LOCUS       NM_010436               1414 bp    mRNA    linear   ROD 25-FEB-2025
DEFINITION  Mus musculus H2A.X variant histone (H2ax), mRNA.
ACCESSION   NM_010436
VERSION     NM_010436.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (bases 1 to 1414)
  AUTHORS   Cho,S.H., Kim,J.H. and Kim,S.
  TITLE     Perturbed cell cycle phase-dependent positioning and nuclear
            migration of retinal progenitors along the apico-basal axis
            underlie global retinal disorganization in the LCA8-like mouse
            model
  JOURNAL   Dev Biol 517, 39-54 (2025)
   PUBMED   39284539
REFERENCE   2  (bases 1 to 1414)
  AUTHORS   Dias Mirandela,M., Zoch,A., Leismann,J., Webb,S., Berrens,R.V.,
            Valsakumar,D., Kabayama,Y., Auchynnikava,T., Schito,M.,
            Chowdhury,T., MacLeod,D., Xiang,X., Zou,J., Rappsilber,J.,
            Allshire,R.C., Voigt,P., Cook,A.G., Barau,J. and O'Carroll,D.
  TITLE     Two-factor authentication underpins the precision of the piRNA
            pathway
  JOURNAL   Nature 634 (8035), 979-985 (2024)
   PUBMED   39294378
REFERENCE   3  (bases 1 to 1414)
  AUTHORS   Dong,M.Z., Ouyang,Y.C., Gao,S.C., Gu,L.J., Guo,J.N., Sun,S.M.,
            Wang,Z.B. and Sun,Q.Y.
  TITLE     Protein phosphatase 4 maintains the survival of primordial
            follicles by regulating autophagy in oocytes
  JOURNAL   Cell Death Dis 15 (9), 658 (2024)
   PUBMED   39245708
  REMARK    Publication Status: Online-Only
REFERENCE   4  (bases 1 to 1414)
  AUTHORS   Nedomova,M., Haberecht-Muller,S., Moller,S., Venz,S.,
            Prochazkova,M., Prochazka,J., Sedlak,F., Chawengsaksophak,K.,
            Hammer,E., Kasparek,P., Adamek,M., Sedlacek,R., Konvalinka,J.,
            Kruger,E. and Grantz Saskova,K.
  TITLE     DDI2 protease controls embryonic development and inflammation via
            TCF11/NRF1
  JOURNAL   iScience 27 (10), 110893 (2024)
   PUBMED   39328932
  REMARK    Publication Status: Online-Only
REFERENCE   5  (bases 1 to 1414)
  AUTHORS   Wu,Y., Chen,S., Huang,G., Zhang,L., Zhong,L., Feng,Y., Wen,P. and
            Liu,J.
  TITLE     Transcriptome analysis reveals EBF1 ablation-induced injuries in
            cardiac system
  JOURNAL   Theranostics 14 (12), 4894-4915 (2024)
   PUBMED   39239522
  REMARK    Publication Status: Online-Only
REFERENCE   6  (bases 1 to 1414)
  AUTHORS   Shaytan,A.K., Landsman,D. and Panchenko,A.R.
  TITLE     Nucleosome adaptability conferred by sequence and structural
            variations in histone H2A-H2B dimers
  JOURNAL   Curr Opin Struct Biol 32, 48-57 (2015)
   PUBMED   25731851
  REMARK    Review article
REFERENCE   7  (bases 1 to 1414)
  AUTHORS   Yagi,H., Kato,T., Nagata,T., Habu,T., Nozaki,M., Matsushiro,A.,
            Nishimune,Y. and Morita,T.
  TITLE     Regulation of the mouse histone H2A.X gene promoter by the
            transcription factor E2F and CCAAT binding protein
  JOURNAL   J Biol Chem 270 (32), 18759-18765 (1995)
   PUBMED   7642525
REFERENCE   8  (bases 1 to 1414)
  AUTHORS   Nagata,T., Kato,T., Morita,T., Nozaki,M., Kubota,H., Yagi,H. and
            Matsushiro,A.
  TITLE     Polyadenylated and 3' processed mRNAs are transcribed from the
            mouse histone H2A.X gene
  JOURNAL   Nucleic Acids Res 19 (9), 2441-2447 (1991)
   PUBMED   2041781
REFERENCE   9  (bases 1 to 1414)
  AUTHORS   Pantazis,P. and Bonner,W.M.
  TITLE     Quantitative determination of histone modification. H2A acetylation
            and phosphorylation
  JOURNAL   J Biol Chem 256 (9), 4669-4675 (1981)
   PUBMED   7217105
REFERENCE   10 (bases 1 to 1414)
  AUTHORS   West,M.H. and Bonner,W.M.
  TITLE     Histone 2A, a heteromorphous family of eight protein species
  JOURNAL   Biochemistry 19 (14), 3238-3245 (1980)
   PUBMED   7407044
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC010336.1.
            
            On Jun 19, 2003 this sequence version replaced NM_010436.1.
            
            Summary: Histones are basic nuclear proteins that are responsible
            for the nucleosome structure of the chromosomal fiber in
            eukaryotes. Two molecules of each of the four core histones (H2A,
            H2B, H3, and H4) form an octamer, around which approximately 146 bp
            of DNA is wrapped in repeating units, called nucleosomes. The
            linker histone, H1, interacts with linker DNA between nucleosomes
            and functions in the compaction of chromatin into higher order
            structures. This gene encodes a replication-independent histone
            that is a member of the histone H2A family. [provided by RefSeq,
            Nov 2015].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript is intronless :: BC010336.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria          :: based on single protein-coding
                                               transcript
            replication-independent histone :: PMID: 25731851
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
FEATURES             Location/Qualifiers
     source          1..1414
                     /organism="Mus musculus"
                     /mol_type="mRNA"
                     /strain="FVB/N"
                     /db_xref="taxon:10090"
                     /chromosome="9"
                     /map="9 24.84 cM"
     gene            1..1414
                     /gene="H2ax"
                     /gene_synonym="gammaH2ax; H2A.X; H2afx; Hist5-2ax"
                     /note="H2A.X variant histone"
                     /db_xref="GeneID:15270"
                     /db_xref="MGI:MGI:102688"
     exon            1..1363
                     /gene="H2ax"
                     /gene_synonym="gammaH2ax; H2A.X; H2afx; Hist5-2ax"
                     /inference="alignment:Splign:2.1.0"
     CDS             48..479
                     /gene="H2ax"
                     /gene_synonym="gammaH2ax; H2A.X; H2afx; Hist5-2ax"
                     /note="histone H2A.x; H2a/x; histone 5 protein 2ax; H2A
                     histone family, member X"
                     /codon_start=1
                     /product="histone H2AX"
                     /protein_id="NP_034566.1"
                     /db_xref="CCDS:CCDS23105.1"
                     /db_xref="GeneID:15270"
                     /db_xref="MGI:MGI:102688"
                     /translation="MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERV
                     GAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVT
                     IAQGGVLPNIQAVLLPKKSSATVGPKAPAVGKKASQASQEY"
     regulatory      1329..1334
                     /regulatory_class="polyA_signal_sequence"
                     /gene="H2ax"
                     /gene_synonym="gammaH2ax; H2A.X; H2afx; Hist5-2ax"
                     /note="hexamer: ATTAAA"
     polyA_site      1363
                     /gene="H2ax"
                     /gene_synonym="gammaH2ax; H2A.X; H2afx; Hist5-2ax"
                     /note="major polyA site"
ORIGIN      
        1 gttcgtggtc tctcagcgtt gttcgcagct cttctacctc gtacactatg tccggacgcg
       61 gcaagaccgg cggcaaggcc cgcgccaagg ccaagtcgcg ctcttcacgc gccggccttc
      121 agttccctgt aggccgcgta caccggctgc tgcggaaagg ccactacgcc gagcgcgtgg
      181 gcgcaggcgc gccggtgtac ctggcagcgg tgctcgagta cctcactgcc gagatcctgg
      241 agctggcggg caacgcggcc cgcgacaaca agaagacgcg catcatcccg cgccacctgc
      301 agctggccat ccgcaacgac gaggagctca acaagctgct gggcggcgtg accatcgcgc
      361 agggcggcgt cctgcccaac atccaggccg tgctgctgcc caagaagagc agcgccaccg
      421 tggggcccaa ggcgccggcg gtcggcaaga aggcctcgca ggcctctcag gagtactgag
      481 ggggcccgcg ccgaggccgc ccagccctcc ccacacctcc acaaaggccc ttttaagggc
      541 caccacctcc ctcacagaaa gagctgagcc acttcgggct gcggcggctt gccgcgtccc
      601 catcctttct ctttccctcc tctcccctcc ccgccctcgc gccactcttc cccttacccc
      661 gcacggcctc cggttctgcc acggaggacg cgggcgccgc ggcacctgcc catcccggag
      721 ctcgtgacat cgcttcgccg ttctcggttg tggacgacgg ctccgtgcgg agaggctgcg
      781 gcgccttccc ggagtctcgg cccctcgctc agacgtccgg ccgcggtggg cttgaaggtt
      841 agtccctccg cagctacagc cccggcgtct ttgcttcagc ttggtgctta gccctcgcct
      901 ggacctttga aaagtgactt gattgccggg cttagaggag gagaaatgga tcacattgtt
      961 tccttcggtg tcaccgttgc tggcctcata ccagttgacc ctgtcgccat tcgtaggcca
     1021 gtgtggtgtg gcggggccaa aaatggttgt aatgtgaacc cagtttctct aggaatacct
     1081 cccggcaagg gtcagagaga cgcttaccgg cctgtggaca agagttctat acctgccgca
     1141 ggcgactggc agccgggcct agccatccat cccctcttcc ccagcgactc aactacaacc
     1201 caaacaccta gataccagca caagccggtg aatccctgtc tggactgagc ctctggcttc
     1261 tgaactggaa cttttgcagc tattacaagt ttagaacctt aagtggggag atttaatggg
     1321 ctaattttat taaaggatcg tttggttttg tttttttaaa aaaaaaaaaa aaaaaaaaaa
     1381 aaaaaaaaaa aaaaaaaaaa aaaaaaaaaa aaaa
//
