ID H15_HUMAN Reviewed; 226 AA. AC P16401; Q14529; Q3MJ42; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 205. DE RecName: Full=Histone H1.5; DE AltName: Full=Histone H1a; DE AltName: Full=Histone H1b; DE AltName: Full=Histone H1s-3; GN Name=H1-5 {ECO:0000312|HGNC:HGNC:4719}; GN Synonyms=H1F5, HIST1H1B {ECO:0000312|HGNC:HGNC:4719}; 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], AND TISSUE SPECIFICITY. RX PubMed=9031620; DOI=10.1016/s0378-1119(96)00582-3; RA Albig W., Meergans T., Doenecke D.; RT "Characterization of the H1.5 gene completes the set of human H1 subtype RT genes."; RL Gene 184:141-148(1997). RN [2] 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 [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]. 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 PROTEIN SEQUENCE OF 2-226. RC TISSUE=Spleen; RX PubMed=2613692; DOI=10.1093/oxfordjournals.jbchem.a122941; RA Ohe Y., Hayashi H., Iwai K.; RT "Human spleen histone H1. Isolation and amino acid sequences of three minor RT variants, H1a, H1c, and H1d."; RL J. Biochem. 106:844-857(1989). RN [6] RP PROTEIN SEQUENCE OF 2-17; 37-49; 58-78 AND 89-100, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [7] 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 [8] RP SUBCELLULAR LOCATION. RX PubMed=11746507; DOI=10.1002/jcb.1224; RA Parseghian M.H., Newcomb R.L., Hamkalo B.A.; RT "Distribution of somatic H1 subtypes is non-random on active vs. inactive RT chromatin II: distribution in human adult fibroblasts."; RL J. Cell. Biochem. 83:643-659(2001). RN [9] 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 [10] 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 [11] RP PHOSPHORYLATION AT THR-11; SER-18; THR-138; THR-155; SER-173 AND SER-189. RX PubMed=16377619; DOI=10.1074/jbc.m508957200; RA Sarg B., Helliger W., Talasz H., Forg B., Lindner H.H.; RT "Histone H1 phosphorylation occurs site-specifically during interphase and RT mitosis: identification of a novel phosphorylation site on histone H1."; RL J. Biol. Chem. 281:6573-6580(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-18 AND THR-39, AND RP IDENTIFICATION BY 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 [13] 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 [14] RP PHOSPHORYLATION AT THR-11 BY GSK3B. RX PubMed=19136008; DOI=10.1016/j.jmb.2008.12.047; RA Happel N., Stoldt S., Schmidt B., Doenecke D.; RT "M phase-specific phosphorylation of histone H1.5 at threonine 10 by RT GSK-3."; RL J. Mol. Biol. 386:339-350(2009). RN [15] RP METHYLATION AT LYS-27. RX PubMed=19552482; DOI=10.1021/pr9000652; RA Lu A., Zougman A., Pudelko M., Bebenek M., Ziolkowski P., Mann M., RA Wisniewski J.R.; RT "Mapping of lysine monomethylation of linker histones in human breast and RT its cancer."; RL J. Proteome Res. 8:4207-4215(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-18 AND THR-138, CLEAVAGE OF INITIATOR METHIONINE [LARGE RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [19] 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 [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2; SER-18 AND THR-138, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE 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 [21] 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 [22] 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND SER-18, AND RP IDENTIFICATION BY 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-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 [25] 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 [26] RP VARIANT [LARGE SCALE ANALYSIS] ASP-86. 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 -!- SUBUNIT: Interacts with MSX1. {ECO:0000250|UniProtKB:P43276}. CC -!- INTERACTION: CC P16401; Q9HC52: CBX8; NbExp=2; IntAct=EBI-5327611, EBI-712912; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10997781, CC ECO:0000269|PubMed:15911621}. Chromosome. Note=Mainly localizes with CC heterochromatin (PubMed:15911621). Associates with actively transcribed CC chromatin and not heterochromatin (PubMed:10997781). CC {ECO:0000269|PubMed:10997781, ECO:0000269|PubMed:15911621}. CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the majority of the cell CC lines tested and in testis. {ECO:0000269|PubMed:9031620}. 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 (By similarity). CC Phosphorylated at Thr-11 by GSK3B during mitosis in prometaphase and CC dephosphorylated in telophase. {ECO:0000250, CC ECO:0000269|PubMed:16377619, ECO:0000269|PubMed:19136008}. CC -!- PTM: Citrullination at Arg-57 (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:P43276}. 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; X83509; CAA58498.1; -; Genomic_DNA. DR EMBL; AF531304; AAN06704.1; -; Genomic_DNA. DR EMBL; Z98744; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069101; AAH69101.1; -; mRNA. DR EMBL; BC101581; AAI01582.1; -; mRNA. DR EMBL; BC101583; AAI01584.1; -; mRNA. DR CCDS; CCDS4635.1; -. DR PIR; S51660; S51660. DR RefSeq; NP_005313.1; NM_005322.2. DR PDB; 2RHI; X-ray; 1.66 A; B=23-27. DR PDBsum; 2RHI; -. DR AlphaFoldDB; P16401; -. DR SMR; P16401; -. DR BioGRID; 109264; 576. DR IntAct; P16401; 220. DR MINT; P16401; -. DR STRING; 9606.ENSP00000330074; -. DR GlyGen; P16401; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P16401; -. DR PhosphoSitePlus; P16401; -. DR SwissPalm; P16401; -. DR BioMuta; HIST1H1B; -. DR DMDM; 19856407; -. DR EPD; P16401; -. DR jPOST; P16401; -. DR MassIVE; P16401; -. DR MaxQB; P16401; -. DR PaxDb; 9606-ENSP00000330074; -. DR PeptideAtlas; P16401; -. DR ProteomicsDB; 53351; -. DR Pumba; P16401; -. DR TopDownProteomics; P16401; -. DR Antibodypedia; 54587; 252 antibodies from 22 providers. DR CPTC; P16401; 1 antibody. DR DNASU; 3009; -. DR Ensembl; ENST00000331442.5; ENSP00000330074.4; ENSG00000184357.5. DR GeneID; 3009; -. DR KEGG; hsa:3009; -. DR MANE-Select; ENST00000331442.5; ENSP00000330074.4; NM_005322.3; NP_005313.1. DR UCSC; uc003njx.4; human. DR AGR; HGNC:4719; -. DR CTD; 3009; -. DR DisGeNET; 3009; -. DR GeneCards; H1-5; -. DR HGNC; HGNC:4719; H1-5. DR HPA; ENSG00000184357; Group enriched (bone marrow, lymphoid tissue). DR MIM; 142711; gene. DR neXtProt; NX_P16401; -. DR OpenTargets; ENSG00000184357; -. DR PharmGKB; PA29097; -. DR VEuPathDB; HostDB:ENSG00000184357; -. DR eggNOG; KOG4012; Eukaryota. DR GeneTree; ENSGT00940000162950; -. DR HOGENOM; CLU_052897_7_0_1; -. DR InParanoid; P16401; -. DR OMA; THPSWID; -. DR OrthoDB; 5362469at2759; -. DR PhylomeDB; P16401; -. DR TreeFam; TF313664; -. DR PathwayCommons; P16401; -. DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation. DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF). DR SignaLink; P16401; -. DR SIGNOR; P16401; -. DR BioGRID-ORCS; 3009; 24 hits in 1139 CRISPR screens. DR EvolutionaryTrace; P16401; -. DR GeneWiki; HIST1H1B; -. DR GenomeRNAi; 3009; -. DR Pharos; P16401; Tbio. DR PRO; PR:P16401; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P16401; Protein. DR Bgee; ENSG00000184357; Expressed in bone marrow cell and 75 other cell types or tissues. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0005694; C:chromosome; IDA:HPA. DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. 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:0042826; F:histone deacetylase binding; IPI:UniProtKB. 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:InterPro. DR GO; GO:0006325; P:chromatin organization; IMP:UniProtKB. DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central. DR GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB. DR GO; GO:0007517; P:muscle organ development; 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; IMP:UniProtKB. DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro. DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB. 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 IDEAL; IID00028; -. 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; Winged helix' DNA-binding domain; 1. DR PROSITE; PS51504; H15; 1. DR Genevisible; P16401; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; Citrullination; KW Direct protein sequencing; DNA-binding; Hydroxylation; Methylation; KW Nucleus; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2613692, ECO:0000269|Ref.6, 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..226 FT /note="Histone H1.5" FT /id="PRO_0000195909" FT DOMAIN 39..112 FT /note="H15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837" FT REGION 1..44 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 98..226 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 136..226 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine; partial" FT /evidence="ECO:0000269|Ref.6, 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:0007744|PubMed:21406692" FT MOD_RES 11 FT /note="Phosphothreonine; by GSK3" FT /evidence="ECO:0000269|PubMed:16377619, FT ECO:0000269|PubMed:19136008, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 17 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P43276" FT MOD_RES 18 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16377619, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 27 FT /note="N6-methyllysine" FT /evidence="ECO:0000269|PubMed:19552482" FT MOD_RES 37 FT /note="N6-(beta-hydroxybutyryl)lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P43277" FT MOD_RES 37 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P43276" FT MOD_RES 39 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 49 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P43276" FT MOD_RES 55 FT /note="N6-(beta-hydroxybutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P43277" FT MOD_RES 57 FT /note="Citrulline" FT /evidence="ECO:0000250|UniProtKB:P43276" FT MOD_RES 67 FT /note="N6-(beta-hydroxybutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P43277" FT MOD_RES 78 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P43276" FT MOD_RES 88 FT /note="N6-(beta-hydroxybutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P43277" FT MOD_RES 93 FT /note="N6-(beta-hydroxybutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P43277" FT MOD_RES 109 FT /note="N6-(beta-hydroxybutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P43277" FT MOD_RES 138 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:16377619, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 155 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:16377619" FT MOD_RES 168 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16377619" FT MOD_RES 189 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16377619" FT VARIANT 86 FT /note="G -> D (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036204" FT VARIANT 144 FT /note="K -> R (in dbSNP:rs11970638)" FT /id="VAR_049308" FT VARIANT 211 FT /note="A -> T (in dbSNP:rs34144478)" FT /id="VAR_049309" FT CONFLICT 216..218 FT /note="Missing (in Ref. 5; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 226 AA; 22580 MW; 0BA1402101766FDF CRC64; MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA VAASKERNGL SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK GTGASGSFKL NKKAASGEAK PKAKKAGAAK AKKPAGATPK KAKKAAGAKK AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA AKPKKATKSP AKPKAVKPKA AKPKAAKPKA AKPKAAKAKK AAAKKK //