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Database: UniProt/SWISS-PROT
Entry: H31_HUMAN
LinkDB: H31_HUMAN
Original site: H31_HUMAN 
ID   H31_HUMAN               Reviewed;         136 AA.
AC   P68431; A0PJT7; A5PLR1; P02295; P02296; P16106; Q6ISV8; Q6NWP8;
AC   Q6NWP9; Q6NXU4; Q71DJ3; Q93081;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   20-JUN-2018, entry version 163.
DE   RecName: Full=Histone H3.1;
DE   AltName: Full=Histone H3/a;
DE   AltName: Full=Histone H3/b;
DE   AltName: Full=Histone H3/c;
DE   AltName: Full=Histone H3/d;
DE   AltName: Full=Histone H3/f;
DE   AltName: Full=Histone H3/h;
DE   AltName: Full=Histone H3/i;
DE   AltName: Full=Histone H3/j;
DE   AltName: Full=Histone H3/k;
DE   AltName: Full=Histone H3/l;
GN   Name=HIST1H3A; Synonyms=H3FA;
GN   and
GN   Name=HIST1H3B; Synonyms=H3FL;
GN   and
GN   Name=HIST1H3C; Synonyms=H3FC;
GN   and
GN   Name=HIST1H3D; Synonyms=H3FB;
GN   and
GN   Name=HIST1H3E; Synonyms=H3FD;
GN   and
GN   Name=HIST1H3F; Synonyms=H3FI;
GN   and
GN   Name=HIST1H3G; Synonyms=H3FH;
GN   and
GN   Name=HIST1H3H; Synonyms=H3FK;
GN   and
GN   Name=HIST1H3I; Synonyms=H3FF;
GN   and
GN   Name=HIST1H3J; Synonyms=H3FJ;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
RX   PubMed=6647026; DOI=10.1093/nar/11.21.7409;
RA   Zhong R., Roeder R.G., Heintz N.;
RT   "The primary structure and expression of four cloned human histone
RT   genes.";
RL   Nucleic Acids Res. 11:7409-7425(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3013246;
RA   Marashi F., Helms S., Shiels A., Silverstein S., Greenspan D.S.,
RA   Stein G., Stein J.;
RT   "Enhancer-facilitated expression of prokaryotic and eukaryotic genes
RT   using human histone gene 5' regulatory sequences.";
RL   Biochem. Cell Biol. 64:277-289(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H3FD).
RX   PubMed=1916825; DOI=10.1016/0888-7543(91)90183-F;
RA   Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
RT   "Isolation and characterization of two human H1 histone genes within
RT   clusters of core histone genes.";
RL   Genomics 10:940-948(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8227173; DOI=10.1002/jcb.240520402;
RA   Kardalinou E., Eick S., Albig W., Doenecke D.;
RT   "Association of a human H1 histone gene with an H2A pseudogene and
RT   genes encoding H2B.1 and H3.1 histones.";
RL   J. Cell. Biochem. 52:375-383(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RA   Runge D., Eick S., Doenecke D.;
RT   "Expression of human histone h1.1 and the nearby core histones.";
RL   Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3I).
RX   PubMed=9031620; DOI=10.1016/S0378-1119(96)00582-3;
RA   Albig W., Meergans T., Doenecke D.;
RT   "Characterization of the H1.5 gene completes the set of human H1
RT   subtype genes.";
RL   Gene 184:141-148(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3D; HIST1H3F AND HIST1H3G).
RX   PubMed=9119399; DOI=10.1006/geno.1996.4592;
RA   Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.;
RT   "Human histone gene organization: nonregular arrangement within a
RT   large cluster.";
RL   Genomics 40:314-322(1997).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3H AND HIST1H3J).
RX   PubMed=9439656; DOI=10.1007/s004390050630;
RA   Albig W., Doenecke D.;
RT   "The human histone gene cluster at the D6S105 locus.";
RL   Hum. Genet. 101:284-294(1997).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3A; HIST1H3B; HIST1H3C;
RP   HIST1H3D; HIST1H3E; HIST1H3F; HIST1H3G; HIST1H3H; HIST1H3I; HIST1H3J).
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   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Caudate nucleus, Stomach, and Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [12]
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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [13]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [14]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Spleen;
RX   PubMed=7309716;
RA   Ohe Y., Iwai K.;
RT   "Human spleen histone H3. Isolation and amino acid sequence.";
RL   J. Biochem. 90:1205-1211(1981).
RN   [15]
RP   PROTEIN SEQUENCE OF 2-20, METHYLATION AT LYS-10; LYS-28 AND LYS-37,
RP   PHOSPHORYLATION AT THR-4; SER-11 AND SER-29, ACETYLATION AT LYS-10 AND
RP   LYS-15, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16185088; DOI=10.1021/bi050906n;
RA   Garcia B.A., Barber C.M., Hake S.B., Ptak C., Turner F.B., Busby S.A.,
RA   Shabanowitz J., Moran R.G., Allis C.D., Hunt D.F.;
RT   "Modifications of human histone H3 variants during mitosis.";
RL   Biochemistry 44:13202-13213(2005).
RN   [16]
RP   PROTEIN SEQUENCE OF 58-64; 117-120 AND 124-135, AND PHOSPHORYLATION AT
RP   SER-11 AND SER-29.
RX   PubMed=10464286; DOI=10.1074/jbc.274.36.25543;
RA   Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,
RA   Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
RT   "Identification of a novel phosphorylation site on histone H3 coupled
RT   with mitotic chromosome condensation.";
RL   J. Biol. Chem. 274:25543-25549(1999).
RN   [17]
RP   METHYLATION AT LYS-10.
RX   PubMed=11242053; DOI=10.1038/35065132;
RA   Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.;
RT   "Methylation of histone H3 lysine 9 creates a binding site for HP1
RT   proteins.";
RL   Nature 410:116-120(2001).
RN   [18]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=11856369; DOI=10.1046/j.1356-9597.2001.00498.x;
RA   Goto H., Yasui Y., Nigg E.A., Inagaki M.;
RT   "Aurora-B phosphorylates Histone H3 at serine28 with regard to the
RT   mitotic chromosome condensation.";
RL   Genes Cells 7:11-17(2002).
RN   [19]
RP   PHOSPHORYLATION AT SER-11 AND THR-12.
RX   PubMed=12560483; DOI=10.1093/nar/gkg176;
RA   Preuss U., Landsberg G., Scheidtmann K.H.;
RT   "Novel mitosis-specific phosphorylation of histone H3 at Thr11
RT   mediated by Dlk/ZIP kinase.";
RL   Nucleic Acids Res. 31:878-885(2003).
RN   [20]
RP   METHYLATION AT ARG-18.
RX   PubMed=15471871; DOI=10.1074/jbc.M410021200;
RA   Ananthanarayanan M., Li S., Balasubramaniyan N., Suchy F.J.,
RA   Walsh M.J.;
RT   "Ligand-dependent activation of the farnesoid X-receptor directs
RT   arginine methylation of histone H3 by CARM1.";
RL   J. Biol. Chem. 279:54348-54357(2004).
RN   [21]
RP   METHYLATION AT LYS-80.
RX   PubMed=15525939; DOI=10.1038/nature03114;
RA   Huyen Y., Zgheib O., Ditullio R.A. Jr., Gorgoulis V.G., Zacharatos P.,
RA   Petty T.J., Sheston E.A., Mellert H.S., Stavridi E.S.,
RA   Halazonetis T.D.;
RT   "Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand
RT   breaks.";
RL   Nature 432:406-411(2004).
RN   [22]
RP   CITRULLINATION AT ARG-9 AND ARG-18, AND METHYLATION AT ARG-18.
RX   PubMed=15345777; DOI=10.1126/science.1101400;
RA   Wang Y., Wysocka J., Sayegh J., Lee Y.-H., Perlin J.R., Leonelli L.,
RA   Sonbuchner L.S., McDonald C.H., Cook R.G., Dou Y., Roeder R.G.,
RA   Clarke S., Stallcup M.R., Allis C.D., Coonrod S.A.;
RT   "Human PAD4 regulates histone arginine methylation levels via
RT   demethylimination.";
RL   Science 306:279-283(2004).
RN   [23]
RP   PHOSPHORYLATION AT THR-4; SER-11 AND SER-29.
RX   PubMed=15681610; DOI=10.1101/gad.1267105;
RA   Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
RT   "The kinase haspin is required for mitotic histone H3 Thr 3
RT   phosphorylation and normal metaphase chromosome alignment.";
RL   Genes Dev. 19:472-488(2005).
RN   [24]
RP   PHOSPHORYLATION AT SER-29.
RX   PubMed=15684425; DOI=10.1074/jbc.M410521200;
RA   Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
RT   "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage
RT   kinase-like mitogen-activated protein triple kinase alpha.";
RL   J. Biol. Chem. 280:13545-13553(2005).
RN   [25]
RP   METHYLATION AT LYS-37 AND LYS-38, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=15983376; DOI=10.1073/pnas.0503189102;
RA   Coon J.J., Ueberheide B., Syka J.E.P., Dryhurst D.D., Ausio J.,
RA   Shabanowitz J., Hunt D.F.;
RT   "Protein identification using sequential ion/ion reactions and tandem
RT   mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:9463-9468(2005).
RN   [26]
RP   ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, METHYLATION AT
RP   LYS-5; LYS-10; LYS-19; LYS-28; LYS-37; LYS-65; LYS-80 AND LYS-123, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16267050; DOI=10.1074/jbc.M509266200;
RA   Hake S.B., Garcia B.A., Duncan E.M., Kauer M., Dellaire G.,
RA   Shabanowitz J., Bazett-Jones D.P., Allis C.D., Hunt D.F.;
RT   "Expression patterns and post-translational modifications associated
RT   with mammalian histone H3 variants.";
RL   J. Biol. Chem. 281:559-568(2006).
RN   [27]
RP   METHYLATION AT LYS-5 AND LYS-10, ACETYLATION AT LYS-10; LYS-15 AND
RP   LYS-24, PHOSPHORYLATION AT SER-11 AND SER-29, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=16457588; DOI=10.1021/pr050266a;
RA   Thomas C.E., Kelleher N.L., Mizzen C.A.;
RT   "Mass spectrometric characterization of human histone H3: a bird's eye
RT   view.";
RL   J. Proteome Res. 5:240-247(2006).
RN   [28]
RP   UBIQUITINATION.
RX   PubMed=16678110; DOI=10.1016/j.molcel.2006.03.035;
RA   Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H.,
RA   Tempst P., Xiong Y., Zhang Y.;
RT   "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin
RT   ligase facilitates cellular response to DNA damage.";
RL   Mol. Cell 22:383-394(2006).
RN   [29]
RP   ACETYLATION AT LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28, METHYLATION
RP   AT LYS-28; LYS-37 AND LYS-80, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16627869; DOI=10.1074/mcp.M600007-MCP200;
RA   Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,
RA   Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
RT   "Quantitative proteomic analysis of post-translational modifications
RT   of human histones.";
RL   Mol. Cell. Proteomics 5:1314-1325(2006).
RN   [30]
RP   ACETYLATION AT LYS-10 AND LYS-15, METHYLATION AT ARG-18, AND
RP   CITRULLINATION AT ARG-18.
RX   PubMed=16497732; DOI=10.1210/me.2005-0365;
RA   Miao F., Li S., Chavez V., Lanting L., Natarajan R.;
RT   "Coactivator-associated arginine methyltransferase-1 enhances nuclear
RT   factor-kappaB-mediated gene transcription through methylation of
RT   histone H3 at arginine 17.";
RL   Mol. Endocrinol. 20:1562-1573(2006).
RN   [31]
RP   CITRULLINATION AT ARG-3; ARG-9; ARG-18 AND ARG-27.
RX   PubMed=16567635; DOI=10.1073/pnas.0509639103;
RA   Arita K., Shimizu T., Hashimoto H., Hidaka Y., Yamada M., Sato M.;
RT   "Structural basis for histone N-terminal recognition by human
RT   peptidylarginine deiminase 4.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5291-5296(2006).
RN   [32]
RP   METHYLATION AT ARG-3 BY PRMT6.
RX   PubMed=18079182; DOI=10.1101/gad.447007;
RA   Hyllus D., Stein C., Schnabel K., Schiltz E., Imhof A., Dou Y.,
RA   Hsieh J., Bauer U.M.;
RT   "PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4
RT   trimethylation.";
RL   Genes Dev. 21:3369-3380(2007).
RN   [33]
RP   ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28; LYS-37;
RP   LYS-57 AND LYS-80, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24;
RP   LYS-28; LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=17194708; DOI=10.1074/jbc.M607900200;
RA   Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
RA   Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
RT   "Organismal differences in post-translational modifications in
RT   histones H3 and H4.";
RL   J. Biol. Chem. 282:7641-7655(2007).
RN   [34]
RP   ACETYLATION AT LYS-37.
RX   PubMed=17189264; DOI=10.1074/jbc.M607909200;
RA   Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
RA   Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT   "Identification of histone H3 lysine 36 acetylation as a highly
RT   conserved histone modification.";
RL   J. Biol. Chem. 282:7632-7640(2007).
RN   [35]
RP   METHYLATION AT ARG-3 BY PRMT6.
RX   PubMed=17898714; DOI=10.1038/nature06166;
RA   Guccione E., Bassi C., Casadio F., Martinato F., Cesaroni M.,
RA   Schuchlautz H., Luescher B., Amati B.;
RT   "Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are
RT   mutually exclusive.";
RL   Nature 449:933-937(2007).
RN   [36]
RP   PHOSPHORYLATION AT THR-12 BY CHEK1.
RX   PubMed=18243098; DOI=10.1016/j.cell.2007.12.013;
RA   Shimada M., Niida H., Zineldeen D.H., Tagami H., Tanaka M., Saito H.,
RA   Nakanishi M.;
RT   "Chk1 is a histone H3 threonine 11 kinase that regulates DNA damage-
RT   induced transcriptional repression.";
RL   Cell 132:221-232(2008).
RN   [37]
RP   METHYLATION AT ARG-3 BY PRMT6.
RX   PubMed=18077460; DOI=10.1074/jbc.C700192200;
RA   Iberg A.N., Espejo A., Cheng D., Kim D., Michaud-Levesque J.,
RA   Richard S., Bedford M.T.;
RT   "Arginine methylation of the histone H3 tail impedes effector
RT   binding.";
RL   J. Biol. Chem. 283:3006-3010(2008).
RN   [38]
RP   PHOSPHORYLATION AT THR-12.
RX   PubMed=18066052; DOI=10.1038/ncb1668;
RA   Metzger E., Yin N., Wissmann M., Kunowska N., Fischer K.,
RA   Friedrichs N., Patnaik D., Higgins J.M., Potier N., Scheidtmann K.H.,
RA   Buettner R., Schule R.;
RT   "Phosphorylation of histone H3 at threonine 11 establishes a novel
RT   chromatin mark for transcriptional regulation.";
RL   Nat. Cell Biol. 10:53-60(2008).
RN   [39]
RP   ACETYLATION AT LYS-116 AND LYS-123.
RX   PubMed=19520870; DOI=10.1074/jbc.M109.003202;
RA   Manohar M., Mooney A.M., North J.A., Nakkula R.J., Picking J.W.,
RA   Edon A., Fishel R., Poirier M.G., Ottesen J.J.;
RT   "Acetylation of histone H3 at the nucleosome dyad alters DNA-histone
RT   binding.";
RL   J. Biol. Chem. 284:23312-23321(2009).
RN   [40]
RP   PHOSPHORYLATION AT TYR-42.
RX   PubMed=19783980; DOI=10.1038/nature08448;
RA   Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,
RA   Green A.R., Kouzarides T.;
RT   "JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from
RT   chromatin.";
RL   Nature 461:819-822(2009).
RN   [41]
RP   PHOSPHORYLATION AT SER-58 AND THR-81.
RX   PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
RA   Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,
RA   Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,
RA   Mann M.;
RT   "Quantitative interaction proteomics and genome-wide profiling of
RT   epigenetic histone marks and their readers.";
RL   Cell 142:967-980(2010).
RN   [42]
RP   PHOSPHORYLATION AT THR-7.
RX   PubMed=20228790; DOI=10.1038/nature08839;
RA   Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
RA   Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
RA   Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
RT   "Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation
RT   at histone H3K4.";
RL   Nature 464:792-796(2010).
RN   [43]
RP   CROTONYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-57.
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.,
RA   Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT   "Identification of 67 histone marks and histone lysine crotonylation
RT   as a new type of histone modification.";
RL   Cell 146:1016-1028(2011).
RN   [44]
RP   METHYLATION AT LYS-57.
RX   PubMed=22387026; DOI=10.1016/j.molcel.2012.01.019;
RA   Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A.,
RA   Carey M.F., Grunstein M.;
RT   "Histone H3 lysine 56 methylation regulates DNA replication through
RT   its interaction with PCNA.";
RL   Mol. Cell 46:7-17(2012).
RN   [45]
RP   CAUTION.
RX   PubMed=22483618; DOI=10.1016/j.molcel.2012.03.002;
RA   Herranz N., Dave N., Millanes-Romero A., Morey L., Diaz V.M.,
RA   Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C., Di Croce L.,
RA   Garcia de Herreros A., Peiro S.;
RT   "Lysyl oxidase-like 2 deaminates lysine 4 in histone H3.";
RL   Mol. Cell 46:369-376(2012).
RN   [46]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., 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   [47]
RP   RETRACTION.
RX   PubMed=27392148; DOI=10.1016/j.molcel.2016.06.013;
RA   Herranz N., Dave N., Millanes-Romero A., Morey L., Diaz V.M.,
RA   Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C., Di Croce L.,
RA   Garcia de Herreros A., Peiro S.;
RL   Mol. Cell 63:180-180(2016).
RN   [48]
RP   SUCCINYLATION AT LYS-15; LYS-57; LYS-80 AND LYS-123.
RX   PubMed=22389435; DOI=10.1074/mcp.M111.015875;
RA   Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT   "Lysine succinylation and lysine malonylation in histones.";
RL   Mol. Cell. Proteomics 11:100-107(2012).
RN   [49]
RP   INVOLVEMENT IN GLM, AND VARIANT GLM MET-28.
RX   PubMed=22286216; DOI=10.1038/ng.1102;
RG   St. Jude Children's Research Hospital-Washington University Pediatric Cancer Genome Project;
RA   Wu G., Broniscer A., McEachron T.A., Lu C., Paugh B.S., Becksfort J.,
RA   Qu C., Ding L., Huether R., Parker M., Zhang J., Gajjar A., Dyer M.A.,
RA   Mullighan C.G., Gilbertson R.J., Mardis E.R., Wilson R.K.,
RA   Downing J.R., Ellison D.W., Zhang J., Baker S.J.;
RT   "Somatic histone H3 alterations in pediatric diffuse intrinsic pontine
RT   gliomas and non-brainstem glioblastomas.";
RL   Nat. Genet. 44:251-253(2012).
RN   [50]
RP   ACETYLATION AT LYS-123.
RX   PubMed=23415232; DOI=10.1016/j.cell.2013.01.032;
RA   Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M.,
RA   Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R.,
RA   Schneider R.;
RT   "Regulation of transcription through acetylation of H3K122 on the
RT   lateral surface of the histone octamer.";
RL   Cell 152:859-872(2013).
RN   [51]
RP   ALLYSINE AT LYS-5.
RX   PubMed=27735137; DOI=10.1111/febs.13922;
RA   Herranz N., Dave N., Millanes-Romero A., Pascual-Reguant L., Morey L.,
RA   Diaz V.M., Lorenz-Fonfria V., Gutierrez-Gallego R., Jeronimo C.,
RA   Iturbide A., Di Croce L., Garcia de Herreros A., Peiro S.;
RT   "Lysyl oxidase-like 2 (LOXL2) oxidizes trimethylated lysine 4 in
RT   histone H3.";
RL   FEBS J. 283:4263-4273(2016).
RN   [52]
RP   BUTYRYLATION AT LYS-10; LYS-19 AND LYS-24.
RX   PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
RA   Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
RA   Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
RA   Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C.,
RA   Panne D., Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
RT   "Dynamic competing histone H4 K5K8 acetylation and butyrylation are
RT   hallmarks of highly active gene promoters.";
RL   Mol. Cell 62:169-180(2016).
RN   [53]
RP   HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28;
RP   LYS-57; LYS-80 AND LYS-123.
RX   PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA   Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA   Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA   Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA   White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT   "Metabolic regulation of gene expression by histone lysine beta-
RT   hydroxybutyrylation.";
RL   Mol. Cell 62:194-206(2016).
RN   [54]
RP   HYDROXYBUTYRYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24; LYS-28;
RP   LYS-37; LYS-57; LYS-65; LYS-80 AND LYS-123.
RX   PubMed=24681537; DOI=10.1038/nchembio.1497;
RA   Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H.,
RA   Debernardi A., Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z.,
RA   Allis C.D., Ren B., Khochbin S., Zhao Y.;
RT   "Lysine 2-hydroxyisobutyrylation is a widely distributed active
RT   histone mark.";
RL   Nat. Chem. Biol. 10:365-370(2014).
RN   [55]
RP   INVOLVEMENT IN SOFT TISSUE SARCOMAS, VARIANTS ILE-37 AND MET-37, AND
RP   CHARACTERIZATION OF VARIANTS ILE-37 AND MET-37.
RX   PubMed=27174990; DOI=10.1126/science.aac7272;
RA   Lu C., Jain S.U., Hoelper D., Bechet D., Molden R.C., Ran L.,
RA   Murphy D., Venneti S., Hameed M., Pawel B.R., Wunder J.S.,
RA   Dickson B.C., Lundgren S.M., Jani K.S., De Jay N.,
RA   Papillon-Cavanagh S., Andrulis I.L., Sawyer S.L., Grynspan D.,
RA   Turcotte R.E., Nadaf J., Fahiminiyah S., Muir T.W., Majewski J.,
RA   Thompson C.B., Chi P., Garcia B.A., Allis C.D., Jabado N., Lewis P.W.;
RT   "Histone H3K36 mutations promote sarcomagenesis through altered
RT   histone methylation landscape.";
RL   Science 352:844-849(2016).
RN   [56]
RP   ADP-RIBOSYLATION AT SER-11 AND SER-29.
RX   PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
RA   Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
RA   Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
RT   "Serine ADP-ribosylation depends on HPF1.";
RL   Mol. Cell 0:0-0(2017).
RN   [57]
RP   SUCCINYLATION AT LYS-80.
RX   PubMed=29211711; DOI=10.1038/nature25003;
RA   Wang Y., Guo Y.R., Liu K., Yin Z., Liu R., Xia Y., Tan L., Yang P.,
RA   Lee J.H., Li X.J., Hawke D., Zheng Y., Qian X., Lyu J., He J.,
RA   Xing D., Tao Y.J., Lu Z.;
RT   "KAT2A coupled with the alpha-KGDH complex acts as a histone H3
RT   succinyltransferase.";
RL   Nature 552:273-277(2017).
RN   [58]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 8-15 IN COMPLEX WITH YWHAZ.
RX   PubMed=16246723; DOI=10.1016/j.molcel.2005.08.032;
RA   Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B.,
RA   Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W.,
RA   Clayton A.L., Endicott J.A., Mahadevan L.C.;
RT   "Molecular basis for the recognition of phosphorylated and
RT   phosphoacetylated histone h3 by 14-3-3.";
RL   Mol. Cell 20:199-211(2005).
RN   [59]
RP   X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-20 IN COMPLEX WITH CHD1.
RX   PubMed=16372014; DOI=10.1038/nature04290;
RA   Flanagan J.F., Mi L.-Z., Chruszcz M., Cymborowski M., Clines K.L.,
RA   Kim Y., Minor W., Rastinejad F., Khorasanizadeh S.;
RT   "Double chromodomains cooperate to recognize the methylated histone H3
RT   tail.";
RL   Nature 438:1181-1185(2005).
RN   [60]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   PubMed=15951514; DOI=10.1093/nar/gki663;
RA   Tsunaka Y., Kajimura N., Tate S., Morikawa K.;
RT   "Alteration of the nucleosomal DNA path in the crystal structure of a
RT   human nucleosome core particle.";
RL   Nucleic Acids Res. 33:3424-3434(2005).
RN   [61]
RP   CHARACTERIZATION OF VARIANT GLM MET-28.
RX   PubMed=23603901; DOI=10.1101/gad.217778.113;
RA   Chan K.M., Fang D., Gan H., Hashizume R., Yu C., Schroeder M.,
RA   Gupta N., Mueller S., James C.D., Jenkins R., Sarkaria J., Zhang Z.;
RT   "The histone H3.3K27M mutation in pediatric glioma reprograms H3K27
RT   methylation and gene expression.";
RL   Genes Dev. 27:985-990(2013).
RN   [62]
RP   VARIANT MET-37.
RX   PubMed=28067913; DOI=10.1038/ng.3757;
RA   Papillon-Cavanagh S., Lu C., Gayden T., Mikael L.G., Bechet D.,
RA   Karamboulas C., Ailles L., Karamchandani J., Marchione D.M.,
RA   Garcia B.A., Weinreb I., Goldstein D., Lewis P.W., Dancu O.M.,
RA   Dhaliwal S., Stecho W., Howlett C.J., Mymryk J.S., Barrett J.W.,
RA   Nichols A.C., Allis C.D., Majewski J., Jabado N.;
RT   "Impaired H3K36 methylation defines a subset of head and neck squamous
RT   cell carcinomas.";
RL   Nat. Genet. 49:180-185(2017).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
CC       compact DNA into chromatin, limiting DNA accessibility to the
CC       cellular machineries which require DNA as a template. Histones
CC       thereby play a central role in transcription regulation, DNA
CC       repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and
CC       nucleosome remodeling.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC       molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC       heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC       approximately 147 bp of DNA. {ECO:0000269|PubMed:16246723,
CC       ECO:0000269|PubMed:16372014}.
CC   -!- INTERACTION:
CC       O43918:AIRE; NbExp=20; IntAct=EBI-79722, EBI-1753081;
CC       Q9Y294:ASF1A; NbExp=9; IntAct=EBI-79722, EBI-749553;
CC       Q9NPI1:BRD7; NbExp=2; IntAct=EBI-79722, EBI-711221;
CC       P83916:CBX1; NbExp=12; IntAct=EBI-79722, EBI-78129;
CC       Q13185:CBX3; NbExp=5; IntAct=EBI-79722, EBI-78176;
CC       P45973:CBX5; NbExp=9; IntAct=EBI-79722, EBI-78219;
CC       Q9Y232:CDYL; NbExp=5; IntAct=EBI-79722, EBI-1387386;
CC       Q9UER7-1:DAXX; NbExp=6; IntAct=EBI-79722, EBI-287635;
CC       Q8WUP2:FBLIM1; NbExp=11; IntAct=EBI-79722, EBI-3864120;
CC       P62805:HIST2H4B; NbExp=6; IntAct=EBI-79722, EBI-302023;
CC       P42858:HTT; NbExp=2; IntAct=EBI-79722, EBI-466029;
CC       Q9UNL4:ING4; NbExp=3; IntAct=EBI-79722, EBI-2866661;
CC       P38991:IPL1 (xeno); NbExp=2; IntAct=EBI-79722, EBI-9319;
CC       O75164:KDM4A; NbExp=7; IntAct=EBI-79722, EBI-936709;
CC       Q03164:KMT2A; NbExp=11; IntAct=EBI-79722, EBI-591370;
CC       Q9Y468:L3MBTL1; NbExp=2; IntAct=EBI-79722, EBI-1265089;
CC       P49736:MCM2; NbExp=5; IntAct=EBI-79722, EBI-374819;
CC       Q99549:MPHOSPH8; NbExp=5; IntAct=EBI-79722, EBI-2653928;
CC       P49321:NASP; NbExp=6; IntAct=EBI-79722, EBI-716205;
CC       P49321-2:NASP; NbExp=12; IntAct=EBI-79722, EBI-7038920;
CC       Q9BVI0:PHF20; NbExp=6; IntAct=EBI-79722, EBI-2560802;
CC       A8MW92:PHF20L1; NbExp=2; IntAct=EBI-79722, EBI-2560834;
CC       P14618-1:PKM; NbExp=3; IntAct=EBI-79722, EBI-4304679;
CC       Q8WTS6:SETD7; NbExp=3; IntAct=EBI-79722, EBI-1268586;
CC       P25554:SGF29 (xeno); NbExp=11; IntAct=EBI-79722, EBI-21678;
CC       Q96ES7:SGF29; NbExp=25; IntAct=EBI-79722, EBI-743117;
CC       Q12888:TP53BP1; NbExp=5; IntAct=EBI-79722, EBI-396540;
CC       P61964:WDR5; NbExp=11; IntAct=EBI-79722, EBI-540834;
CC       P63104:YWHAZ; NbExp=3; IntAct=EBI-79722, EBI-347088;
CC       Q8R5C8:Zmynd11 (xeno); NbExp=4; IntAct=EBI-79722, EBI-647813;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression
CC       strongly decreases as cell division slows down during the process
CC       of differentiation.
CC   -!- PTM: Acetylation is generally linked to gene activation.
CC       Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
CC       (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
CC       favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123
CC       (H3K122ac) by EP300/p300 plays a central role in chromatin
CC       structure: localizes at the surface of the histone octamer and
CC       stimulates transcription, possibly by promoting nucleosome
CC       instability. {ECO:0000269|PubMed:11242053,
CC       ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:15471871,
CC       ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050,
CC       ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:16497732,
CC       ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17194708,
CC       ECO:0000269|PubMed:19520870, ECO:0000269|PubMed:23415232}.
CC   -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
CC       PADI4 impairs methylation and represses transcription.
CC       {ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:15471871,
CC       ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635}.
CC   -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
CC       linked to gene activation. Symmetric dimethylation at Arg-9
CC       (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
CC       dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
CC       repression and is mutually exclusive with H3 Lys-5 methylation
CC       (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
CC       regardless of their transcription state and is enriched on
CC       inactive promoters, while it is absent on active promoters.
CC       {ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:15471871,
CC       ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
CC       ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:17194708,
CC       ECO:0000269|PubMed:17898714, ECO:0000269|PubMed:18077460,
CC       ECO:0000269|PubMed:18079182}.
CC   -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80
CC       (H3K79me) are linked to gene activation. Methylation at Lys-5
CC       (H3K4me) facilitates subsequent acetylation of H3 and H4.
CC       Methylation at Lys-80 (H3K79me) is associated with DNA double-
CC       strand break (DSB) responses and is a specific target for TP53BP1.
CC       Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to
CC       gene repression. Methylation at Lys-10 (H3K9me) is a specific
CC       target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
CC       subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
CC       H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
CC       require preliminary monoubiquitination of H2B at 'Lys-120'.
CC       Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
CC       in inactive X chromosome chromatin. Monomethylation at Lys-57
CC       (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA
CC       and is required for DNA replication. {ECO:0000269|PubMed:10464286,
CC       ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11856369,
CC       ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15525939,
CC       ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15983376,
CC       ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050,
CC       ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:16497732,
CC       ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17189264,
CC       ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:22387026}.
CC   -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase
CC       and dephosphorylated during anaphase. Phosphorylation at Ser-11
CC       (H3S10ph) by AURKB is crucial for chromosome condensation and
CC       cell-cycle progression during mitosis and meiosis. In addition
CC       phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
CC       important during interphase because it enables the transcription
CC       of genes following external stimulation, like mitogens, stress,
CC       growth factors or UV irradiation and result in the activation of
CC       genes, such as c-fos and c-jun. Phosphorylation at Ser-11
CC       (H3S10ph), which is linked to gene activation, prevents
CC       methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
CC       and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
CC       dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
CC       heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
CC       essential regulatory mechanism for neoplastic cell transformation.
CC       Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5
CC       or AURKB during mitosis or upon ultraviolet B irradiation.
CC       Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for
CC       epigenetic transcriptional activation that prevents demethylation
CC       of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
CC       phosphorylated at Thr-12 (H3T11ph) from prophase to early
CC       anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
CC       by PKN1 is a specific tag for epigenetic transcriptional
CC       activation that promotes demethylation of Lys-10 (H3K9me) by
CC       KDM4C/JMJD2C. Phosphorylation at Thr-12 (H3T11ph) by chromatin-
CC       associated CHEK1 regulates the transcription of cell cycle
CC       regulatory genes by modulating acetylation of Lys-10 (H3K9ac).
CC       Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of
CC       CBX5 (HP1 alpha) from chromatin. {ECO:0000269|PubMed:10464286,
CC       ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:11856369,
CC       ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610,
CC       ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:16185088,
CC       ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588,
CC       ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16627869,
CC       ECO:0000269|PubMed:17194708, ECO:0000269|PubMed:18066052,
CC       ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:19783980,
CC       ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:20850016}.
CC   -!- PTM: Monoubiquitinated by RAG1 in lymphoid cells,
CC       monoubiquitination is required for V(D)J recombination (By
CC       similarity). Ubiquitinated by the CUL4-DDB-RBX1 complex in
CC       response to ultraviolet irradiation. This may weaken the
CC       interaction between histones and DNA and facilitate DNA
CC       accessibility to repair proteins. {ECO:0000250|UniProtKB:Q6LED0,
CC       ECO:0000269|PubMed:16678110}.
CC   -!- PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is
CC       mediated by LOXL2. Allysine formation by LOXL2 only takes place on
CC       H3K4me3 and results in gene repression.
CC       {ECO:0000269|PubMed:27735137}.
CC   -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC       cells and marks testis-specific genes in post-meiotic cells,
CC       including X-linked genes that escape sex chromosome inactivation
CC       in haploid cells. Crotonylation marks active promoters and
CC       enhancers and confers resistance to transcriptional repressors. It
CC       is also associated with post-meiotically activated genes on
CC       autosomes. {ECO:0000269|PubMed:21925322}.
CC   -!- PTM: Butyrylation of histones marks active promoters and competes
CC       with histone acetylation. It is present during late
CC       spermatogenesis. {ECO:0000250|UniProtKB:P68433}.
CC   -!- PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with
CC       a maximum frequency around the transcription start sites of genes
CC       (PubMed:29211711). It gives a specific tag for epigenetic
CC       transcription activation (PubMed:29211711).
CC       {ECO:0000269|PubMed:29211711}.
CC   -!- DISEASE: Glioma (GLM) [MIM:137800]: Gliomas are benign or
CC       malignant central nervous system neoplasms derived from glial
CC       cells. They comprise astrocytomas and glioblastoma multiforme that
CC       are derived from astrocytes, oligodendrogliomas derived from
CC       oligodendrocytes and ependymomas derived from ependymocytes.
CC       {ECO:0000269|PubMed:22286216}. Note=The gene represented in this
CC       entry is involved in disease pathogenesis. HIST1H3B mutations
CC       affecting residue Lys-28 involved in post-translational
CC       modifications of histone H3.1 are recurrent in malignant,
CC       aggressive gliomas including pediatric non-brain stem glioblastoma
CC       and diffuse intrinsic pontine glioma (DIPG) (PubMed:22286216). The
CC       mechanism through which mutations lead to tumorigenesis involves
CC       altered histone methylation, impaired regulation of Polycomb
CC       repressive complex 2 (PRC2) activity, and aberrant epigenetic
CC       regulation of gene expression (PubMed:23603901).
CC       {ECO:0000269|PubMed:22286216, ECO:0000269|PubMed:23603901}.
CC   -!- DISEASE: Note=HIST1H3B or HIST1H3C mutations affecting residue
CC       Lys-37 of histone H3.1 are involved in the pathogenesis of
CC       pediatric undifferentiated soft tissue sarcomas. The mechanism
CC       through which mutations lead to tumorigenesis involves altered
CC       histones methylation with gain of global H3K27 methylation,
CC       altered Polycomb repressive complex 1 (PRC1) activity, aberrant
CC       epigenetic regulation of gene expression and impaired
CC       differentiation of mesenchimal progenitor cells.
CC       {ECO:0000269|PubMed:27174990}.
CC   -!- MISCELLANEOUS: This histone is only present in mammals and is
CC       enriched in acetylation of Lys-15 and dimethylation of Lys-10
CC       (H3K9me2).
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC   -!- CAUTION: The original paper reporting lysine deamination at Lys-5
CC       by LOXL2 has been retracted due to inappropriate manipulation of
CC       figure data (PubMed:22483618, PubMed:27392148). However, this
CC       modification was confirmed in a subsequent publication
CC       (PubMed:27735137). {ECO:0000269|PubMed:27735137,
CC       ECO:0000305|PubMed:22483618, ECO:0000305|PubMed:27392148}.
DR   EMBL; X00090; CAA24952.1; -; Genomic_DNA.
DR   EMBL; M26150; AAA52651.1; -; Genomic_DNA.
DR   EMBL; M60746; AAA63185.1; -; Genomic_DNA.
DR   EMBL; X57128; CAA40407.1; -; Genomic_DNA.
DR   EMBL; Z46261; CAA86403.1; -; Genomic_DNA.
DR   EMBL; X83550; CAA58540.1; -; Genomic_DNA.
DR   EMBL; Z80784; CAB02546.1; -; Genomic_DNA.
DR   EMBL; Z80785; CAB02547.1; -; Genomic_DNA.
DR   EMBL; Z80786; CAB02548.1; -; Genomic_DNA.
DR   EMBL; Z83735; CAB06030.1; -; Genomic_DNA.
DR   EMBL; Z83737; CAB06032.1; -; Genomic_DNA.
DR   EMBL; AF531274; AAN10051.1; -; Genomic_DNA.
DR   EMBL; AF531275; AAN10052.1; -; Genomic_DNA.
DR   EMBL; AF531276; AAN10053.1; -; Genomic_DNA.
DR   EMBL; AF531277; AAN10054.1; -; Genomic_DNA.
DR   EMBL; AF531278; AAN10055.1; -; Genomic_DNA.
DR   EMBL; AF531279; AAN10056.1; -; Genomic_DNA.
DR   EMBL; AF531280; AAN10057.1; -; Genomic_DNA.
DR   EMBL; AF531281; AAN10058.1; -; Genomic_DNA.
DR   EMBL; AF531282; AAN10059.1; -; Genomic_DNA.
DR   EMBL; AF531283; AAN10060.1; -; Genomic_DNA.
DR   EMBL; AK311991; BAG34929.1; -; mRNA.
DR   EMBL; AK313905; BAG36628.1; -; mRNA.
DR   EMBL; AK314142; BAG36832.1; -; mRNA.
DR   EMBL; AK316611; BAG38198.1; -; mRNA.
DR   EMBL; CR542014; CAG46811.1; -; mRNA.
DR   EMBL; CR542011; CAG46808.1; -; mRNA.
DR   EMBL; CR541983; CAG46780.1; -; mRNA.
DR   EMBL; CR541858; CAG46656.1; -; mRNA.
DR   EMBL; Z98744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL009179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL031777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC031333; AAH31333.1; -; mRNA.
DR   EMBL; BC066245; AAH66245.1; -; mRNA.
DR   EMBL; BC066246; AAH66246.1; -; mRNA.
DR   EMBL; BC066247; AAH66247.1; -; mRNA.
DR   EMBL; BC066884; AAH66884.1; -; mRNA.
DR   EMBL; BC067490; AAH67490.1; -; mRNA.
DR   EMBL; BC067491; AAH67491.1; -; mRNA.
DR   EMBL; BC067492; AAH67492.1; -; mRNA.
DR   EMBL; BC067493; AAH67493.1; -; mRNA.
DR   EMBL; BC069133; AAH69133.1; -; mRNA.
DR   EMBL; BC069303; AAH69303.1; -; mRNA.
DR   EMBL; BC069305; AAH69305.2; -; mRNA.
DR   EMBL; BC069818; AAH69818.1; -; mRNA.
DR   EMBL; BC096128; AAH96128.1; -; mRNA.
DR   EMBL; BC096129; AAH96129.1; -; mRNA.
DR   EMBL; BC096130; AAH96130.1; -; mRNA.
DR   EMBL; BC096131; AAH96131.1; -; mRNA.
DR   EMBL; BC096132; AAH96132.1; -; mRNA.
DR   EMBL; BC096133; AAH96133.1; -; mRNA.
DR   EMBL; BC096134; AAH96134.1; -; mRNA.
DR   EMBL; BC099630; AAH99630.1; -; mRNA.
DR   EMBL; BC127610; AAI27611.1; -; mRNA.
DR   EMBL; BC143046; AAI43047.1; -; mRNA.
DR   EMBL; BC148243; AAI48244.1; -; mRNA.
DR   EMBL; BC148250; AAI48251.1; -; mRNA.
DR   CCDS; CCDS4570.1; -.
DR   CCDS; CCDS4573.1; -.
DR   CCDS; CCDS4576.1; -.
DR   CCDS; CCDS4590.1; -.
DR   CCDS; CCDS4596.1; -.
DR   CCDS; CCDS4600.1; -.
DR   CCDS; CCDS4602.1; -.
DR   CCDS; CCDS4627.1; -.
DR   CCDS; CCDS4636.1; -.
DR   CCDS; CCDS4638.1; -.
DR   PIR; I37446; HSHU3.
DR   RefSeq; NP_003520.1; NM_003529.2.
DR   RefSeq; NP_003521.2; NM_003530.4.
DR   RefSeq; NP_003522.1; NM_003531.2.
DR   RefSeq; NP_003523.1; NM_003532.2.
DR   RefSeq; NP_003524.1; NM_003533.2.
DR   RefSeq; NP_003525.1; NM_003534.2.
DR   RefSeq; NP_003526.1; NM_003535.2.
DR   RefSeq; NP_003527.1; NM_003536.2.
DR   RefSeq; NP_003528.1; NM_003537.3.
DR   RefSeq; NP_066298.1; NM_021018.2.
DR   UniGene; Hs.132854; -.
DR   UniGene; Hs.247813; -.
DR   UniGene; Hs.247814; -.
DR   UniGene; Hs.248176; -.
DR   UniGene; Hs.443021; -.
DR   UniGene; Hs.484990; -.
DR   UniGene; Hs.532144; -.
DR   UniGene; Hs.533292; -.
DR   UniGene; Hs.546315; -.
DR   UniGene; Hs.586261; -.
DR   UniGene; Hs.591778; -.
DR   UniGene; Hs.626666; -.
DR   PDB; 1CS9; NMR; -; A=131-136.
DR   PDB; 1CT6; NMR; -; A=131-136.
DR   PDB; 1O9S; X-ray; 1.75 A; K/L=2-10.
DR   PDB; 1Q3L; X-ray; 1.64 A; P=2-16.
DR   PDB; 2B2T; X-ray; 2.45 A; D=2-20.
DR   PDB; 2B2U; X-ray; 2.95 A; D=2-16.
DR   PDB; 2B2V; X-ray; 2.65 A; D=2-16.
DR   PDB; 2B2W; X-ray; 2.40 A; D=2-20.
DR   PDB; 2C1J; X-ray; 2.60 A; C/D=8-15.
DR   PDB; 2C1N; X-ray; 2.00 A; C/E=8-15.
DR   PDB; 2CO0; X-ray; 2.25 A; B/D=2-16.
DR   PDB; 2CV5; X-ray; 2.50 A; A/E=1-136.
DR   PDB; 2KWJ; NMR; -; B=2-21.
DR   PDB; 2KWK; NMR; -; B=2-21.
DR   PDB; 2L75; NMR; -; B=2-14.
DR   PDB; 2LBM; NMR; -; C=2-16.
DR   PDB; 2M0O; NMR; -; B=32-42.
DR   PDB; 2NDF; NMR; -; B=13-25.
DR   PDB; 2NDG; NMR; -; B=13-25.
DR   PDB; 2OQ6; X-ray; 2.00 A; C/D=8-15.
DR   PDB; 2OT7; X-ray; 2.14 A; C/D=8-15.
DR   PDB; 2OX0; X-ray; 1.95 A; C/D=8-15.
DR   PDB; 2RI7; X-ray; 1.45 A; P=2-10.
DR   PDB; 2UXN; X-ray; 2.72 A; E=2-22.
DR   PDB; 2V85; X-ray; 2.00 A; D/E=2-13.
DR   PDB; 2V89; X-ray; 1.10 A; D/E=2-10.
DR   PDB; 2VNF; X-ray; 1.76 A; B/D=2-11.
DR   PDB; 2VPG; X-ray; 1.60 A; P/R=2-19.
DR   PDB; 2X0L; X-ray; 3.00 A; C=6-17.
DR   PDB; 3A1B; X-ray; 2.29 A; A=2-21.
DR   PDB; 3AFA; X-ray; 2.50 A; A/E=1-136.
DR   PDB; 3AVR; X-ray; 1.80 A; B=18-39.
DR   PDB; 3AYW; X-ray; 2.90 A; A/E=1-136.
DR   PDB; 3AZE; X-ray; 3.00 A; A/E=1-136.
DR   PDB; 3AZF; X-ray; 2.70 A; A/E=1-136.
DR   PDB; 3AZG; X-ray; 2.40 A; A/E=1-136.
DR   PDB; 3AZH; X-ray; 3.49 A; A/E=1-136.
DR   PDB; 3AZI; X-ray; 2.70 A; A/E=1-136.
DR   PDB; 3AZJ; X-ray; 2.89 A; A/E=1-136.
DR   PDB; 3AZK; X-ray; 3.20 A; A/E=1-136.
DR   PDB; 3AZL; X-ray; 2.70 A; A/E=1-136.
DR   PDB; 3AZM; X-ray; 2.89 A; A/E=1-136.
DR   PDB; 3AZN; X-ray; 3.00 A; A/E=1-136.
DR   PDB; 3B95; X-ray; 2.99 A; P=2-16.
DR   PDB; 3KMT; X-ray; 1.78 A; G/H/I=26-33.
DR   PDB; 3KQI; X-ray; 1.78 A; B=2-13.
DR   PDB; 3LQI; X-ray; 1.92 A; R/S/T=2-10.
DR   PDB; 3LQJ; X-ray; 1.90 A; Q/T=2-10.
DR   PDB; 3MP1; X-ray; 2.60 A; P=2-6.
DR   PDB; 3O34; X-ray; 1.90 A; B=14-33.
DR   PDB; 3O35; X-ray; 1.76 A; D/E=24-32.
DR   PDB; 3O37; X-ray; 2.00 A; E/F/G/H=2-11.
DR   PDB; 3QJ6; X-ray; 2.30 A; T=74-84.
DR   PDB; 3RIG; X-ray; 2.00 A; C/D=5-16.
DR   PDB; 3RIY; X-ray; 1.55 A; C/D=5-16.
DR   PDB; 3SOU; X-ray; 1.80 A; D/E=2-10.
DR   PDB; 3SOW; X-ray; 1.95 A; C/D=2-10.
DR   PDB; 3U31; X-ray; 2.20 A; B=5-14.
DR   PDB; 3U3D; X-ray; 2.40 A; B=5-14.
DR   PDB; 3U4S; X-ray; 2.15 A; C/D=8-15.
DR   PDB; 3U5N; X-ray; 1.95 A; C/D=2-21.
DR   PDB; 3U5O; X-ray; 2.70 A; I/J/K/L/M/N/O/P=2-23.
DR   PDB; 3U5P; X-ray; 2.80 A; I/J/K/L/M/N/O/P=2-29.
DR   PDB; 3UEE; X-ray; 2.61 A; B/D=2-13.
DR   PDB; 3UEF; X-ray; 2.45 A; B/D=2-13.
DR   PDB; 3UIG; X-ray; 2.40 A; P/Q=2-16.
DR   PDB; 3UII; X-ray; 2.60 A; P/Q=2-11.
DR   PDB; 3UIK; X-ray; 2.70 A; P/Q=2-11.
DR   PDB; 3V43; X-ray; 1.47 A; Q=2-19.
DR   PDB; 3W96; X-ray; 3.00 A; A/E=1-136.
DR   PDB; 3W97; X-ray; 3.20 A; A/E=1-136.
DR   PDB; 3W98; X-ray; 3.42 A; A/E=29-136.
DR   PDB; 3W99; X-ray; 3.00 A; A/E=1-136.
DR   PDB; 3WA9; X-ray; 3.07 A; A/E=1-136.
DR   PDB; 3WAA; X-ray; 3.20 A; A/E=1-136.
DR   PDB; 3WKJ; X-ray; 2.80 A; A/E=1-136.
DR   PDB; 3X1S; X-ray; 2.81 A; A/E=2-136.
DR   PDB; 3X1T; X-ray; 2.81 A; A/E=2-136.
DR   PDB; 3X1U; X-ray; 3.25 A; A/E=2-136.
DR   PDB; 3X1V; X-ray; 2.92 A; A/E=2-136.
DR   PDB; 3ZG6; X-ray; 2.20 A; F=5-14.
DR   PDB; 3ZVY; X-ray; 1.95 A; C/D=2-9.
DR   PDB; 4A0J; X-ray; 2.80 A; C/D=2-7.
DR   PDB; 4A0N; X-ray; 2.74 A; C=2-7.
DR   PDB; 4A7J; X-ray; 1.90 A; B=1-16.
DR   PDB; 4BD3; NMR; -; B=32-42.
DR   PDB; 4C1Q; X-ray; 2.30 A; C=2-10.
DR   PDB; 4F4U; X-ray; 2.00 A; C/D=5-16.
DR   PDB; 4F56; X-ray; 1.70 A; C/D=5-16.
DR   PDB; 4FWF; X-ray; 2.70 A; E=2-21.
DR   PDB; 4HON; X-ray; 1.80 A; F/G=7-16.
DR   PDB; 4I51; X-ray; 1.90 A; C/D=4-12.
DR   PDB; 4L7X; X-ray; 1.35 A; U=2-13.
DR   PDB; 4LK9; X-ray; 1.60 A; B=2-22.
DR   PDB; 4LKA; X-ray; 1.61 A; B=2-22.
DR   PDB; 4LLB; X-ray; 2.50 A; C/D=2-22.
DR   PDB; 4LXL; X-ray; 1.87 A; D=8-15.
DR   PDB; 4N4H; X-ray; 2.30 A; B=22-43.
DR   PDB; 4QBQ; X-ray; 2.41 A; P=2-9.
DR   PDB; 4QBR; X-ray; 1.90 A; E/P=2-8.
DR   PDB; 4QBS; X-ray; 1.80 A; P=2-8.
DR   PDB; 4TN7; X-ray; 2.20 A; E/F=30-44.
DR   PDB; 4U68; X-ray; 1.80 A; D/E/F=5-15.
DR   PDB; 4UP0; X-ray; 1.28 A; F=2-16.
DR   PDB; 4UY4; X-ray; 1.86 A; C/D=2-7.
DR   PDB; 4X3K; X-ray; 1.45 A; C/D=24-30.
DR   PDB; 4Y6L; X-ray; 1.60 A; C/D=7-13.
DR   PDB; 4YHP; X-ray; 2.53 A; P/Q=2-17.
DR   PDB; 4YHZ; X-ray; 2.30 A; P=2-13.
DR   PDB; 4YM5; X-ray; 4.00 A; A/E=1-136.
DR   PDB; 4YM6; X-ray; 3.51 A; A/E=1-136.
DR   PDB; 4Z0R; X-ray; 1.75 A; D=2-16.
DR   PDB; 4Z2M; X-ray; 2.98 A; G/I=35-136.
DR   PDB; 5AV5; X-ray; 2.40 A; A/E=1-136.
DR   PDB; 5AV6; X-ray; 2.20 A; A/E=1-136.
DR   PDB; 5AV8; X-ray; 2.20 A; A/E=1-136.
DR   PDB; 5AV9; X-ray; 2.20 A; A/E=1-136.
DR   PDB; 5AVB; X-ray; 2.40 A; A/E=1-136.
DR   PDB; 5AVC; X-ray; 2.40 A; A/E=1-136.
DR   PDB; 5B24; X-ray; 3.60 A; A/E=1-136.
DR   PDB; 5B2I; X-ray; 3.00 A; A/E=1-136.
DR   PDB; 5B2J; X-ray; 2.60 A; A/E=1-136.
DR   PDB; 5B31; X-ray; 2.20 A; A/E=1-136.
DR   PDB; 5C11; X-ray; 2.80 A; B=2-11.
DR   PDB; 5C13; X-ray; 2.10 A; D/F/H/P=2-11.
DR   PDB; 5C3I; X-ray; 3.50 A; B/F/J/N/R/V=1-136.
DR   PDB; 5CPI; X-ray; 2.90 A; A/E=1-136.
DR   PDB; 5CPJ; X-ray; 3.15 A; A/E=1-136.
DR   PDB; 5CPK; X-ray; 2.63 A; A/E=1-136.
DR   PDB; 5D6Y; X-ray; 2.29 A; a/b/c/d=20-29.
DR   PDB; 5DAH; X-ray; 2.61 A; C/D=20-30.
DR   PDB; 5FB0; X-ray; 2.70 A; D/F=2-16.
DR   PDB; 5FB1; X-ray; 2.10 A; C=2-16.
DR   PDB; 5FFV; X-ray; 1.30 A; C/D=10-20.
DR   PDB; 5GH9; X-ray; 1.45 A; B=45-58.
DR   PDB; 5GSE; X-ray; 3.14 A; A/E/K/O=1-136.
DR   PDB; 5GSU; X-ray; 3.10 A; A/E=2-136.
DR   PDB; 5GT0; X-ray; 2.82 A; A/E=2-136.
DR   PDB; 5GT3; X-ray; 2.91 A; A/E=2-136.
DR   PDB; 5GTC; X-ray; 2.70 A; A/E=1-136.
DR   PDB; 5H6Q; X-ray; 2.53 A; C=2-21.
DR   PDB; 5H6R; X-ray; 2.60 A; C=2-21.
DR   PDB; 5HJB; X-ray; 2.70 A; B=4-9.
DR   PDB; 5HJC; X-ray; 2.60 A; B=16-24.
DR   PDB; 5HJD; X-ray; 2.81 A; B/D/F/H/I/J/L/M=15-21.
DR   PDB; 5HYN; X-ray; 2.95 A; D/I/O/T=22-34.
DR   PDB; 5IQL; X-ray; 2.10 A; B=25-32.
DR   PDB; 5J3V; X-ray; 3.05 A; C/D=12-28.
DR   PDB; 5J9S; X-ray; 2.70 A; B=16-40.
DR   PDB; 5JHN; X-ray; 1.67 A; F/G=4-14.
DR   PDB; 5JIN; X-ray; 1.85 A; F/G=4-14.
DR   PDB; 5JIY; X-ray; 1.48 A; F/G=4-14.
DR   PDB; 5JJ0; X-ray; 1.72 A; F/G=4-14.
DR   PDB; 5JRG; X-ray; 2.50 A; A/E=1-136.
DR   PDB; 5KJH; X-ray; 2.27 A; D=23-33, E=19-38.
DR   PDB; 5KJI; X-ray; 2.71 A; E=19-38.
DR   PDB; 5KKL; X-ray; 2.94 A; B=23-27.
DR   PDB; 5LUG; X-ray; 1.70 A; E/F/G/H=2-11.
DR   PDB; 5M5G; X-ray; 2.27 A; D=23-33.
DR   PDB; 5MR8; X-ray; 1.74 A; C=2-10.
DR   PDB; 5OY3; X-ray; 2.14 A; B=18-34.
DR   PDB; 5SVX; X-ray; 1.56 A; B=2-12.
DR   PDB; 5SVY; X-ray; 1.05 A; B=2-12.
DR   PDB; 5SZB; X-ray; 1.20 A; H=2-19.
DR   PDB; 5SZC; X-ray; 1.19 A; H=2-19.
DR   PDB; 5T0K; X-ray; 1.70 A; P/Q=2-16.
DR   PDB; 5T0M; X-ray; 1.90 A; C/P=2-16.
DR   PDB; 5T1G; X-ray; 1.90 A; B=39-53.
DR   PDB; 5T1I; X-ray; 1.60 A; C=39-53.
DR   PDB; 5T8R; X-ray; 2.40 A; E/G=2-11.
DR   PDB; 5TBN; NMR; -; C=2-12.
DR   PDB; 5TDR; X-ray; 1.42 A; B=2-12.
DR   PDB; 5TDW; X-ray; 1.70 A; B=2-12.
DR   PDB; 5U2J; X-ray; 1.60 A; C/D=2-17.
DR   PDB; 5V21; X-ray; 2.42 A; B=30-44.
DR   PDB; 5V22; X-ray; 2.40 A; B=30-44.
DR   PDB; 5VA6; X-ray; 2.40 A; C/D=20-37.
DR   PDB; 5VAB; X-ray; 1.70 A; F=2-11.
DR   PDB; 5VGE; X-ray; 2.60 A; C=41-49.
DR   PDB; 5WLE; X-ray; 1.95 A; C=2-13.
DR   PDB; 5WVO; X-ray; 2.00 A; D=2-37.
DR   PDB; 5WXG; X-ray; 1.70 A; P=2-8.
DR   PDB; 5WXH; X-ray; 1.30 A; D/P=2-8.
DR   PDB; 5WYI; X-ray; 2.00 A; E=120-127.
DR   PDB; 5X60; X-ray; 2.69 A; C=2-21.
DR   PDB; 5XF3; X-ray; 2.60 A; A/E=1-136.
DR   PDB; 5XF4; X-ray; 2.87 A; A/E=1-136.
DR   PDB; 5XF5; X-ray; 2.82 A; A/E=1-136.
DR   PDB; 5XFQ; X-ray; 2.40 A; E/F=30-42.
DR   PDB; 5XFR; X-ray; 2.25 A; C/D=34-41.
DR   PDB; 5XNV; X-ray; 2.70 A; B=25-32.
DR   PDB; 5Y20; X-ray; 2.41 A; P=2-8.
DR   PDB; 6AXJ; X-ray; 2.38 A; E/F/G/H=22-32.
DR   PDB; 6BHD; X-ray; 1.25 A; B=4-20.
DR   PDB; 6BHE; X-ray; 1.35 A; B=4-20.
DR   PDB; 6BHG; X-ray; 1.45 A; B=4-20.
DR   PDB; 6BHH; X-ray; 1.85 A; B=4-20.
DR   PDB; 6BHI; X-ray; 1.40 A; B=5-20.
DR   PDB; 6ETX; EM; 4.80 A; I/M=1-136.
DR   PDBsum; 1CS9; -.
DR   PDBsum; 1CT6; -.
DR   PDBsum; 1O9S; -.
DR   PDBsum; 1Q3L; -.
DR   PDBsum; 2B2T; -.
DR   PDBsum; 2B2U; -.
DR   PDBsum; 2B2V; -.
DR   PDBsum; 2B2W; -.
DR   PDBsum; 2C1J; -.
DR   PDBsum; 2C1N; -.
DR   PDBsum; 2CO0; -.
DR   PDBsum; 2CV5; -.
DR   PDBsum; 2KWJ; -.
DR   PDBsum; 2KWK; -.
DR   PDBsum; 2L75; -.
DR   PDBsum; 2LBM; -.
DR   PDBsum; 2M0O; -.
DR   PDBsum; 2NDF; -.
DR   PDBsum; 2NDG; -.
DR   PDBsum; 2OQ6; -.
DR   PDBsum; 2OT7; -.
DR   PDBsum; 2OX0; -.
DR   PDBsum; 2RI7; -.
DR   PDBsum; 2UXN; -.
DR   PDBsum; 2V85; -.
DR   PDBsum; 2V89; -.
DR   PDBsum; 2VNF; -.
DR   PDBsum; 2VPG; -.
DR   PDBsum; 2X0L; -.
DR   PDBsum; 3A1B; -.
DR   PDBsum; 3AFA; -.
DR   PDBsum; 3AVR; -.
DR   PDBsum; 3AYW; -.
DR   PDBsum; 3AZE; -.
DR   PDBsum; 3AZF; -.
DR   PDBsum; 3AZG; -.
DR   PDBsum; 3AZH; -.
DR   PDBsum; 3AZI; -.
DR   PDBsum; 3AZJ; -.
DR   PDBsum; 3AZK; -.
DR   PDBsum; 3AZL; -.
DR   PDBsum; 3AZM; -.
DR   PDBsum; 3AZN; -.
DR   PDBsum; 3B95; -.
DR   PDBsum; 3KMT; -.
DR   PDBsum; 3KQI; -.
DR   PDBsum; 3LQI; -.
DR   PDBsum; 3LQJ; -.
DR   PDBsum; 3MP1; -.
DR   PDBsum; 3O34; -.
DR   PDBsum; 3O35; -.
DR   PDBsum; 3O37; -.
DR   PDBsum; 3QJ6; -.
DR   PDBsum; 3RIG; -.
DR   PDBsum; 3RIY; -.
DR   PDBsum; 3SOU; -.
DR   PDBsum; 3SOW; -.
DR   PDBsum; 3U31; -.
DR   PDBsum; 3U3D; -.
DR   PDBsum; 3U4S; -.
DR   PDBsum; 3U5N; -.
DR   PDBsum; 3U5O; -.
DR   PDBsum; 3U5P; -.
DR   PDBsum; 3UEE; -.
DR   PDBsum; 3UEF; -.
DR   PDBsum; 3UIG; -.
DR   PDBsum; 3UII; -.
DR   PDBsum; 3UIK; -.
DR   PDBsum; 3V43; -.
DR   PDBsum; 3W96; -.
DR   PDBsum; 3W97; -.
DR   PDBsum; 3W98; -.
DR   PDBsum; 3W99; -.
DR   PDBsum; 3WA9; -.
DR   PDBsum; 3WAA; -.
DR   PDBsum; 3WKJ; -.
DR   PDBsum; 3X1S; -.
DR   PDBsum; 3X1T; -.
DR   PDBsum; 3X1U; -.
DR   PDBsum; 3X1V; -.
DR   PDBsum; 3ZG6; -.
DR   PDBsum; 3ZVY; -.
DR   PDBsum; 4A0J; -.
DR   PDBsum; 4A0N; -.
DR   PDBsum; 4A7J; -.
DR   PDBsum; 4BD3; -.
DR   PDBsum; 4C1Q; -.
DR   PDBsum; 4F4U; -.
DR   PDBsum; 4F56; -.
DR   PDBsum; 4FWF; -.
DR   PDBsum; 4HON; -.
DR   PDBsum; 4I51; -.
DR   PDBsum; 4L7X; -.
DR   PDBsum; 4LK9; -.
DR   PDBsum; 4LKA; -.
DR   PDBsum; 4LLB; -.
DR   PDBsum; 4LXL; -.
DR   PDBsum; 4N4H; -.
DR   PDBsum; 4QBQ; -.
DR   PDBsum; 4QBR; -.
DR   PDBsum; 4QBS; -.
DR   PDBsum; 4TN7; -.
DR   PDBsum; 4U68; -.
DR   PDBsum; 4UP0; -.
DR   PDBsum; 4UY4; -.
DR   PDBsum; 4X3K; -.
DR   PDBsum; 4Y6L; -.
DR   PDBsum; 4YHP; -.
DR   PDBsum; 4YHZ; -.
DR   PDBsum; 4YM5; -.
DR   PDBsum; 4YM6; -.
DR   PDBsum; 4Z0R; -.
DR   PDBsum; 4Z2M; -.
DR   PDBsum; 5AV5; -.
DR   PDBsum; 5AV6; -.
DR   PDBsum; 5AV8; -.
DR   PDBsum; 5AV9; -.
DR   PDBsum; 5AVB; -.
DR   PDBsum; 5AVC; -.
DR   PDBsum; 5B24; -.
DR   PDBsum; 5B2I; -.
DR   PDBsum; 5B2J; -.
DR   PDBsum; 5B31; -.
DR   PDBsum; 5C11; -.
DR   PDBsum; 5C13; -.
DR   PDBsum; 5C3I; -.
DR   PDBsum; 5CPI; -.
DR   PDBsum; 5CPJ; -.
DR   PDBsum; 5CPK; -.
DR   PDBsum; 5D6Y; -.
DR   PDBsum; 5DAH; -.
DR   PDBsum; 5FB0; -.
DR   PDBsum; 5FB1; -.
DR   PDBsum; 5FFV; -.
DR   PDBsum; 5GH9; -.
DR   PDBsum; 5GSE; -.
DR   PDBsum; 5GSU; -.
DR   PDBsum; 5GT0; -.
DR   PDBsum; 5GT3; -.
DR   PDBsum; 5GTC; -.
DR   PDBsum; 5H6Q; -.
DR   PDBsum; 5H6R; -.
DR   PDBsum; 5HJB; -.
DR   PDBsum; 5HJC; -.
DR   PDBsum; 5HJD; -.
DR   PDBsum; 5HYN; -.
DR   PDBsum; 5IQL; -.
DR   PDBsum; 5J3V; -.
DR   PDBsum; 5J9S; -.
DR   PDBsum; 5JHN; -.
DR   PDBsum; 5JIN; -.
DR   PDBsum; 5JIY; -.
DR   PDBsum; 5JJ0; -.
DR   PDBsum; 5JRG; -.
DR   PDBsum; 5KJH; -.
DR   PDBsum; 5KJI; -.
DR   PDBsum; 5KKL; -.
DR   PDBsum; 5LUG; -.
DR   PDBsum; 5M5G; -.
DR   PDBsum; 5MR8; -.
DR   PDBsum; 5OY3; -.
DR   PDBsum; 5SVX; -.
DR   PDBsum; 5SVY; -.
DR   PDBsum; 5SZB; -.
DR   PDBsum; 5SZC; -.
DR   PDBsum; 5T0K; -.
DR   PDBsum; 5T0M; -.
DR   PDBsum; 5T1G; -.
DR   PDBsum; 5T1I; -.
DR   PDBsum; 5T8R; -.
DR   PDBsum; 5TBN; -.
DR   PDBsum; 5TDR; -.
DR   PDBsum; 5TDW; -.
DR   PDBsum; 5U2J; -.
DR   PDBsum; 5V21; -.
DR   PDBsum; 5V22; -.
DR   PDBsum; 5VA6; -.
DR   PDBsum; 5VAB; -.
DR   PDBsum; 5VGE; -.
DR   PDBsum; 5WLE; -.
DR   PDBsum; 5WVO; -.
DR   PDBsum; 5WXG; -.
DR   PDBsum; 5WXH; -.
DR   PDBsum; 5WYI; -.
DR   PDBsum; 5X60; -.
DR   PDBsum; 5XF3; -.
DR   PDBsum; 5XF4; -.
DR   PDBsum; 5XF5; -.
DR   PDBsum; 5XFQ; -.
DR   PDBsum; 5XFR; -.
DR   PDBsum; 5XNV; -.
DR   PDBsum; 5Y20; -.
DR   PDBsum; 6AXJ; -.
DR   PDBsum; 6BHD; -.
DR   PDBsum; 6BHE; -.
DR   PDBsum; 6BHG; -.
DR   PDBsum; 6BHH; -.
DR   PDBsum; 6BHI; -.
DR   PDBsum; 6ETX; -.
DR   ProteinModelPortal; P68431; -.
DR   SMR; P68431; -.
DR   BioGrid; 113946; 308.
DR   BioGrid; 113947; 6.
DR   BioGrid; 113948; 11.
DR   BioGrid; 113949; 201.
DR   BioGrid; 113950; 6.
DR   BioGrid; 113951; 7.
DR   BioGrid; 113952; 5.
DR   BioGrid; 113953; 9.
DR   BioGrid; 113954; 24.
DR   BioGrid; 114458; 9.
DR   CORUM; P68431; -.
DR   DIP; DIP-29371N; -.
DR   ELM; P68431; -.
DR   IntAct; P68431; 428.
DR   MINT; P68431; -.
DR   STRING; 9606.ENSP00000444823; -.
DR   iPTMnet; P68431; -.
DR   PhosphoSitePlus; P68431; -.
DR   SwissPalm; P68431; -.
DR   BioMuta; HIST1H3A; -.
DR   DMDM; 55977055; -.
DR   EPD; P68431; -.
DR   MaxQB; P68431; -.
DR   PaxDb; P68431; -.
DR   PeptideAtlas; P68431; -.
DR   PRIDE; P68431; -.
DR   ProteomicsDB; 57541; -.
DR   TopDownProteomics; P68431; -.
DR   DNASU; 8350; -.
DR   DNASU; 8352; -.
DR   DNASU; 8353; -.
DR   DNASU; 8355; -.
DR   DNASU; 8356; -.
DR   DNASU; 8357; -.
DR   Ensembl; ENST00000356476; ENSP00000366999; ENSG00000197409.
DR   Ensembl; ENST00000359303; ENSP00000352252; ENSG00000197153.
DR   Ensembl; ENST00000369163; ENSP00000358160; ENSG00000278828.
DR   Ensembl; ENST00000612966; ENSP00000484658; ENSG00000278272.
DR   Ensembl; ENST00000613854; ENSP00000480826; ENSG00000275714.
DR   Ensembl; ENST00000614378; ENSP00000484638; ENSG00000273983.
DR   Ensembl; ENST00000614911; ENSP00000482271; ENSG00000274750.
DR   Ensembl; ENST00000616365; ENSP00000483283; ENSG00000275379.
DR   Ensembl; ENST00000618052; ENSP00000484095; ENSG00000277775.
DR   Ensembl; ENST00000621411; ENSP00000484841; ENSG00000274267.
DR   Ensembl; ENST00000634733; ENSP00000489282; ENSG00000274750.
DR   GeneID; 8350; -.
DR   GeneID; 8351; -.
DR   GeneID; 8352; -.
DR   GeneID; 8353; -.
DR   GeneID; 8354; -.
DR   GeneID; 8355; -.
DR   GeneID; 8356; -.
DR   GeneID; 8357; -.
DR   GeneID; 8358; -.
DR   GeneID; 8968; -.
DR   KEGG; hsa:8350; -.
DR   KEGG; hsa:8351; -.
DR   KEGG; hsa:8352; -.
DR   KEGG; hsa:8353; -.
DR   KEGG; hsa:8354; -.
DR   KEGG; hsa:8355; -.
DR   KEGG; hsa:8356; -.
DR   KEGG; hsa:8357; -.
DR   KEGG; hsa:8358; -.
DR   KEGG; hsa:8968; -.
DR   UCSC; uc003nfp.2; human.
DR   CTD; 8350; -.
DR   CTD; 8351; -.
DR   CTD; 8352; -.
DR   CTD; 8353; -.
DR   CTD; 8354; -.
DR   CTD; 8355; -.
DR   CTD; 8356; -.
DR   CTD; 8357; -.
DR   CTD; 8358; -.
DR   CTD; 8968; -.
DR   DisGeNET; 8350; -.
DR   DisGeNET; 8351; -.
DR   DisGeNET; 8352; -.
DR   DisGeNET; 8353; -.
DR   DisGeNET; 8354; -.
DR   DisGeNET; 8355; -.
DR   DisGeNET; 8356; -.
DR   DisGeNET; 8357; -.
DR   DisGeNET; 8358; -.
DR   DisGeNET; 8968; -.
DR   EuPathDB; HostDB:ENSG00000197153.4; -.
DR   EuPathDB; HostDB:ENSG00000197409.7; -.
DR   EuPathDB; HostDB:ENSG00000273983.1; -.
DR   EuPathDB; HostDB:ENSG00000274267.1; -.
DR   EuPathDB; HostDB:ENSG00000274750.2; -.
DR   EuPathDB; HostDB:ENSG00000275379.1; -.
DR   EuPathDB; HostDB:ENSG00000275714.1; -.
DR   EuPathDB; HostDB:ENSG00000277775.1; -.
DR   EuPathDB; HostDB:ENSG00000278272.1; -.
DR   EuPathDB; HostDB:ENSG00000278828.1; -.
DR   GeneCards; HIST1H3A; -.
DR   GeneCards; HIST1H3B; -.
DR   GeneCards; HIST1H3C; -.
DR   GeneCards; HIST1H3D; -.
DR   GeneCards; HIST1H3E; -.
DR   GeneCards; HIST1H3F; -.
DR   GeneCards; HIST1H3G; -.
DR   GeneCards; HIST1H3H; -.
DR   GeneCards; HIST1H3I; -.
DR   GeneCards; HIST1H3J; -.
DR   HGNC; HGNC:4766; HIST1H3A.
DR   HGNC; HGNC:4776; HIST1H3B.
DR   HGNC; HGNC:4768; HIST1H3C.
DR   HGNC; HGNC:4767; HIST1H3D.
DR   HGNC; HGNC:4769; HIST1H3E.
DR   HGNC; HGNC:4773; HIST1H3F.
DR   HGNC; HGNC:4772; HIST1H3G.
DR   HGNC; HGNC:4775; HIST1H3H.
DR   HGNC; HGNC:4771; HIST1H3I.
DR   HGNC; HGNC:4774; HIST1H3J.
DR   HPA; CAB070190; -.
DR   HPA; HPA042570; -.
DR   MalaCards; HIST1H3A; -.
DR   MIM; 137800; phenotype.
DR   MIM; 602810; gene.
DR   MIM; 602811; gene.
DR   MIM; 602812; gene.
DR   MIM; 602813; gene.
DR   MIM; 602814; gene.
DR   MIM; 602815; gene.
DR   MIM; 602816; gene.
DR   MIM; 602817; gene.
DR   MIM; 602818; gene.
DR   MIM; 602819; gene.
DR   neXtProt; NX_P68431; -.
DR   OpenTargets; ENSG00000197153; -.
DR   OpenTargets; ENSG00000197409; -.
DR   OpenTargets; ENSG00000273983; -.
DR   OpenTargets; ENSG00000274267; -.
DR   OpenTargets; ENSG00000274750; -.
DR   OpenTargets; ENSG00000275379; -.
DR   OpenTargets; ENSG00000275714; -.
DR   OpenTargets; ENSG00000277775; -.
DR   OpenTargets; ENSG00000278272; -.
DR   OpenTargets; ENSG00000278828; -.
DR   PharmGKB; PA29148; -.
DR   eggNOG; KOG1745; Eukaryota.
DR   eggNOG; COG2036; LUCA.
DR   GeneTree; ENSGT00760000118967; -.
DR   HOVERGEN; HBG001172; -.
DR   InParanoid; P68431; -.
DR   KO; K11253; -.
DR   OMA; ASEAYYL; -.
DR   OrthoDB; EOG09370ZG5; -.
DR   PhylomeDB; P68431; -.
DR   TreeFam; TF314241; -.
DR   Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR   Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-HSA-3214842; HDMs demethylate histones.
DR   Reactome; R-HSA-3214847; HATs acetylate histones.
DR   Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR   Reactome; R-HSA-3247509; Chromatin modifying enzymes.
DR   Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR   Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-HSA-5334118; DNA methylation.
DR   Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR   Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR   Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
DR   Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-HSA-912446; Meiotic recombination.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR   SIGNOR; P68431; -.
DR   ChiTaRS; HIST1H3B; human.
DR   ChiTaRS; HIST1H3F; human.
DR   EvolutionaryTrace; P68431; -.
DR   GeneWiki; HIST1H3A; -.
DR   GeneWiki; HIST1H3B; -.
DR   GeneWiki; HIST1H3C; -.
DR   GeneWiki; HIST1H3D; -.
DR   GeneWiki; HIST1H3E; -.
DR   GeneWiki; HIST1H3F; -.
DR   GeneWiki; HIST1H3G; -.
DR   GeneWiki; HIST1H3H; -.
DR   GeneWiki; HIST1H3I; -.
DR   GeneWiki; HIST1H3J; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000197153; -.
DR   CleanEx; HS_HIST1H3A; -.
DR   CleanEx; HS_HIST1H3B; -.
DR   CleanEx; HS_HIST1H3C; -.
DR   CleanEx; HS_HIST1H3D; -.
DR   CleanEx; HS_HIST1H3E; -.
DR   CleanEx; HS_HIST1H3F; -.
DR   CleanEx; HS_HIST1H3G; -.
DR   CleanEx; HS_HIST1H3H; -.
DR   CleanEx; HS_HIST1H3I; -.
DR   Genevisible; P68431; HS.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
DR   GO; GO:0000788; C:nuclear nucleosome; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0006325; P:chromatin organization; TAS:Reactome.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; TAS:Reactome.
DR   GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:UniProtKB.
DR   GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
DR   GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR   GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
DR   GO; GO:0060968; P:regulation of gene silencing; IDA:BHF-UCL.
DR   GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
DR   GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
DR   GO; GO:0032200; P:telomere organization; TAS:BHF-UCL.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ADP-ribosylation; Chromosome;
KW   Citrullination; Complete proteome; Direct protein sequencing;
KW   Disease mutation; DNA-binding; Hydroxylation; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:16185088}.
FT   CHAIN         2    136       Histone H3.1.
FT                                /FTId=PRO_0000221245.
FT   MOD_RES       3      3       Asymmetric dimethylarginine; by PRMT6;
FT                                alternate. {ECO:0000269|PubMed:17898714,
FT                                ECO:0000269|PubMed:18077460,
FT                                ECO:0000269|PubMed:18079182}.
FT   MOD_RES       3      3       Citrulline; alternate.
FT                                {ECO:0000269|PubMed:16567635}.
FT   MOD_RES       4      4       Phosphothreonine; by HASPIN.
FT                                {ECO:0000269|PubMed:15681610,
FT                                ECO:0000269|PubMed:16185088}.
FT   MOD_RES       5      5       Allysine; alternate.
FT                                {ECO:0000269|PubMed:27735137}.
FT   MOD_RES       5      5       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES       5      5       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES       5      5       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES       5      5       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES       5      5       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:17194708}.
FT   MOD_RES       5      5       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES       5      5       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES       7      7       Phosphothreonine; by PKC.
FT                                {ECO:0000269|PubMed:20228790}.
FT   MOD_RES       9      9       Citrulline; alternate.
FT                                {ECO:0000269|PubMed:15345777,
FT                                ECO:0000269|PubMed:16567635}.
FT   MOD_RES       9      9       Symmetric dimethylarginine; by PRMT5;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P68433}.
FT   MOD_RES      10     10       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:11242053,
FT                                ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      10     10       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:11242053,
FT                                ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      10     10       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      10     10       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES      10     10       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:16497732,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      10     10       N6-butyryllysine; alternate.
FT                                {ECO:0000269|PubMed:27105113}.
FT   MOD_RES      10     10       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      10     10       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:11242053,
FT                                ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      11     11       ADP-ribosylserine; alternate.
FT                                {ECO:0000269|PubMed:28190768}.
FT   MOD_RES      11     11       Phosphoserine; alternate; by AURKB,
FT                                AURKC, RPS6KA3, RPS6KA4 and RPS6KA5.
FT                                {ECO:0000269|PubMed:10464286,
FT                                ECO:0000269|PubMed:11856369,
FT                                ECO:0000269|PubMed:12560483,
FT                                ECO:0000269|PubMed:15681610,
FT                                ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16457588}.
FT   MOD_RES      12     12       Phosphothreonine; by PKC and CHEK1.
FT                                {ECO:0000269|PubMed:12560483,
FT                                ECO:0000269|PubMed:18066052,
FT                                ECO:0000269|PubMed:18243098}.
FT   MOD_RES      15     15       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      15     15       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES      15     15       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:16497732,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      15     15       N6-succinyllysine; alternate.
FT                                {ECO:0000269|PubMed:22389435}.
FT   MOD_RES      18     18       Asymmetric dimethylarginine; by CARM1;
FT                                alternate. {ECO:0000269|PubMed:15345777,
FT                                ECO:0000269|PubMed:15471871,
FT                                ECO:0000269|PubMed:16497732}.
FT   MOD_RES      18     18       Citrulline; alternate.
FT                                {ECO:0000269|PubMed:15345777,
FT                                ECO:0000269|PubMed:16497732,
FT                                ECO:0000269|PubMed:16567635}.
FT   MOD_RES      19     19       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      19     19       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES      19     19       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      19     19       N6-butyryllysine; alternate.
FT                                {ECO:0000269|PubMed:27105113}.
FT   MOD_RES      19     19       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      19     19       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      24     24       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      24     24       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES      24     24       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16457588,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      24     24       N6-butyryllysine; alternate.
FT                                {ECO:0000269|PubMed:27105113}.
FT   MOD_RES      24     24       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      24     24       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:17194708}.
FT   MOD_RES      27     27       Citrulline.
FT                                {ECO:0000269|PubMed:16567635}.
FT   MOD_RES      28     28       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      28     28       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      28     28       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      28     28       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES      28     28       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      28     28       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      28     28       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      29     29       ADP-ribosylserine; alternate.
FT                                {ECO:0000269|PubMed:28190768}.
FT   MOD_RES      29     29       Phosphoserine; alternate; by AURKB, AURKC
FT                                and RPS6KA5.
FT                                {ECO:0000269|PubMed:10464286,
FT                                ECO:0000269|PubMed:11856369,
FT                                ECO:0000269|PubMed:15681610,
FT                                ECO:0000269|PubMed:15684425,
FT                                ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16457588}.
FT   MOD_RES      37     37       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:15983376,
FT                                ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      37     37       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:15983376,
FT                                ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      37     37       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      37     37       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:17189264,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      37     37       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:15983376,
FT                                ECO:0000269|PubMed:16185088,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      38     38       N6-methyllysine.
FT                                {ECO:0000269|PubMed:15983376}.
FT   MOD_RES      42     42       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:19783980}.
FT   MOD_RES      57     57       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:17194708,
FT                                ECO:0000269|PubMed:22387026}.
FT   MOD_RES      57     57       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      57     57       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES      57     57       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:17194708}.
FT   MOD_RES      57     57       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      57     57       N6-methyllysine; by EHMT2; alternate.
FT                                {ECO:0000269|PubMed:17194708,
FT                                ECO:0000269|PubMed:22387026}.
FT   MOD_RES      57     57       N6-succinyllysine; alternate.
FT                                {ECO:0000269|PubMed:22389435}.
FT   MOD_RES      58     58       Phosphoserine.
FT                                {ECO:0000269|PubMed:20850016}.
FT   MOD_RES      65     65       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      65     65       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      80     80       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P68433}.
FT   MOD_RES      80     80       N6,N6-dimethyllysine; alternate.
FT                                {ECO:0000269|PubMed:15525939,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      80     80       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES      80     80       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES      80     80       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:17194708}.
FT   MOD_RES      80     80       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:15525939,
FT                                ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES      80     80       N6-succinyllysine; alternate.
FT                                {ECO:0000269|PubMed:22389435,
FT                                ECO:0000269|PubMed:29211711}.
FT   MOD_RES      81     81       Phosphothreonine.
FT                                {ECO:0000269|PubMed:20850016}.
FT   MOD_RES      87     87       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P84243}.
FT   MOD_RES     108    108       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q71DI3}.
FT   MOD_RES     116    116       N6-acetyllysine.
FT                                {ECO:0000269|PubMed:19520870}.
FT   MOD_RES     123    123       N6-(2-hydroxyisobutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:24681537}.
FT   MOD_RES     123    123       N6-(beta-hydroxybutyryl)lysine;
FT                                alternate. {ECO:0000269|PubMed:27105115}.
FT   MOD_RES     123    123       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:19520870,
FT                                ECO:0000269|PubMed:23415232}.
FT   MOD_RES     123    123       N6-methyllysine; alternate.
FT                                {ECO:0000269|PubMed:16267050,
FT                                ECO:0000269|PubMed:17194708}.
FT   MOD_RES     123    123       N6-succinyllysine; alternate.
FT                                {ECO:0000269|PubMed:22389435}.
FT   VARIANT      28     28       K -> M (in GLM; non-brain stem pediatric
FT                                glioblastoma and diffuse intrinsic
FT                                pontine glioma; somatic mutation; results
FT                                in a global decrease of H3K27me3 levels).
FT                                {ECO:0000269|PubMed:22286216,
FT                                ECO:0000269|PubMed:23603901}.
FT                                /FTId=VAR_079018.
FT   VARIANT      37     37       K -> I (probable disease-associated
FT                                mutation found in pediatric
FT                                undifferentiated soft tissue sarcoma
FT                                samples; somatic mutation; results in
FT                                global decrease of H3K36me2 and H3K36me3
FT                                levels and increased H3K27me3 levels).
FT                                {ECO:0000269|PubMed:27174990}.
FT                                /FTId=VAR_079019.
FT   VARIANT      37     37       K -> M (probable disease-associated
FT                                mutation found in pediatric
FT                                undifferentiated soft tissue sarcoma
FT                                samples; somatic mutation; also found in
FT                                a subset of human papillomavirus-negative
FT                                head and neck squamous cell carcinomas;
FT                                results in global decrease of H3K36me2
FT                                and H3K36me3 levels and increased
FT                                H3K27me3 levels).
FT                                {ECO:0000269|PubMed:27174990,
FT                                ECO:0000269|PubMed:28067913}.
FT                                /FTId=VAR_079020.
FT   CONFLICT     70     70       R -> C (in Ref. 13; AAH67493).
FT                                {ECO:0000305}.
FT   CONFLICT    100    100       Y -> T (in Ref. 7; CAB02546).
FT                                {ECO:0000305}.
FT   CONFLICT    122    122       P -> L (in Ref. 13; AAH66884).
FT                                {ECO:0000305}.
FT   CONFLICT    135    135       Missing (in Ref. 2; AAA52651).
FT                                {ECO:0000305}.
FT   STRAND        4      7       {ECO:0000244|PDB:5SVY}.
FT   STRAND        9     15       {ECO:0000244|PDB:5WVO}.
FT   STRAND       25     27       {ECO:0000244|PDB:4X3K}.
FT   STRAND       32     34       {ECO:0000244|PDB:5VA6}.
FT   STRAND       35     37       {ECO:0000244|PDB:5V22}.
FT   STRAND       45     49       {ECO:0000244|PDB:5T1I}.
FT   HELIX        50     58       {ECO:0000244|PDB:5C3I}.
FT   HELIX        65     77       {ECO:0000244|PDB:5AV6}.
FT   STRAND       80     82       {ECO:0000244|PDB:5AV6}.
FT   HELIX        87    114       {ECO:0000244|PDB:5AV6}.
FT   STRAND      118    120       {ECO:0000244|PDB:5AV6}.
FT   HELIX       122    132       {ECO:0000244|PDB:5AV6}.
SQ   SEQUENCE   136 AA;  15404 MW;  9B89008EA50A0EF6 CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA
//
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