H12_MOUSE
ID H12_MOUSE Reviewed; 212 AA.
AC P15864;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Histone H1.2;
DE AltName: Full=H1 VAR.1;
DE AltName: Full=H1c;
GN Name=H1-2 {ECO:0000250|UniProtKB:P16403};
GN Synonyms=H1f2 {ECO:0000312|MGI:MGI:1931526},
GN Hist1h1c {ECO:0000312|MGI:MGI:1931526};
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].
RX PubMed=2780558; DOI=10.1073/pnas.86.18.7002;
RA Cheng G., Nandi A., Clerk S., Skoultchi A.I.;
RT "Different 3'-end processing produces two independently regulated mRNAs
RT from a single H1 histone gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7002-7006(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2824517; DOI=10.1016/s0021-9258(18)45499-3;
RA Yang Y.-S., Brown D.T., Wellman S.E., Sittman D.B.;
RT "Isolation and characterization of a mouse fully replication-dependent H1
RT gene within a genomic cluster of core histone genes.";
RL J. Biol. Chem. 262:17118-17125(1987).
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 [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 [5]
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 [6]
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 [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
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 [8]
RP CROTONYLATION AT LYS-34; LYS-64; LYS-85; LYS-159 AND LYS-168.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J.,
RA Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation as a
RT new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-17, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-97, 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 [10]
RP CITRULLINATION AT ARG-54, AND MUTAGENESIS OF 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).
RN [11]
RP HYDROXYBUTYRYLATION AT LYS-23; LYS-26; LYS-27; LYS-46; LYS-52; LYS-63;
RP LYS-64; LYS-75; LYS-81; LYS-85; LYS-90; LYS-97; LYS-110; LYS-117; LYS-121;
RP LYS-129; LYS-136; LYS-148; LYS-159; LYS-168 AND LYS-212.
RX PubMed=24681537; DOI=10.1038/nchembio.1497;
RA Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A.,
RA Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA Khochbin S., Zhao Y.;
RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT mark.";
RL Nat. Chem. Biol. 10:365-370(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 ECO:0000269|PubMed:12808097, ECO:0000269|PubMed:16377562}.
CC -!- INTERACTION:
CC P15864; Q99MD9: Nasp; NbExp=3; IntAct=EBI-913436, EBI-913410;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in
CC euchromatin. {ECO:0000250}.
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. {ECO:0000250}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes.
CC {ECO:0000269|PubMed:21925322}.
CC -!- PTM: ADP-ribosylated on Ser-187 in response to DNA damage.
CC {ECO:0000250|UniProtKB:P16403}.
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: Hydroxybutyrylation of histones is induced by starvation.
CC {ECO:0000250|UniProtKB:P43277}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Triple-deficient mice (H1-
CC 2, H1-3 and H1-4) die by midgestation with a broad range of defects.
CC These embryos have about 50% of the normal ratio of H1 to nucleosomes,
CC demonstrating that critical levels of total H1 histones are essential
CC for mouse embryogenesis. {ECO:0000269|PubMed:12808097,
CC 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; M25365; AAA37808.1; -; Genomic_DNA.
DR EMBL; J03482; AAA37807.1; -; Genomic_DNA.
DR EMBL; Y12291; CAA72970.1; -; Genomic_DNA.
DR EMBL; AY158905; AAO06216.1; -; Genomic_DNA.
DR CCDS; CCDS26361.1; -.
DR PIR; A28470; A28470.
DR PIR; B35245; B35245.
DR RefSeq; NP_056601.1; NM_015786.3.
DR AlphaFoldDB; P15864; -.
DR SMR; P15864; -.
DR BioGRID; 206061; 27.
DR DIP; DIP-35245N; -.
DR IntAct; P15864; 7.
DR MINT; P15864; -.
DR STRING; 10090.ENSMUSP00000045816; -.
DR iPTMnet; P15864; -.
DR PhosphoSitePlus; P15864; -.
DR EPD; P15864; -.
DR jPOST; P15864; -.
DR PaxDb; P15864; -.
DR PeptideAtlas; P15864; -.
DR PRIDE; P15864; -.
DR ProteomicsDB; 271491; -.
DR Antibodypedia; 25499; 500 antibodies from 30 providers.
DR DNASU; 50708; -.
DR Ensembl; ENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181.
DR GeneID; 50708; -.
DR KEGG; mmu:50708; -.
DR UCSC; uc007puq.3; mouse.
DR CTD; 50708; -.
DR MGI; MGI:1931526; H1f2.
DR VEuPathDB; HostDB:ENSMUSG00000036181; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000163082; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P15864; -.
DR OMA; FPTGNRP; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P15864; -.
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; 50708; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Hist1h1c; mouse.
DR PRO; PR:P15864; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P15864; protein.
DR Bgee; ENSMUSG00000036181; Expressed in vault of skull and 257 other tissues.
DR ExpressionAtlas; P15864; baseline and differential.
DR Genevisible; P15864; MM.
DR GO; GO:0000791; C:euchromatin; IDA:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
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:23806337"
FT CHAIN 2..212
FT /note="Histone H1.2"
FT /id="PRO_0000195915"
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 98..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..212
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:P16403"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 23
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 26
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 27
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 34
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 34
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 34
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 46
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 52
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 52
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 54
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 63
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 64
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 64
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 64
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 75
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 81
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 85
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 85
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 85
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 90
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 90
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 90
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 97
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 97
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 97
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 104
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P02253"
FT MOD_RES 106
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 110
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 117
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 121
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 129
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 136
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 148
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 159
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 159
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 168
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 168
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 186
FT /note="N6-methyllysine; by EHMT1 and EHMT2"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 187
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P16403"
FT MOD_RES 212
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MUTAGEN 54
FT /note="R->A: Mimics the charge change that accompanies
FT citrullination, resulting in impaired nucleosome-binding."
FT /evidence="ECO:0000269|PubMed:24463520"
FT MUTAGEN 54
FT /note="R->K: Retains the positive charge, resulting in
FT slightly decreased nucleosome-binding."
FT /evidence="ECO:0000269|PubMed:24463520"
SQ SEQUENCE 212 AA; 21267 MW; 2872A9BCD50C840D CRC64;
MSEAAPAAPA AAPPAEKAPA KKKAAKKPAG VRRKASGPPV SELITKAVAA SKERSGVSLA
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GILVQTKGTG ASGSFKLNKK AASGEAKPQA
KKAGAAKAKK PAGAAKKPKK ATGAATPKKA AKKTPKKAKK PAAAAVTKKV AKSPKKAKVT
KPKKVKSASK AVKPKAAKPK VAKAKKVAAK KK
