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Entry version 198 (13 Feb 2019)
Sequence version 2 (23 Jan 2007)
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Protein

Histone H2A type 1-B/E

Gene

HIST1H2AB

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.

<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

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

GO - Biological processi

  • chromatin organization Source: GO_Central
  • negative regulation of cell population proliferation Source: UniProtKB

<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-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
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-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-3214815 HDACs deacetylate histones
R-HSA-3214847 HATs acetylate histones
R-HSA-3214858 RMTs methylate histone arginines
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-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689901 Metalloprotease DUBs
R-HSA-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-HSA-73728 RNA Polymerase I Promoter Opening
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation

<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 H2A type 1-B/E
Alternative name(s):
Histone H2A.2
Histone H2A/a
Histone H2A/m
<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:HIST1H2AB
Synonyms:H2AFM
AND
Name:HIST1H2AE
Synonyms:H2AFA
<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

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000277075.2
HostDB:ENSG00000278463.1

Human Gene Nomenclature Database

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HGNCi
HGNC:4734 HIST1H2AB
HGNC:4724 HIST1H2AE

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602786 gene
602795 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P04908

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

<p>This section 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2S → A: Blocks the inhibition of transcription by RPS6KA5/MSK1. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
3012
8335

Open Targets

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OpenTargetsi
ENSG00000277075
ENSG00000278463

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA29111

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
HIST1H2AE

Domain mapping of disease mutations (DMDM)

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DMDMi
124028530

<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 methionineiRemoved3 Publications
<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_00000552372 – 130Histone H2A type 1-B/EAdd BLAST129

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 residuei2N-acetylserine3 Publications1
Modified residuei2Phosphoserine; by RPS6KA52 Publications1
Modified residuei4Citrulline; alternate1 Publication1
Modified residuei4Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei6N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei6N6-acetyllysine; alternateBy similarity1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-succinyllysine; alternate1 Publication1
Modified residuei14N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei37N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei37N6-crotonyllysine; alternate1 Publication1
Modified residuei75N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei76N6-(2-hydroxyisobutyryl)lysine1 Publication1
Modified residuei96N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei96N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei96N6-succinyllysine; alternate1 Publication1
Modified residuei105N5-methylglutamine1 Publication1
Modified residuei119N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei119N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei119N6-crotonyllysine; alternate1 Publication1
Modified residuei120N6-crotonyllysine; alternate1 Publication1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate4 Publications
Modified residuei121Phosphothreonine; by DCAF12 Publications1
Modified residuei126N6-crotonyllysine1 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

Deiminated on Arg-4 in granulocytes upon calcium entry.1 Publication
Monoubiquitination of Lys-120 (H2AK119Ub) by RING1, TRIM27 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Monoubiquitination of Lys-120 (H2AK119Ub) by TRIM27 may promote transformation of cells in a number of breast cancers (PubMed:25470042). Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. Deubiquitinated by USP51 at Lys-14 and Lys-16 (H2AK13Ub and H2AK15Ub, respectively) after damaged DNA is repaired (PubMed:27083998). H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.12 Publications
Phosphorylation on Ser-2 (H2AS1ph) is enhanced during mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly represses transcription. Acetylation of H3 inhibits Ser-2 phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121 (H2AT120ph) by DCAF1 is present in the regulatory region of many tumor suppresor genes and down-regulates their transcription.6 Publications
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (PubMed:24352239).1 Publication
Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex may play a crucial role in the germ-cell lineage.By similarity
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P04908

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P04908

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

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PaxDbi
P04908

PeptideAtlas

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PeptideAtlasi
P04908

PRoteomics IDEntifications database

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PRIDEi
P04908

ProteomicsDB human proteome resource

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ProteomicsDBi
51756

Consortium for Top Down Proteomics

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TopDownProteomicsi
P04908

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P04908

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

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PhosphoSitePlusi
P04908

SwissPalm database of S-palmitoylation events

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SwissPalmi
P04908

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000277075 Expressed in 129 organ(s), highest expression level in stomach

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P04908 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P04908 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB012242
HPA041189

<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
109266, 32 interactors
113931, 74 interactors

Database of interacting proteins

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DIPi
DIP-44197N

Protein interaction database and analysis system

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IntActi
P04908, 106 interactors

Molecular INTeraction database

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MINTi
P04908

STRING: functional protein association networks

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STRINGi
9606.ENSP00000303373

<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

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CV5X-ray2.50C/G1-130[»]
2RVQNMR-C1-130[»]
3A6NX-ray2.70C/G1-130[»]
3AFAX-ray2.50C/G1-130[»]
3AN2X-ray3.60C/G1-130[»]
3AV1X-ray2.50C/G1-130[»]
3AV2X-ray2.80C/G1-130[»]
3AYWX-ray2.90C/G1-130[»]
3AZEX-ray3.00C/G1-130[»]
3AZFX-ray2.70C/G1-130[»]
3AZGX-ray2.40C/G1-130[»]
3AZHX-ray3.49C/G1-130[»]
3AZIX-ray2.70C/G1-130[»]
3AZJX-ray2.89C/G1-130[»]
3AZKX-ray3.20C/G1-130[»]
3AZLX-ray2.70C/G1-130[»]
3AZMX-ray2.89C/G1-130[»]
3AZNX-ray3.00C/G1-130[»]
3W96X-ray3.00C/G11-130[»]
3W97X-ray3.20C/G1-130[»]
3W98X-ray3.42C/G1-130[»]
3W99X-ray3.00C/G1-130[»]
3WKJX-ray2.80C/G1-130[»]
3WTPX-ray2.67C/G1-130[»]
3X1SX-ray2.81C/G2-130[»]
3X1VX-ray2.92C/G2-130[»]
4YM5X-ray4.00C/G1-130[»]
4YM6X-ray3.51C/G1-130[»]
4Z5TX-ray2.80C/G1-130[»]
5AV5X-ray2.40C/G1-130[»]
5AV6X-ray2.20C/G1-130[»]
5AV8X-ray2.20C/G1-130[»]
5AV9X-ray2.20C/G1-130[»]
5AVBX-ray2.40C/G1-130[»]
5AVCX-ray2.40C/G1-130[»]
5AY8X-ray2.80C/G1-130[»]
5B0YX-ray2.56C/G1-130[»]
5B0ZX-ray1.99C/G1-130[»]
5B24X-ray3.60C/G1-130[»]
5B2IX-ray3.00C/G1-130[»]
5B2JX-ray2.60C/G1-130[»]
5B31X-ray2.20C1-130[»]
5B32X-ray2.35C1-130[»]
5B40X-ray3.33C/G1-130[»]
5CPIX-ray2.90C/G1-130[»]
5CPJX-ray3.15C/G1-130[»]
5CPKX-ray2.63C/G1-130[»]
5GSEX-ray3.14C/G/M1-130[»]
5GTCX-ray2.70C/G1-130[»]
5GXQX-ray2.85C/G1-130[»]
5JRGX-ray2.50C/G1-130[»]
5X7XX-ray2.18C/G1-130[»]
5XF3X-ray2.60C/G1-130[»]
5XF4X-ray2.87C/G1-130[»]
5XF5X-ray2.82C/G1-130[»]
5Y0CX-ray2.09C/G1-130[»]
5Y0DX-ray1.99C/G1-130[»]
6A5Lelectron microscopy5.60c/g1-130[»]
6A5Oelectron microscopy9.90c/g1-130[»]
6A5Pelectron microscopy7.00c/g1-130[»]
6A5Relectron microscopy8.70c/g1-130[»]
6A5Telectron microscopy6.70c/g1-130[»]
6A5Uelectron microscopy7.60c/g1-130[»]
6A5Velectron microscopy6.90c/g1-130[»]
6BUZelectron microscopy3.92C/G1-130[»]
6HKTX-ray9.700/2/C/G/M/Q/W/c/g/m/q/w1-130[»]
6HTSelectron microscopy4.80K/O1-130[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P04908

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

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SMRi
P04908

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P04908

<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 H2A family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1756 Eukaryota
COG5262 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153092

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234652

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG009342

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P04908

KEGG Orthology (KO)

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KOi
K11251

Identification of Orthologs from Complete Genome Data

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OMAi
GWITKFP

Database of Orthologous Groups

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OrthoDBi
1504122at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P04908

TreeFam database of animal gene trees

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TreeFami
TF300137

Family and domain databases

Conserved Domains Database

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CDDi
cd00074 H2A, 1 hit

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
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00620 HISTONEH2A

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00414 H2A, 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
PS00046 HISTONE_H2A, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

<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.

P04908-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR
110 120 130
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK
Length:130
Mass (Da):14,135
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:i9CFE6184B2CC89F5
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 conflicti38 – 39GN → AH in CAA24951 (PubMed:6647026).Curated2

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 14037.9 Da from positions 2 - 130. Determined by ESI. Monoisotopic with N-acetylserine.1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X00089 Genomic DNA Translation: CAA24951.1
M60752 Genomic DNA Translation: AAA63191.1
Z83741 Genomic DNA Translation: CAB06036.1
AY131983 Genomic DNA Translation: AAN59964.1
AY131986 Genomic DNA Translation: AAN59967.1
AL031777 Genomic DNA No translation available.
BC093836 mRNA Translation: AAH93836.1
BC093862 mRNA Translation: AAH93862.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4574.1
CCDS4595.1

Protein sequence database of the Protein Information Resource

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PIRi
B26318 HSHUA5
G40335

NCBI Reference Sequences

More...
RefSeqi
NP_003504.2, NM_003513.2
NP_066390.1, NM_021052.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.121017
Hs.248174
Hs.709162

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000303910; ENSP00000303373; ENSG00000277075
ENST00000615868; ENSP00000483842; ENSG00000278463

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3012
8335

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3012
hsa:8335

<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
X00089 Genomic DNA Translation: CAA24951.1
M60752 Genomic DNA Translation: AAA63191.1
Z83741 Genomic DNA Translation: CAB06036.1
AY131983 Genomic DNA Translation: AAN59964.1
AY131986 Genomic DNA Translation: AAN59967.1
AL031777 Genomic DNA No translation available.
BC093836 mRNA Translation: AAH93836.1
BC093862 mRNA Translation: AAH93862.1
CCDSiCCDS4574.1
CCDS4595.1
PIRiB26318 HSHUA5
G40335
RefSeqiNP_003504.2, NM_003513.2
NP_066390.1, NM_021052.2
UniGeneiHs.121017
Hs.248174
Hs.709162

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CV5X-ray2.50C/G1-130[»]
2RVQNMR-C1-130[»]
3A6NX-ray2.70C/G1-130[»]
3AFAX-ray2.50C/G1-130[»]
3AN2X-ray3.60C/G1-130[»]
3AV1X-ray2.50C/G1-130[»]
3AV2X-ray2.80C/G1-130[»]
3AYWX-ray2.90C/G1-130[»]
3AZEX-ray3.00C/G1-130[»]
3AZFX-ray2.70C/G1-130[»]
3AZGX-ray2.40C/G1-130[»]
3AZHX-ray3.49C/G1-130[»]
3AZIX-ray2.70C/G1-130[»]
3AZJX-ray2.89C/G1-130[»]
3AZKX-ray3.20C/G1-130[»]
3AZLX-ray2.70C/G1-130[»]
3AZMX-ray2.89C/G1-130[»]
3AZNX-ray3.00C/G1-130[»]
3W96X-ray3.00C/G11-130[»]
3W97X-ray3.20C/G1-130[»]
3W98X-ray3.42C/G1-130[»]
3W99X-ray3.00C/G1-130[»]
3WKJX-ray2.80C/G1-130[»]
3WTPX-ray2.67C/G1-130[»]
3X1SX-ray2.81C/G2-130[»]
3X1VX-ray2.92C/G2-130[»]
4YM5X-ray4.00C/G1-130[»]
4YM6X-ray3.51C/G1-130[»]
4Z5TX-ray2.80C/G1-130[»]
5AV5X-ray2.40C/G1-130[»]
5AV6X-ray2.20C/G1-130[»]
5AV8X-ray2.20C/G1-130[»]
5AV9X-ray2.20C/G1-130[»]
5AVBX-ray2.40C/G1-130[»]
5AVCX-ray2.40C/G1-130[»]
5AY8X-ray2.80C/G1-130[»]
5B0YX-ray2.56C/G1-130[»]
5B0ZX-ray1.99C/G1-130[»]
5B24X-ray3.60C/G1-130[»]
5B2IX-ray3.00C/G1-130[»]
5B2JX-ray2.60C/G1-130[»]
5B31X-ray2.20C1-130[»]
5B32X-ray2.35C1-130[»]
5B40X-ray3.33C/G1-130[»]
5CPIX-ray2.90C/G1-130[»]
5CPJX-ray3.15C/G1-130[»]
5CPKX-ray2.63C/G1-130[»]
5GSEX-ray3.14C/G/M1-130[»]
5GTCX-ray2.70C/G1-130[»]
5GXQX-ray2.85C/G1-130[»]
5JRGX-ray2.50C/G1-130[»]
5X7XX-ray2.18C/G1-130[»]
5XF3X-ray2.60C/G1-130[»]
5XF4X-ray2.87C/G1-130[»]
5XF5X-ray2.82C/G1-130[»]
5Y0CX-ray2.09C/G1-130[»]
5Y0DX-ray1.99C/G1-130[»]
6A5Lelectron microscopy5.60c/g1-130[»]
6A5Oelectron microscopy9.90c/g1-130[»]
6A5Pelectron microscopy7.00c/g1-130[»]
6A5Relectron microscopy8.70c/g1-130[»]
6A5Telectron microscopy6.70c/g1-130[»]
6A5Uelectron microscopy7.60c/g1-130[»]
6A5Velectron microscopy6.90c/g1-130[»]
6BUZelectron microscopy3.92C/G1-130[»]
6HKTX-ray9.700/2/C/G/M/Q/W/c/g/m/q/w1-130[»]
6HTSelectron microscopy4.80K/O1-130[»]
ProteinModelPortaliP04908
SMRiP04908
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109266, 32 interactors
113931, 74 interactors
DIPiDIP-44197N
IntActiP04908, 106 interactors
MINTiP04908
STRINGi9606.ENSP00000303373

PTM databases

iPTMnetiP04908
PhosphoSitePlusiP04908
SwissPalmiP04908

Polymorphism and mutation databases

BioMutaiHIST1H2AE
DMDMi124028530

Proteomic databases

EPDiP04908
jPOSTiP04908
PaxDbiP04908
PeptideAtlasiP04908
PRIDEiP04908
ProteomicsDBi51756
TopDownProteomicsiP04908

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3012
8335
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000303910; ENSP00000303373; ENSG00000277075
ENST00000615868; ENSP00000483842; ENSG00000278463
GeneIDi3012
8335
KEGGihsa:3012
hsa:8335

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3012
8335
DisGeNETi3012
8335
EuPathDBiHostDB:ENSG00000277075.2
HostDB:ENSG00000278463.1

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HIST1H2AB
HIST1H2AE
HGNCiHGNC:4734 HIST1H2AB
HGNC:4724 HIST1H2AE
HPAiCAB012242
HPA041189
MIMi602786 gene
602795 gene
neXtProtiNX_P04908
OpenTargetsiENSG00000277075
ENSG00000278463
PharmGKBiPA29111

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1756 Eukaryota
COG5262 LUCA
GeneTreeiENSGT00940000153092
HOGENOMiHOG000234652
HOVERGENiHBG009342
InParanoidiP04908
KOiK11251
OMAiGWITKFP
OrthoDBi1504122at2759
PhylomeDBiP04908
TreeFamiTF300137

Enzyme and pathway databases

ReactomeiR-HSA-1221632 Meiotic synapsis
R-HSA-171306 Packaging Of Telomere Ends
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-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-3214815 HDACs deacetylate histones
R-HSA-3214847 HATs acetylate histones
R-HSA-3214858 RMTs methylate histone arginines
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-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5689901 Metalloprotease DUBs
R-HSA-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-HSA-73728 RNA Polymerase I Promoter Opening
R-HSA-73777 RNA Polymerase I Chain Elongation
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-9018519 Estrogen-dependent gene expression
R-HSA-912446 Meiotic recombination
R-HSA-977225 Amyloid fiber formation

Miscellaneous databases

EvolutionaryTraceiP04908

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
HIST1H2AB
HIST1H2AE

Protein Ontology

More...
PROi
PR:P04908

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000277075 Expressed in 129 organ(s), highest expression level in stomach
ExpressionAtlasiP04908 baseline and differential
GenevisibleiP04908 HS

Family and domain databases

CDDicd00074 H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR002119 Histone_H2A
IPR007125 Histone_H2A/H2B/H3
IPR032454 Histone_H2A_C
IPR032458 Histone_H2A_CS
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PF16211 Histone_H2A_C, 1 hit
PRINTSiPR00620 HISTONEH2A
SMARTiView protein in SMART
SM00414 H2A, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046 HISTONE_H2A, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiH2A1B_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: P04908
Secondary accession number(s): P28001, Q76P63
<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: August 13, 1987
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 198 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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