H14_HUMAN
ID H14_HUMAN Reviewed; 219 AA.
AC P10412; Q4VB25;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Histone H1.4;
DE AltName: Full=Histone H1b;
DE AltName: Full=Histone H1s-4;
GN Name=H1-4 {ECO:0000312|HGNC:HGNC:4718};
GN Synonyms=H1F4 {ECO:0000312|HGNC:HGNC:4718},
GN HIST1H1E {ECO:0000312|HGNC:HGNC:4718};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1916825; DOI=10.1016/0888-7543(91)90183-f;
RA Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
RT "Isolation and characterization of two human H1 histone genes within
RT clusters of core histone genes.";
RL Genomics 10:940-948(1991).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-219, AND METHYLATION AT LYS-26.
RC TISSUE=Spleen;
RX PubMed=3782055; DOI=10.1093/oxfordjournals.jbchem.a121722;
RA Ohe Y., Hayashi H., Iwai K.;
RT "Human spleen histone H1. Isolation and amino acid sequence of a main
RT variant, H1b.";
RL J. Biochem. 100:359-368(1986).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10997781; DOI=10.1023/a:1009262819961;
RA Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A.;
RT "The distribution of somatic H1 subtypes is non-random on active vs.
RT inactive chromatin: distribution in human fetal fibroblasts.";
RL Chromosome Res. 8:405-424(2000).
RN [7]
RP ACETYLATION AT LYS-26.
RX PubMed=15469825; DOI=10.1016/j.molcel.2004.08.031;
RA Vaquero A., Scher M., Lee D., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "Human SirT1 interacts with histone H1 and promotes formation of
RT facultative heterochromatin.";
RL Mol. Cell 16:93-105(2004).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15911621; DOI=10.1074/jbc.m501627200;
RA Th'ng J.P., Sung R., Ye M., Hendzel M.J.;
RT "H1 family histones in the nucleus. Control of binding and localization by
RT the C-terminal domain.";
RL J. Biol. Chem. 280:27809-27814(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-187, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-18; THR-146 AND SER-187, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-18 AND SER-187, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP ADP-RIBOSYLATION AT SER-150.
RX PubMed=27723750; DOI=10.1038/nchembio.2180;
RA Leidecker O., Bonfiglio J.J., Colby T., Zhang Q., Atanassov I., Zaja R.,
RA Palazzo L., Stockum A., Ahel I., Matic I.;
RT "Serine is a new target residue for endogenous ADP-ribosylation on
RT histones.";
RL Nat. Chem. Biol. 12:998-1000(2016).
RN [22]
RP INVOLVEMENT IN RMNS.
RX PubMed=28475857; DOI=10.1016/j.ajhg.2017.03.010;
RG Childhood Overgrowth Collaboration;
RA Tatton-Brown K., Loveday C., Yost S., Clarke M., Ramsay E., Zachariou A.,
RA Elliott A., Wylie H., Ardissone A., Rittinger O., Stewart F., Temple I.K.,
RA Cole T., Mahamdallie S., Seal S., Ruark E., Rahman N.;
RT "Mutations in epigenetic regulation genes are a major cause of overgrowth
RT with intellectual disability.";
RL Am. J. Hum. Genet. 100:725-736(2017).
RN [23]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-128.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 -!- INTERACTION:
CC P10412; Q8IY81: FTSJ3; NbExp=2; IntAct=EBI-358163, EBI-744088;
CC P10412; Q9Y468: L3MBTL1; NbExp=7; IntAct=EBI-358163, EBI-1265089;
CC P10412; P16333: NCK1; NbExp=2; IntAct=EBI-358163, EBI-389883;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in
CC heterochromatin. Dysplays a punctuate staining pattern in the nucleus.
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:0000250|UniProtKB:P43275}.
CC -!- PTM: Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1.
CC {ECO:0000269|PubMed:15469825}.
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:0000250|UniProtKB:P43274}.
CC -!- PTM: ADP-ribosylated on Ser-150 in response to DNA damage.
CC {ECO:0000269|PubMed:27723750}.
CC -!- DISEASE: Rahman syndrome (RMNS) [MIM:617537]: An autosomal dominant
CC syndrome characterized by intellectual disability and overgrowth
CC manifesting as increased birth length, height, weight, and/or head
CC circumference. {ECO:0000269|PubMed:28475857}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: This variant accounts for 60% of histone H1.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; M60748; AAA63187.1; -; Genomic_DNA.
DR EMBL; AF531302; AAN06702.1; -; Genomic_DNA.
DR EMBL; AL353759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096168; AAH96168.1; -; mRNA.
DR EMBL; BC096169; AAH96169.1; -; mRNA.
DR EMBL; BC099632; AAH99632.1; -; mRNA.
DR CCDS; CCDS4586.1; -.
DR PIR; C40335; HSHU1B.
DR RefSeq; NP_005312.1; NM_005321.2.
DR PDB; 3TZD; X-ray; 1.81 A; T=19-36.
DR PDB; 5JJZ; X-ray; 2.00 A; B=21-32.
DR PDB; 6H8P; X-ray; 1.98 A; C/D=18-32.
DR PDB; 7K5Y; EM; 2.76 A; U=1-219.
DR PDB; 7K63; EM; 3.03 A; U=1-35, U=111-219.
DR PDBsum; 3TZD; -.
DR PDBsum; 5JJZ; -.
DR PDBsum; 6H8P; -.
DR PDBsum; 7K5Y; -.
DR PDBsum; 7K63; -.
DR AlphaFoldDB; P10412; -.
DR SMR; P10412; -.
DR BioGRID; 109263; 449.
DR IntAct; P10412; 207.
DR MINT; P10412; -.
DR STRING; 9606.ENSP00000307705; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; P10412; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P10412; -.
DR PhosphoSitePlus; P10412; -.
DR SwissPalm; P10412; -.
DR BioMuta; HIST1H1E; -.
DR DMDM; 121919; -.
DR EPD; P10412; -.
DR jPOST; P10412; -.
DR MassIVE; P10412; -.
DR MaxQB; P10412; -.
DR PaxDb; P10412; -.
DR PeptideAtlas; P10412; -.
DR PRIDE; P10412; -.
DR ProteomicsDB; 52602; -.
DR TopDownProteomics; P10412; -.
DR Antibodypedia; 25545; 483 antibodies from 22 providers.
DR DNASU; 3008; -.
DR Ensembl; ENST00000304218.6; ENSP00000307705.4; ENSG00000168298.7.
DR GeneID; 3008; -.
DR KEGG; hsa:3008; -.
DR MANE-Select; ENST00000304218.6; ENSP00000307705.4; NM_005321.3; NP_005312.1.
DR UCSC; uc003ngq.4; human.
DR CTD; 3008; -.
DR DisGeNET; 3008; -.
DR GeneCards; H1-4; -.
DR GeneReviews; H1-4; -.
DR HGNC; HGNC:4718; H1-4.
DR HPA; ENSG00000168298; Group enriched (bone marrow, brain).
DR MalaCards; H1-4; -.
DR MIM; 142220; gene.
DR MIM; 617537; phenotype.
DR neXtProt; NX_P10412; -.
DR OpenTargets; ENSG00000168298; -.
DR VEuPathDB; HostDB:ENSG00000168298; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155501; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P10412; -.
DR OMA; PPWVDMI; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P10412; -.
DR TreeFam; TF313664; -.
DR PathwayCommons; P10412; -.
DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; P10412; -.
DR SIGNOR; P10412; -.
DR BioGRID-ORCS; 3008; 70 hits in 1087 CRISPR screens.
DR ChiTaRS; HIST1H1E; human.
DR GeneWiki; HIST1H1E; -.
DR GenomeRNAi; 3008; -.
DR Pharos; P10412; Tbio.
DR PRO; PR:P10412; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P10412; protein.
DR Bgee; ENSG00000168298; Expressed in calcaneal tendon and 108 other tissues.
DR ExpressionAtlas; P10412; baseline and differential.
DR Genevisible; P10412; HS.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IMP:UniProtKB.
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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:Ensembl.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IEA:Ensembl.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR IDEAL; IID00538; -.
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 3D-structure; Acetylation; ADP-ribosylation; Chromosome; Citrullination;
KW Direct protein sequencing; DNA-binding; Hydroxylation;
KW Intellectual disability; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3782055,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..219
FT /note="Histone H1.4"
FT /id="PRO_0000195908"
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:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15865"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43274"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 26
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:15469825"
FT MOD_RES 26
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:3782055"
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:0000250|UniProtKB:P43274"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43274"
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:0000250|UniProtKB:P43274"
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:0007744|PubMed:20068231"
FT MOD_RES 150
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000269|PubMed:27723750"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT VARIANT 128
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs768731472)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036203"
FT VARIANT 152
FT /note="K -> R (in dbSNP:rs2298090)"
FT /id="VAR_049307"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:3TZD"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:7K5Y"
FT HELIX 59..69
FT /evidence="ECO:0007829|PDB:7K5Y"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:7K5Y"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:7K5Y"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:7K5Y"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:7K5Y"
SQ SEQUENCE 219 AA; 21865 MW; 1720FECCCBEBCC7F CRC64;
MSETAPAAPA APAPAEKTPV KKKARKSAGA AKRKASGPPV SELITKAVAA SKERSGVSLA
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA
KKAGAAKAKK PAGAAKKPKK ATGAATPKKS AKKTPKKAKK PAAAAGAKKA KSPKKAKAAK
PKKAPKSPAK AKAVKPKAAK PKTAKPKAAK PKKAAAKKK
