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P27661

- H2AX_MOUSE

UniProt

P27661 - H2AX_MOUSE

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Protein
Histone H2AX
Gene
H2afx, H2a.x, H2ax, Hist5-2ax
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Nucleus. Chromosome 8 Publications

GO - Cellular componenti

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

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 – 11Removed
Chaini2 – 143142Histone H2AX
PRO_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) Inferred
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.
Acetylation at Lys-37 increases in S and G2 phases. This modification has been proposed to be important for DNA double-strand break repair (1 Publication).2 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.

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.

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

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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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 141 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

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