H14_MOUSE
ID H14_MOUSE Reviewed; 219 AA.
AC P43274; Q5EBH3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Histone H1.4;
DE AltName: Full=H1 VAR.2;
DE AltName: Full=H1e;
GN Name=H1-4 {ECO:0000250|UniProtKB:P10412};
GN Synonyms=H1f4 {ECO:0000312|MGI:MGI:1931527},
GN Hist1h1e {ECO:0000312|MGI:MGI:1931527};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=8190634; DOI=10.1093/nar/22.8.1421;
RA Dong Y., Sirotkin A.M., Yang Y.-S., Brown D.T., Sittman D.B.,
RA Skoultchi A.I.;
RT "Isolation and characterization of two replication-dependent mouse H1
RT histone genes.";
RL Nucleic Acids Res. 22:1421-1428(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8416974; DOI=10.1016/s0021-9258(18)54210-1;
RA Brown D.T., Sittman D.B.;
RT "Identification through overexpression and tagging of the variant type of
RT the mouse H1e and H1c genes.";
RL J. Biol. Chem. 268:713-718(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=9655912; DOI=10.1016/s0167-4781(98)00062-1;
RA Franke K., Drabent B., Doenecke D.;
RT "Expression of murine H1 histone genes during postnatal development.";
RL Biochim. Biophys. Acta 1398:232-242(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12808097; DOI=10.1128/mcb.23.13.4559-4572.2003;
RA Fan Y., Nikitina T., Morin-Kensicki E.M., Zhao J., Magnuson T.R.,
RA Woodcock C.L., Skoultchi A.I.;
RT "H1 linker histones are essential for mouse development and affect
RT nucleosome spacing in vivo.";
RL Mol. Cell. Biol. 23:4559-4572(2003).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN GENE REGULATION.
RX PubMed=16377562; DOI=10.1016/j.cell.2005.10.028;
RA Fan Y., Nikitina T., Zhao J., Fleury T.J., Bhattacharyya R.,
RA Bouhassira E.E., Stein A., Woodcock C.L., Skoultchi A.I.;
RT "Histone H1 depletion in mammals alters global chromatin structure but
RT causes specific changes in gene regulation.";
RL Cell 123:1199-1212(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-18, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-17, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-34, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP CITRULLINATION AT ARG-54.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes
CC forming the macromolecular structure known as the chromatin fiber.
CC Histones H1 are necessary for the condensation of nucleosome chains
CC into higher-order structured fibers. Acts also as a regulator of
CC individual gene transcription through chromatin remodeling, nucleosome
CC spacing and DNA methylation. {ECO:0000269|PubMed:12808097,
CC ECO:0000269|PubMed:16377562}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in
CC heterochromatin. Dysplays a punctuate staining pattern in the nucleus.
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity binding to
CC chromatin. {ECO:0000250}.
CC -!- PTM: Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the
CC DNA-binding site of H1 and results in its displacement from chromatin
CC and global chromatin decondensation, thereby promoting pluripotency and
CC stem cell maintenance. {ECO:0000269|PubMed:24463520}.
CC -!- PTM: ADP-ribosylated on Ser-55, Ser-113 and Ser-150 in response to DNA
CC damage. {ECO:0000250|UniProtKB:P10412}.
CC -!- PTM: H1 histones are progressively phosphorylated during the cell
CC cycle, becoming maximally phosphorylated during late G2 phase and M
CC phase, and being dephosphorylated sharply thereafter.
CC {ECO:0000250|UniProtKB:P43275}.
CC -!- PTM: Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.
CC {ECO:0000250|UniProtKB:P10412}.
CC -!- PTM: Hydroxybutyrylation of histones is induced by starvation.
CC {ECO:0000250|UniProtKB:P43277}.
CC -!- DISRUPTION PHENOTYPE: Triple-deficient mice (H1-2, H1-3 and H1-4) die
CC by midgestation with a broad range of defects. These embryos have about
CC 50% of the normal ratio of H1 to nucleosomes. This proves at least that
CC a correct stoichiometry of linker histone deposition on chromatin is
CC essential. {ECO:0000269|PubMed:12808097, ECO:0000269|PubMed:16377562}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; L26163; AAA37760.1; -; Genomic_DNA.
DR EMBL; L04141; AAA37814.1; -; Genomic_DNA.
DR EMBL; Y12292; CAA72971.1; -; Genomic_DNA.
DR EMBL; BC089600; AAH89600.1; -; mRNA.
DR CCDS; CCDS26355.1; -.
DR PIR; I49742; I49742.
DR RefSeq; NP_056602.1; NM_015787.4.
DR AlphaFoldDB; P43274; -.
DR SMR; P43274; -.
DR BioGRID; 206062; 15.
DR IntAct; P43274; 10.
DR MINT; P43274; -.
DR STRING; 10090.ENSMUSP00000057308; -.
DR MoonProt; P43274; -.
DR iPTMnet; P43274; -.
DR PhosphoSitePlus; P43274; -.
DR EPD; P43274; -.
DR jPOST; P43274; -.
DR MaxQB; P43274; -.
DR PaxDb; P43274; -.
DR PeptideAtlas; P43274; -.
DR PRIDE; P43274; -.
DR ProteomicsDB; 269642; -.
DR Antibodypedia; 25545; 483 antibodies from 22 providers.
DR DNASU; 50709; -.
DR Ensembl; ENSMUST00000062045; ENSMUSP00000057308; ENSMUSG00000051627.
DR GeneID; 50709; -.
DR KEGG; mmu:50709; -.
DR UCSC; uc007puj.3; mouse.
DR CTD; 50709; -.
DR MGI; MGI:1931527; H1f4.
DR VEuPathDB; HostDB:ENSMUSG00000051627; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155501; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P43274; -.
DR OMA; PPWVDMI; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P43274; -.
DR TreeFam; TF313664; -.
DR BioGRID-ORCS; 50709; 7 hits in 75 CRISPR screens.
DR PRO; PR:P43274; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P43274; protein.
DR Bgee; ENSMUSG00000051627; Expressed in undifferentiated genital tubercle and 85 other tissues.
DR Genevisible; P43274; MM.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0032564; F:dATP binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; ISO:MGI.
DR GO; GO:0030527; F:structural constituent of chromatin; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IMP:MGI.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IGI:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IGI:MGI.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:MGI.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Chromosome; Citrullination; DNA-binding;
KW Hydroxylation; Methylation; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:23806337"
FT CHAIN 2..219
FT /note="Histone H1.4"
FT /id="PRO_0000195917"
FT DOMAIN 36..109
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..219
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15865"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 26
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT MOD_RES 26
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT MOD_RES 34
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 34
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 54
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 64
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 85
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 90
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 106
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT MOD_RES 150
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P10412"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10412"
SQ SEQUENCE 219 AA; 21977 MW; 9463467F699F3625 CRC64;
MSETAPAAPA APAPAEKTPV KKKARKAAGG AKRKTSGPPV SELITKAVAA SKERSGVSLA
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA
KRAGAAKAKK PAGAAKKPKK AAGTATAKKS TKKTPKKAKK PAAAAGAKKA KSPKKAKATK
AKKAPKSPAK AKTVKPKAAK PKTSKPKAAK PKKTAAKKK
