H13_HUMAN
ID H13_HUMAN Reviewed; 221 AA.
AC P16402; B2R751; Q2M2I2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Histone H1.3;
DE AltName: Full=Histone H1c;
DE AltName: Full=Histone H1s-2;
GN Name=H1-3 {ECO:0000312|HGNC:HGNC:4717};
GN Synonyms=H1F3 {ECO:0000312|HGNC:HGNC:4717},
GN HIST1H1D {ECO:0000312|HGNC:HGNC:4717};
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 MRNA].
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 PROTEIN SEQUENCE OF 2-221.
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 [8]
RP NOMENCLATURE.
RX PubMed=8003976; DOI=10.1002/pro.5560030406;
RA Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A.;
RT "A proposal for a coherent mammalian histone H1 nomenclature correlated
RT with amino acid sequences.";
RL Protein Sci. 3:575-587(1994).
RN [9]
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 [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND IDENTIFICATION BY
RP 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 [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 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 SER-2 AND THR-18, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [18]
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 [19]
RP HYDROXYBUTYRYLATION AT LYS-35; LYS-47; LYS-53; LYS-65; LYS-76; LYS-86;
RP LYS-91; LYS-107 AND LYS-170.
RX PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lysine beta-
RT hydroxybutyrylation.";
RL Mol. Cell 62:194-206(2016).
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 -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=According to
CC PubMed:15911621 more commonly found in euchromatin. According to
CC PubMed:10997781 is associated with inactive chromatin.
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: Citrullination at Arg-55 (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:P43277}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; M60747; AAA63186.1; -; Genomic_DNA.
DR EMBL; AF531303; AAN06703.1; -; Genomic_DNA.
DR EMBL; AK312845; BAG35698.1; -; mRNA.
DR EMBL; AL031777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55548.1; -; Genomic_DNA.
DR EMBL; BC104874; AAI04875.1; -; mRNA.
DR EMBL; BC111971; AAI11972.1; -; mRNA.
DR CCDS; CCDS4597.1; -.
DR PIR; B40335; B40335.
DR RefSeq; NP_005311.1; NM_005320.2.
DR AlphaFoldDB; P16402; -.
DR SMR; P16402; -.
DR BioGRID; 109262; 292.
DR CORUM; P16402; -.
DR IntAct; P16402; 44.
DR MINT; P16402; -.
DR STRING; 9606.ENSP00000244534; -.
DR GlyGen; P16402; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P16402; -.
DR PhosphoSitePlus; P16402; -.
DR SwissPalm; P16402; -.
DR BioMuta; HIST1H1D; -.
DR DMDM; 121925; -.
DR EPD; P16402; -.
DR jPOST; P16402; -.
DR MassIVE; P16402; -.
DR MaxQB; P16402; -.
DR PaxDb; P16402; -.
DR PeptideAtlas; P16402; -.
DR PRIDE; P16402; -.
DR ProteomicsDB; 53352; -.
DR Antibodypedia; 58672; 139 antibodies from 16 providers.
DR DNASU; 3007; -.
DR Ensembl; ENST00000244534.7; ENSP00000244534.6; ENSG00000124575.7.
DR GeneID; 3007; -.
DR KEGG; hsa:3007; -.
DR MANE-Select; ENST00000244534.7; ENSP00000244534.6; NM_005320.3; NP_005311.1.
DR UCSC; uc003nhd.4; human.
DR CTD; 3007; -.
DR DisGeNET; 3007; -.
DR GeneCards; H1-3; -.
DR HGNC; HGNC:4717; H1-3.
DR HPA; ENSG00000124575; Tissue enhanced (bone marrow, brain).
DR MIM; 142210; gene.
DR neXtProt; NX_P16402; -.
DR OpenTargets; ENSG00000124575; -.
DR VEuPathDB; HostDB:ENSG00000124575; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000155501; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P16402; -.
DR OMA; CAANYKF; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P16402; -.
DR TreeFam; TF313664; -.
DR PathwayCommons; P16402; -.
DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; P16402; -.
DR BioGRID-ORCS; 3007; 19 hits in 1076 CRISPR screens.
DR ChiTaRS; HIST1H1D; human.
DR GeneWiki; HIST1H1D; -.
DR GenomeRNAi; 3007; -.
DR Pharos; P16402; Tbio.
DR PRO; PR:P16402; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P16402; protein.
DR Bgee; ENSG00000124575; Expressed in adrenal tissue and 118 other tissues.
DR Genevisible; P16402; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IDA: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 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; Direct protein sequencing;
KW DNA-binding; Hydroxylation; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2613692,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:25944712"
FT CHAIN 2..221
FT /note="Histone H1.3"
FT /id="PRO_0000195907"
FT DOMAIN 37..110
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 90..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..221
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:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 35
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 47
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 53
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 55
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43277"
FT MOD_RES 65
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 76
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 86
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 91
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 105
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:A7MAZ5"
FT MOD_RES 107
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 170
FT /note="N6-(beta-hydroxybutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:27105115"
FT VARIANT 75
FT /note="E -> K (in dbSNP:rs2050949)"
FT /id="VAR_049306"
SQ SEQUENCE 221 AA; 22350 MW; DB987FE8DE034D12 CRC64;
MSETAPLAPT IPAPAEKTPV KKKAKKAGAT AGKRKASGPP VSELITKAVA ASKERSGVSL
AALKKALAAA GYDVEKNNSR IKLGLKSLVS KGTLVQTKGT GASGSFKLNK KAASGEGKPK
AKKAGAAKPR KPAGAAKKPK KVAGAATPKK SIKKTPKKVK KPATAAGTKK VAKSAKKVKT
PQPKKAAKSP AKAKAPKPKA AKPKSGKPKV TKAKKAAPKK K
