H12_HUMAN
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 03-AUG-2022, entry version 214.
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},
GN HIST1H1C {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=10.1006/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].
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).
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=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}.
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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 AlphaFoldDB; P16403; -.
DR SMR; P16403; -.
DR BioGRID; 109261; 651.
DR DIP; DIP-36359N; -.
DR IntAct; P16403; 233.
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; P16403; -.
DR PeptideAtlas; P16403; -.
DR PRIDE; P16403; -.
DR ProteomicsDB; 53353; -.
DR TopDownProteomics; P16403; -.
DR Antibodypedia; 25499; 500 antibodies from 30 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 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; 1565299at2759; -.
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 BioGRID-ORCS; 3006; 35 hits in 1084 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 174 other tissues.
DR Genevisible; P16403; HS.
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: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; 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
