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UniProtKB - Q6FI13 (H2A2A_HUMAN)

Entry version 174 (02 Jun 2021)
Sequence version 3 (23 Jan 2007)
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Protein

Histone H2A type 2-A

Gene

H2AC18

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionDNA-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q6FI13

Reactome - a knowledgebase of biological pathways and processes

More...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-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-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-9609690, HCMV Early Events
R-HSA-9610379, HCMV Late Events
R-HSA-9616222, Transcriptional regulation of granulopoiesis
R-HSA-9670095, Inhibition of DNA recombination at telomere
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%5Fand%5Ftaxonomy%5Fsection">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 2-A
Alternative name(s):
H2A-clustered histone 18Imported
H2A-clustered histone 19Imported
Histone H2A.2
Histone H2A/o
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:H2AC18Imported
Synonyms:H2AFO, HIST2H2AA, HIST2H2AA3Imported
AND
Name:H2AC19
Synonyms:HIST2H2AA4Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

More...HGNCi		HGNC:4736, H2AC18
HGNC:29668, H2AC19

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		142720, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q6FI13

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000203812.2
HostDB:ENSG00000272196.2

<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

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%5Fand%5Fbiotech%5Fsection">'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

More...DisGeNETi		723790
8337

Open Targets

More...OpenTargetsi		ENSG00000272196

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA29113

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q6FI13, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		HIST2H2AA4

Domain mapping of disease mutations (DMDM)

More...DMDMi		74757558

<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%5Fprocessing%5Fsection">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 methionineiRemoved2 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000552322 – 130Histone H2A type 2-AAdd 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-acetylserine2 Publications1
Modified residuei2Phosphoserine; by RPS6KA51 Publication1
Modified residuei4Citrulline; alternate1 Publication1
Modified residuei4Symmetric dimethylarginine; by PRMT5; alternateBy similarity1
Modified residuei6N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei6N6-acetyllysine; alternate1 Publication1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternate1 Publication1
Modified residuei10N6-(beta-hydroxybutyryl)lysine; alternate1 Publication1
Modified residuei10N6-lactoyllysine; alternateBy similarity1
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%5Fprocessing%5Fsection">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-glutaryllysine; alternate1 Publication1
Modified residuei96N6-succinyllysine; alternate1 Publication1
Modified residuei100N6-glutaryllysine1 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 residuei119N6-glutaryllysine; alternate1 Publication1
Modified residuei120N6-crotonyllysine; alternate1 Publication1
Modified residuei120N6-glutaryllysine; alternate1 Publication1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate5 Publications
Modified residuei121Phosphothreonine; by DCAF12 Publications1
Modified residuei126N6-crotonyllysine; alternate1 Publication1
Modified residuei126N6-glutaryllysine; alternate1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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, TRIM37 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 TRIM37 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.13 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.5 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
Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.By similarity

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q6FI13

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q6FI13

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q6FI13

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q6FI13

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

More...PaxDbi		Q6FI13

PeptideAtlas

More...PeptideAtlasi		Q6FI13

PRoteomics IDEntifications database

More...PRIDEi		Q6FI13

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		66294

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q6FI13

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q6FI13

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

More...PhosphoSitePlusi		Q6FI13

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q6FI13

<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

More...Bgeei		ENSG00000203812, Expressed in stomach and 113 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q6FI13, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000203812, Tissue enhanced (bone)
ENSG00000272196, Group enriched (blood, lymphoid tissue)

<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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		113933, 48 interactors
593221, 22 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q6FI13

Database of interacting proteins

More...DIPi		DIP-33167N

Protein interaction database and analysis system

More...IntActi		Q6FI13, 32 interactors

Molecular INTeraction database

More...MINTi		Q6FI13

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000475814

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q6FI13, protein

<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

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

More...SMRi		Q6FI13

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 22DisorderedSequence analysisAdd BLAST22

<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

More...eggNOGi		KOG1756, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000156302

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_062828_3_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q6FI13

Identification of Orthologs from Complete Genome Data

More...OMAi		KTDSHKP

Database of Orthologous Groups

More...OrthoDBi		1504122at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q6FI13

TreeFam database of animal gene trees

More...TreeFami		TF300137

Family and domain databases

Conserved Domains Database

More...CDDi		cd00074, H2A, 1 hit

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

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00620, HISTONEH2A

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00414, H2A, 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
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q6FI13-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRGKQGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV 
        60         70         80         90        100
YMAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGK 
       110        120        130
VTIAQGGVLP NIQAVLLPKK TESHHKAKGK
Length:130
Mass (Da):14,095
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:i53AEDC6CE3FE8317
GO

<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 13997.9 Da. Determined by ESI. Monoisotopic with N-acetylserine.1 Publication

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
L19779 mRNA Translation: AAC24465.1
AY131971 Genomic DNA Translation: AAN59957.1
AK312163 mRNA Translation: BAG35097.1
CR536525 mRNA Translation: CAG38762.1
CR541872 mRNA Translation: CAG46670.1
AL591493 Genomic DNA Translation: CAI12562.1
AL591493 Genomic DNA Translation: CAI12565.1
CH878687 Genomic DNA Translation: EAW50859.1
BC096705 mRNA Translation: AAH96705.1
BC096739 mRNA Translation: AAH96739.1
BC098171 mRNA Translation: AAH98171.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS30849.1
CCDS934.1

Protein sequence database of the Protein Information Resource

More...PIRi		S06742

NCBI Reference Sequences

More...RefSeqi		NP_001035807.1, NM_001040874.1
NP_003507.1, NM_003516.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000369159; ENSP00000358155; ENSG00000203812
ENST00000607355; ENSP00000475814; ENSG00000272196

Database of genes from NCBI RefSeq genomes

More...GeneIDi		723790
8337

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:723790
hsa:8337

UCSC genome browser

More...UCSCi		uc001esw.4, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19779 mRNA Translation: AAC24465.1
AY131971 Genomic DNA Translation: AAN59957.1
AK312163 mRNA Translation: BAG35097.1
CR536525 mRNA Translation: CAG38762.1
CR541872 mRNA Translation: CAG46670.1
AL591493 Genomic DNA Translation: CAI12562.1
AL591493 Genomic DNA Translation: CAI12565.1
CH878687 Genomic DNA Translation: EAW50859.1
BC096705 mRNA Translation: AAH96705.1
BC096739 mRNA Translation: AAH96739.1
BC098171 mRNA Translation: AAH98171.1
CCDSiCCDS30849.1
CCDS934.1
PIRiS06742
RefSeqiNP_001035807.1, NM_001040874.1
NP_003507.1, NM_003516.2

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
6SE6electron microscopy3.50C/G1-130[»]
6SEEelectron microscopy4.20C/G1-130[»]
6SEFelectron microscopy3.70C/G1-130[»]
6SEGelectron microscopy3.10C/G1-130[»]
6Y5Delectron microscopy4.10C/G/O/S1-130[»]
7JZVelectron microscopy3.90N/n2-130[»]
SMRiQ6FI13
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi113933, 48 interactors
593221, 22 interactors
CORUMiQ6FI13
DIPiDIP-33167N
IntActiQ6FI13, 32 interactors
MINTiQ6FI13
STRINGi9606.ENSP00000475814

PTM databases

iPTMnetiQ6FI13
PhosphoSitePlusiQ6FI13
SwissPalmiQ6FI13

Genetic variation databases

BioMutaiHIST2H2AA4
DMDMi74757558

Proteomic databases

EPDiQ6FI13
jPOSTiQ6FI13
MassIVEiQ6FI13
MaxQBiQ6FI13
PaxDbiQ6FI13
PeptideAtlasiQ6FI13
PRIDEiQ6FI13
ProteomicsDBi66294
TopDownProteomicsiQ6FI13

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		73310, 85 antibodies
75563, 65 antibodies

The DNASU plasmid repository

More...DNASUi		8337

Genome annotation databases

EnsembliENST00000369159; ENSP00000358155; ENSG00000203812
ENST00000607355; ENSP00000475814; ENSG00000272196
GeneIDi723790
8337
KEGGihsa:723790
hsa:8337
UCSCiuc001esw.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		723790
8337
DisGeNETi723790
8337

GeneCards: human genes, protein and diseases

More...GeneCardsi		H2AC18
H2AC19
HGNCiHGNC:4736, H2AC18
HGNC:29668, H2AC19
HPAiENSG00000203812, Tissue enhanced (bone)
ENSG00000272196, Group enriched (blood, lymphoid tissue)
MIMi142720, gene
neXtProtiNX_Q6FI13
OpenTargetsiENSG00000272196
PharmGKBiPA29113
VEuPathDBiHostDB:ENSG00000203812.2
HostDB:ENSG00000272196.2

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1756, Eukaryota
GeneTreeiENSGT00940000156302
HOGENOMiCLU_062828_3_1_1
InParanoidiQ6FI13
OMAiKTDSHKP
OrthoDBi1504122at2759
PhylomeDBiQ6FI13
TreeFamiTF300137

Enzyme and pathway databases

PathwayCommonsiQ6FI13
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-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-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-9609690, HCMV Early Events
R-HSA-9610379, HCMV Late Events
R-HSA-9616222, Transcriptional regulation of granulopoiesis
R-HSA-9670095, Inhibition of DNA recombination at telomere
R-HSA-977225, Amyloid fiber formation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		723790, 71 hits in 533 CRISPR screens
8337, 195 hits in 888 CRISPR screens

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

More...ChiTaRSi		HIST2H2AA3, human
HIST2H2AA4, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		HIST2H2AA3
PharosiQ6FI13, Tbio

Protein Ontology

More...PROi		PR:Q6FI13
RNActiQ6FI13, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000203812, Expressed in stomach and 113 other tissues
GenevisibleiQ6FI13, 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

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 nameiH2A2A_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: Q6FI13
Secondary accession number(s): B2R5F0, P20670
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 174 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, Reference proteome

Documents

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