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P16104 (H2AX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2AX

Short name=H2a/x
Alternative name(s):
Histone H2A.X
Gene names
Name:H2AFX
Synonyms:H2AX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length143 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.7 Ref.10 Ref.13 Ref.16

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. 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 MRE11A, 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. Ref.10 Ref.13 Ref.16 Ref.18 Ref.20

Subcellular location

Nucleus. Chromosome Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.18.

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-H2AX or H2AX139ph) in response to DNA double strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks, and may also occur during meiotic recombination events and 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) may occur at synaptonemal complexes during leptotene as an ATM-dependent response to the formation of programmed DSBs by SPO11. Ser-140 phosphorylation (H2AX139ph) may subsequently occurs at unsynapsed regions of both autosomes and the XY bivalent during zygotene, downstream of ATR and BRCA1 activation. 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) may occur at sites of DNA-recombination subsequent to activation of 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.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.26 Ref.27 Ref.31

Monoubiquitination of Lys-120 (H2AXK119ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression By similarity. 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.

Acetylation at Lys-37 increases in S and G2 phases. This modification has been proposed to play a role in DNA double-strand break repair By similarity.

Sequence similarities

Belongs to the histone H2A family.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA recombination
DNA repair
Meiosis
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from direct assay PubMed 17974976. Source: UniProtKB

DNA repair

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Inferred from direct assay PubMed 15149599. Source: BHF-UCL

double-strand break repair

Non-traceable author statement Ref.27. Source: UniProtKB

double-strand break repair via homologous recombination

Traceable author statement. Source: Reactome

meiotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

nucleosome assembly

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of DNA repair

Non-traceable author statement Ref.27. Source: UniProtKB

response to ionizing radiation

Non-traceable author statement Ref.27. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentXY body

Inferred from electronic annotation. Source: Ensembl

condensed nuclear chromosome

Inferred from electronic annotation. Source: Ensembl

male germ cell nucleus

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

nucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay PubMed 17974976. Source: UniProtKB

replication fork

Inferred from electronic annotation. Source: Ensembl

site of double-strand break

Inferred from direct assay PubMed 21270334. Source: MGI

   Molecular_functionDNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

enzyme binding

Inferred from physical interaction Ref.27. Source: UniProtKB

histone binding

Inferred from physical interaction Ref.27. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.20PubMed 17498979. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 143142Histone H2AX
PRO_0000055242

Regions

Motif140 – 1412[ST]-Q motif

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine By similarity
Modified residue61N6-acetyllysine By similarity
Modified residue101N6-acetyllysine By similarity
Modified residue371N6-acetyllysine By similarity
Modified residue1401Phosphoserine; by ATM, ATR and PRKDC Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.28 Ref.29 Ref.31
Modified residue1431Phosphotyrosine; by WSTF Ref.26 Ref.27
Cross-link14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.30
Cross-link16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.30
Cross-link120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Mutagenesis1411Q → N: Reduced phosphorylation of S-140 in response to DNA damage. Ref.5
Mutagenesis1431Y → F: Displays a reduced apoptotic response. S-140 phosphorylation is reduced. Ref.26 Ref.27
Sequence conflict781R → L in CAG33360. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P16104 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D4683775C2E6C3A9

FASTA14315,145
        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 
TSATVGPKAP SGGKKATQAS QEY 

« Hide

References

« Hide 'large scale' references
[1]"H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals."
Mannironi C., Bonner W.M., Hatch C.L.
Nucleic Acids Res. 17:9113-9126(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]NIEHS SNPs program
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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].
Tissue: Lung and Placenta.
[5]"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, MUTAGENESIS OF GLN-141.
[6]"Megabase chromatin domains involved in DNA double-strand breaks in vivo."
Rogakou E.P., Boon C., Redon C., Bonner W.M.
J. Cell Biol. 146:905-916(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[7]"A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage."
Paull T.T., Rogakou E.P., Yamazaki V., Kirchgessner C.U., Gellert M., Bonner W.M.
Curr. Biol. 10:886-895(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[8]"Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139."
Rogakou E.P., Nieves-Neira W., Boon C., Pommier Y., Bonner W.M.
J. Biol. Chem. 275:9390-9395(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-140.
[9]"Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress."
Ward I.M., Chen J.
J. Biol. Chem. 276:47759-47762(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[10]"NBS1 localizes to gamma-H2AX foci through interaction with the FHA/BRCT domain."
Kobayashi J., Tauchi H., Sakamoto S., Nakamura A., Morishima K., Matsuura S., Kobayashi T., Tamai K., Tanimoto K., Komatsu K.
Curr. Biol. 12:1846-1851(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NBN AND BRCA1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[11]"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: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[12]"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: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[13]"MDC1 is a mediator of the mammalian DNA damage checkpoint."
Stewart G.S., Wang B., Bignell C.R., Taylor A.M.R., Elledge S.J.
Nature 421:961-966(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDC1 AND TP53BP1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[14]"DNA-PK is activated by nucleosomes and phosphorylates H2AX within the nucleosomes in an acetylation-dependent manner."
Park E.-J., Chan D.W., Park J.-H., Oettinger M.A., Kwon J.
Nucleic Acids Res. 31:6819-6827(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-140.
[15]"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.
[16]"Mdc1 couples DNA double-strand break recognition by Nbs1 with its H2AX-dependent chromatin retention."
Lukas C., Melander F., Stucki M., Falck J., Bekker-Jensen S., Goldberg M., Lerenthal Y., Jackson S.P., Bartek J., Lukas J.
EMBO J. 23:2674-2683(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MDC1 AND NBN, SUBCELLULAR LOCATION.
[17]"Doxorubicin activates ATM-dependent phosphorylation of multiple downstream targets in part through the generation of reactive oxygen species."
Kurz E.U., Douglas P., Lees-Miller S.P.
J. Biol. Chem. 279:53272-53281(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-140.
[18]"Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II."
Mischo H.E., Hemmerich P., Grosse F., Zhang S.
J. Biol. Chem. 280:9586-9594(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DHX9, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
[19]"gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair."
Chowdhury D., Keogh M.-C., Ishii H., Peterson C.L., Buratowski S., Lieberman J.
Mol. Cell 20:801-809(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION.
[20]"Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[21]"RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins."
Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J., Lukas C., Lukas J.
Cell 131:887-900(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[22]"RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly."
Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.
Cell 131:901-914(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[23]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[24]"The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage."
Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K., Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M., Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L., Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R., Durocher D.
Cell 136:420-434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[25]"RNF168 binds and amplifies ubiquitin conjugates on damaged chromosomes to allow accumulation of repair proteins."
Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H., Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J., Lukas J., Lukas C.
Cell 136:435-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[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, MUTAGENESIS OF TYR-143.
[27]"Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions."
Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.
Nature 458:591-596(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-143, MUTAGENESIS OF TYR-143.
[28]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[29]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage signaling."
Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E., Vermeulen W., Marteijn J.A., Sixma T.K.
Cell 150:1182-1195(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
[31]"Specific recognition of phosphorylated tail of H2AX by the tandem BRCT domains of MCPH1 revealed by complex structure."
Shao Z., Li F., Sy S.M., Yan W., Zhang Z., Gong D., Wen B., Huen M.S., Gong Q., Wu J., Shi Y.
J. Struct. Biol. 177:459-468(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-143, PHOSPHORYLATION AT SER-140.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14850 mRNA. Translation: CAA32968.1.
CR457079 mRNA. Translation: CAG33360.1.
DQ015918 Genomic DNA. Translation: AAY22178.1.
BC004915 mRNA. Translation: AAH04915.1.
BC011694 mRNA. Translation: AAH11694.1.
BC013416 mRNA. Translation: AAH13416.1.
CCDSCCDS8410.1.
PIRS07631.
RefSeqNP_002096.1. NM_002105.2.
UniGeneHs.477879.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YDPX-ray1.90P78-86[»]
2AZMX-ray2.41C/D134-143[»]
2D31X-ray3.20C/F78-86[»]
2DYPX-ray2.50C78-86[»]
3SHVX-ray2.10C/D134-143[»]
3SQDX-ray2.15C/D134-143[»]
3SZMX-ray2.63I/J/K/L/M/N/O/P134-143[»]
3U3ZX-ray1.50B140-143[»]
ProteinModelPortalP16104.
SMRP16104. Positions 14-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109268. 205 interactions.
DIPDIP-33604N.
IntActP16104. 160 interactions.
MINTMINT-1338182.
STRING9606.ENSP00000364310.

PTM databases

PhosphoSiteP16104.

Polymorphism databases

DMDM121992.

Proteomic databases

MaxQBP16104.
PaxDbP16104.
PRIDEP16104.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375167; ENSP00000364310; ENSG00000188486.
ENST00000530167; ENSP00000434024; ENSG00000188486.
GeneID3014.
KEGGhsa:3014.
UCSCuc001pvg.3. human.

Organism-specific databases

CTD3014.
GeneCardsGC11M118998.
HGNCHGNC:4739. H2AFX.
HPACAB012264.
MIM601772. gene.
neXtProtNX_P16104.
PharmGKBPA29116.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5262.
HOGENOMHOG000234652.
HOVERGENHBG009342.
InParanoidP16104.
KOK11251.
OMASKGECIN.
OrthoDBEOG7M0NTR.
PhylomeDBP16104.
TreeFamTF300137.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

BgeeP16104.
CleanExHS_H2AFX.
GenevestigatorP16104.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
[Graphical view]
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00620. HISTONEH2A.
SMARTSM00414. H2A. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00046. HISTONE_H2A. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSH2AFX. human.
EvolutionaryTraceP16104.
GeneWikiH2AFX.
GenomeRNAi3014.
NextBio11948.
PROP16104.
SOURCESearch...

Entry information

Entry nameH2AX_HUMAN
AccessionPrimary (citable) accession number: P16104
Secondary accession number(s): Q4ZGJ7, Q6IAS5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM