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Entry version 174 (03 Jul 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Histone H3.1

Gene

HIST1H3A

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

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

Miscellaneous

This histone is only present in mammals and is enriched in acetylation of Lys-15 and dimethylation of Lys-10 (H3K9me2).

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The original paper reporting lysine deamination at Lys-5 by LOXL2 has been retracted due to inappropriate manipulation of figure data (PubMed:22483618, PubMed:27392148).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

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

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Reactomei
R-HSA-1266695 Interleukin-7 signaling
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-3214815 HDACs deacetylate histones
R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-3214842 HDMs demethylate histones
R-HSA-3214847 HATs acetylate histones
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-3247509 Chromatin modifying enzymes
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-73772 RNA Polymerase I Promoter Escape
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

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SIGNORi
P68431

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone H3.1
Alternative name(s):
Histone H3/a
Histone H3/b
Histone H3/c
Histone H3/d
Histone H3/f
Histone H3/h
Histone H3/i
Histone H3/j
Histone H3/k
Histone H3/l
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HIST1H3A
Synonyms:H3FA
AND
Name:HIST1H3B
Synonyms:H3FL
AND
Name:HIST1H3C
Synonyms:H3FC
AND
Name:HIST1H3D
Synonyms:H3FB
AND
Name:HIST1H3E
Synonyms:H3FD
AND
Name:HIST1H3F
Synonyms:H3FI
AND
Name:HIST1H3G
Synonyms:H3FH
AND
Name:HIST1H3H
Synonyms:H3FK
AND
Name:HIST1H3I
Synonyms:H3FF
AND
Name:HIST1H3J
Synonyms:H3FJ
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:4766 HIST1H3A
HGNC:4776 HIST1H3B
HGNC:4768 HIST1H3C
HGNC:4767 HIST1H3D
HGNC:4769 HIST1H3E
HGNC:4773 HIST1H3F
HGNC:4772 HIST1H3G
HGNC:4775 HIST1H3H
HGNC:4771 HIST1H3I
HGNC:4774 HIST1H3J

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602810 gene
602811 gene
602812 gene
602813 gene
602814 gene
602815 gene
602816 gene
602817 gene
602818 gene
602819 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P68431

<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)1 Publication
The gene represented in this entry is involved in disease pathogenesis. HIST1H3B mutations affecting residue Lys-28 involved in post-translational modifications of histone H3.1 are recurrent in malignant, aggressive gliomas including pediatric non-brain stem glioblastoma and diffuse intrinsic pontine glioma (DIPG) (PubMed:22286216). The mechanism through which mutations lead to tumorigenesis involves altered histone methylation, impaired regulation of Polycomb repressive complex 2 (PRC2) activity, and aberrant epigenetic regulation of gene expression (PubMed:23603901).2 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.
Related information in OMIM
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_07901828K → M in GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels. 2 PublicationsCorresponds to variant dbSNP:rs1057519904EnsemblClinVar.1
HIST1H3B or HIST1H3C mutations affecting residue Lys-37 of histone H3.1 are involved in the pathogenesis of pediatric undifferentiated soft tissue sarcomas. The mechanism through which mutations lead to tumorigenesis involves altered histones methylation with gain of global H3K27 methylation, altered Polycomb repressive complex 1 (PRC1) activity, aberrant epigenetic regulation of gene expression and impaired differentiation of mesenchimal progenitor cells.1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
8350
8351
8352
8353
8354
8355
8356
8357
8358
8968

MalaCards human disease database

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MalaCardsi
HIST1H3A
MIMi137800 phenotype

Open Targets

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OpenTargetsi
ENSG00000197153
ENSG00000197409
ENSG00000273983
ENSG00000274267
ENSG00000274750
ENSG00000275379
ENSG00000275714
ENSG00000277775
ENSG00000278272
ENSG00000278828

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29148

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HIST1H3A

Domain mapping of disease mutations (DMDM)

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DMDMi
55977055

<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 methionineiRemoved1 Publication
<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_00002212452 – 136Histone H3.1Add 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; alternate3 Publications1
Modified residuei5N6,N6-dimethyllysine; alternate3 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; alternate3 Publications1
Modified residuei7Phosphothreonine; by PKC1 Publication1
Modified residuei9Citrulline; alternate2 Publications1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei10N6,N6,N6-trimethyllysine; alternate5 Publications1
Modified residuei10N6,N6-dimethyllysine; alternate5 Publications1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-acetyllysine; alternate6 Publications1
Modified residuei10N6-butyryllysine; alternate1 Publication1
Modified residuei10N6-crotonyllysine; alternate1 Publication1
Modified residuei10N6-methyllysine; alternate5 Publications1
Modified residuei11ADP-ribosylserine; alternate2 Publications1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA56 Publications1
Modified residuei12Phosphothreonine; by PKC and CHEK13 Publications1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei15N6-acetyllysine; alternate6 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; alternate3 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; alternate4 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; alternate4 Publications1
Modified residuei28N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei28N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei28N6-acetyllysine; alternate2 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 residuei37N6,N6,N6-trimethyllysine; alternate5 Publications1
Modified residuei37N6,N6-dimethyllysine; alternate5 Publications1
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei37N6-acetyllysine; alternate2 Publications1
Modified residuei37N6-methyllysine; alternate5 Publications1
Modified residuei38N6-methyllysine1 Publication1
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; alternate4 Publications1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei80N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei80N6-acetyllysine; alternate1 Publication1
Modified residuei80N6-methyllysine; alternate4 Publications1
Modified residuei80N6-succinyllysine; alternate2 Publications1
Modified residuei81Phosphothreonine1 Publication1
Modified residuei87PhosphoserineBy similarity1
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.9 Publications
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication.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 Thr-12 (H3T11ph) by chromatin-associated CHEK1 regulates the transcription of cell cycle regulatory genes by modulating acetylation of Lys-10 (H3K9ac). Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin.17 Publications
Monoubiquitinated by RAG1 in lymphoid cells, monoubiquitination is required for V(D)J recombination (By similarity). Ubiquitinated by the CUL4-DDB-RBX1 complex in response to ultraviolet irradiation. This may weaken the interaction between histones and DNA and facilitate DNA accessibility to repair proteins.By similarity1 Publication
Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression.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:30257210). 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).1 Publication

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P68431

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P68431

MaxQB - The MaxQuant DataBase

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MaxQBi
P68431

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

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PaxDbi
P68431

PeptideAtlas

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PeptideAtlasi
P68431

PRoteomics IDEntifications database

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PRIDEi
P68431

ProteomicsDB human proteome resource

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ProteomicsDBi
57541

Consortium for Top Down Proteomics

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TopDownProteomicsi
P68431

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P68431

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

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PhosphoSitePlusi
P68431

SwissPalm database of S-palmitoylation events

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SwissPalmi
P68431

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000197153 Expressed in 43 organ(s), highest expression level in stomach

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P68431 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB070190
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.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113946, 354 interactors
113947, 8 interactors
113948, 14 interactors
113949, 205 interactors
113950, 8 interactors
113951, 8 interactors
113952, 7 interactors
113953, 10 interactors
113954, 25 interactors
114458, 10 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P68431

Database of interacting proteins

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DIPi
DIP-29371N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P68431

Protein interaction database and analysis system

More...
IntActi
P68431, 434 interactors

Molecular INTeraction database

More...
MINTi
P68431

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000484841

<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
P68431

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P68431

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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

Belongs to the histone H3 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1745 Eukaryota
COG2036 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00960000186578

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P68431

KEGG Orthology (KO)

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KOi
K11253

Identification of Orthologs from Complete Genome Data

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OMAi
ASEAYYL

Database of Orthologous Groups

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OrthoDBi
1564596at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P68431

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<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.

P68431-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY
110 120 130
LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,404
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9B89008EA50A0EF6
GO

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 conflicti70R → C in AAH67493 (PubMed:15489334).Curated1
Sequence conflicti100Y → T in CAB02546 (PubMed:9119399).Curated1
Sequence conflicti122P → L in AAH66884 (PubMed:15489334).Curated1
Sequence conflicti135Missing in AAA52651 (PubMed:3013246).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07901828K → M in GLM; non-brain stem pediatric glioblastoma and diffuse intrinsic pontine glioma; somatic mutation; results in a global decrease of H3K27me3 levels. 2 PublicationsCorresponds to variant dbSNP:rs1057519904EnsemblClinVar.1
Natural variantiVAR_07901937K → I Probable disease-associated mutation found in pediatric undifferentiated soft tissue sarcoma samples; somatic mutation; results in global decrease of H3K36me2 and H3K36me3 levels and increased H3K27me3 levels. 1 Publication1
Natural variantiVAR_07902037K → M Probable disease-associated mutation found in pediatric undifferentiated soft tissue sarcoma samples; 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. 2 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
X00090 Genomic DNA Translation: CAA24952.1
M26150 Genomic DNA Translation: AAA52651.1
M60746 Genomic DNA Translation: AAA63185.1
X57128 Genomic DNA Translation: CAA40407.1
Z46261 Genomic DNA Translation: CAA86403.1
X83550 Genomic DNA Translation: CAA58540.1
Z80784 Genomic DNA Translation: CAB02546.1
Z80785 Genomic DNA Translation: CAB02547.1
Z80786 Genomic DNA Translation: CAB02548.1
Z83735 Genomic DNA Translation: CAB06030.1
Z83737 Genomic DNA Translation: CAB06032.1
AF531274 Genomic DNA Translation: AAN10051.1
AF531275 Genomic DNA Translation: AAN10052.1
AF531276 Genomic DNA Translation: AAN10053.1
AF531277 Genomic DNA Translation: AAN10054.1
AF531278 Genomic DNA Translation: AAN10055.1
AF531279 Genomic DNA Translation: AAN10056.1
AF531280 Genomic DNA Translation: AAN10057.1
AF531281 Genomic DNA Translation: AAN10058.1
AF531282 Genomic DNA Translation: AAN10059.1
AF531283 Genomic DNA Translation: AAN10060.1
AK311991 mRNA Translation: BAG34929.1
AK313905 mRNA Translation: BAG36628.1
AK314142 mRNA Translation: BAG36832.1
AK316611 mRNA Translation: BAG38198.1
CR542014 mRNA Translation: CAG46811.1
CR542011 mRNA Translation: CAG46808.1
CR541983 mRNA Translation: CAG46780.1
CR541858 mRNA Translation: CAG46656.1
Z98744 Genomic DNA No translation available.
AL009179 Genomic DNA No translation available.
AL031777 Genomic DNA No translation available.
BC031333 mRNA Translation: AAH31333.1
BC066245 mRNA Translation: AAH66245.1
BC066246 mRNA Translation: AAH66246.1
BC066247 mRNA Translation: AAH66247.1
BC066884 mRNA Translation: AAH66884.1
BC067490 mRNA Translation: AAH67490.1
BC067491 mRNA Translation: AAH67491.1
BC067492 mRNA Translation: AAH67492.1
BC067493 mRNA Translation: AAH67493.1
BC069133 mRNA Translation: AAH69133.1
BC069303 mRNA Translation: AAH69303.1
BC069305 mRNA Translation: AAH69305.2
BC069818 mRNA Translation: AAH69818.1
BC096128 mRNA Translation: AAH96128.1
BC096129 mRNA Translation: AAH96129.1
BC096130 mRNA Translation: AAH96130.1
BC096131 mRNA Translation: AAH96131.1
BC096132 mRNA Translation: AAH96132.1
BC096133 mRNA Translation: AAH96133.1
BC096134 mRNA Translation: AAH96134.1
BC099630 mRNA Translation: AAH99630.1
BC127610 mRNA Translation: AAI27611.1
BC143046 mRNA Translation: AAI43047.1
BC148243 mRNA Translation: AAI48244.1
BC148250 mRNA Translation: AAI48251.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4570.1
CCDS4573.1
CCDS4576.1
CCDS4590.1
CCDS4596.1
CCDS4600.1
CCDS4602.1
CCDS4627.1
CCDS4636.1
CCDS4638.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I37446 HSHU3

NCBI Reference Sequences

More...
RefSeqi
NP_003520.1, NM_003529.2
NP_003521.2, NM_003530.4
NP_003522.1, NM_003531.2
NP_003523.1, NM_003532.2
NP_003524.1, NM_003533.2
NP_003525.1, NM_003534.2
NP_003526.1, NM_003535.2
NP_003527.1, NM_003536.2
NP_003528.1, NM_003537.3
NP_066298.1, NM_021018.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000356476; ENSP00000366999; ENSG00000197409
ENST00000359303; ENSP00000352252; ENSG00000197153
ENST00000369163; ENSP00000358160; ENSG00000278828
ENST00000612966; ENSP00000484658; ENSG00000278272
ENST00000613854; ENSP00000480826; ENSG00000275714
ENST00000614378; ENSP00000484638; ENSG00000273983
ENST00000614911; ENSP00000482271; ENSG00000274750
ENST00000616365; ENSP00000483283; ENSG00000275379
ENST00000618052; ENSP00000484095; ENSG00000277775
ENST00000621411; ENSP00000484841; ENSG00000274267
ENST00000634733; ENSP00000489282; ENSG00000274750

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8350
8351
8352
8353
8354
8355
8356
8357
8358
8968

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8350
hsa:8351
hsa:8352
hsa:8353
hsa:8354
hsa:8355
hsa:8356
hsa:8357
hsa:8358
hsa:8968

UCSC genome browser

More...
UCSCi
uc003nfp.2 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00090 Genomic DNA Translation: CAA24952.1
M26150 Genomic DNA Translation: AAA52651.1
M60746 Genomic DNA Translation: AAA63185.1
X57128 Genomic DNA Translation: CAA40407.1
Z46261 Genomic DNA Translation: CAA86403.1
X83550 Genomic DNA Translation: CAA58540.1
Z80784 Genomic DNA Translation: CAB02546.1
Z80785 Genomic DNA Translation: CAB02547.1
Z80786 Genomic DNA Translation: CAB02548.1
Z83735 Genomic DNA Translation: CAB06030.1
Z83737 Genomic DNA Translation: CAB06032.1
AF531274 Genomic DNA Translation: AAN10051.1
AF531275 Genomic DNA Translation: AAN10052.1
AF531276 Genomic DNA Translation: AAN10053.1
AF531277 Genomic DNA Translation: AAN10054.1
AF531278 Genomic DNA Translation: AAN10055.1
AF531279 Genomic DNA Translation: AAN10056.1
AF531280 Genomic DNA Translation: AAN10057.1
AF531281 Genomic DNA Translation: AAN10058.1
AF531282 Genomic DNA Translation: AAN10059.1
AF531283 Genomic DNA Translation: AAN10060.1
AK311991 mRNA Translation: BAG34929.1
AK313905 mRNA Translation: BAG36628.1
AK314142 mRNA Translation: BAG36832.1
AK316611 mRNA Translation: BAG38198.1
CR542014 mRNA Translation: CAG46811.1
CR542011 mRNA Translation: CAG46808.1
CR541983 mRNA Translation: CAG46780.1
CR541858 mRNA Translation: CAG46656.1
Z98744 Genomic DNA No translation available.
AL009179 Genomic DNA No translation available.
AL031777 Genomic DNA No translation available.
BC031333 mRNA Translation: AAH31333.1
BC066245 mRNA Translation: AAH66245.1
BC066246 mRNA Translation: AAH66246.1
BC066247 mRNA Translation: AAH66247.1
BC066884 mRNA Translation: AAH66884.1
BC067490 mRNA Translation: AAH67490.1
BC067491 mRNA Translation: AAH67491.1
BC067492 mRNA Translation: AAH67492.1
BC067493 mRNA Translation: AAH67493.1
BC069133 mRNA Translation: AAH69133.1
BC069303 mRNA Translation: AAH69303.1
BC069305 mRNA Translation: AAH69305.2
BC069818 mRNA Translation: AAH69818.1
BC096128 mRNA Translation: AAH96128.1
BC096129 mRNA Translation: AAH96129.1
BC096130 mRNA Translation: AAH96130.1
BC096131 mRNA Translation: AAH96131.1
BC096132 mRNA Translation: AAH96132.1
BC096133 mRNA Translation: AAH96133.1
BC096134 mRNA Translation: AAH96134.1
BC099630 mRNA Translation: AAH99630.1
BC127610 mRNA Translation: AAI27611.1
BC143046 mRNA Translation: AAI43047.1
BC148243 mRNA Translation: AAI48244.1
BC148250 mRNA Translation: AAI48251.1
CCDSiCCDS4570.1
CCDS4573.1
CCDS4576.1
CCDS4590.1
CCDS4596.1
CCDS4600.1
CCDS4602.1
CCDS4627.1
CCDS4636.1
CCDS4638.1
PIRiI37446 HSHU3
RefSeqiNP_003520.1, NM_003529.2
NP_003521.2, NM_003530.4
NP_003522.1, NM_003531.2
NP_003523.1, NM_003532.2
NP_003524.1, NM_003533.2
NP_003525.1, NM_003534.2
NP_003526.1, NM_003535.2
NP_003527.1, NM_003536.2
NP_003528.1, NM_003537.3
NP_066298.1, NM_021018.2

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
1CS9NMR-A131-136[»]
1CT6NMR-A131-136[»]
1O9SX-ray1.75K/L2-10[»]
1Q3LX-ray1.64P2-16[»]
2B2TX-ray2.45D2-20[»]
2B2UX-ray2.95D2-16[»]
2B2VX-ray2.65D2-16[»]
2B2WX-ray2.40D2-20[»]
2C1JX-ray2.60C/D8-15[»]
2C1NX-ray2.00C/E8-15[»]
2CO0X-ray2.25B/D2-16[»]
2CV5X-ray2.50A/E1-136[»]
2KWJNMR-B2-21[»]
2KWKNMR-B2-21[»]
2L75NMR-B2-14[»]
2LBMNMR-C2-16[»]
2M0ONMR-B32-42[»]
2NDFNMR-B13-25[»]
2NDGNMR-B13-25[»]
2OQ6X-ray2.00C/D8-15[»]
2OT7X-ray2.14C/D8-15[»]
2OX0X-ray1.95C/D8-15[»]
2RI7X-ray1.45P2-10[»]
2UXNX-ray2.72E2-22[»]
2V85X-ray2.00D/E2-13[»]
2V89X-ray1.10D/E2-10[»]
2VNFX-ray1.76B/D2-11[»]
2VPGX-ray1.60P/R2-19[»]
2X0LX-ray3.00C6-17[»]
3A1BX-ray2.29A2-21[»]
3AFAX-ray2.50A/E1-136[»]
3AVRX-ray1.80B18-39[»]
3AYWX-ray2.90A/E1-136[»]
3AZEX-ray3.00A/E1-136[»]
3AZFX-ray2.70A/E1-136[»]
3AZGX-ray2.40A/E1-136[»]
3AZHX-ray3.49A/E1-136[»]
3AZIX-ray2.70A/E1-136[»]
3AZJX-ray2.89A/E1-136[»]
3AZKX-ray3.20A/E1-136[»]
3AZLX-ray2.70A/E1-136[»]
3AZMX-ray2.89A/E1-136[»]
3AZNX-ray3.00A/E1-136[»]
3B95X-ray2.99P2-16[»]
3KMTX-ray1.78G/H/I26-33[»]
3KQIX-ray1.78B2-13[»]
3LQIX-ray1.92R/S/T2-10[»]
3LQJX-ray1.90Q/T2-10[»]
3MP1X-ray2.60P2-6[»]
3O34X-ray1.90B14-33[»]
3O35X-ray1.76D/E24-32[»]
3O37X-ray2.00E/F/G/H2-11[»]
3QJ6X-ray2.30T74-84[»]
3RIGX-ray2.00C/D5-16[»]
3RIYX-ray1.55C/D5-16[»]
3SOUX-ray1.80D/E2-10[»]
3SOWX-ray1.95C/D2-10[»]
3U31X-ray2.20B5-14[»]
3U3DX-ray2.40B5-14[»]
3U4SX-ray2.15C/D8-15[»]
3U5NX-ray1.95C/D2-21[»]
3U5OX-ray2.70I/J/K/L/M/N/O/P2-23[»]
3U5PX-ray2.80I/J/K/L/M/N/O/P2-29[»]
3UEEX-ray2.61B/D2-13[»]
3UEFX-ray2.45B/D2-13[»]
3UIGX-ray2.40P/Q2-16[»]
3UIIX-ray2.60P/Q2-11[»]
3UIKX-ray2.70P/Q2-11[»]
3V43X-ray1.47Q2-19[»]
3W96X-ray3.00A/E1-136[»]
3W97X-ray3.20A/E1-136[»]
3W98X-ray3.42A/E29-136[»]
3W99X-ray3.00A/E1-136[»]
3WA9X-ray3.07A/E1-136[»]
3WAAX-ray3.20A/E1-136[»]
3WKJX-ray2.80A/E1-136[»]
3X1SX-ray2.81A/E2-136[»]
3X1TX-ray2.81A/E2-136[»]
3X1UX-ray3.25A/E2-136[»]
3X1VX-ray2.92A/E2-136[»]
3ZG6X-ray2.20F5-14[»]
3ZVYX-ray1.95C/D2-9[»]
4A0JX-ray2.80C/D2-7[»]
4A0NX-ray2.74C2-7[»]
4A7JX-ray1.90B1-16[»]
4BD3NMR-B32-42[»]
4C1QX-ray2.30C2-10[»]
4F4UX-ray2.00C/D5-16[»]
4F56X-ray1.70C/D5-16[»]
4FWFX-ray2.70E2-21[»]
4HONX-ray1.80F/G7-16[»]
4I51X-ray1.90C/D4-12[»]
4L7XX-ray1.35U2-13[»]
4LK9X-ray1.60B2-22[»]
4LKAX-ray1.61B2-22[»]
4LLBX-ray2.50C/D2-22[»]
4LXLX-ray1.87D8-15[»]
4N4HX-ray2.30B22-43[»]
4QBQX-ray2.41P2-9[»]
4QBRX-ray1.90E/P2-8[»]
4QBSX-ray1.80P2-8[»]
4TN7X-ray2.20E/F30-44[»]
4U68X-ray1.80D/E/F5-15[»]
4UP0X-ray1.28F2-16[»]
4UY4X-ray1.86C/D2-7[»]
4X3KX-ray1.45C/D24-30[»]
4Y6LX-ray1.60C/D7-13[»]
4YHPX-ray2.53P/Q2-17[»]
4YHZX-ray2.30P2-13[»]
4YM5X-ray4.00A/E1-136[»]
4YM6X-ray3.51A/E1-136[»]
4Z0RX-ray1.75D2-16[»]
4Z2MX-ray2.98G/I35-136[»]
5AV5X-ray2.40A/E1-136[»]
5AV6X-ray2.20A/E1-136[»]
5AV8X-ray2.20A/E1-136[»]
5AV9X-ray2.20A/E1-136[»]
5AVBX-ray2.40A/E1-136[»]
5AVCX-ray2.40A/E1-136[»]
5B24X-ray3.60A/E1-136[»]
5B2IX-ray3.00A/E1-136[»]
5B2JX-ray2.60A/E1-136[»]
5B31X-ray2.20A/E1-136[»]
5C11X-ray2.80B2-11[»]
5C13X-ray2.10D/F/H/P2-11[»]
5C3IX-ray3.50B/F/J/N/R/V1-136[»]
5CPIX-ray2.90A/E1-136[»]
5CPJX-ray3.15A/E1-136[»]
5CPKX-ray2.63A/E1-136[»]
5D6YX-ray2.29a/b/c/d20-29[»]
5DAHX-ray2.61C/D20-30[»]
5FB0X-ray2.70D/F2-16[»]
5FB1X-ray2.10C2-16[»]
5FFVX-ray1.30C/D10-20[»]
5GH9X-ray1.45B45-58[»]
5GSEX-ray3.14A/E/K/O1-136[»]
5GSUX-ray3.10A/E2-136[»]
5GT0X-ray2.82A/E2-136[»]
5GT3X-ray2.91A/E2-136[»]
5GTCX-ray2.70A/E1-136[»]
5H6QX-ray2.53C2-21[»]
5H6RX-ray2.60C2-21[»]
5HJBX-ray2.70B4-9[»]
5HJCX-ray2.60B16-24[»]
5HJDX-ray2.81B/D/F/H/I/J/L/M15-21[»]
5HYNX-ray2.95D/I/O/T22-34[»]
5IQLX-ray2.10B25-32[»]
5J3VX-ray3.05C/D12-28[»]
5J9SX-ray2.70B16-40[»]
5JHNX-ray1.67F/G4-14[»]
5JINX-ray1.85F/G4-14[»]
5JIYX-ray1.48F/G4-14[»]
5JJ0X-ray1.72F/G4-14[»]
5JRGX-ray2.50A/E1-136[»]
5KJHX-ray2.27D23-33[»]
E19-38[»]
5KJIX-ray2.71E19-38[»]
5KKLX-ray2.94B23-27[»]
5LUGX-ray1.70E/F/G/H2-11[»]
5M5GX-ray2.27D23-33[»]
5MR8X-ray1.74C2-10[»]
5NNCX-ray2.22C/D5-21[»]
5NNDX-ray1.82D/E5-21[»]
5OY3X-ray2.14B18-34[»]
5SVXX-ray1.56B2-12[»]
5SVYX-ray1.05B2-12[»]
5SZBX-ray1.20H2-19[»]
5SZCX-ray1.19H2-19[»]
5T0KX-ray1.70P/Q2-16[»]
5T0MX-ray1.90C/P2-16[»]
5T1GX-ray1.90B39-53[»]
5T1IX-ray1.60C39-53[»]
5T8RX-ray2.40E/G2-11[»]
5TBNNMR-C2-12[»]
5TDRX-ray1.42B2-12[»]
5TDWX-ray1.70B2-12[»]
5U2JX-ray1.60C/D2-17[»]
5V21X-ray2.42B30-44[»]
5V22X-ray2.40B30-44[»]
5VA6X-ray2.40C/D20-37[»]
5VABX-ray1.70F2-11[»]
5VGEX-ray2.60C41-49[»]
5VNBX-ray2.40K22-31[»]
5WFCX-ray2.28D23-33[»]
5WLEX-ray1.95C2-13[»]
5WVOX-ray2.00D2-37[»]
5WXGX-ray1.70P2-8[»]
5WXHX-ray1.30D/P2-8[»]
5WYIX-ray2.00E120-127[»]
5X60X-ray2.69C2-21[»]
5XF3X-ray2.60A/E1-136[»]
5XF4X-ray2.87A/E1-136[»]
5XF5X-ray2.82A/E1-136[»]
5XFQX-ray2.40E/F30-42[»]
5XFRX-ray2.25C/D34-41[»]
5XNVX-ray2.70B25-32[»]
5XTZX-ray2.10E23-32[»]
5Y0CX-ray2.09A/E1-136[»]
5Y0DX-ray1.99A/E1-136[»]
5Y20X-ray2.41P2-8[»]
5Y2FX-ray2.53C6-14[»]
5Z23X-ray2.73A/E1-75[»]
A/E116-136[»]
5Z30X-ray2.45A/E1-136[»]
6AXJX-ray2.38E/F/G/H22-32[»]
6AZEX-ray2.45P2-7[»]
6BHDX-ray1.25B4-20[»]
6BHEX-ray1.35B4-20[»]
6BHGX-ray1.45B4-20[»]
6BHHX-ray1.85B4-20[»]
6BHIX-ray1.40B5-20[»]
6D07X-ray2.10C/D2-16[»]
6D08X-ray2.10C/D2-16[»]
6E83NMR-A2-13[»]
6E86NMR-A2-9[»]
6F6DX-ray1.82B18-34[»]
6HKTX-ray9.70A/E/K/O/U/Y/a/e/k/o/u/y1-136[»]
6HTSelectron microscopy4.80I/M1-136[»]
6MILX-ray1.93B/D2-20[»]
6MIMX-ray2.52B/D6-14[»]
6MINX-ray1.90B6-12[»]
6MIOX-ray1.85B6-12[»]
6MIQX-ray1.75C6-12[»]
SMRiP68431
ModBaseiSearch...

Protein-protein interaction databases

BioGridi113946, 354 interactors
113947, 8 interactors
113948, 14 interactors
113949, 205 interactors
113950, 8 interactors
113951, 8 interactors
113952, 7 interactors
113953, 10 interactors
113954, 25 interactors
114458, 10 interactors
CORUMiP68431
DIPiDIP-29371N
ELMiP68431
IntActiP68431, 434 interactors
MINTiP68431
STRINGi9606.ENSP00000484841

PTM databases

iPTMnetiP68431
PhosphoSitePlusiP68431
SwissPalmiP68431

Polymorphism and mutation databases

BioMutaiHIST1H3A
DMDMi55977055

Proteomic databases

EPDiP68431
jPOSTiP68431
MaxQBiP68431
PaxDbiP68431
PeptideAtlasiP68431
PRIDEiP68431
ProteomicsDBi57541
TopDownProteomicsiP68431

Protocols and materials databases

ABCD curated depository of sequenced antibodies

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ABCDi
P68431

The DNASU plasmid repository

More...
DNASUi
8350
8352
8353
8355
8356
8357
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356476; ENSP00000366999; ENSG00000197409
ENST00000359303; ENSP00000352252; ENSG00000197153
ENST00000369163; ENSP00000358160; ENSG00000278828
ENST00000612966; ENSP00000484658; ENSG00000278272
ENST00000613854; ENSP00000480826; ENSG00000275714
ENST00000614378; ENSP00000484638; ENSG00000273983
ENST00000614911; ENSP00000482271; ENSG00000274750
ENST00000616365; ENSP00000483283; ENSG00000275379
ENST00000618052; ENSP00000484095; ENSG00000277775
ENST00000621411; ENSP00000484841; ENSG00000274267
ENST00000634733; ENSP00000489282; ENSG00000274750
GeneIDi8350
8351
8352
8353
8354
8355
8356
8357
8358
8968
KEGGihsa:8350
hsa:8351
hsa:8352
hsa:8353
hsa:8354
hsa:8355
hsa:8356
hsa:8357
hsa:8358
hsa:8968
UCSCiuc003nfp.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8350
8351
8352
8353
8354
8355
8356
8357
8358
8968
DisGeNETi8350
8351
8352
8353
8354
8355
8356
8357
8358
8968

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HIST1H3A
HIST1H3B
HIST1H3C
HIST1H3D
HIST1H3E
HIST1H3F
HIST1H3G
HIST1H3H
HIST1H3I
HIST1H3J
HGNCiHGNC:4766 HIST1H3A
HGNC:4776 HIST1H3B
HGNC:4768 HIST1H3C
HGNC:4767 HIST1H3D
HGNC:4769 HIST1H3E
HGNC:4773 HIST1H3F
HGNC:4772 HIST1H3G
HGNC:4775 HIST1H3H
HGNC:4771 HIST1H3I
HGNC:4774 HIST1H3J
HPAiCAB070190
HPA042570
MalaCardsiHIST1H3A
MIMi137800 phenotype
602810 gene
602811 gene
602812 gene
602813 gene
602814 gene
602815 gene
602816 gene
602817 gene
602818 gene
602819 gene
neXtProtiNX_P68431
OpenTargetsiENSG00000197153
ENSG00000197409
ENSG00000273983
ENSG00000274267
ENSG00000274750
ENSG00000275379
ENSG00000275714
ENSG00000277775
ENSG00000278272
ENSG00000278828
PharmGKBiPA29148

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00960000186578
InParanoidiP68431
KOiK11253
OMAiASEAYYL
OrthoDBi1564596at2759
PhylomeDBiP68431
TreeFamiTF314241

Enzyme and pathway databases

ReactomeiR-HSA-1266695 Interleukin-7 signaling
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-3214815 HDACs deacetylate histones
R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-3214842 HDMs demethylate histones
R-HSA-3214847 HATs acetylate histones
R-HSA-3214858 RMTs methylate histone arginines
R-HSA-3247509 Chromatin modifying enzymes
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-73772 RNA Polymerase I Promoter Escape
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
SIGNORiP68431

Miscellaneous databases

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

More...
ChiTaRSi
HIST1H3B human
HIST1H3F human
EvolutionaryTraceiP68431

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
HIST1H3A
HIST1H3B
HIST1H3C
HIST1H3D
HIST1H3E
HIST1H3F
HIST1H3G
HIST1H3H
HIST1H3I
HIST1H3J

Protein Ontology

More...
PROi
PR:P68431

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000197153 Expressed in 43 organ(s), highest expression level in stomach
GenevisibleiP68431 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...

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 nameiH31_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: P68431
Secondary accession number(s): A0PJT7
, A5PLR1, P02295, P02296, P16106, Q6ISV8, Q6NWP8, Q6NWP9, Q6NXU4, Q71DJ3, Q93081
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 3, 2019
This is version 174 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
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