Histone H2A.x - Mus musculus (Mouse)

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P27661 (H2AX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 128. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Histone H2A.x
Short name=H2a/x

Gene names

Name:	H2afx
Synonyms:	H2a.x, H2ax, Hist5-2ax

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	143 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25
Subunit structure	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. May interact with numerous proteins required for DNA damage signaling and repair when phosphorylated on Ser-140. These include MDC1, TP53BP1 and the MRN complex, composed of MRE11A, RAD50, and NBN. Interaction with the MRN complex is likely mediated at least in part by NBN. May also interact with DHX9/NDHII when phosphorylated on Ser-140 and MCPH1 when phosphorylated at Ser-140 or Tyr-143.
Subcellular location	Nucleus. Chromosome Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.20 Ref.21 Ref.28.
Tissue specificity	Most abundant in testis, thymus and spleen. Ref.9
Developmental stage	Synthesized in G1 as well as in S-phase.
Domain	The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.
Post-translational modification	Phosphorylated on Ser-140 (to form gamma-H2AFX 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). Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.17 Ref.18 Ref.20 Ref.25 Ref.26 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. Acetylation at Lys-37 increases in S and G2 phases. This modification has been proposed to be important for DNA double-strand break repair (Ref.27).
Miscellaneous	Haploinsufficient for the suppression of genomic instability. This phenotype is further exacerbated in the absence of TP53.
Sequence similarities	Belongs to the histone H2A family.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA recombination DNA repair Meiosis
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	double-strand break repair via homologous recombination Inferred from mutant phenotype Ref.12. Source: MGI meiosis Inferred from electronic annotation. Source: UniProtKB-KW nucleosome assembly Inferred from electronic annotation. Source: InterPro spermatogenesis Inferred from mutant phenotype Ref.12. Source: MGI
Cellular_component	XY body Inferred from direct assay PubMed 18070917 PubMed 18316482 PubMed 19074312. Source: MGI chromosome, telomeric region Inferred from electronic annotation. Source: Compara condensed nuclear chromosome Inferred from direct assay PubMed 20551173. Source: MGI male germ cell nucleus Inferred from direct assay PubMed 17696610. Source: MGI nuclear chromatin Inferred from direct assay PubMed 17696610. Source: MGI nucleoplasm Traceable author statement. Source: Reactome nucleosome Inferred from electronic annotation. Source: UniProtKB-KW replication fork Inferred from direct assay PubMed 15364958. Source: MGI
Molecular_function	damaged DNA binding Inferred from direct assay Ref.12. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Aifm1	Q9Z0X1	3	EBI-495621,EBI-773597

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 143

142

Histone H2A.x

PRO_0000055243

Regions

Motif

140 – 141

[ST]-Q motif

Amino acid modifications

Modified residue

N-acetylserine Ref.5

Modified residue

Phosphoserine Ref.5

Modified residue

N6-acetyllysine; by CREBBP and EP300 Ref.27

Modified residue

140

Phosphoserine; by ATM, ATR and PRKDC Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.17 Ref.18 Ref.20 Ref.25

Modified residue

143

Phosphotyrosine; by WSTF Ref.26

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

120

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Experimental info

Mutagenesis

K → A: No effect on radiosensitivity; when associated with A-10, A-14 and A-16. Ref.27

Mutagenesis

K → A: No effect on radiosensitivity; when associated with A-6, A-14 and A-16. Ref.27

Mutagenesis

K → A: No effect on radiosensitivity; when associated with A-6, A-10 and A-16. Ref.27

Mutagenesis

K → A: No effect on radiosensitivity; when associated with A-6, A-10 and A-14. Ref.27

Mutagenesis

K → 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. Ref.27

Mutagenesis

K → R: No effect on phosphorylation after DNA damage, but increased radiosensitivity. Further increase in radiosensitivity; when associated with A-140. Ref.27

Mutagenesis

119 – 120

KK → AA: Complete loss of ubiquitination and increased radiosensitivity.

Mutagenesis

137

S → A: Increased genomic instability and radiosensitivity; when associated with A-140. Ref.14

Mutagenesis

140

S → 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. Ref.14 Ref.23 Ref.27

Sequences

Sequence

Length

Mass (Da)

Tools

P27661 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A3683760C13CC2B9
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FASTA

143

15,143

        10         20         30         40         50         60 
MSGRGKTGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGHY AERVGAGAPV YLAAVLEYLT 

        70         80         90        100        110        120 
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGG VTIAQGGVLP NIQAVLLPKK 

       130        140 
SSATVGPKAP AVGKKASQAS QEY

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Polyadenylated and 3' processed mRNAs are transcribed from the mouse histone H2A.X gene." Nagata T., Kato T., Morita T., Nozaki M., Kubota H., Yagi H., Matsushiro A. Nucleic Acids Res. 19:2441-2447(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: 129/Sv.
[2]	"Structure of the mouse H2A.X gene and physical linkage to the UPS locus on chromosome 9: assignment of the human H2A.X gene to 11q23 by sequence analysis." Porcher C., Grandchamp B. Genomics 25:312-313(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: C3H. Tissue: Placenta.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Mammary gland.
[4]	"Histone 2A, a heteromorphous family of eight protein species." West M.H.P., Bonner W.M. Biochemistry 19:3238-3245(1980) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
[5]	"Quantitative determination of histone modification. H2A acetylation and phosphorylation." Pantazis P., Bonner W.M. J. Biol. Chem. 256:4669-4675(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-2, ACETYLATION AT SER-2.
[6]	"DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139." Rogakou E.P., Pilch D.R., Orr A.H., Ivanova V.S., Bonner W.M. J. Biol. Chem. 273:5858-5868(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-140.
[7]	"ATM phosphorylates histone H2AX in response to DNA double-strand breaks." Burma S., Chen B.P., Murphy M., Kurimasa A., Chen D.J. J. Biol. Chem. 276:42462-42467(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[8]	"AID is required to initiate Nbs1/gamma-H2AX focus formation and mutations at sites of class switching." Petersen S., Casellas R., Reina-San-Martin B., Chen H.T., Difilippantonio M.J., Wilson P.C., Hanitsch L., Celeste A., Muramatsu M., Pilch D.R., Redon C., Ried T., Bonner W.M., Honjo T., Nussenzweig M.C., Nussenzweig A. Nature 414:660-665(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[9]	"Recombinational DNA double-strand breaks in mice precede synapsis." Mahadevaiah S.K., Turner J.M.A., Baudat F., Rogakou E.P., de Boer P., Blanco-Rodriguez J., Jasin M., Keeney S., Bonner W.M., Burgoyne P.S. Nat. Genet. 27:271-276(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140, TISSUE SPECIFICITY.
[10]	"DNA damage-induced G2-M checkpoint activation by histone H2AX and 53BP1." Fernandez-Capetillo O., Chen H.-T., Celeste A., Ward I., Romanienko P.J., Morales J.C., Naka K., Xia Z., Camerini-Otero R.D., Motoyama N., Carpenter P.B., Bonner W.M., Chen J., Nussenzweig A. Nat. Cell Biol. 4:993-997(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[11]	"Increased ionizing radiation sensitivity and genomic instability in the absence of histone H2AX." Bassing C.H., Chua K.F., Sekiguchi J., Suh H., Whitlow S.R., Fleming J.C., Monroe B.C., Ciccone D.N., Yan C., Vlasakova K., Livingston D.M., Ferguson D.O., Scully R., Alt F.W. Proc. Natl. Acad. Sci. U.S.A. 99:8173-8178(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"Genomic instability in mice lacking histone H2AX." Celeste A., Petersen S., Romanienko P.J., Fernandez-Capetillo O., Chen H.T., Sedelnikova O.A., Reina-San-Martin B., Coppola V., Meffre E., Difilippantonio M.J., Redon C., Pilch D.R., Olaru A., Eckhaus M., Camerini-Otero R.D., Tessarollo L., Livak F., Manova K. , Bonner W.M., Nussenzweig M.C., Nussenzweig A. Science 296:922-927(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Histone H2AX: a dosage-dependent suppressor of oncogenic translocations and tumors." Bassing C.H., Suh H., Ferguson D.O., Chua K.F., Manis J., Eckersdorff M., Gleason M., Bronson R., Lee C., Alt F.W. Cell 114:359-370(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"H2AX haploinsufficiency modifies genomic stability and tumor susceptibility." Celeste A., Difilippantonio S., Difilippantonio M.J., Fernandez-Capetillo O., Pilch D.R., Sedelnikova O.A., Eckhaus M., Ried T., Bonner W.M., Nussenzweig A. Cell 114:371-383(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-137 AND SER-140.
[15]	"H2AX is required for chromatin remodeling and inactivation of sex chromosomes in male mouse meiosis." Fernandez-Capetillo O., Mahadevaiah S.K., Celeste A., Romanienko P.J., Camerini-Otero R.D., Bonner W.M., Manova K., Burgoyne P., Nussenzweig A. Dev. Cell 4:497-508(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[16]	"Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX." Ward I.M., Minn K., Jorda K.G., Chen J. J. Biol. Chem. 278:19579-19582(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TP53BP1.
[17]	"Phosphorylation of histone H2AX and activation of Mre11, Rad50, and Nbs1 in response to replication-dependent DNA double-strand breaks induced by mammalian DNA topoisomerase I cleavage complexes." Furuta T., Takemura H., Liao Z.-Y., Aune G.J., Redon C., Sedelnikova O.A., Pilch D.R., Rogakou E.P., Celeste A., Chen H.T., Nussenzweig A., Aladjem M.I., Bonner W.M., Pommier Y. J. Biol. Chem. 278:20303-20312(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-140.
[18]	"H2AX regulates meiotic telomere clustering." Fernandez-Capetillo O., Liebe B., Scherthan H., Nussenzweig A. J. Cell Biol. 163:15-20(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-140.
[19]	"Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks." Celeste A., Fernandez-Capetillo O., Kruhlak M.J., Pilch D.R., Staudt D.W., Lee A., Bonner R.F., Bonner W.M., Nussenzweig A. Nat. Cell Biol. 5:675-679(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[20]	"ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation." Stiff T., O'Driscoll M., Rief N., Iwabuchi K., Loebrich M., Jeggo P.A. Cancer Res. 64:2390-2396(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[21]	"BRCA1, histone H2AX phosphorylation, and male meiotic sex chromosome inactivation." Turner J.M.A., Aprelikova O., Xu X., Wang R., Kim S., Chandramouli G.V.R., Barrett J.C., Burgoyne P.S., Deng C.-X. Curr. Biol. 14:2135-2142(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[22]	"A pathway of double-strand break rejoining dependent upon ATM, Artemis, and proteins locating to gamma-H2AX foci." Riballo E., Kuehne M., Rief N., Doherty A., Smith G.C.M., Recio M.-J., Reis C., Dahm K., Fricke A., Krempler A., Parker A.R., Jackson S.P., Gennery A., Jeggo P.A., Loebrich M. Mol. Cell 16:715-724(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"Control of sister chromatid recombination by histone H2AX." Xie A., Puget N., Shim I., Odate S., Jarzyna I., Bassing C.H., Alt F.W., Scully R. Mol. Cell 16:1017-1025(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF SER-140.
[24]	"Functional interaction of H2AX, NBS1, and p53 in ATM-dependent DNA damage responses and tumor suppression." Kang J., Ferguson D., Song H., Bassing C., Eckersdorff M., Alt F.W., Xu Y. Mol. Cell. Biol. 25:661-670(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[25]	"Silencing of unsynapsed meiotic chromosomes in the mouse." Turner J.M.A., Mahadevaiah S.K., Fernandez-Capetillo O., Nussenzweig A., Xu X., Deng C.-X., Burgoyne P.S. Nat. Genet. 37:41-47(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-140.
[26]	"WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity." Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A., Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P., Hofmann K., Patel D.J., Elledge S.J., Allis C.D. Nature 457:57-62(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-143.
[27]	"Acetylation of H2AX on lysine 36 plays a key role in the DNA double-strand break repair pathway." Jiang X., Xu Y., Price B.D. FEBS Lett. 584:2926-2930(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-37, MUTAGENESIS OF LYS-6; LYS-10; LYS-14; LYS-16; LYS-37; 119-LYS-LYS-120 AND SER-140.
[28]	"HORMAD2 is essential for synapsis surveillance during meiotic prophase via the recruitment of ATR activity." Kogo H., Tsutsumi M., Inagaki H., Ohye T., Kiyonari H., Kurahashi H. Genes Cells 17:897-912(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X58069 mRNA. Translation: CAA41099.1. Z35401 Genomic DNA. Translation: CAA84585.1. BC005468 mRNA. Translation: AAH05468.1. BC010336 mRNA. Translation: AAH10336.1.
IPI	IPI00230264.
PIR	I48406.
RefSeq	NP_034566.1. NM_010436.2.
UniGene	Mm.245931.
3D structure databases
ProteinModelPortal	P27661.
SMR	P27661. Positions 14-119.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27661. 2 interactions.
MINT	MINT-1864212.
STRING	10090.ENSMUSP00000051432.
PTM databases
PhosphoSite	P27661.
Proteomic databases
PaxDb	P27661.
PRIDE	P27661.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000052686; ENSMUSP00000051432; ENSMUSG00000049932.
GeneID	15270.
KEGG	mmu:15270.
Organism-specific databases
CTD	3014.
MGI	MGI:102688. H2afx.
Phylogenomic databases
eggNOG	COG5262.
GeneTree	ENSGT00690000101783.
HOGENOM	HOG000234652.
HOVERGEN	HBG009342.
InParanoid	P27661.
KO	K11251.
OMA	RRGHYAE.
OrthoDB	EOG4TXBTD.
Enzyme and pathway databases
Reactome	REACT_118161. Cell Cycle. REACT_120463. Meiosis. REACT_27235. Meiotic Recombination (mouse). REACT_75800. Meiotic Synapsis (mouse).
Gene expression databases
Bgee	P27661.
CleanEx	MM_H2AFX.
Genevestigator	P27661.
GermOnline	ENSMUSG00000049932. Mus musculus.
Family and domain databases
Gene3D	1.10.20.10. 1 hit.
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view]
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00620. HISTONEH2A.
SMART	SM00414. H2A. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00046. HISTONE_H2A. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	287897.
SOURCE	Search...

Entry information

Entry name

H2AX_MOUSE

Accession

Primary (citable) accession number: P27661

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents