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Entry version 191 (16 Oct 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Histone H3.1t

Gene

HIST3H3

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.

<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-110328 Recognition and association of DNA glycosylase with site containing an affected pyrimidine
R-HSA-110329 Cleavage of the damaged pyrimidine
R-HSA-110330 Recognition and association of DNA glycosylase with site containing an affected purine
R-HSA-110331 Cleavage of the damaged purine
R-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-912446 Meiotic recombination

SIGNOR Signaling Network Open Resource

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SIGNORi
Q16695

<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 H3.1t
Short name:
H3/t
Short name:
H3t
Alternative name(s):
H3/g
<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:HIST3H3
Synonyms:H3FT
<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 1

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:4778 HIST3H3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602820 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q16695

<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

Organism-specific databases

DisGeNET

More...
DisGeNETi
8290

Open Targets

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OpenTargetsi
ENSG00000168148

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29153

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q16695

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
HIST3H3

Domain mapping of disease mutations (DMDM)

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DMDMi
18202512

<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_00002212482 – 136Histone H3.1tAdd BLAST135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3Asymmetric dimethylarginine; by PRMT6; alternateBy similarity1
Modified residuei3Citrulline; alternateBy similarity1
Modified residuei4Phosphothreonine; by HASPINBy similarity1
Modified residuei5Allysine; alternateBy similarity1
Modified residuei5N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei5N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei5N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei5N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei5N6-acetyllysine; alternateBy similarity1
Modified residuei5N6-methyllysine; alternateBy similarity1
Modified residuei7Phosphothreonine; by PKCBy similarity1
Modified residuei9Citrulline; alternateBy similarity1
Modified residuei9Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei10N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei10N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei10N6-acetyllysine; alternateBy similarity1
Modified residuei10N6-methyllysine; alternateBy similarity1
Modified residuei11ADP-ribosylserine; alternateBy similarity1
Modified residuei11Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5By similarity1
Modified residuei12Phosphothreonine; by PKCBy similarity1
Modified residuei15N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei15N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei15N6-acetyllysine; alternateBy similarity1
Modified residuei15N6-succinyllysine; alternateBy similarity1
Modified residuei18Asymmetric dimethylarginine; by CARM1; alternateBy similarity1
Modified residuei18Citrulline; alternateBy similarity1
Modified residuei19N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei19N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei19N6-acetyllysine; alternateCombined sources1
Modified residuei19N6-butyryllysine; alternateBy similarity1
Modified residuei19N6-methyllysine; alternateBy similarity1
Modified residuei24N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei24N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei24N6-acetyllysine; alternateCombined sources1
Modified residuei24N6-butyryllysine; alternateBy similarity1
Modified residuei24N6-methyllysine; alternateBy similarity1
Modified residuei27CitrullineBy similarity1
Modified residuei28N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei28N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei28N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei28N6-acetyllysine; alternateBy similarity1
Modified residuei28N6-methyllysine; alternateBy similarity1
Modified residuei29ADP-ribosylserine; alternateBy similarity1
Modified residuei29Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5Combined sources1
Modified residuei37N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei37N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei37N6-acetyllysine; alternateBy similarity1
Modified residuei37N6-methyllysine; alternateBy similarity1
Modified residuei38N6-methyllysineBy similarity1
Modified residuei42PhosphotyrosineBy similarity1
Modified residuei57N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei57N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei57N6-(beta-hydroxybutyryl)lysine; alternateBy similarity1
Modified residuei57N6-acetyllysine; alternateBy similarity1
Modified residuei57N6-methyllysine; by EHMT2; alternateBy similarity1
Modified residuei57N6-succinyllysine; alternateBy similarity1
Modified residuei58Phosphoserine1 Publication1
Modified residuei65N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei65N6-methyllysine; alternateBy similarity1
Modified residuei80N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei80N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei80N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei80N6-acetyllysine; alternateBy similarity1
Modified residuei80N6-methyllysine; alternateBy similarity1
Modified residuei80N6-succinyllysine; alternateBy similarity1
Modified residuei81Phosphothreonine1 Publication1
Modified residuei87PhosphoserineBy similarity1
Modified residuei108PhosphothreonineBy similarity1
Modified residuei116N6-acetyllysineBy similarity1
Modified residuei123N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei123N6-acetyllysine; alternateBy similarity1
Modified residuei123N6-methyllysine; alternateBy similarity1
Modified residuei123N6-succinyllysine; alternateBy similarity1

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

Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (By similarity).By similarity
Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription.By similarity
Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene repression and is mutually exclusive with H3 Lys-5 methylation (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes regardless of their transcription state and is enriched on inactive promoters, while it is absent on active promoters (By similarity).By similarity
Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80 (H3K79me) are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me) require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication (By similarity).By similarity
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 (By similarity).By similarity
Ubiquitinated.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 (By similarity).By similarity
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. It gives a specific tag for epigenetic transcription activation.By similarity
Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac).By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q16695

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q16695

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q16695

MaxQB - The MaxQuant DataBase

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MaxQBi
Q16695

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

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PaxDbi
Q16695

PeptideAtlas

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PeptideAtlasi
Q16695

PRoteomics IDEntifications database

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PRIDEi
Q16695

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
61035

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q16695

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q16695

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

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PhosphoSitePlusi
Q16695

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q16695

<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 a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in testicular cells.

<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
ENSG00000168148 Expressed in 61 organ(s), highest expression level in right testis

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q16695 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB001386
CAB003812
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.

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113895, 242 interactors

Database of interacting proteins

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DIPi
DIP-922N

Protein interaction database and analysis system

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IntActi
Q16695, 159 interactors

Molecular INTeraction database

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MINTi
Q16695

STRING: functional protein association networks

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STRINGi
9606.ENSP00000355657

<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
Q16695

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q16695

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

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

Belongs to the histone H3 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1745 Eukaryota
COG2036 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00960000186578

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000155290

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q16695

KEGG Orthology (KO)

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KOi
K11253

Identification of Orthologs from Complete Genome Data

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OMAi
VTIMRRT

Database of Orthologous Groups

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OrthoDBi
1564596at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q16695

TreeFam database of animal gene trees

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TreeFami
TF314241

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

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

The PANTHER Classification System

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PANTHERi
PTHR11426 PTHR11426, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00125 Histone, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00622 HISTONEH3

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00428 H3, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47113 SSF47113, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00322 HISTONE_H3_1, 1 hit

<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.

Q16695-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARTKQTARK STGGKAPRKQ LATKVARKSA PATGGVKKPH RYRPGTVALR
60 70 80 90 100
EIRRYQKSTE LLIRKLPFQR LMREIAQDFK TDLRFQSSAV MALQEACESY
110 120 130
LVGLFEDTNL CVIHAKRVTI MPKDIQLARR IRGERA
Length:136
Mass (Da):15,508
Last modified:January 23, 2007 - v3
<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:i37375A2C3A377B2B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
Z49861 Genomic DNA Translation: CAA90020.1
AF531308 Genomic DNA Translation: AAN39284.1
CR542013 mRNA Translation: CAG46810.1
AK312217 mRNA Translation: BAG35150.1
AL139288 Genomic DNA No translation available.
CH471098 Genomic DNA Translation: EAW69877.1
BC069079 mRNA Translation: AAH69079.1
BC101837 mRNA Translation: AAI01838.1
BC101839 mRNA Translation: AAI01840.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS1572.1

Protein sequence database of the Protein Information Resource

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PIRi
S57473

NCBI Reference Sequences

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RefSeqi
NP_003484.1, NM_003493.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000366696; ENSP00000355657; ENSG00000168148
ENST00000644869; ENSP00000494070; ENSG00000285435

Database of genes from NCBI RefSeq genomes

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GeneIDi
8290

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:8290

UCSC genome browser

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UCSCi
uc001hsx.1 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
Z49861 Genomic DNA Translation: CAA90020.1
AF531308 Genomic DNA Translation: AAN39284.1
CR542013 mRNA Translation: CAG46810.1
AK312217 mRNA Translation: BAG35150.1
AL139288 Genomic DNA No translation available.
CH471098 Genomic DNA Translation: EAW69877.1
BC069079 mRNA Translation: AAH69079.1
BC101837 mRNA Translation: AAI01838.1
BC101839 mRNA Translation: AAI01840.1
CCDSiCCDS1572.1
PIRiS57473
RefSeqiNP_003484.1, NM_003493.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V1DX-ray3.10C2-22[»]
2YBPX-ray2.02C/D31-42[»]
2YBSX-ray2.32C/D31-42[»]
3A6NX-ray2.70A/E1-136[»]
3T6RX-ray1.95D2-8[»]
4V2VX-ray2.00C/D26-30[»]
4V2WX-ray1.81C17-36[»]
SMRiQ16695
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi113895, 242 interactors
DIPiDIP-922N
IntActiQ16695, 159 interactors
MINTiQ16695
STRINGi9606.ENSP00000355657

PTM databases

iPTMnetiQ16695
PhosphoSitePlusiQ16695
SwissPalmiQ16695

Polymorphism and mutation databases

BioMutaiHIST3H3
DMDMi18202512

Proteomic databases

EPDiQ16695
jPOSTiQ16695
MassIVEiQ16695
MaxQBiQ16695
PaxDbiQ16695
PeptideAtlasiQ16695
PRIDEiQ16695
ProteomicsDBi61035
TopDownProteomicsiQ16695

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
8290

Genome annotation databases

EnsembliENST00000366696; ENSP00000355657; ENSG00000168148
ENST00000644869; ENSP00000494070; ENSG00000285435
GeneIDi8290
KEGGihsa:8290
UCSCiuc001hsx.1 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8290
DisGeNETi8290

GeneCards: human genes, protein and diseases

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GeneCardsi
HIST3H3
HGNCiHGNC:4778 HIST3H3
HPAiCAB001386
CAB003812
HPA042570
MIMi602820 gene
neXtProtiNX_Q16695
OpenTargetsiENSG00000168148
PharmGKBiPA29153

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1745 Eukaryota
COG2036 LUCA
GeneTreeiENSGT00960000186578
HOGENOMiHOG000155290
InParanoidiQ16695
KOiK11253
OMAiVTIMRRT
OrthoDBi1564596at2759
PhylomeDBiQ16695
TreeFamiTF314241

Enzyme and pathway databases

ReactomeiR-HSA-110328 Recognition and association of DNA glycosylase with site containing an affected pyrimidine
R-HSA-110329 Cleavage of the damaged pyrimidine
R-HSA-110330 Recognition and association of DNA glycosylase with site containing an affected purine
R-HSA-110331 Cleavage of the damaged purine
R-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-2299718 Condensation of Prophase Chromosomes
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-912446 Meiotic recombination
SIGNORiQ16695

Miscellaneous databases

EvolutionaryTraceiQ16695

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
HIST3H3

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
8290
PharosiQ16695

Protein Ontology

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PROi
PR:Q16695

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000168148 Expressed in 61 organ(s), highest expression level in right testis
GenevisibleiQ16695 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiH31T_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: Q16695
Secondary accession number(s): B2R5K3, Q6FGU4
<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: September 26, 2001
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 191 of the entry and version 3 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, 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
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