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 04-NOV-2026, entry version 234. DE RecName: Full=Histone H1.2 {ECO:0000303|PubMed:38530350}; 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 FUNCTION, AND MUTAGENESIS OF 120-VAL--VAL-132. RX PubMed=26581166; DOI=10.1038/srep16714; RA Kim J.M., Kim K., Punj V., Liang G., Ulmer T.S., Lu W., An W.; RT "Linker histone H1.2 establishes chromatin compaction and gene silencing RT through recognition of H3K27me3."; RL Sci. Rep. 5:16714-16714(2015). RN [28] 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 [29] RP PHOSPHORYLATION AT SER-173. RX PubMed=28539972; DOI=10.1186/s13072-017-0135-3; RA Liao R., Mizzen C.A.; RT "Site-specific regulation of histone H1 phosphorylation in pluripotent cell RT differentiation."; RL Epigenetics Chromatin 10:29-29(2017). RN [30] RP SUBCELLULAR LOCATION. RX PubMed=29301938; DOI=10.1074/jbc.m117.810184; RA Chen J., Teo B.H.D., Cai Y., Wee S.Y.K., Lu J.; RT "The linker histone H1.2 is a novel component of the nucleolar organizer RT regions."; RL J. Biol. Chem. 293:2358-2369(2018). RN [31] RP BENZOYLATION AT LYS-26 AND LYS-148. RX PubMed=30154464; DOI=10.1038/s41467-018-05567-w; RA Huang H., Zhang D., Wang Y., Perez-Neut M., Han Z., Zheng Y.G., Hao Q., RA Zhao Y.; RT "Lysine benzoylation is a histone mark regulated by SIRT2."; RL Nat. Commun. 9:3374-3374(2018). RN [32] 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). RN [33] RP METHACRYLATION AT LYS-46; LYS-52; LYS-63; LYS-64; LYS-85; LYS-90 AND RP LYS-106. RX PubMed=34961760; DOI=10.1038/s41421-021-00344-4; RA Delaney K., Tan M., Zhu Z., Gao J., Dai L., Kim S., Ding J., He M., RA Halabelian L., Yang L., Nagarajan P., Parthun M.R., Lee S., Khochbin S., RA Zheng Y.G., Zhao Y.; RT "Histone lysine methacrylation is a dynamic post-translational modification RT regulated by HAT1 and SIRT2."; RL Cell Discov. 7:122-122(2021). RN [34] RP ISONICOTINYLATION AT LYS-34; LYS-90; LYS-117; LYS-148 AND LYS-168. RX PubMed=34545082; DOI=10.1038/s41467-021-25867-y; RA Jiang Y., Li Y., Liu C., Zhang L., Lv D., Weng Y., Cheng Z., Chen X., RA Zhan J., Zhang H.; RT "Isonicotinylation is a histone mark induced by the anti-tuberculosis RT first-line drug isoniazid."; RL Nat. Commun. 12:5548-5548(2021). RN [35] RP FUNCTION. RX PubMed=37922872; DOI=10.1016/j.molcel.2023.10.003; RA Pascal C., Zonszain J., Hameiri O., Gargi-Levi C., Lev-Maor G., Tammer L., RA Levy T., Tarabeih A., Roy V.R., Ben-Salmon S., Elbaz L., Eid M., Hakim T., RA Abu Rabe'a S., Shalev N., Jordan A., Meshorer E., Ast G.; RT "Human histone H1 variants impact splicing outcome by controlling RNA RT polymerase II elongation."; RL Mol. Cell 83:3801-3817(2023). RN [36] RP FUNCTION. RX PubMed=37429872; DOI=10.1038/s41467-023-39846-y; RA Liu C., Yu J., Song A., Wang M., Hu J., Chen P., Zhao J., Li G.; RT "Histone H1 facilitates restoration of H3K27me3 during DNA replication by RT chromatin compaction."; RL Nat. Commun. 14:4081-4081(2023). RN [37] RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT THR-165. RX PubMed=38530350; DOI=10.7554/elife.91306; RA Salinas-Pena M., Rebollo E., Jordan A.; RT "Imaging analysis of six human histone H1 variants reveals universal RT enrichment of H1.2, H1.3, and H1.5 at the nuclear periphery and nucleolar RT H1X presence."; RL Elife 12:0-0(2024). RN [38] RP FUNCTION, AND INDUCTION. RX PubMed=40516528; DOI=10.1016/j.molcel.2025.05.031; RA Matthews R.E., Danac J.M.C., Naden E.L., Farleigh Smith L.E., Lestari S., RA Gungi A., Appert A., Buttress T., Verma A., Sinclair O., Chong F., RA Suberu J., Antrobus R., Bonev B., Dawson M.A., Reid A.J., Timms R.T., RA Ahringer J., Tchasovnikarova I.A.; RT "CRAMP1 drives linker histone expression to enable Polycomb repression."; RL Mol. Cell 0:0-0(2025). RN [39] RP INDUCTION. RX PubMed=40516529; DOI=10.1016/j.molcel.2025.04.006; RA Ingham A., de Vega I.A., Morlot L., Gittens W., Hendriks I.A., RA Kakulidis E.S., Freire R., Davey N.E., Duxin J.P., Lund Nielsen M., RA Mailand N.; RT "CRAMP1-dependent histone H1 biogenesis is essential for topoisomerase II RT inhibitor tolerance."; RL Mol. Cell 0:0-0(2025). RN [40] RP DEAMIDATION AT ASN-76 AND ASN-77, AND ACETYLATION AT LYS-75. RX PubMed=40240600; DOI=10.1038/s41586-025-08835-0; RA Tian Y., Feng T., Zhang J., Meng Q., Zhan W., Tang M., Liu C., Li M., RA Tao W., Shu Y., Zhang Y., Chen F., Takeda S., Zhu Q., Lu X., Zhu W.G.; RT "Histone H1 deamidation facilitates chromatin relaxation for DNA repair."; RL Nature 0:0-0(2025). RN [41] {ECO:0007744|PDB:8H0V, ECO:0007744|PDB:8H0W} RP STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH NUCLEOSOME, FUNCTION, AND RP SUBUNIT. RX PubMed=36435862; DOI=10.1038/s41467-022-35003-z; RA Hirano R., Ehara H., Kujirai T., Uejima T., Takizawa Y., Sekine S.I., RA Kurumizaka H.; RT "Structural basis of RNA polymerase II transcription on the chromatosome RT containing linker histone H1."; RL Nat. Commun. 13:7287-7287(2022). CC -!- FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes CC forming the macromolecular structure known as the chromatin fiber CC (PubMed:26581166, PubMed:38530350). Histone H1-2 is required for the CC condensation of nucleosome chains into higher-order structured fibers CC (PubMed:38530350). Compared to other histone H1 variants, H1-2 plays an CC essential role in nucleosome condensation: its absence leads to global CC chromatin decompaction, which is not observed when depleting other CC histone H1 variants (PubMed:38530350). Histone H1-2 also acts as a CC histone reader: specifically recognizes and binds histone H3 CC trimethylated at 'lys-27' (H3K27me3) (PubMed:26581166). Histones H1 CC also promote formation of the H3K27me3 mark by the PRC2/EED-EZH2 CC complex, possibly by facilitating restoration of H3K27me3 post- CC replication (PubMed:37429872, PubMed:40516528). Together with histone CC H1-3, histone H1-2 acts as a regulator of splicing, most specifically CC exon skipping and intron retention events: histone H1-2 has a high CC affinity for exons and regulates splicing by affecting RNA polymerase CC II (RNAPII) elongation (PubMed:37922872). Also acts as a regulator of CC individual gene transcription through chromatin remodeling, nucleosome CC spacing and DNA methylation (PubMed:38530350). CC {ECO:0000269|PubMed:26581166, ECO:0000269|PubMed:37429872, CC ECO:0000269|PubMed:37922872, ECO:0000269|PubMed:38530350, CC ECO:0000269|PubMed:40516528}. CC -!- SUBUNIT: Associates with nucleosomes, promoting condensation into CC higher-order structured chromatin (PubMed:36435862). Interacts with CC TSC22D1 isoforms 2 and 5 (PubMed:34681573). CC {ECO:0000269|PubMed:34681573, ECO:0000269|PubMed:36435862}. CC -!- INTERACTION: CC P16403; Q9UIG0: BAZ1B; NbExp=2; IntAct=EBI-358372, EBI-927482; CC P16403; Q9NR30: DDX21; NbExp=2; IntAct=EBI-358372, EBI-357942; CC P16403; Q8IY81: FTSJ3; NbExp=2; IntAct=EBI-358372, EBI-744088; CC P16403; Q8IUE6: H2AC21; NbExp=2; IntAct=EBI-358372, EBI-1642157; CC P16403; Q16778: H2BC21; NbExp=2; IntAct=EBI-358372, EBI-1056125; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:38530350}. Nucleus, CC nucleolus {ECO:0000269|PubMed:29301938, ECO:0000269|PubMed:38530350}. CC Chromosome {ECO:0000269|PubMed:26581166, ECO:0000269|PubMed:29301938, CC ECO:0000269|PubMed:38530350}. Note=Enriched at the nuclear periphery CC and colocalizes with compacted DNA (heterochromatin) (PubMed:26581166, CC PubMed:38530350). Enriched within lamina-associated domains CC (PubMed:38530350). {ECO:0000269|PubMed:26581166, CC ECO:0000269|PubMed:38530350}. CC -!- INDUCTION: Expression is activated by transcription factor CRAMP1, in CC collaboration with NPAT and GON4L. {ECO:0000269|PubMed:40516528, CC ECO:0000269|PubMed:40516529}. CC -!- DOMAIN: The C-terminal domain is required for high-affinity binding to CC chromatin. {ECO:0000250|UniProtKB:Q02539}. CC -!- PTM: Deamidation of Asn-76 and Asn-77 by CTPS1 in response to DNA CC damage promotes subsequent acetylation of histo75 (H1K75ac). CC {ECO:0000250|UniProtKB:P10412}. CC -!- PTM: Acetylated at Lys-75 (H1K75ac) by EP300 following deamidation of CC Asn-76 and Asn-77 by CTPS1 in response to DNA damage, thereby CC increasing chromatin accessibility to facilitate the recruitment of DNA CC repair proteins. {ECO:0000250|UniProtKB:P10412}. 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 Phosphorylation at Thr-165 is associated with condensed chromosomes, CC with maximum levels occurring at metaphase and drastically dropping CC down at later mitotic phases (PubMed:38530350). During interphase, CC phosphorylation at Thr-165 is enriched within nucleoli CC (PubMed:38530350). {ECO:0000250|UniProtKB:P15864, CC ECO:0000269|PubMed:38530350}. 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_005319.4. DR PDB; 8H0V; EM; 3.80 A; u=1-213. DR PDB; 8H0W; EM; 4.60 A; u=1-213. DR PDB; 8KE0; EM; 4.00 A; K=1-213. DR AlphaFoldDB; P16403; -. DR EMDB; EMD-34415; -. DR EMDB; EMD-34416; -. DR EMDB; EMD-37149; -. DR SMR; P16403; -. DR BioGRID; 109261; 870. DR DIP; DIP-36359N; -. DR FunCoup; P16403; 1336. DR IntAct; P16403; 377. DR STRING; 9606.ENSP00000339566; -. DR BindingDB; P16403; -. DR ChEMBL; CHEMBL5724671; -. 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 jPOST; P16403; -. DR MassIVE; P16403; -. DR PaxDb; 9606-ENSP00000339566; -. DR PeptideAtlas; P16403; -. DR PRIDE; P16403; -. DR ProteomicsDB; 53353; -. DR Pumba; P16403; -. DR TopDownProteomics; P16403; -. DR Antibodypedia; 25499; 633 antibodies from 35 providers. DR DNASU; 3006; -. DR Ensembl; ENST00000343677.4; ENSP00000339566.3; ENSG00000187837.5. DR Ensembl; ENST00000718281.1; ENSP00000520720.1; ENSG00000187837.5. 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 CIViC; 3006; 1 evidence item across 1 molecular profile. DR ClinPGx; PA29094; -. DR CTD; 3006; -. DR DisGeNET; 3006; -. DR GeneCards; H1-2; -. DR HGNC; HGNC:4716; H1-2. DR HPA; ENSG00000187837; Low tissue specificity. DR MalaCards; H1-2; -. DR MIM; 142710; gene. DR OpenTargets; ENSG00000187837; -. DR VEuPathDB; HostDB:ENSG00000187837; -. DR eggNOG; KOG4012; Eukaryota. DR GeneTree; ENSGT00940000163082; -. DR HOGENOM; CLU_052897_7_0_1; -. DR InParanoid; P16403; -. DR OMA; AHPTYQK; -. DR OrthoDB; 9486420at2759; -. DR PAN-GO; P16403; 6 GO annotations based on evolutionary models. DR PhylomeDB; P16403; -. 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 Agora; ENSG00000187837; -. DR BioGRID-ORCS; 3006; 42 hits in 1159 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. 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:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB. DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0061628; F:histone H3K27me3 reader activity; IDA: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; IDA:UniProtKB. DR GO; GO:0030261; P:chromosome condensation; IDA:UniProtKB. DR GO; GO:0140718; P:facultative heterochromatin formation; IDA:GO_Central. 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:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB. DR CDD; cd00073; H15; 1. DR FunFam; 1.10.10.10:FF:000075; Histone H1 like; 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. 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; Proteomics identification; 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 1..17 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 119..140 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..160 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 169..186 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..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 26 FT /note="N6-benzoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:30154464" 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-isonicotinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:34545082" 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; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 46 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000269|PubMed:34961760" 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 52 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000269|PubMed:34961760" 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 63 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000269|PubMed:34961760" 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 64 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000269|PubMed:34961760" FT MOD_RES 75 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:24681537" FT MOD_RES 75 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:40240600" FT MOD_RES 76 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:40240600" FT MOD_RES 77 FT /note="Deamidated asparagine" FT /evidence="ECO:0000269|PubMed:40240600" 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 85 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000269|PubMed:34961760" 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 90 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:34545082" FT MOD_RES 90 FT /note="N6-methacryllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P10412" 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 106 FT /note="N6-methacryllysine" FT /evidence="ECO:0000250|UniProtKB:P10412" 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 117 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:34545082" 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 148 FT /note="N6-benzoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:30154464" FT MOD_RES 148 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:34545082" 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 165 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:38530350" 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 168 FT /note="N6-isonicotinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:34545082" FT MOD_RES 173 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:28539972" 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 120..132 FT /note="VKKAGGTKPKKPV->AKKAGGAKPKKPA: Impared ability to FT recognize and bind histone H3 trimethylated at 'lys-27' FT (H3K27me3)." FT /evidence="ECO:0000269|PubMed:26581166" 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 //