H2afx

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.

GO - Molecular functionⁱ

damaged DNA binding
Source: MGI
Inferred from direct assayⁱ
- 11934988
enzyme binding Source: MGI
histone binding Source: MGI
protein heterodimerization activity Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cellular response to DNA damage stimulus Source: UniProtKB
cellular response to gamma radiation Source: MGI
cellular senescence Source: Ensembl
cerebral cortex development Source: Ensembl
chromatin silencing Source: GO_Central
DNA repair
Source: MGI
Inferred from direct assayⁱ
- 15364958
double-strand break repair via homologous recombination
Source: MGI
Inferred from mutant phenotypeⁱ
- 11934988
meiotic cell cycle Source: UniProtKB-KW
spermatogenesis
Source: MGI
Inferred from mutant phenotypeⁱ
- 11934988

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding
Biological process	Cell cycle, DNA damage, DNA recombination, DNA repair, Meiosis

Enzyme and pathway databases

Reactomeⁱ	R-MMU-171306 Packaging Of Telomere Ends R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex R-MMU-212300 PRC2 methylates histones and DNA R-MMU-2299718 Condensation of Prophase Chromosomes R-MMU-2559580 Oxidative Stress Induced Senescence R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP) R-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence R-MMU-3214858 RMTs methylate histone arginines R-MMU-427359 SIRT1 negatively regulates rRNA expression R-MMU-427413 NoRC negatively regulates rRNA expression R-MMU-5250924 B-WICH complex positively regulates rRNA expression R-MMU-5578749 Transcriptional regulation by small RNAs R-MMU-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 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-606279 Deposition of new CENPA-containing nucleosomes at the centromere R-MMU-69473 G2/M DNA damage checkpoint R-MMU-73728 RNA Polymerase I Promoter Opening R-MMU-73777 RNA Polymerase I Chain Elongation R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-MMU-9018519 Estrogen-dependent gene expression

Reactomeⁱ

R-MMU-171306 Packaging Of Telomere Ends
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-212300 PRC2 methylates histones and DNA
R-MMU-2299718 Condensation of Prophase Chromosomes
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence
R-MMU-3214858 RMTs methylate histone arginines
R-MMU-427359 SIRT1 negatively regulates rRNA expression
R-MMU-427413 NoRC negatively regulates rRNA expression
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5578749 Transcriptional regulation by small RNAs
R-MMU-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
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-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-MMU-69473 G2/M DNA damage checkpoint
R-MMU-73728 RNA Polymerase I Promoter Opening
R-MMU-73777 RNA Polymerase I Chain Elongation
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9018519 Estrogen-dependent gene expression

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Histone H2AX Short name: H2a/x Alternative name(s): Histone H2A.X
Gene namesⁱ	Name:H2afx Synonyms:H2a.x, H2ax, Hist5-2ax
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 9

Organism-specific databases

MGIⁱ	MGI:102688 H2afx

Keywords - Cellular componentⁱ

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	6	K → A: No effect on radiosensitivity; when associated with A-10, A-14 and A-16. 1 Publication	1
Mutagenesisⁱ	10	K → A: No effect on radiosensitivity; when associated with A-6, A-14 and A-16. 1 Publication	1
Mutagenesisⁱ	14	K → A: No effect on radiosensitivity; when associated with A-6, A-10 and A-16. 1 Publication	1
Mutagenesisⁱ	16	K → A: No effect on radiosensitivity; when associated with A-6, A-10 and A-14. 1 Publication	1
Mutagenesisⁱ	37	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. 1 Publication	1
Mutagenesisⁱ	37	K → R: No effect on phosphorylation after DNA damage, but increased radiosensitivity. Further increase in radiosensitivity; when associated with A-140. 1 Publication	1
Mutagenesisⁱ	119 – 120	KK → AA: Complete loss of ubiquitination and increased radiosensitivity. 1 Publication	2
Mutagenesisⁱ	137	S → A: Increased genomic instability and radiosensitivity; when associated with A-140. 1 Publication	1
Mutagenesisⁱ	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. 3 Publications	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000055243	2 – 143	Histone H2AXAdd BLAST		142

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	2	N-acetylserine1 Publication	1
Modified residueⁱ	2	Phosphoserine1 Publication	1
Modified residueⁱ	6	N6-acetyllysineCombined sources	1
Modified residueⁱ	10	N6-acetyllysineCombined sources	1
Cross-linkⁱ	14	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linkⁱ	16	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residueⁱ	37	N6-acetyllysine; by CREBBP and EP3001 Publication	1
Cross-linkⁱ	120	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residueⁱ	121	PhosphoserineCombined sources	1
Modified residueⁱ	122	PhosphoserineCombined sources	1
Cross-linkⁱ	128	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linkⁱ	135	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	137	PhosphoserineCombined sources	1
Modified residueⁱ	140	Phosphoserine; by ATM, ATR and PRKDCCombined sources9 Publications	1
Modified residueⁱ	143	Phosphotyrosine; by WSTF1 Publication	1

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

EPDⁱ	P27661
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P27661
PaxDbⁱ	P27661
PeptideAtlas More...PeptideAtlasⁱ	P27661
PRIDEⁱ	P27661
TopDownProteomicsⁱ	P27661

PTM databases

iPTMnetⁱ	P27661
PhosphoSitePlusⁱ	P27661

Expressionⁱ

Tissue specificityⁱ

Most abundant in testis, thymus and spleen.1 Publication

Developmental stageⁱ

Synthesized in G1 as well as in S-phase.

Gene expression databases

Bgeeⁱ	ENSMUSG00000049932 Expressed in 288 organ(s), highest expression level in neocortex
CleanExⁱ	MM_H2AFX
Genevisibleⁱ	P27661 MM

Interactionⁱ

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

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Aifm1	Q9Z0X1	3	EBI-495621,EBI-773597
Fancd2	Q80V62	2	EBI-495621,EBI-7268304

GO - Molecular functionⁱ

enzyme binding Source: MGI
histone binding Source: MGI
protein heterodimerization activity Source: InterPro

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	200313, 14 interactors
IntActⁱ	P27661, 13 interactors
Molecular INTeraction database More...MINTⁱ	P27661
STRINGⁱ	10090.ENSMUSP00000051432

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P27661
SMRⁱ	P27661
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	140 – 141	[ST]-Q motif		2

Domainⁱ

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

Sequence similaritiesⁱ

Belongs to the histone H2A family.Curated

Phylogenomic databases

eggNOGⁱ	KOG1756 Eukaryota COG5262 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00910000143981
HOGENOMⁱ	HOG000234652
HOVERGENⁱ	HBG009342
InParanoidⁱ	P27661
KEGG Orthology (KO) More...KOⁱ	K11251
OMAⁱ	AXLEYLA
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0XGD
PhylomeDBⁱ	P27661
TreeFamⁱ	TF300137

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00074 H2A, 1 hit
Gene3Dⁱ	1.10.20.10, 1 hit
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
PRINTSⁱ	PR00620 HISTONEH2A
SMARTⁱ	View protein in SMART SM00414 H2A, 1 hit
SUPFAMⁱ	SSF47113 SSF47113, 1 hit
PROSITEⁱ	View protein in PROSITE PS00046 HISTONE_H2A, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P27661-1 [UniParc]FASTA Add 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

Checksum:ⁱA3683760C13CC2B9

GO

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS23105.1
PIRⁱ	I48406
NCBI Reference Sequences More...RefSeqⁱ	NP_034566.1, NM_010436.2
UniGeneⁱ	Mm.245931

Genome annotation databases

Ensemblⁱ	ENSMUST00000052686; ENSMUSP00000051432; ENSMUSG00000049932
GeneIDⁱ	15270
KEGGⁱ	mmu:15270
UCSC genome browser More...UCSCⁱ	uc009pcy.1 mouse

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P27661	Histone H2AX	)	HUMAN		143	UniRef90_P16104
Histone H2A		CALJA		143
Histone H2A		MACMU		143
Histone H2A		PANTR		143
Histone H2A		MACFA		143
+45

Protein	Similar proteins		Species	Score	Length	Source
P27661	Histone H2AX	)	HUMAN		143	UniRef50_P16104
Histone H2A.1		CANAL		132
Histone H2A.2	)	YEAST		132
Histone H2A.2		ASHGO		131
Histone H2A.2		CANGA		131
+806

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
CCDSⁱ	CCDS23105.1
PIRⁱ	I48406
RefSeqⁱ	NP_034566.1, NM_010436.2
UniGeneⁱ	Mm.245931

3D structure databases

ProteinModelPortalⁱ	P27661
SMRⁱ	P27661
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	200313, 14 interactors
IntActⁱ	P27661, 13 interactors
MINTⁱ	P27661
STRINGⁱ	10090.ENSMUSP00000051432

PTM databases

iPTMnetⁱ	P27661
PhosphoSitePlusⁱ	P27661

Proteomic databases

EPDⁱ	P27661
MaxQBⁱ	P27661
PaxDbⁱ	P27661
PeptideAtlasⁱ	P27661
PRIDEⁱ	P27661
TopDownProteomicsⁱ	P27661

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000052686; ENSMUSP00000051432; ENSMUSG00000049932
GeneIDⁱ	15270
KEGGⁱ	mmu:15270
UCSCⁱ	uc009pcy.1 mouse

Organism-specific databases

CTDⁱ	3014
MGIⁱ	MGI:102688 H2afx

Phylogenomic databases

eggNOGⁱ	KOG1756 Eukaryota COG5262 LUCA
GeneTreeⁱ	ENSGT00910000143981
HOGENOMⁱ	HOG000234652
HOVERGENⁱ	HBG009342
InParanoidⁱ	P27661
KOⁱ	K11251
OMAⁱ	AXLEYLA
OrthoDBⁱ	EOG091G0XGD
PhylomeDBⁱ	P27661
TreeFamⁱ	TF300137

Enzyme and pathway databases

Reactomeⁱ	R-MMU-171306 Packaging Of Telomere Ends R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex R-MMU-212300 PRC2 methylates histones and DNA R-MMU-2299718 Condensation of Prophase Chromosomes R-MMU-2559580 Oxidative Stress Induced Senescence R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP) R-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence R-MMU-3214858 RMTs methylate histone arginines R-MMU-427359 SIRT1 negatively regulates rRNA expression R-MMU-427413 NoRC negatively regulates rRNA expression R-MMU-5250924 B-WICH complex positively regulates rRNA expression R-MMU-5578749 Transcriptional regulation by small RNAs R-MMU-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 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-606279 Deposition of new CENPA-containing nucleosomes at the centromere R-MMU-69473 G2/M DNA damage checkpoint R-MMU-73728 RNA Polymerase I Promoter Opening R-MMU-73777 RNA Polymerase I Chain Elongation R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-MMU-9018519 Estrogen-dependent gene expression

Reactomeⁱ

R-MMU-171306 Packaging Of Telomere Ends
R-MMU-201722 Formation of the beta-catenin:TCF transactivating complex
R-MMU-212300 PRC2 methylates histones and DNA
R-MMU-2299718 Condensation of Prophase Chromosomes
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-2559586 DNA Damage/Telomere Stress Induced Senescence
R-MMU-3214858 RMTs methylate histone arginines
R-MMU-427359 SIRT1 negatively regulates rRNA expression
R-MMU-427413 NoRC negatively regulates rRNA expression
R-MMU-5250924 B-WICH complex positively regulates rRNA expression
R-MMU-5578749 Transcriptional regulation by small RNAs
R-MMU-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
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-606279 Deposition of new CENPA-containing nucleosomes at the centromere
R-MMU-69473 G2/M DNA damage checkpoint
R-MMU-73728 RNA Polymerase I Promoter Opening
R-MMU-73777 RNA Polymerase I Chain Elongation
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-MMU-9018519 Estrogen-dependent gene expression

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P27661
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000049932 Expressed in 288 organ(s), highest expression level in neocortex
CleanExⁱ	MM_H2AFX
Genevisibleⁱ	P27661 MM

Family and domain databases

CDDⁱ	cd00074 H2A, 1 hit
Gene3Dⁱ	1.10.20.10, 1 hit
InterProⁱ	View protein in InterPro IPR009072 Histone-fold IPR002119 Histone_H2A IPR007125 Histone_H2A/H2B/H3 IPR032454 Histone_H2A_C IPR032458 Histone_H2A_CS
Pfamⁱ	View protein in Pfam PF00125 Histone, 1 hit PF16211 Histone_H2A_C, 1 hit
PRINTSⁱ	PR00620 HISTONEH2A
SMARTⁱ	View protein in SMART SM00414 H2A, 1 hit
SUPFAMⁱ	SSF47113 SSF47113, 1 hit
PROSITEⁱ	View protein in PROSITE PS00046 HISTONE_H2A, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	H2AX_MOUSE
Accessionⁱ	P27661Primary (citable) accession number: P27661
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
	Last sequence update:	January 23, 2007
	Last modified:	October 10, 2018
	This is version 181 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P27661 (H2AX_MOUSE)

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Histone H2AX

Select a section on the left to see content.

<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

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

Nucleus

Other locations

Cytoskeleton

Nucleus

Other locations

Keywords - Cellular componenti

<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

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<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

<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

GO - Molecular functioni

Protein-protein interaction databases

<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

<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

Motif

<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

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<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

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

Miscellaneous databases

Gene expression databases

Family and domain databases

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<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

Documents

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ