H11_MOUSE
ID H11_MOUSE Reviewed; 213 AA.
AC P43275; Q5SZ98;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Histone H1.1;
DE AltName: Full=H1 VAR.3;
DE AltName: Full=Histone H1a;
DE Short=H1a;
GN Name=H1-1 {ECO:0000250|UniProtKB:Q02539};
GN Synonyms=H1a, H1f1 {ECO:0000312|MGI:MGI:1931523}, Hist1h1a;
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;
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], AND TISSUE SPECIFICITY.
RC STRAIN=129/Sv;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP PHOSPHORYLATION.
RX PubMed=8639656; DOI=10.1021/bi951914e;
RA Talasz H., Helliger W., Puschendorf B., Lindner H.;
RT "In vivo phosphorylation of histone H1 variants during the cell cycle.";
RL Biochemistry 35:1761-1767(1996).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=10666340; DOI=10.1006/excr.1999.4767;
RA Rabini S., Franke K., Saftig P., Bode C., Doenecke D., Drabent B.;
RT "Spermatogenesis in mice is not affected by histone H1.1 deficiency.";
RL Exp. Cell Res. 255:114-124(2000).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
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; LYS-17; LYS-77; LYS-92 AND
RP LYS-121, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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-56.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DFFB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in
CC euchromatin. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Restricted to thymus, testis and spleen. Present
CC also in lymphocytic and neuronal cells. Increases in testis starting
CC with a low level at day 5 and reaching high concentrations in 20-day
CC old and adult animals. {ECO:0000269|PubMed:9655912}.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity binding to
CC chromatin. {ECO:0000250}.
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:0000269|PubMed:8639656}.
CC -!- PTM: Citrullination at Arg-56 (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: Hydroxybutyrylation of histones is induced by starvation.
CC {ECO:0000250|UniProtKB:P43277}.
CC -!- DISRUPTION PHENOTYPE: Deficient-mice developed normally until the adult
CC stage. No anatomic abnormalities are detected, mice are fertile and
CC they show normal spermatogenesis and testicular morphology. The lack of
CC phenotype may be due to a compensatory function of other histone H1
CC subtypes. {ECO:0000269|PubMed:10666340}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; L26164; AAA37761.1; -; Genomic_DNA.
DR EMBL; Y12290; CAA72969.1; -; Genomic_DNA.
DR EMBL; AY158903; AAO06214.1; -; Genomic_DNA.
DR EMBL; AL590388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466561; EDL32534.1; -; Genomic_DNA.
DR EMBL; BC116820; AAI16821.1; -; mRNA.
DR EMBL; BC116850; AAI16851.1; -; mRNA.
DR CCDS; CCDS26369.1; -.
DR PIR; S43949; S43949.
DR RefSeq; NP_085112.1; NM_030609.3.
DR AlphaFoldDB; P43275; -.
DR SMR; P43275; -.
DR BioGRID; 219818; 19.
DR IntAct; P43275; 4.
DR MINT; P43275; -.
DR STRING; 10090.ENSMUSP00000062030; -.
DR iPTMnet; P43275; -.
DR PhosphoSitePlus; P43275; -.
DR EPD; P43275; -.
DR jPOST; P43275; -.
DR PaxDb; P43275; -.
DR PeptideAtlas; P43275; -.
DR PRIDE; P43275; -.
DR ProteomicsDB; 271372; -.
DR Antibodypedia; 25489; 356 antibodies from 23 providers.
DR DNASU; 80838; -.
DR Ensembl; ENSMUST00000055770; ENSMUSP00000062030; ENSMUSG00000049539.
DR GeneID; 80838; -.
DR KEGG; mmu:80838; -.
DR UCSC; uc007puz.2; mouse.
DR CTD; 80838; -.
DR MGI; MGI:1931523; H1f1.
DR VEuPathDB; HostDB:ENSMUSG00000049539; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000163269; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P43275; -.
DR OMA; QFKIAKF; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P43275; -.
DR TreeFam; TF313664; -.
DR Reactome; R-MMU-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR BioGRID-ORCS; 80838; 5 hits in 73 CRISPR screens.
DR PRO; PR:P43275; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P43275; protein.
DR Bgee; ENSMUSG00000049539; Expressed in spermatid and 59 other tissues.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0031982; C:vesicle; IDA:CAFA.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; IDA:CAFA.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IDA:CAFA.
DR GO; GO:0007283; P:spermatogenesis; IGI: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; Chromosome; Citrullination; DNA-binding; Hydroxylation;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..213
FT /note="Histone H1.1"
FT /id="PRO_0000195914"
FT DOMAIN 38..111
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..213
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A3K5"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A3K5"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 36
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A3K5"
FT MOD_RES 54
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 56
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 66
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4A3K5"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 87
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 92
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:G3N131"
FT MOD_RES 108
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 121
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 213 AA; 21785 MW; 03A46320A100B203 CRC64;
MSETAPVAQA ASTATEKPAA AKKTKKPAKA AAPRKKPAGP SVSELIVQAV SSSKERSGVS
LAALKKSLAA AGYDVEKNNS RIKLGLKSLV NKGTLVQTKG TGAAGSFKLN KKAESKAITT
KVSVKAKASG AAKKPKKTAG AAAKKTVKTP KKPKKPAVSK KTSKSPKKPK VVKAKKVAKS
PAKAKAVKPK ASKAKVTKPK TPAKPKKAAP KKK
