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histone H4 [Mus musculus]

NCBI Reference Sequence: NP_291074.1

Identical Proteins FASTA Graphics 

LOCUS       NP_291074                103 aa            linear   ROD 30-APR-2024
DEFINITION  histone H4 [Mus musculus].
ACCESSION   NP_291074 NP_001157146
VERSION     NP_291074.1
DBSOURCE    REFSEQ: accession NM_033596.3
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  (residues 1 to 103)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 103)
  AUTHORS   Ghule,P.N., Xie,R.L., Medina,R., Colby,J.L., Jones,S.N., Lian,J.B.,
            Stein,J.L., van Wijnen,A.J. and Stein,G.S.
  TITLE     Fidelity of histone gene regulation is obligatory for genome
            replication and stability
  JOURNAL   Mol Cell Biol 34 (14), 2650-2659 (2014)
   PUBMED   24797072
  REMARK    GeneRIF: Results show that deregulation of histone H4 results in
            catastrophic cellular and molecular defects that lead to genomic
            instability.
REFERENCE   3  (residues 1 to 103)
  AUTHORS   Liu,L.J., Xie,R., Hussain,S., Lian,J.B., Rivera-Perez,J.,
            Jones,S.N., Stein,J.L., Stein,G.S. and van Wijnen,A.J.
  TITLE     Functional coupling of transcription factor HiNF-P and histone H4
            gene expression during pre- and post-natal mouse development
  JOURNAL   Gene 483 (1-2), 1-10 (2011)
   PUBMED   21605641
  REMARK    GeneRIF: The in vivo co-expression of Hinfp and histone H4 genes is
            consistent with the biological function of Hinfp as a principal
            transcriptional regulator of histone H4 gene expression during
            mouse development.
REFERENCE   4  (residues 1 to 103)
  AUTHORS   Xie,R., Medina,R., Zhang,Y., Hussain,S., Colby,J., Ghule,P.,
            Sundararajan,S., Keeler,M., Liu,L.J., van der Deen,M., Mitra,P.,
            Lian,J.B., Rivera-Perez,J.A., Jones,S.N., Stein,J.L., van
            Wijnen,A.J. and Stein,G.S.
  TITLE     The histone gene activator HINFP is a nonredundant cyclin E/CDK2
            effector during early embryonic cell cycles
  JOURNAL   Proc Natl Acad Sci U S A 106 (30), 12359-12364 (2009)
   PUBMED   19590016
  REMARK    GeneRIF: Data indicate that the CDK2/cyclin
            E/p220(NPAT)/HINFP/histone gene signaling pathway at the G1/S phase
            transition is an essential, nonredundant cell cycle regulatory
            mechanism that is established early in embryogenesis.
REFERENCE   5  (residues 1 to 103)
  AUTHORS   Aqeilan,R.I., Hassan,M.Q., de Bruin,A., Hagan,J.P., Volinia,S.,
            Palumbo,T., Hussain,S., Lee,S.H., Gaur,T., Stein,G.S., Lian,J.B.
            and Croce,C.M.
  TITLE     The WWOX tumor suppressor is essential for postnatal survival and
            normal bone metabolism
  JOURNAL   J Biol Chem 283 (31), 21629-21639 (2008)
   PUBMED   18487609
REFERENCE   6  (residues 1 to 103)
  AUTHORS   Suh,J.M., Zeve,D., McKay,R., Seo,J., Salo,Z., Li,R., Wang,M. and
            Graff,J.M.
  TITLE     Adipose is a conserved dosage-sensitive antiobesity gene
  JOURNAL   Cell Metab 6 (3), 195-207 (2007)
   PUBMED   17767906
REFERENCE   7  (residues 1 to 103)
  AUTHORS   Marzluff,W.F., Gongidi,P., Woods,K.R., Jin,J. and Maltais,L.J.
  TITLE     The human and mouse replication-dependent histone genes
  JOURNAL   Genomics 80 (5), 487-498 (2002)
   PUBMED   12408966
REFERENCE   8  (residues 1 to 103)
  AUTHORS   Cotten,M., Gick,O., Vasserot,A., Schaffner,G. and Birnstiel,M.L.
  TITLE     Specific contacts between mammalian U7 snRNA and histone precursor
            RNA are indispensable for the in vitro 3' RNA processing reaction
  JOURNAL   EMBO J 7 (3), 801-808 (1988)
   PUBMED   3396543
REFERENCE   9  (residues 1 to 103)
  AUTHORS   Stauber,C., Luscher,B., Eckner,R., Lotscher,E. and Schumperli,D.
  TITLE     A signal regulating mouse histone H4 mRNA levels in a mammalian
            cell cycle mutant and sequences controlling RNA 3' processing are
            both contained within the same 80-bp fragment
  JOURNAL   EMBO J 5 (12), 3297-3303 (1986)
   PUBMED   3816761
REFERENCE   10 (residues 1 to 103)
  AUTHORS   Seiler-Tuyns,A. and Birnstiel,M.L.
  TITLE     Structure and expression in L-cells of a cloned H4 histone gene of
            the mouse
  JOURNAL   J Mol Biol 151 (4), 607-625 (1981)
   PUBMED   6276563
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC125099.3.
            
            On Sep 15, 2009 this sequence version replaced NP_001157146.1.
            
            Summary: Histones are basic nuclear proteins that are responsible
            for the nucleosome structure of the chromosomal fiber in
            eukaryotes. This structure consists of approximately 146 bp of DNA
            wrapped around a nucleosome, an octamer composed of pairs of each
            of the four core histones (H2A, H2B, H3, and H4). The chromatin
            fiber is further compacted through the interaction of a linker
            histone, H1, with the DNA between the nucleosomes to form higher
            order chromatin structures. This gene is intronless and encodes a
            replication-dependent histone that is a member of the histone H4
            family. [provided by RefSeq, Aug 2015].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            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 :: BX520915.1, BC051566.1 [ECO:0000345]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria        :: based on single protein-coding
                                             transcript
            replication-dependent histone :: PMID: 12408966
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..103
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="3"
                     /map="3 41.7 cM"
     Protein         1..103
                     /product="histone H4"
                     /note="histone 2, H4; histone cluster 2, H4"
                     /calculated_mol_wt=11236
     Region          1..103
                     /region_name="PLN00035"
                     /note="histone H4; Provisional"
                     /db_xref="CDD:177669"
     Region          1..20
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P62806.2)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylserine.
                     /evidence=ECO:0000250|UniProtKB:P62803; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            2
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000269|PubMed:16980586; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            4
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000269|PubMed:16699504;
                     Omega-N-methylarginine, by PRMT1, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62805; Symmetric
                     dimethylarginine, by PRMT5 and PRMT7, alternate.
                     /evidence=ECO:0000269|PubMed:16699504; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            6
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753,
                     ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            9
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753,
                     ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            13
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753,
                     ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            13
                     /site_type="methylation"
                     /note="N6-methyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62805; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            17
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:30279482,
                     ECO:0007744|PubMed:23576753, ECO:0007744|PubMed:23806337;
                     propagated from UniProtKB/Swiss-Prot (P62806.2)"
     Site            21
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine, alternate.
                     /evidence=ECO:0000269|PubMed:15145825;
                     N6,N6-dimethyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62803; N6-methyllysine,
                     alternate. /evidence=ECO:0000250|UniProtKB:P62803;
                     propagated from UniProtKB/Swiss-Prot (P62806.2)"
     Site            32
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            48
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            52
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:17947660,
                     ECO:0007744|PubMed:18034455, ECO:0007744|PubMed:21183079;
                     propagated from UniProtKB/Swiss-Prot (P62806.2)"
     Site            81
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            89
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0007744|PubMed:18034455,
                     ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     Site            92
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P62805; propagated from
                     UniProtKB/Swiss-Prot (P62806.2)"
     CDS             1..103
                     /gene="H4c14"
                     /gene_synonym="H4; H4c1; H4c11; H4c12; H4c16; H4c2; H4c3;
                     H4c4; H4c6; H4c8; H4c9; H4f16; Hist2h4"
                     /coded_by="NM_033596.3:14..325"
                     /db_xref="CCDS:CCDS51002.1"
                     /db_xref="GeneID:97122"
                     /db_xref="MGI:MGI:2140113"
ORIGIN      
        1 msgrgkggkg lgkggakrhr kvlrdniqgi tkpairrlar rggvkrisgl iyeetrgvlk
       61 vflenvirda vtytehakrk tvtamdvvya lkrqgrtlyg fgg
//
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