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UniProtKB - P27661 (H2AX_MOUSE)

Entry version 201 (02 Jun 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Histone H2AX

Gene

H2ax

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation.

15 Publications

Miscellaneous

Haploinsufficient for the suppression of genomic instability. This phenotype is further exacerbated in the absence of TP53.

<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
Biological processCell cycle, DNA damage, DNA recombination, DNA repair, Meiosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-110330, Recognition and association of DNA glycosylase with site containing an affected purine
R-MMU-110331, Cleavage of the damaged purine
R-MMU-212300, PRC2 methylates histones and DNA
R-MMU-2299718, Condensation of Prophase Chromosomes
R-MMU-2559586, DNA Damage/Telomere Stress Induced Senescence
R-MMU-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693571, Nonhomologous End-Joining (NHEJ)
R-MMU-5693607, Processing of DNA double-strand break ends
R-MMU-606279, Deposition of new CENPA-containing nucleosomes at the centromere
R-MMU-69473, G2/M DNA damage checkpoint
R-MMU-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9670095, Inhibition of DNA recombination at telomere

<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 H2AX
Short name:
H2a/x
Alternative name(s):
Histone H2A.X
<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:H2axImported
Synonyms:H2a.x, H2afxImported, Hist5-2ax
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 9

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:102688, H2ax

<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>Mutagenesisi6K → A: No effect on radiosensitivity; when associated with A-10, A-14 and A-16. 1 Publication1
Mutagenesisi10K → A: No effect on radiosensitivity; when associated with A-6, A-14 and A-16. 1 Publication1
Mutagenesisi14K → A: No effect on radiosensitivity; when associated with A-6, A-10 and A-16. 1 Publication1
Mutagenesisi16K → A: No effect on radiosensitivity; when associated with A-6, A-10 and A-14. 1 Publication1
Mutagenesisi37K → A: Increased radiosensitivity. No effect on phosphorylation after DNA damage. No effect on Ser-140 phosphorylation, nor on TP53BP1 recruitment to DNA double-strand breaks. 1 Publication1
Mutagenesisi37K → R: No effect on phosphorylation after DNA damage, but increased radiosensitivity. Further increase in radiosensitivity; when associated with A-140. 1 Publication1
Mutagenesisi119 – 120KK → AA: Complete loss of ubiquitination and increased radiosensitivity. 1 Publication2
Mutagenesisi137S → A: Increased genomic instability and radiosensitivity; when associated with A-140. 1 Publication1
Mutagenesisi140S → A: Increased genomic instability and radiosensitivity; when associated with A-137. Reduced homologous recombination. No effect on Lys-40 acetylation. Further increase in radiosensitivity; when associated with R-37. 3 Publications1

<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 methionineiRemoved1 Publication
<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_00000552432 – 143Histone H2AXAdd BLAST142

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-acetylserine1 Publication1
Modified residuei2Phosphoserine1 Publication1
Modified residuei6N6-acetyllysineCombined sources1
Modified residuei10N6-acetyllysineCombined sources1
Modified residuei10N6-lactoyllysine; alternateBy similarity1
<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)By similarity
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei37N6-acetyllysine; by CREBBP and EP3001 Publication1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei121PhosphoserineCombined sources1
Modified residuei122PhosphoserineCombined sources1
Cross-linki128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei137PhosphoserineCombined sources1
Modified residuei140Phosphoserine; by ATM, ATR and PRKDCCombined sources9 Publications1
Modified residuei143Phosphotyrosine; by WSTF1 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

Phosphorylated on Ser-140 (to form gamma-H2AX or H2AX139ph) in response to DNA double strand breaks (DSBs) generated by exogenous genotoxic agents, by stalled replication forks, by meiotic recombination events and during immunoglobulin class switching in lymphocytes. Phosphorylation can extend up to several thousand nucleosomes from the actual site of the DSB and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Widespread phosphorylation may also serve to amplify the damage signal or aid repair of persistent lesions. Phosphorylation of Ser-140 (H2AX139ph) in response to ionizing radiation is mediated by both ATM and PRKDC while defects in DNA replication induce Ser-140 phosphorylation (H2AX139ph) subsequent to activation of ATR and PRKDC. Dephosphorylation of Ser-140 by PP2A is required for DNA DSB repair. In meiosis, Ser-140 phosphorylation (H2AX139ph) first occurs at synaptonemal complexes during leptotene and is an ATM-dependent response to the formation of programmed DSBs by SPO11. Ser-140 phosphorylation (H2AX139ph) subsequently occurs at unsynapsed regions of both autosomes and the XY bivalent during zygotene and is ATR- and BRCA1-dependent. Ser-140 phosphorylation (H2AX139ph) may also be required for transcriptional repression of unsynapsed chromatin and meiotic sex chromosome inactivation (MSCI), whereby the X and Y chromosomes condense in pachytene to form the heterochromatic XY-body. During immunoglobulin class switch recombination in lymphocytes, Ser-140 phosphorylation (H2AX139ph) at sites of DNA-recombination requires the activation-induced cytidine deaminase AICDA. Phosphorylation at Tyr-143 (H2AXY142ph) by BAZ1B/WSTF determines the relative recruitment of either DNA repair or pro-apoptotic factors. Phosphorylation at Tyr-143 (H2AXY142ph) favors the recruitment of APBB1/FE65 and pro-apoptosis factors such as MAPK8/JNK1, triggering apoptosis. In contrast, dephosphorylation of Tyr-143 by EYA proteins (EYA1, EYA2, EYA3 or EYA4) favors the recruitment of MDC1-containing DNA repair complexes to the tail of phosphorylated Ser-140 (H2AX139ph).11 Publications
Monoubiquitination of Lys-120 (H2AXK119ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression. 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. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events (By similarity).By similarity
Acetylation at Lys-37 increases in S and G2 phases. This modification has been proposed to be important for DNA double-strand break repair (PubMed:20488183).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P27661

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P27661

MaxQB - The MaxQuant DataBase

More...MaxQBi		P27661

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

More...PaxDbi		P27661

PeptideAtlas

More...PeptideAtlasi		P27661

PRoteomics IDEntifications database

More...PRIDEi		P27661

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		271118

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P27661

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P27661

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

More...PhosphoSitePlusi		P27661

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P27661

<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

Most abundant in testis, thymus and spleen.1 Publication

<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

Synthesized in G1 as well as in S-phase.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000049932, Expressed in neocortex and 310 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P27661, MM

<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.

Interacts with numerous proteins required for DNA damage signaling and repair when phosphorylated on Ser-140. These include MDC1, TP53BP1, BRCA1 and the MRN complex, composed of MRE11, RAD50, and NBN. Interaction with the MRN complex is mediated at least in part by NBN.

Also interacts with DHX9/NDHII when phosphorylated on Ser-140 and MCPH1 when phosphorylated at Ser-140 or Tyr-143.

Interacts with ARRB2; the interaction is detected in the nucleus upon OR1D2 stimulation.

Interacts with WRAP53/TCAB1.

By similarity

<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		200313, 21 interactors

Protein interaction database and analysis system

More...IntActi		P27661, 14 interactors

Molecular INTeraction database

More...MINTi		P27661

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000051432

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P27661, 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

3D structure databases

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

More...SMRi		P27661

Database of comparative protein structure models

More...ModBasei		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
Regioni121 – 143DisorderedSequence analysisAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi140 – 141[ST]-Q motif2

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.

<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		ENSGT01020000230360

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_062828_3_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P27661

Identification of Orthologs from Complete Genome Data

More...OMAi		AXLEYLA

Database of Orthologous Groups

More...OrthoDBi		1504122at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P27661

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.

P27661-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRGKTGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGHY AERVGAGAPV 
        60         70         80         90        100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGG 
       110        120        130        140 
VTIAQGGVLP NIQAVLLPKK SSATVGPKAP AVGKKASQAS QEY
Length:143
Mass (Da):15,143
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:iA3683760C13CC2B9
GO

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
X58069 mRNA Translation: CAA41099.1
Z35401 Genomic DNA Translation: CAA84585.1
BC005468 mRNA Translation: AAH05468.1
BC010336 mRNA Translation: AAH10336.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS23105.1

Protein sequence database of the Protein Information Resource

More...PIRi		I48406

NCBI Reference Sequences

More...RefSeqi		NP_034566.1, NM_010436.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000052686; ENSMUSP00000051432; ENSMUSG00000049932

Database of genes from NCBI RefSeq genomes

More...GeneIDi		15270

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:15270

UCSC genome browser

More...UCSCi		uc009pcy.1, mouse

<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
X58069 mRNA Translation: CAA41099.1
Z35401 Genomic DNA Translation: CAA84585.1
BC005468 mRNA Translation: AAH05468.1
BC010336 mRNA Translation: AAH10336.1
CCDSiCCDS23105.1
PIRiI48406
RefSeqiNP_034566.1, NM_010436.2

3D structure databases

SMRiP27661
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi200313, 21 interactors
IntActiP27661, 14 interactors
MINTiP27661
STRINGi10090.ENSMUSP00000051432

PTM databases

iPTMnetiP27661
PhosphoSitePlusiP27661
SwissPalmiP27661

Proteomic databases

EPDiP27661
jPOSTiP27661
MaxQBiP27661
PaxDbiP27661
PeptideAtlasiP27661
PRIDEiP27661
ProteomicsDBi271118
TopDownProteomicsiP27661

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3220, 1521 antibodies

The DNASU plasmid repository

More...DNASUi		15270

Genome annotation databases

EnsembliENSMUST00000052686; ENSMUSP00000051432; ENSMUSG00000049932
GeneIDi15270
KEGGimmu:15270
UCSCiuc009pcy.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3014
MGIiMGI:102688, H2ax

Phylogenomic databases

eggNOGiKOG1756, Eukaryota
GeneTreeiENSGT01020000230360
HOGENOMiCLU_062828_3_1_1
InParanoidiP27661
OMAiAXLEYLA
OrthoDBi1504122at2759
PhylomeDBiP27661
TreeFamiTF300137

Enzyme and pathway databases

ReactomeiR-MMU-110330, Recognition and association of DNA glycosylase with site containing an affected purine
R-MMU-110331, Cleavage of the damaged purine
R-MMU-212300, PRC2 methylates histones and DNA
R-MMU-2299718, Condensation of Prophase Chromosomes
R-MMU-2559586, DNA Damage/Telomere Stress Induced Senescence
R-MMU-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693571, Nonhomologous End-Joining (NHEJ)
R-MMU-5693607, Processing of DNA double-strand break ends
R-MMU-606279, Deposition of new CENPA-containing nucleosomes at the centromere
R-MMU-69473, G2/M DNA damage checkpoint
R-MMU-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9670095, Inhibition of DNA recombination at telomere

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		15270, 9 hits in 53 CRISPR screens

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

More...ChiTaRSi		H2afx, mouse

Protein Ontology

More...PROi		PR:P27661
RNActiP27661, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000049932, Expressed in neocortex and 310 other tissues
GenevisibleiP27661, MM

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 nameiH2AX_MOUSE
<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: P27661
<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: August 1, 1992
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 201 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

<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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families
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