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   27-MAR-2024, entry version 173.
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=10.1016/s0888-7543(02)96850-3;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 21.
DR   IntAct; P43275; 5.
DR   MINT; P43275; -.
DR   STRING; 10090.ENSMUSP00000062030; -.
DR   GlyGen; P43275; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P43275; -.
DR   PhosphoSitePlus; P43275; -.
DR   SwissPalm; P43275; -.
DR   EPD; P43275; -.
DR   jPOST; P43275; -.
DR   PaxDb; 10090-ENSMUSP00000062030; -.
DR   PeptideAtlas; P43275; -.
DR   ProteomicsDB; 271372; -.
DR   Pumba; P43275; -.
DR   Antibodypedia; 25489; 410 antibodies from 23 providers.
DR   DNASU; 80838; -.
DR   Ensembl; ENSMUST00000055770.4; ENSMUSP00000062030.2; ENSMUSG00000049539.4.
DR   GeneID; 80838; -.
DR   KEGG; mmu:80838; -.
DR   UCSC; uc007puz.2; mouse.
DR   AGR; MGI:1931523; -.
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; HKEEART; -.
DR   OrthoDB; 5362469at2759; -.
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; 6 hits in 79 CRISPR screens.
DR   PRO; PR:P43275; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; P43275; Protein.
DR   Bgee; ENSMUSG00000049539; Expressed in spermatid and 61 other cell types or 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; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   PANTHER; PTHR11467; HISTONE H1; 1.
DR   PANTHER; PTHR11467:SF177; HISTONE H1.1; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//