H10_HUMAN
ID H10_HUMAN Reviewed; 194 AA.
AC P07305; B2R6I0; B4DRD6; Q6FG88; Q8N6R3;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Histone H1.0;
DE AltName: Full=Histone H1';
DE AltName: Full=Histone H1(0);
DE Contains:
DE RecName: Full=Histone H1.0, N-terminally processed;
GN Name=H1-0 {ECO:0000312|HGNC:HGNC:4714};
GN Synonyms=H1F0 {ECO:0000312|HGNC:HGNC:4714}, H1FV;
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] (ISOFORM 1).
RX PubMed=3084796; DOI=10.1016/0022-2836(86)90446-8;
RA Doenecke D., Tonjes R.;
RT "Differential distribution of lysine and arginine residues in the closely
RT related histones H1 and H5. Analysis of a human H1 gene.";
RL J. Mol. Biol. 187:461-464(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Placenta;
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 [8]
RP PARTIAL PROTEIN SEQUENCE (RNA EDITED VERSION), IDENTIFICATION BY MASS
RP SPECTROMETRY, RNA EDITING, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=18993075; DOI=10.1016/j.cub.2008.09.059;
RA Zougman A., Ziolkowski P., Mann M., Wisniewski J.R.;
RT "Evidence for insertional RNA editing in humans.";
RL Curr. Biol. 18:1760-1765(2008).
RN [9]
RP ACETYLATION AT THR-2, CLEAVAGE OF INITIATOR METHIONINE, AND DEAMIDATION AT
RP ASN-4.
RX PubMed=9582379; DOI=10.1074/jbc.273.21.13324;
RA Lindner H., Sarg B., Hoertnagl B., Helliger W.;
RT "The microheterogeneity of the mammalian H1(0) histone. Evidence for an
RT age-dependent deamidation.";
RL J. Biol. Chem. 273:13324-13330(1998).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP ADP-RIBOSYLATION AT SER-104.
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).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures. The histones H1.0 are found in
CC cells that are in terminal stages of differentiation or that have low
CC rates of cell division.
CC -!- INTERACTION:
CC P07305; Q8IYW5: RNF168; NbExp=2; IntAct=EBI-725224, EBI-914207;
CC P07305; P04014: E1; Xeno; NbExp=2; IntAct=EBI-725224, EBI-7014446;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837,
CC ECO:0000269|PubMed:18993075}. Chromosome {ECO:0000255|PROSITE-
CC ProRule:PRU00837, ECO:0000269|PubMed:18993075}. Note=The RNA edited
CC version has been localized to nuclear speckles. During mitosis, it
CC appears in the vicinity of condensed chromosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07305-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07305-2; Sequence=VSP_042163;
CC -!- INDUCTION: Both the unedited and the RNA edited versions are induced by
CC butyrate (at protein level). Only RNA edited version is induced by DTT,
CC vinblastine or TNF (at protein level). {ECO:0000269|PubMed:18993075}.
CC -!- PTM: Phosphorylated on Ser-17 in RNA edited version.
CC {ECO:0000269|PubMed:18993075}.
CC -!- PTM: ADP-ribosylated on Ser-104 in response to DNA damage.
CC {ECO:0000269|PubMed:27723750}.
CC -!- RNA EDITING: Modified_positions=Not_applicable; Note=Partially edited.
CC In approximately 3.6% of the mRNA molecules, a new initiator methionine
CC is created by a single uridine insertion in the 5'-UTR, causing an N-
CC terminal extension of 99 amino acids. The existence of the RNA edited
CC version is supported by direct protein sequencing by MS/MS of the
CC following peptides specific to that version: 12-21; 22-33; 37-47; 48-
CC 67; 68-83; 84-94 and 97-113. The RNA edited version is called ET-H1.0.
CC {ECO:0000269|PubMed:18993075};
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Histone H1 entry;
CC URL="https://en.wikipedia.org/wiki/Histone_H1";
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DR EMBL; X03473; CAA27190.1; -; Genomic_DNA.
DR EMBL; CR456502; CAG30388.1; -; mRNA.
DR EMBL; CR542220; CAG47016.1; -; mRNA.
DR EMBL; AK299209; BAG61248.1; -; mRNA.
DR EMBL; AK312583; BAG35477.1; -; mRNA.
DR EMBL; Z97630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60188.1; -; Genomic_DNA.
DR EMBL; BC000145; AAH00145.1; -; mRNA.
DR EMBL; BC029046; AAH29046.1; -; mRNA.
DR CCDS; CCDS13956.1; -. [P07305-1]
DR PIR; A24850; HSHU10.
DR RefSeq; NP_005309.1; NM_005318.3. [P07305-1]
DR PDB; 6HQ1; NMR; -; A=24-97.
DR PDB; 6LA2; X-ray; 3.89 A; S/T=1-194.
DR PDB; 6LA8; X-ray; 3.40 A; S=1-194.
DR PDB; 6LA9; X-ray; 3.70 A; S/T=1-194.
DR PDB; 6LAB; X-ray; 3.20 A; U/V=1-194.
DR PDB; 6N88; EM; 6.20 A; C=1-194.
DR PDB; 6N89; EM; 7.50 A; B=1-194.
DR PDB; 7COW; X-ray; 2.86 A; S/T=2-194.
DR PDB; 7DBP; EM; 4.50 A; K=2-194.
DR PDB; 7K5X; EM; 2.93 A; U=1-194.
DR PDBsum; 6HQ1; -.
DR PDBsum; 6LA2; -.
DR PDBsum; 6LA8; -.
DR PDBsum; 6LA9; -.
DR PDBsum; 6LAB; -.
DR PDBsum; 6N88; -.
DR PDBsum; 6N89; -.
DR PDBsum; 7COW; -.
DR PDBsum; 7DBP; -.
DR PDBsum; 7K5X; -.
DR AlphaFoldDB; P07305; -.
DR SMR; P07305; -.
DR BioGRID; 109260; 147.
DR DIP; DIP-41775N; -.
DR ELM; P07305; -.
DR IntAct; P07305; 80.
DR MINT; P07305; -.
DR STRING; 9606.ENSP00000344504; -.
DR BindingDB; P07305; -.
DR ChEMBL; CHEMBL3707465; -.
DR GlyGen; P07305; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P07305; -.
DR PhosphoSitePlus; P07305; -.
DR BioMuta; H1F0; -.
DR DMDM; 121897; -.
DR EPD; P07305; -.
DR jPOST; P07305; -.
DR MassIVE; P07305; -.
DR MaxQB; P07305; -.
DR PaxDb; P07305; -.
DR PeptideAtlas; P07305; -.
DR PRIDE; P07305; -.
DR ProteomicsDB; 51978; -. [P07305-1]
DR ProteomicsDB; 51979; -. [P07305-2]
DR TopDownProteomics; P07305-1; -. [P07305-1]
DR ABCD; P07305; 2 sequenced antibodies.
DR Antibodypedia; 211; 741 antibodies from 34 providers.
DR DNASU; 3005; -.
DR Ensembl; ENST00000340857.4; ENSP00000344504.2; ENSG00000189060.6. [P07305-1]
DR GeneID; 3005; -.
DR KEGG; hsa:3005; -.
DR MANE-Select; ENST00000340857.4; ENSP00000344504.2; NM_005318.4; NP_005309.1.
DR UCSC; uc003aty.4; human. [P07305-1]
DR CTD; 3005; -.
DR DisGeNET; 3005; -.
DR GeneCards; H1-0; -.
DR HGNC; HGNC:4714; H1-0.
DR HPA; ENSG00000189060; Tissue enhanced (bone).
DR MIM; 142708; gene.
DR neXtProt; NX_P07305; -.
DR OpenTargets; ENSG00000189060; -.
DR PharmGKB; PA29092; -.
DR VEuPathDB; HostDB:ENSG00000189060; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00810000125570; -.
DR HOGENOM; CLU_052897_1_1_1; -.
DR InParanoid; P07305; -.
DR OMA; HPAYSDM; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P07305; -.
DR TreeFam; TF313664; -.
DR PathwayCommons; P07305; -.
DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; P07305; -.
DR BioGRID-ORCS; 3005; 4 hits in 1073 CRISPR screens.
DR ChiTaRS; H1F0; human.
DR GenomeRNAi; 3005; -.
DR Pharos; P07305; Tchem.
DR PRO; PR:P07305; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P07305; protein.
DR Bgee; ENSG00000189060; Expressed in ventricular zone and 204 other tissues.
DR Genevisible; P07305; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; 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:0017053; C:transcription repressor complex; IDA:UniProtKB.
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:0003680; F:minor groove of adenine-thymine-rich DNA binding; IEA:Ensembl.
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:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin assembly; IGI:UniProtKB.
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:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:UniProtKB.
DR CDD; cd00073; H15; 1.
DR DisProt; DP01156; -.
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 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Chromosome; Citrullination; Direct protein sequencing; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; RNA editing.
FT CHAIN 1..194
FT /note="Histone H1.0"
FT /id="PRO_0000423207"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:9582379,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..194
FT /note="Histone H1.0, N-terminally processed"
FT /id="PRO_0000195904"
FT DOMAIN 24..97
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..194
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="N-acetylthreonine; partial; in Histone H1.0, N-
FT terminally processed"
FT /evidence="ECO:0000269|PubMed:9582379,
FT ECO:0007744|PubMed:19413330"
FT MOD_RES 4
FT /note="Deamidated asparagine; partial"
FT /evidence="ECO:0000269|PubMed:9582379"
FT MOD_RES 42
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 104
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000269|PubMed:27723750"
FT VAR_SEQ 3..19
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042163"
FT VARIANT 1
FT /note="M -> MLGKGRQRRRRQRQRQSPVPRPSDRPAGLGLAKPARRALPTPEPGRK
FT SSDSSLASPGAALQTGPVVRGSGADPEAGFAQPPTRAGPLEGAFNSRTRQATM (in
FT RNA edited version)"
FT /id="VAR_054789"
FT CONFLICT 65
FT /note="D -> H (in Ref. 7; AAH29046)"
FT /evidence="ECO:0000305"
FT HELIX 28..36
FT /evidence="ECO:0007829|PDB:7COW"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:7COW"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:7COW"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:7K5X"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:7COW"
SQ SEQUENCE 194 AA; 20863 MW; 03ED6F01919F8BE1 CRC64;
MTENSTSAPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI QKYIKSHYKV
GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKSDE PKKSVAFKKT KKEIKKVATP
KKASKPKKAA SKAPTKKPKA TPVKKAKKKL AATPKKAKKP KTVKAKPVKA SKPKKAKPVK
PKAKSSAKRA GKKK
