A/D58-136[»]
5BNXX-ray2.31A58-136[»]
5DWQX-ray2.36F/G14-31[»]
5DX0X-ray2.05F/G/H/I14-31[»]
5JA4X-ray2.42A58-136[»]
5JJYX-ray2.05B30-43[»]
5JLBX-ray1.50B30-43[»]
5KDMX-ray3.50A2-136[»]
5X7XX-ray2.18A/E1-136[»]
6A5Lelectron microscopy5.60a/e1-136[»]
6A5Oelectron microscopy9.90a/e1-136[»]
6A5Pelectron microscopy7.00a/e1-136[»]
6A5Relectron microscopy8.70a/e1-136[»]
6A5Telectron microscopy6.70a/e1-136[»]
6A5Uelectron microscopy7.60a/e1-136[»]
6A5Velectron microscopy6.90a/e1-136[»]
6HBONMR-B2-10[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P84243

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

More...SMRi		P84243

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P84243

<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.1 Publication

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

Belongs to the histone H3 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1745 Eukaryota
COG2036 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182954

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG001172

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P84243

KEGG Orthology (KO)

More...KOi		K11253

Identification of Orthologs from Complete Genome Data

More...OMAi		RIEPEYR

Database of Orthologous Groups

More...OrthoDBi		1564596at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P84243

TreeFam database of animal gene trees

More...TreeFami		TF314241

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.20.10, 1 hit

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_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>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 5 potential isoforms that are computationally mapped.Show allAlign All

P84243-1 [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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EMV3K7EMV3_HUMAN
Histone H3
H3F3B
92Annotation 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>
K7EK07K7EK07_HUMAN
Histone H3
H3F3B
132Annotation 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>
B4DEB1B4DEB1_HUMAN
Histone H3
H3F3A
123Annotation 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>
K7ES00K7ES00_HUMAN
Histone H3.3
H3F3B
151Annotation score:

Annotation score:1 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>
K7EP01K7EP01_HUMAN
Histone H3.3
H3F3B
113Annotation score:

Annotation score:1 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 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 conflicti9R → L in AAH81561 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07902128K → M in GLM; glioblastoma multiforme samples and diffuse intrinsic pontine glioma; somatic mutation; more prevalent in pediatric than adult malignancies; results in reduced allosteric activation of PRC2 causing a global decrease of H3K27me3 levels; has no effect on H3K4me3 or H3K36me3 levels. 3 PublicationsCorresponds to variant dbSNP:rs1057519903EnsemblClinVar.1
Natural variantiVAR_07902235G → R in GLM; glioblastoma multiforme samples; somatic mutation; also found in osteosarcoma samples; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. 2 Publications1
Natural variantiVAR_07902335G → V in GLM; glioblastoma multiforme samples; somatic mutation; affects regulation of gene expression and results in up-regulation of MYCN; results in global decrease of H3K36me2 and H3K36me3 levels; has no effect on H3K27me3 levels. 3 Publications1
Natural variantiVAR_07902435G → W Probable disease-associated mutation found in giant cell tumors of bone; somatic mutation. 1 Publication1
Natural variantiVAR_07902537K → M Probable disease-associated mutation found in chondroblastoma and clear cell chondrosarcoma; somatic mutation; also found in a subset of human papillomavirus-negative head and neck squamous cell carcinomas; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels. 3 Publications1

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
M11354 mRNA Translation: AAA52653.1
M11353 mRNA Translation: AAA52654.1
Z48950 Genomic DNA Translation: CAA88778.1
X05855, X05856, X05857 Genomic DNA Translation: CAA29288.1 Sequence problems.
AF218029 mRNA Translation: AAG17271.1
BX537379 mRNA Translation: CAD97621.1
AL512343 Genomic DNA No translation available.
BC001124 mRNA Translation: AAH01124.1
BC006497 mRNA Translation: AAH06497.1
BC012813 mRNA Translation: AAH12813.1
BC017558 mRNA Translation: AAH17558.1
BC029405 mRNA Translation: AAH29405.1
BC038989 mRNA Translation: AAH38989.1
BC066901 mRNA No translation available.
BC067757 mRNA No translation available.
BC081560 mRNA Translation: AAH81560.1
BC081561 mRNA Translation: AAH81561.1
BC095447 mRNA Translation: AAH95447.1
BC108701 mRNA Translation: AAI08702.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11729.1
CCDS1550.1

Protein sequence database of the Protein Information Resource

More...PIRi		A27501 HSHU33

NCBI Reference Sequences

More...RefSeqi		NP_002098.1, NM_002107.4
NP_005315.1, NM_005324.4

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.180877
Hs.533624
Hs.726012

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000254810; ENSP00000254810; ENSG00000132475
ENST00000366813; ENSP00000355778; ENSG00000163041
ENST00000366815; ENSP00000355780; ENSG00000163041
ENST00000366816; ENSP00000355781; ENSG00000163041
ENST00000586607; ENSP00000466020; ENSG00000132475
ENST00000587560; ENSP00000468714; ENSG00000132475
ENST00000589599; ENSP00000465813; ENSG00000132475

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3020
3021

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3020
hsa:3021

UCSC genome browser

More...UCSCi		uc001hpw.4 human

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Histone H3 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11354 mRNA Translation: AAA52653.1
M11353 mRNA Translation: AAA52654.1
Z48950 Genomic DNA Translation: CAA88778.1
X05855, X05856, X05857 Genomic DNA Translation: CAA29288.1 Sequence problems.
AF218029 mRNA Translation: AAG17271.1
BX537379 mRNA Translation: CAD97621.1
AL512343 Genomic DNA No translation available.
BC001124 mRNA Translation: AAH01124.1
BC006497 mRNA Translation: AAH06497.1
BC012813 mRNA Translation: AAH12813.1
BC017558 mRNA Translation: AAH17558.1
BC029405 mRNA Translation: AAH29405.1
BC038989 mRNA Translation: AAH38989.1
BC066901 mRNA No translation available.
BC067757 mRNA No translation available.
BC081560 mRNA Translation: AAH81560.1
BC081561 mRNA Translation: AAH81561.1
BC095447 mRNA Translation: AAH95447.1
BC108701 mRNA Translation: AAI08702.1
CCDSiCCDS11729.1
CCDS1550.1
PIRiA27501 HSHU33
RefSeqiNP_002098.1, NM_002107.4
NP_005315.1, NM_005324.4
UniGeneiHs.180877
Hs.533624
Hs.726012

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L43NMR-A2-13[»]
3ASKX-ray2.90P/Q/R2-14[»]
3ASLX-ray1.41B2-12[»]
3AV2X-ray2.80A/E1-136[»]
3JVKX-ray1.80C13-20[»]
3MUKX-ray1.75D22-29[»]
3MULX-ray1.65D13-20[»]
3QL9X-ray0.93C2-16[»]
3QLAX-ray1.60C/F2-16[»]
3QLCX-ray2.50C/D2-16[»]
3WTPX-ray2.67E1-136[»]
4GNEX-ray1.47B2-8[»]
4GNFX-ray1.55C2-16[»]
4GNGX-ray1.73B/F2-16[»]
4GU0X-ray3.10E/F2-27[»]
4GURX-ray2.51C2-22[»]
4GUSX-ray2.23C2-22[»]
4GY5X-ray2.96E/F2-18[»]
4H9NX-ray1.95A2-136[»]
4H9OX-ray2.05A2-136[»]
4H9PX-ray2.20A2-136[»]
4H9QX-ray1.95A2-136[»]
4H9RX-ray2.20A2-136[»]
4H9SX-ray2.60A/B2-136[»]
4HGAX-ray2.80B1-136[»]
4L58X-ray1.48B2-13[»]
4N4IX-ray2.00B20-43[»]
4O62X-ray1.78D2-12[»]
4QQ4X-ray1.75C/D2-16[»]
4TMPX-ray2.30B/D2-12[»]
4U7TX-ray2.90F/G2-13[»]
4W5AX-ray2.60C/D/F2-16[»]
5B32X-ray2.35A/E1-136[»]
5B33X-ray2.92A/E1-136[»]
5BNVX-ray2.79A/D58-136[»]
5BNXX-ray2.31A58-136[»]
5DWQX-ray2.36F/G14-31[»]
5DX0X-ray2.05F/G/H/I14-31[»]
5JA4X-ray2.42A58-136[»]
5JJYX-ray2.05B30-43[»]
5JLBX-ray1.50B30-43[»]
5KDMX-ray3.50A2-136[»]
5X7XX-ray2.18A/E1-136[»]
6A5Lelectron microscopy5.60a/e1-136[»]
6A5Oelectron microscopy9.90a/e1-136[»]
6A5Pelectron microscopy7.00a/e1-136[»]
6A5Relectron microscopy8.70a/e1-136[»]
6A5Telectron microscopy6.70a/e1-136[»]
6A5Uelectron microscopy7.60a/e1-136[»]
6A5Velectron microscopy6.90a/e1-136[»]
6HBONMR-B2-10[»]
ProteinModelPortaliP84243
SMRiP84243
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109272, 138 interactors
109273, 30 interactors
CORUMiP84243
DIPiDIP-40046N
IntActiP84243, 61 interactors
MINTiP84243
STRINGi9606.ENSP00000355778

PTM databases

iPTMnetiP84243
PhosphoSitePlusiP84243
SwissPalmiP84243

Polymorphism and mutation databases

BioMutaiH3F3A
DMDMi55977062

Proteomic databases

EPDiP84243
jPOSTiP84243
MaxQBiP84243
PaxDbiP84243
PeptideAtlasiP84243
PRIDEiP84243
ProteomicsDBi57757
TopDownProteomicsiP84243

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		3020
3021
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254810; ENSP00000254810; ENSG00000132475
ENST00000366813; ENSP00000355778; ENSG00000163041
ENST00000366815; ENSP00000355780; ENSG00000163041
ENST00000366816; ENSP00000355781; ENSG00000163041
ENST00000586607; ENSP00000466020; ENSG00000132475
ENST00000587560; ENSP00000468714; ENSG00000132475
ENST00000589599; ENSP00000465813; ENSG00000132475
GeneIDi3020
3021
KEGGihsa:3020
hsa:3021
UCSCiuc001hpw.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3020
3021
DisGeNETi3020
3021
EuPathDBiHostDB:ENSG00000132475.8
HostDB:ENSG00000163041.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		H3F3A
H3F3B

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0135637
HGNCiHGNC:4764 H3F3A
HGNC:4765 H3F3B
HPAiCAB011481
CAB037166
CAB037178
CAB037187
CAB037221
HPA042570
MalaCardsiH3F3A
MIMi137800 phenotype
601058 gene
601128 gene
neXtProtiNX_P84243
OpenTargetsiENSG00000132475
ENSG00000163041
PharmGKBiPA29140

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00950000182954
HOVERGENiHBG001172
InParanoidiP84243
KOiK11253
OMAiRIEPEYR
OrthoDBi1564596at2759
PhylomeDBiP84243
TreeFamiTF314241

Enzyme and pathway databases

ReactomeiR-HSA-1912408 Pre-NOTCH Transcription and Translation
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-212300 PRC2 methylates histones and DNA
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-HSA-427359 SIRT1 negatively regulates rRNA expression
R-HSA-427389 ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression
R-HSA-427413 NoRC negatively regulates rRNA expression
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5334118 DNA methylation
R-HSA-5578749 Transcriptional regulation by small RNAs
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
R-HSA-73728 RNA Polymerase I Promoter Opening
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SIGNORiP84243

Miscellaneous databases

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

More...ChiTaRSi		H3F3B human
EvolutionaryTraceiP84243

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		H3F3A

Protein Ontology

More...PROi		PR:P84243

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000132475 Expressed in 238 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiP84243 baseline and differential
GenevisibleiP84243 HS

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 nameiH33_HUMAN
<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: P84243
Secondary accession number(s): P06351
, P33155, Q5VV55, Q5VV56, Q66I33, 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: April 10, 2019
This is version 164 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  6. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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