ID H12_HUMAN Reviewed; 213 AA. AC P16403; A8K4I2; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 223. DE RecName: Full=Histone H1.2; DE AltName: Full=Histone H1c; DE AltName: Full=Histone H1d; DE AltName: Full=Histone H1s-1; GN Name=H1-2 {ECO:0000312|HGNC:HGNC:4716}; GN Synonyms=H1F2 {ECO:0000312|HGNC:HGNC:4716}, HIST1H1C GN {ECO:0000312|HGNC:HGNC:4716}; 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=2759094; RA Eick S., Nicolai M., Mumberg D., Doenecke D.; RT "Human H1 histones: conserved and varied sequence elements in two H1 RT subtype genes."; RL Eur. J. Cell Biol. 49:110-115(1989). 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 MRNA]. 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 MRNA]. RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [5] 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 [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]. RC TISSUE=Uterus; 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 PROTEIN SEQUENCE OF 2-213. 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 [9] RP PROTEIN SEQUENCE OF 2-17; 34-46; 55-75 AND 86-97, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT SER-2, METHYLATION AT LYS-34, AND IDENTIFICATION RP 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 [10] RP PROTEIN SEQUENCE OF 2-17; 34-46; 55-63 AND 65-75, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [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=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 [17] RP METHYLATION AT LYS-187 BY EHMT1 AND EHMT2, MUTAGENESIS OF LYS-187, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20334638; DOI=10.1186/1756-8935-3-7; RA Weiss T., Hergeth S., Zeissler U., Izzo A., Tropberger P., Zee B.M., RA Dundr M., Garcia B.A., Daujat S., Schneider R.; RT "Histone H1 variant-specific lysine methylation by G9a/KMT1C and RT Glp1/KMT1D."; RL Epigenetics Chromatin 3:7-7(2010). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2 AND THR-146, 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 CROTONYLATION AT LYS-34; LYS-64; LYS-85; LYS-90; LYS-97; LYS-159 AND RP 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 [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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 [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=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 [23] 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 [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [25] 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-213. 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). RN [26] 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 [27] RP ADP-RIBOSYLATION AT SER-188. 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 [28] RP INTERACTION WITH TSC22D1 ISOFORMS 2 AND 5. RX PubMed=34681573; DOI=10.3390/ijms222010913; RA Kamimura R., Uchida D., Kanno S.I., Shiraishi R., Hyodo T., Sawatani Y., RA Shimura M., Hasegawa T., Tsubura-Okubo M., Yaguchi E., Komiyama Y., RA Fukumoto C., Izumi S., Fujita A., Wakui T., Kawamata H.; RT "Identification of Binding Proteins for TSC22D1 Family Proteins Using Mass RT Spectrometry."; RL Int. J. Mol. Sci. 22:0-0(2021). 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 TSC22D1 isoforms 2 and 5. CC {ECO:0000269|PubMed:34681573}. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in CC euchromatin. Distribution goes in parallel with DNA concentration. 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:P15864}. 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: 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:P15864}. CC -!- PTM: ADP-ribosylated on Ser-188 in response to DNA damage. CC {ECO:0000269|PubMed:27723750}. 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; X57129; CAA40408.1; -; Genomic_DNA. DR EMBL; AF531300; AAN06700.1; -; Genomic_DNA. DR EMBL; AK290947; BAF83636.1; -; mRNA. DR EMBL; AB451259; BAG70073.1; -; mRNA. DR EMBL; AB451385; BAG70199.1; -; mRNA. DR EMBL; U91328; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471087; EAW55515.1; -; Genomic_DNA. DR EMBL; BC002649; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS4577.1; -. DR PIR; S26364; HSHU11. DR RefSeq; NP_005310.1; NM_005319.3. DR PDB; 8H0V; EM; 3.80 A; u=1-213. DR PDB; 8H0W; EM; 4.60 A; u=1-213. DR PDBsum; 8H0V; -. DR PDBsum; 8H0W; -. DR AlphaFoldDB; P16403; -. DR SMR; P16403; -. DR BioGRID; 109261; 718. DR DIP; DIP-36359N; -. DR IntAct; P16403; 243. DR MINT; P16403; -. DR STRING; 9606.ENSP00000339566; -. DR GlyGen; P16403; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P16403; -. DR PhosphoSitePlus; P16403; -. DR SwissPalm; P16403; -. DR BioMuta; HIST1H1C; -. DR DMDM; 417101; -. DR EPD; P16403; -. DR jPOST; P16403; -. DR MassIVE; P16403; -. DR MaxQB; P16403; -. DR PaxDb; 9606-ENSP00000339566; -. DR PeptideAtlas; P16403; -. DR PRIDE; P16403; -. DR ProteomicsDB; 53353; -. DR Pumba; P16403; -. DR TopDownProteomics; P16403; -. DR Antibodypedia; 25499; 595 antibodies from 31 providers. DR DNASU; 3006; -. DR Ensembl; ENST00000343677.4; ENSP00000339566.3; ENSG00000187837.4. DR GeneID; 3006; -. DR KEGG; hsa:3006; -. DR MANE-Select; ENST00000343677.4; ENSP00000339566.3; NM_005319.4; NP_005310.1. DR UCSC; uc003nfw.4; human. DR AGR; HGNC:4716; -. DR CTD; 3006; -. DR DisGeNET; 3006; -. DR GeneCards; H1-2; -. DR HGNC; HGNC:4716; H1-2. DR HPA; ENSG00000187837; Low tissue specificity. DR MIM; 142710; gene. DR neXtProt; NX_P16403; -. DR OpenTargets; ENSG00000187837; -. DR PharmGKB; PA29094; -. DR VEuPathDB; HostDB:ENSG00000187837; -. DR eggNOG; KOG4012; Eukaryota. DR GeneTree; ENSGT00940000163082; -. DR HOGENOM; CLU_052897_7_0_1; -. DR InParanoid; P16403; -. DR OMA; FPTGNRP; -. DR OrthoDB; 5362469at2759; -. DR PhylomeDB; P16403; -. DR TreeFam; TF313664; -. DR PathwayCommons; P16403; -. DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation. DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF). DR SignaLink; P16403; -. DR SIGNOR; P16403; -. DR BioGRID-ORCS; 3006; 42 hits in 1159 CRISPR screens. DR ChiTaRS; HIST1H1C; human. DR GeneWiki; HIST1H1C; -. DR GenomeRNAi; 3006; -. DR Pharos; P16403; Tbio. DR PRO; PR:P16403; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P16403; Protein. DR Bgee; ENSG00000187837; Expressed in calcaneal tendon and 176 other cell types or tissues. DR GO; GO:0000791; C:euchromatin; 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; 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: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; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR11467; HISTONE H1; 1. DR PANTHER; PTHR11467:SF86; HISTONE H1.2; 1. 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; P16403; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; 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.10, FT ECO:0000269|Ref.9, 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 CHAIN 2..213 FT /note="Histone H1.2" FT /id="PRO_0000195906" 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..213 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 171..190 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..213 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.10, ECO:0000269|Ref.9, 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 MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 17 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P15864" 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:0000269|Ref.9" 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:0000250|UniProtKB:P15864" 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:0000269|PubMed:21925322" 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:0000269|PubMed:21925322" FT MOD_RES 97 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P15864" 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:0007744|PubMed:20068231" 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 187 FT /note="N6-methyllysine; by EHMT1 and EHMT2" FT /evidence="ECO:0000269|PubMed:20334638" FT MOD_RES 188 FT /note="ADP-ribosylserine" FT /evidence="ECO:0000269|PubMed:27723750" FT MOD_RES 213 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000269|PubMed:24681537" FT VARIANT 18 FT /note="A -> V (in dbSNP:rs2230653)" FT /id="VAR_003618" FT VARIANT 113 FT /note="S -> A (in dbSNP:rs34810376)" FT /id="VAR_049304" FT VARIANT 124 FT /note="G -> A (in dbSNP:rs12111009)" FT /id="VAR_049305" FT MUTAGEN 187 FT /note="K->R: Abolishes methylation." FT /evidence="ECO:0000269|PubMed:20334638" SQ SEQUENCE 213 AA; 21365 MW; AA66EA1901D8D56B CRC64; MSETAPAAPA AAPPAEKAPV KKKAAKKAGG TPRKASGPPV SELITKAVAA SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKV KKAGGTKPKK PVGAAKKPKK AAGGATPKKS AKKTPKKAKK PAAATVTKKV AKSPKKAKVA KPKKAAKSAA KAVKPKAAKP KVVKPKKAAP KKK //