Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27661

- H2AX_MOUSE

UniProt

P27661 - H2AX_MOUSE

Protein

Histone H2AX

Gene

H2afx

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    GO - Molecular functioni

    1. damaged DNA binding Source: MGI
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA repair Source: MGI
    2. double-strand break repair via homologous recombination Source: MGI
    3. meiotic nuclear division Source: UniProtKB-KW
    4. nucleosome assembly Source: InterPro
    5. spermatogenesis Source: MGI

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA recombination, DNA repair, Meiosis

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198626. Meiotic synapsis.
    REACT_198629. Meiotic recombination.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:102688. H2afx.

    Subcellular locationi

    GO - Cellular componenti

    1. chromatin Source: MGI
    2. chromosome Source: UniProtKB
    3. chromosome, telomeric region Source: Ensembl
    4. condensed nuclear chromosome Source: MGI
    5. male germ cell nucleus Source: MGI
    6. nuclear chromatin Source: MGI
    7. nucleoplasm Source: Reactome
    8. nucleosome Source: UniProtKB-KW
    9. nucleus Source: UniProtKB
    10. replication fork Source: MGI
    11. site of double-strand break Source: MGI
    12. XY body Source: MGI

    Keywords - Cellular componenti

    Chromosome, Nucleosome core, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi6 – 61K → A: No effect on radiosensitivity; when associated with A-10, A-14 and A-16. 1 Publication
    Mutagenesisi10 – 101K → A: No effect on radiosensitivity; when associated with A-6, A-14 and A-16. 1 Publication
    Mutagenesisi14 – 141K → A: No effect on radiosensitivity; when associated with A-6, A-10 and A-16. 1 Publication
    Mutagenesisi16 – 161K → A: No effect on radiosensitivity; when associated with A-6, A-10 and A-14. 1 Publication
    Mutagenesisi37 – 371K → 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
    Mutagenesisi37 – 371K → R: No effect on phosphorylation after DNA damage, but increased radiosensitivity. Further increase in radiosensitivity; when associated with A-140. 1 Publication
    Mutagenesisi119 – 1202KK → AA: Complete loss of ubiquitination and increased radiosensitivity.
    Mutagenesisi137 – 1371S → A: Increased genomic instability and radiosensitivity; when associated with A-140. 1 Publication
    Mutagenesisi140 – 1401S → 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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 143142Histone H2AXPRO_0000055243Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei6 – 61N6-acetyllysine1 Publication
    Modified residuei10 – 101N6-acetyllysine1 Publication
    Cross-linki14 – 14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki16 – 16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei37 – 371N6-acetyllysine; by CREBBP and EP3001 Publication
    Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei140 – 1401Phosphoserine; by ATM, ATR and PRKDC9 Publications
    Modified residuei143 – 1431Phosphotyrosine; by WSTF1 Publication

    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).3 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP27661.
    PRIDEiP27661.

    PTM databases

    PhosphoSiteiP27661.

    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

    BgeeiP27661.
    CleanExiMM_H2AFX.
    GenevestigatoriP27661.

    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. 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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Aifm1Q9Z0X13EBI-495621,EBI-773597
    Fancd2Q80V622EBI-495621,EBI-7268304

    Protein-protein interaction databases

    BioGridi200313. 8 interactions.
    IntActiP27661. 11 interactions.
    MINTiMINT-1864212.
    STRINGi10090.ENSMUSP00000051432.

    Structurei

    3D structure databases

    ProteinModelPortaliP27661.
    SMRiP27661. Positions 14-119.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi140 – 1412[ST]-Q motif

    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

    eggNOGiCOG5262.
    GeneTreeiENSGT00750000117535.
    HOGENOMiHOG000234652.
    HOVERGENiHBG009342.
    InParanoidiP27661.
    KOiK11251.
    OMAiNTCSISK.
    OrthoDBiEOG7M0NTR.
    PhylomeDBiP27661.
    TreeFamiTF300137.

    Family and domain databases

    Gene3Di1.10.20.10. 1 hit.
    InterProiIPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view]
    PfamiPF00125. Histone. 1 hit.
    [Graphical view]
    PRINTSiPR00620. HISTONEH2A.
    SMARTiSM00414. H2A. 1 hit.
    [Graphical view]
    SUPFAMiSSF47113. SSF47113. 1 hit.
    PROSITEiPS00046. HISTONE_H2A. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P27661-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRGKTGGK ARAKAKSRSS RAGLQFPVGR VHRLLRKGHY AERVGAGAPV    50
    YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGG 100
    VTIAQGGVLP NIQAVLLPKK SSATVGPKAP AVGKKASQAS QEY 143
    Length:143
    Mass (Da):15,143
    Last modified:January 23, 2007 - v2
    Checksum:iA3683760C13CC2B9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiMm.245931.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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. Positions 14-119.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200313. 8 interactions.
    IntActi P27661. 11 interactions.
    MINTi MINT-1864212.
    STRINGi 10090.ENSMUSP00000051432.

    PTM databases

    PhosphoSitei P27661.

    Proteomic databases

    PaxDbi P27661.
    PRIDEi P27661.

    Protocols and materials databases

    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 COG5262.
    GeneTreei ENSGT00750000117535.
    HOGENOMi HOG000234652.
    HOVERGENi HBG009342.
    InParanoidi P27661.
    KOi K11251.
    OMAi NTCSISK.
    OrthoDBi EOG7M0NTR.
    PhylomeDBi P27661.
    TreeFami TF300137.

    Enzyme and pathway databases

    Reactomei REACT_198626. Meiotic synapsis.
    REACT_198629. Meiotic recombination.
    REACT_200667. NoRC negatively regulates rRNA expression.
    REACT_214440. NoRC negatively regulates rRNA expression.
    REACT_27235. Meiotic Recombination.
    REACT_75800. Meiotic Synapsis.

    Miscellaneous databases

    NextBioi 287897.
    PROi P27661.
    SOURCEi Search...

    Gene expression databases

    Bgeei P27661.
    CleanExi MM_H2AFX.
    Genevestigatori P27661.

    Family and domain databases

    Gene3Di 1.10.20.10. 1 hit.
    InterProi IPR009072. Histone-fold.
    IPR007125. Histone_core_D.
    IPR002119. Histone_H2A.
    [Graphical view ]
    Pfami PF00125. Histone. 1 hit.
    [Graphical view ]
    PRINTSi PR00620. HISTONEH2A.
    SMARTi SM00414. H2A. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47113. SSF47113. 1 hit.
    PROSITEi PS00046. HISTONE_H2A. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
    9. Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140, TISSUE SPECIFICITY.
    10. Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-140.
    11. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. 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. 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. 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. Cited for: FUNCTION, PHOSPHORYLATION AT SER-140.
    26. 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.
    29. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiH2AX_MOUSE
    AccessioniPrimary (citable) accession number: P27661
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, 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

    External Data

    Dasty 3