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
//